ID SOX10_HUMAN Reviewed; 466 AA. AC P56693; B4DV62; Q6FHW7; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1999, sequence version 1. DT 27-MAR-2024, entry version 216. DE RecName: Full=Transcription factor SOX-10; GN Name=SOX10; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT WS4C LEU-ARG-161 INS. RX PubMed=9462749; DOI=10.1038/ng0298-171; RA Pingault V., Bondurand N., Kuhlbrodt K., Goerich D.E., Prehu M.O., RA Puliti A., Herbarth B., Hermans-Borgmeyer I., Legius E., Matthijs G., RA Amiel J., Lyonnet S., Ceccherini I., Romeo G., Clayton-Smith J., Read A.P., RA Wegner M., Goossens M.; RT "SOX10 mutations in patients with Waardenburg-Hirschsprung disease."; RL Nat. Genet. 18:171-173(1998). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9760192; DOI=10.1007/s004390050793; RA Pusch C., Hustert E., Pfeifer D., Sudbeck P., Kist R., Roe B., Wang Z., RA Balling R., Blin N., Scherer G.; RT "The SOX10/Sox10 gene from human and mouse: sequence, expression, and RT transactivation by the encoded HMG domain transcription factor."; RL Hum. Genet. 103:115-123(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Small intestine; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., RA Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Placenta, and Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP CHARACTERIZATION. RX PubMed=9722528; DOI=10.1074/jbc.273.36.23033; RA Kuhlbrodt K., Schmidt C., Sock E., Pingault V., Bondurand N., Goossens M., RA Wegner M.; RT "Functional analysis of Sox10 mutations found in human Waardenburg- RT Hirschsprung patients."; RL J. Biol. Chem. 273:23033-23038(1998). RN [10] RP NUCLEOCYTOPLASMIC SHUTTLING, AND SUBCELLULAR LOCATION. RX PubMed=12138193; DOI=10.1128/mcb.22.16.5826-5834.2002; RA Rehberg S., Lischka P., Glaser G., Stamminger T., Wegner M., Rosorius O.; RT "Sox10 is an active nucleocytoplasmic shuttle protein, and shuttling is RT crucial for Sox10-mediated transactivation."; RL Mol. Cell. Biol. 22:5826-5834(2002). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [12] RP FUNCTION, AND INTERACTION WITH PAX3. RX PubMed=21965087; DOI=10.1007/s00439-011-1098-2; RA Zhang H., Chen H., Luo H., An J., Sun L., Mei L., He C., Jiang L., RA Jiang W., Xia K., Li J.D., Feng Y.; RT "Functional analysis of Waardenburg syndrome-associated PAX3 and SOX10 RT mutations: report of a dominant-negative SOX10 mutation in Waardenburg RT syndrome type II."; RL Hum. Genet. 131:491-503(2012). RN [13] RP VARIANT WS2E THR-135. RX PubMed=10441344; DOI=10.1093/hmg/8.9.1785; RA Bondurand N., Kuhlbrodt K., Pingault V., Enderich J., Sajus M., RA Tommerup N., Warburg M., Hennekam R.C.M., Read A.P., Wegner M., RA Goossens M.; RT "A molecular analysis of the Yemenite deaf-blind hypopigmentation syndrome: RT SOX10 dysfunction causes different neurocristopathies."; RL Hum. Mol. Genet. 8:1785-1789(1999). RN [14] RP INVOLVEMENT IN PCWH. RX PubMed=10762540; DOI=10.1086/302895; RA Touraine R.L., Attie-Bitach T., Manceau E., Korsch E., Sarda P., RA Pingault V., Encha-Razavi F., Pelet A., Auge J., Nivelon-Chevallier A., RA Holschneider A.M., Munnes M., Doerfler W., Goossens M., Munnich A., RA Vekemans M., Lyonnet S.; RT "Neurological phenotype in Waardenburg syndrome type 4 correlates with RT novel SOX10 truncating mutations and expression in developing brain."; RL Am. J. Hum. Genet. 66:1496-1503(2000). RN [15] RP ERRATUM OF PUBMED:10762540. RA Touraine R.L., Attie-Bitach T., Manceau E., Korsch E., Sarda P., RA Pingault V., Encha-Razavi F., Pelet A., Auge J., Nivelon-Chevallier A., RA Holschneider A.M., Munnes M., Doerfler W., Goossens M., Munnich A., RA Vekemans M., Lyonnet S.; RL Am. J. Hum. Genet. 66:2020-2020(2000). RN [16] RP INVOLVEMENT IN PCWH. RX PubMed=15004559; DOI=10.1038/ng1322; RA Inoue K., Khajavi M., Ohyama T., Hirabayashi S., Wilson J., Reggin J.D., RA Mancias P., Butler I.J., Wilkinson M.F., Wegner M., Lupski J.R.; RT "Molecular mechanism for distinct neurological phenotypes conveyed by RT allelic truncating mutations."; RL Nat. Genet. 36:361-369(2004). RN [17] RP INVOLVEMENT IN WS2E. RX PubMed=17999358; DOI=10.1086/522090; RA Bondurand N., Dastot-Le Moal F., Stanchina L., Collot N., Baral V., RA Marlin S., Attie-Bitach T., Giurgea I., Skopinski L., Reardon W., RA Toutain A., Sarda P., Echaieb A., Lackmy-Port-Lis M., Touraine R., RA Amiel J., Goossens M., Pingault V.; RT "Deletions at the SOX10 gene locus cause Waardenburg syndrome types 2 and RT 4."; RL Am. J. Hum. Genet. 81:1169-1185(2007). RN [18] RP TRANSACTIVATION REGIONS. RX PubMed=31194875; DOI=10.1093/nar/gkz523; RA Haseeb A., Lefebvre V.; RT "The SOXE transcription factors-SOX8, SOX9 and SOX10-share a bi-partite RT transactivation mechanism."; RL Nucleic Acids Res. 47:6917-6931(2019). RN [19] RP VARIANT WS4C VAL-157. RX PubMed=18348274; DOI=10.1002/ajmg.a.32181; RA Morin M., Vinuela A., Rivera T., Villamar M., Moreno-Pelayo M.A., RA Moreno F., del Castillo I.; RT "A de novo missense mutation in the gene encoding the SOX10 transcription RT factor in a Spanish sporadic case of Waardenburg syndrome type IV."; RL Am. J. Med. Genet. A 146:1032-1037(2008). RN [20] RP VARIANT PCWH PRO-174. RX PubMed=19208381; DOI=10.1002/ajmg.a.32657; RA Barnett C.P., Mendoza-Londono R., Blaser S., Gillis J., Dupuis L., RA Levin A.V., Chiang P.W., Spector E., Reardon W.; RT "Aplasia of cochlear nerves and olfactory bulbs in association with SOX10 RT mutation."; RL Am. J. Med. Genet. A 149:431-436(2009). RN [21] RP VARIANTS WS4C TRP-106; PRO-145 AND VAL-157, VARIANTS WS2E ILE-112 AND RP HIS-161, VARIANTS PCWH ILE-112; HIS-131; ASN-150; PRO-174; ALA-175; RP LEU-175; ARG-175 AND ARG-321, CHARACTERIZATION OF VARIANTS WS4C TRP-106; RP PRO-145 AND VAL-157, CHARACTERIZATION OF VARIANTS WS2E ILE-112 AND HIS-161, RP AND CHARACTERIZATION OF VARIANTS PCWH HIS-131; ASN-150; PRO-174; ALA-175; RP LEU-175 AND ARG-175. RX PubMed=21898658; DOI=10.1002/humu.21583; RA Chaoui A., Watanabe Y., Touraine R., Baral V., Goossens M., Pingault V., RA Bondurand N.; RT "Identification and functional analysis of SOX10 missense mutations in RT different subtypes of Waardenburg syndrome."; RL Hum. Mutat. 32:1436-1449(2011). RN [22] RP VARIANTS THR-108; VAL-111; GLY-135; CYS-151 AND CYS-161. RX PubMed=25077900; DOI=10.1210/jc.2014-2110; RA Marcos S., Sarfati J., Leroy C., Fouveaut C., Parent P., Metz C., RA Wolczynski S., Gerard M., Bieth E., Kurtz F., Verier-Mine O., Perrin L., RA Archambeaud F., Cabrol S., Rodien P., Hove H., Prescott T., Lacombe D., RA Christin-Maitre S., Touraine P., Hieronimus S., Dewailly D., Young J., RA Pugeat M., Hardelin J.P., Dode C.; RT "The prevalence of CHD7 missense versus truncating mutations is higher in RT patients with Kallmann syndrome than in typical CHARGE patients."; RL J. Clin. Endocrinol. Metab. 99:E2138-2143(2014). CC -!- FUNCTION: Transcription factor that plays a central role in developing CC and mature glia (By similarity). Specifically activates expression of CC myelin genes, during oligodendrocyte (OL) maturation, such as DUSP15 CC and MYRF, thereby playing a central role in oligodendrocyte maturation CC and CNS myelination (By similarity). Once induced, MYRF cooperates with CC SOX10 to implement the myelination program (By similarity). CC Transcriptional activator of MITF, acting synergistically with PAX3 CC (PubMed:21965087). Transcriptional activator of MBP, via binding to the CC gene promoter (By similarity). {ECO:0000250|UniProtKB:O55170, CC ECO:0000250|UniProtKB:Q04888, ECO:0000269|PubMed:21965087}. CC -!- SUBUNIT: Monomer. Interacts with ARMCX3 at the mitochondrial outer CC membrane surface. Interacts with PAX3 (PubMed:21965087). CC {ECO:0000250|UniProtKB:Q04888, ECO:0000269|PubMed:21965087}. CC -!- INTERACTION: CC P56693; Q5SWW7: C10orf55; NbExp=3; IntAct=EBI-1167533, EBI-12809220; CC P56693; O43186: CRX; NbExp=3; IntAct=EBI-1167533, EBI-748171; CC P56693; Q15038: DAZAP2; NbExp=3; IntAct=EBI-1167533, EBI-724310; CC P56693; Q9ULV5-2: HSF4; NbExp=3; IntAct=EBI-1167533, EBI-12056251; CC P56693; Q92993: KAT5; NbExp=3; IntAct=EBI-1167533, EBI-399080; CC P56693; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-1167533, EBI-11742507; CC P56693; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-1167533, EBI-716006; CC P56693; Q13287: NMI; NbExp=2; IntAct=EBI-1167533, EBI-372942; CC P56693; P23760: PAX3; NbExp=2; IntAct=EBI-1167533, EBI-1167564; CC P56693; P20265: POU3F2; NbExp=3; IntAct=EBI-1167533, EBI-1167176; CC P56693; P78424: POU6F2; NbExp=3; IntAct=EBI-1167533, EBI-12029004; CC P56693; P62937-2: PPIA; NbExp=3; IntAct=EBI-1167533, EBI-25884072; CC P56693; P17252: PRKCA; NbExp=3; IntAct=EBI-1167533, EBI-1383528; CC P56693; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-1167533, EBI-9090795; CC P56693; P56693: SOX10; NbExp=2; IntAct=EBI-1167533, EBI-1167533; CC P56693; P63165: SUMO1; NbExp=2; IntAct=EBI-1167533, EBI-80140; CC P56693; P63279: UBE2I; NbExp=2; IntAct=EBI-1167533, EBI-80168; CC P56693; P61981: YWHAG; NbExp=3; IntAct=EBI-1167533, EBI-359832; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12138193}. Nucleus CC {ECO:0000269|PubMed:12138193}. Mitochondrion outer membrane CC {ECO:0000250|UniProtKB:Q04888}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:Q04888}; Cytoplasmic side CC {ECO:0000250|UniProtKB:Q04888}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P56693-1; Sequence=Displayed; CC Name=2; CC IsoId=P56693-2; Sequence=VSP_053874; CC -!- TISSUE SPECIFICITY: Expressed in fetal brain and in adult brain, heart, CC small intestine and colon. CC -!- DOMAIN: The transactivation domains TAM and TAC (for transactivation CC domain in the middle and at the C-terminus, respectively) are required CC to contact transcriptional coactivators and basal transcriptional CC machinery components and thereby induce gene transactivation. CC {ECO:0000250|UniProtKB:P48436}. CC -!- DISEASE: Waardenburg syndrome 2E (WS2E) [MIM:611584]: An autosomal CC dominant auditory-pigmentary disorder characterized by sensorineural CC deafness, pigmentary disturbances of the hair, skin and eyes, and CC absence of dystopia canthorum which is the lateral displacement of the CC inner canthus of each eye. Individuals with WS2E may have neurologic CC abnormalities, including mental impairment, myelination defects, and CC ataxia. Some patients can manifest features of Kallmann syndrome. CC {ECO:0000269|PubMed:10441344, ECO:0000269|PubMed:17999358, CC ECO:0000269|PubMed:21898658}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Waardenburg syndrome 4C (WS4C) [MIM:613266]: A disorder CC characterized by the association of Waardenburg features CC (depigmentation and deafness) with the absence of enteric ganglia in CC the distal part of the intestine (Hirschsprung disease). CC {ECO:0000269|PubMed:18348274, ECO:0000269|PubMed:21898658, CC ECO:0000269|PubMed:9462749}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Peripheral demyelinating neuropathy, central dysmyelinating CC leukodystrophy, Waardenburg syndrome and Hirschsprung disease (PCWH) CC [MIM:609136]: A complex neurocristopathy that includes features of 4 CC distinct syndromes: peripheral demyelinating neuropathy, central CC dysmyelinating leukodystrophy, Waardenburg syndrome and Hirschsprung CC disease. {ECO:0000269|PubMed:10762540, ECO:0000269|PubMed:15004559, CC ECO:0000269|PubMed:19208381, ECO:0000269|PubMed:21898658}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/43768/SOX10"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ001183; CAA04576.1; -; mRNA. DR EMBL; CR456584; CAG30470.1; -; mRNA. DR EMBL; BT020029; AAV38832.1; -; mRNA. DR EMBL; AK300945; BAG62574.1; -; mRNA. DR EMBL; CR536571; CAG38808.1; -; mRNA. DR EMBL; AL031587; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC002824; AAH02824.1; -; mRNA. DR EMBL; BC007595; AAH07595.1; -; mRNA. DR CCDS; CCDS13964.1; -. [P56693-1] DR RefSeq; NP_008872.1; NM_006941.3. [P56693-1] DR AlphaFoldDB; P56693; -. DR SMR; P56693; -. DR BioGRID; 112546; 66. DR IntAct; P56693; 64. DR MINT; P56693; -. DR STRING; 9606.ENSP00000380093; -. DR iPTMnet; P56693; -. DR PhosphoSitePlus; P56693; -. DR BioMuta; SOX10; -. DR DMDM; 6175075; -. DR jPOST; P56693; -. DR MassIVE; P56693; -. DR MaxQB; P56693; -. DR PaxDb; 9606-ENSP00000380093; -. DR PeptideAtlas; P56693; -. DR ProteomicsDB; 5245; -. DR ProteomicsDB; 56933; -. [P56693-1] DR Antibodypedia; 3774; 1203 antibodies from 48 providers. DR DNASU; 6663; -. DR Ensembl; ENST00000360880.6; ENSP00000354130.2; ENSG00000100146.20. [P56693-1] DR Ensembl; ENST00000396884.8; ENSP00000380093.2; ENSG00000100146.20. [P56693-1] DR GeneID; 6663; -. DR KEGG; hsa:6663; -. DR MANE-Select; ENST00000396884.8; ENSP00000380093.2; NM_006941.4; NP_008872.1. DR UCSC; uc003aun.2; human. [P56693-1] DR AGR; HGNC:11190; -. DR CTD; 6663; -. DR DisGeNET; 6663; -. DR GeneCards; SOX10; -. DR GeneReviews; SOX10; -. DR HGNC; HGNC:11190; SOX10. DR HPA; ENSG00000100146; Group enriched (brain, salivary gland). DR MalaCards; SOX10; -. DR MIM; 602229; gene. DR MIM; 609136; phenotype. DR MIM; 611584; phenotype. DR MIM; 613266; phenotype. DR neXtProt; NX_P56693; -. DR OpenTargets; ENSG00000100146; -. DR Orphanet; 478; Kallmann syndrome. DR Orphanet; 163746; Peripheral demyelinating neuropathy-central dysmyelinating leukodystrophy-Waardenburg syndrome-Hirschsprung disease. DR Orphanet; 895; Waardenburg syndrome type 2. DR Orphanet; 897; Waardenburg-Shah syndrome. DR PharmGKB; PA36027; -. DR VEuPathDB; HostDB:ENSG00000100146; -. DR eggNOG; KOG0527; Eukaryota. DR GeneTree; ENSGT00940000158046; -. DR HOGENOM; CLU_031800_0_0_1; -. DR InParanoid; P56693; -. DR OMA; ATIQAHY; -. DR OrthoDB; 2902801at2759; -. DR PhylomeDB; P56693; -. DR PathwayCommons; P56693; -. DR Reactome; R-HSA-9619665; EGR2 and SOX10-mediated initiation of Schwann cell myelination. DR Reactome; R-HSA-9764302; Regulation of CDH19 Expression and Function. DR SignaLink; P56693; -. DR SIGNOR; P56693; -. DR BioGRID-ORCS; 6663; 108 hits in 1188 CRISPR screens. DR GeneWiki; SOX10; -. DR GenomeRNAi; 6663; -. DR Pharos; P56693; Tbio. DR PRO; PR:P56693; -. DR Proteomes; UP000005640; Chromosome 22. DR RNAct; P56693; Protein. DR Bgee; ENSG00000100146; Expressed in inferior olivary complex and 164 other cell types or tissues. DR ExpressionAtlas; P56693; baseline and differential. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB. DR GO; GO:0001216; F:DNA-binding transcription activator activity; ISS:UniProtKB. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; TAS:GO_Central. DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB. DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:Ensembl. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:1990841; F:promoter-specific chromatin binding; IEA:Ensembl. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL. DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB. DR GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc. DR GO; GO:0048469; P:cell maturation; IEA:Ensembl. DR GO; GO:0071393; P:cellular response to progesterone stimulus; IEA:Ensembl. DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl. DR GO; GO:0022010; P:central nervous system myelination; ISS:UniProtKB. DR GO; GO:0048589; P:developmental growth; IEA:Ensembl. DR GO; GO:0048546; P:digestive tract morphogenesis; IEA:Ensembl. DR GO; GO:0048484; P:enteric nervous system development; IBA:GO_Central. DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl. DR GO; GO:0032808; P:lacrimal gland development; IEA:Ensembl. DR GO; GO:0030318; P:melanocyte differentiation; IEA:Ensembl. DR GO; GO:0061138; P:morphogenesis of a branching epithelium; IEA:Ensembl. DR GO; GO:0002009; P:morphogenesis of an epithelium; IBA:GO_Central. DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl. DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl. DR GO; GO:0010626; P:negative regulation of Schwann cell proliferation; IEA:Ensembl. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0001755; P:neural crest cell migration; IBA:GO_Central. DR GO; GO:0007405; P:neuroblast proliferation; IEA:Ensembl. DR GO; GO:0014003; P:oligodendrocyte development; ISS:UniProtKB. DR GO; GO:0048709; P:oligodendrocyte differentiation; ISS:UniProtKB. DR GO; GO:0007422; P:peripheral nervous system development; IBA:GO_Central. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl. DR GO; GO:0014015; P:positive regulation of gliogenesis; IEA:Ensembl. DR GO; GO:0031643; P:positive regulation of myelination; IEA:Ensembl. DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; IEA:Ensembl. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:GO_Central. DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; IEA:Ensembl. DR CDD; cd22031; HMG-box_SoxE; 1. DR Gene3D; 1.10.30.10; High mobility group box domain; 1. DR InterPro; IPR009071; HMG_box_dom. DR InterPro; IPR036910; HMG_box_dom_sf. DR InterPro; IPR022151; Sox_N. DR PANTHER; PTHR45803; SOX100B; 1. DR PANTHER; PTHR45803:SF6; TRANSCRIPTION FACTOR SOX-10; 1. DR Pfam; PF00505; HMG_box; 1. DR Pfam; PF12444; Sox_N; 1. DR SMART; SM00398; HMG; 1. DR SUPFAM; SSF47095; HMG-box; 1. DR PROSITE; PS50118; HMG_BOX_2; 1. DR Genevisible; P56693; HS. PE 1: Evidence at protein level; KW Activator; Alternative splicing; Cytoplasm; Deafness; Disease variant; KW DNA-binding; Hirschsprung disease; Kallmann syndrome; Membrane; KW Mitochondrion; Mitochondrion outer membrane; Nucleus; Phosphoprotein; KW Reference proteome; Transcription; Transcription regulation; KW Waardenburg syndrome. FT CHAIN 1..466 FT /note="Transcription factor SOX-10" FT /id="PRO_0000048746" FT DNA_BIND 104..172 FT /note="HMG box" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267" FT REGION 1..67 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 62..102 FT /note="Dimerization (DIM)" FT /evidence="ECO:0000303|PubMed:31194875" FT REGION 160..199 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 212..274 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 228..310 FT /note="Transactivation domain (TAM)" FT /evidence="ECO:0000303|PubMed:31194875" FT REGION 353..466 FT /note="Transactivation domain (TAC)" FT /evidence="ECO:0000303|PubMed:31194875" FT REGION 354..375 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 433..466 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 134..145 FT /note="Nuclear export signal" FT COMPBIAS 53..67 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 160..184 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 251..266 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 436..466 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 24 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19369195" FT VAR_SEQ 262..441 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_053874" FT VARIANT 106 FT /note="R -> W (in WS4C; loss of DNA binding and FT transactivation capacity)" FT /evidence="ECO:0000269|PubMed:21898658" FT /id="VAR_066747" FT VARIANT 108 FT /note="M -> T (found in a patient with Kallmann syndrome)" FT /evidence="ECO:0000269|PubMed:25077900" FT /id="VAR_072981" FT VARIANT 111 FT /note="F -> V (found in a patient with Kallmann syndrome)" FT /evidence="ECO:0000269|PubMed:25077900" FT /id="VAR_072982" FT VARIANT 112 FT /note="M -> I (in WS2E and PCWH; increased DNA binding FT capacity)" FT /evidence="ECO:0000269|PubMed:21898658" FT /id="VAR_066748" FT VARIANT 131 FT /note="N -> H (in PCWH; reduced DNA binding capacity)" FT /evidence="ECO:0000269|PubMed:21898658" FT /id="VAR_066749" FT VARIANT 135 FT /note="S -> G (found in a patient with Kallmann syndrome)" FT /evidence="ECO:0000269|PubMed:25077900" FT /id="VAR_072983" FT VARIANT 135 FT /note="S -> T (in WS2E; without neurologic involvement; FT dbSNP:rs74315515)" FT /evidence="ECO:0000269|PubMed:10441344" FT /id="VAR_021386" FT VARIANT 145 FT /note="L -> P (in WS4C; loss of DNA binding and FT transactivation capacity)" FT /evidence="ECO:0000269|PubMed:21898658" FT /id="VAR_066750" FT VARIANT 150 FT /note="K -> N (in PCWH; loss of DNA binding and FT transactivation capacity)" FT /evidence="ECO:0000269|PubMed:21898658" FT /id="VAR_066751" FT VARIANT 151 FT /note="R -> C (found in a patient with Kallmann syndrome; FT dbSNP:rs1463736052)" FT /evidence="ECO:0000269|PubMed:25077900" FT /id="VAR_072984" FT VARIANT 157 FT /note="A -> V (in WS4C; loss of DNA binding and FT transactivation capacity; dbSNP:rs121909117)" FT /evidence="ECO:0000269|PubMed:18348274, FT ECO:0000269|PubMed:21898658" FT /id="VAR_066752" FT VARIANT 161 FT /note="R -> C (found in a patient with Kallmann syndrome)" FT /evidence="ECO:0000269|PubMed:25077900" FT /id="VAR_072985" FT VARIANT 161 FT /note="R -> H (in WS2E; reduced DNA binding capacity; FT dbSNP:rs750566714)" FT /evidence="ECO:0000269|PubMed:21898658" FT /id="VAR_066753" FT VARIANT 161 FT /note="R -> RLR (in WS4C)" FT /evidence="ECO:0000269|PubMed:9462749" FT /id="VAR_003743" FT VARIANT 174 FT /note="Q -> P (in PCWH; without Hirschsprung disease; FT reduced DNA binding capacity; dbSNP:rs267607081)" FT /evidence="ECO:0000269|PubMed:19208381, FT ECO:0000269|PubMed:21898658" FT /id="VAR_066754" FT VARIANT 175 FT /note="P -> A (in PCWH; reduced DNA binding capacity)" FT /evidence="ECO:0000269|PubMed:21898658" FT /id="VAR_066755" FT VARIANT 175 FT /note="P -> L (in PCWH; reduced DNA binding capacity)" FT /evidence="ECO:0000269|PubMed:21898658" FT /id="VAR_066756" FT VARIANT 175 FT /note="P -> R (in PCWH; reduced DNA binding capacity)" FT /evidence="ECO:0000269|PubMed:21898658" FT /id="VAR_066757" FT VARIANT 321 FT /note="G -> R (in PCWH)" FT /evidence="ECO:0000269|PubMed:21898658" FT /id="VAR_066758" FT CONFLICT 222 FT /note="P -> L (in Ref. 5; CAG38808)" FT /evidence="ECO:0000305" FT CONFLICT 461 FT /note="T -> M (in Ref. 5; CAG38808)" FT /evidence="ECO:0000305" SQ SEQUENCE 466 AA; 49911 MW; FAA1EC108D4DE6A1 CRC64; MAEEQDLSEV ELSPVGSEEP RCLSPGSAPS LGPDGGGGGS GLRASPGPGE LGKVKKEQQD GEADDDKFPV CIREAVSQVL SGYDWTLVPM PVRVNGASKS KPHVKRPMNA FMVWAQAARR KLADQYPHLH NAELSKTLGK LWRLLNESDK RPFIEEAERL RMQHKKDHPD YKYQPRRRKN GKAAQGEAEC PGGEAEQGGT AAIQAHYKSA HLDHRHPGEG SPMSDGNPEH PSGQSHGPPT PPTTPKTELQ SGKADPKRDG RSMGEGGKPH IDFGNVDIGE ISHEVMSNME TFDVAELDQY LPPNGHPGHV SSYSAAGYGL GSALAVASGH SAWISKPPGV ALPTVSPPGV DAKAQVKTET AGPQGPPHYT DQPSTSQIAY TSLSLPHYGS AFPSISRPQF DYSDHQPSGP YYGHSGQASG LYSAFSYMGP SQRPLYTAIS DPSPSGPQSH SPTHWEQPVY TTLSRP //