ID PAX3_HUMAN Reviewed; 479 AA. AC P23760; G5E9C1; Q16448; Q494Z3; Q494Z4; Q53T90; Q6GSJ9; Q86UQ2; Q86UQ3; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 02-SEP-2026, entry version 246. DE RecName: Full=Paired box protein Pax-3; DE AltName: Full=HuP2; GN Name=PAX3; Synonyms=HUP2; 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] (ISOFORMS PAX3G AND PAX3H), AND ALTERNATIVE RP SPLICING. RX PubMed=14639621; DOI=10.1002/ijc.11527; RA Parker C.J., Shawcross S.G., Li H., Wang Q.-Y., Herrington C.S., Kumar S., RA MacKie R.M., Prime W., Renne I.G., Sisley K., Kumar P.; RT "Expression of PAX 3 alternatively spliced transcripts and identification RT of two new isoforms in human tumors of neural crest origin."; RL Int. J. Cancer 108:314-320(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7). 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS PAX3B; 6 AND 7). RC TISSUE=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 [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29 AND 197-479. RX PubMed=7782066; DOI=10.1016/0888-7543(95)80076-x; RA Macina R.A., Barr F.G., Galili N., Riethman H.C.; RT "Genomic organization of the human PAX3 gene: DNA sequence analysis of the RT region disrupted in alveolar rhabdomyosarcoma."; RL Genomics 26:1-8(1995). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 30-195. RX PubMed=2501086; DOI=10.1002/j.1460-2075.1989.tb03490.x; RA Burri M., Tromvoukis Y., Bopp D., Frigerio G., Noll M.; RT "Conservation of the paired domain in metazoans and its structure in three RT isolated human genes."; RL EMBO J. 8:1183-1190(1989). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 196-392, AND VARIANTS WS1 LEU-45 AND RP ASP-99. RX PubMed=7981674; DOI=10.1093/hmg/3.7.1069; RA Tassabehji M., Newton V.E., Leverton K., Turnbull K., Seemanova E., RA Kunze J., Sperling K., Strachan T., Read A.P.; RT "PAX3 gene structure and mutations: close analogies between Waardenburg RT syndrome and the Splotch mouse."; RL Hum. Mol. Genet. 3:1069-1074(1994). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PAX3A AND PAX3B). RX PubMed=7545913; DOI=10.1007/bf00212021; RA Tsukamoto K., Nakamura Y., Niikawa N.; RT "Isolation of two isoforms of the PAX3 gene transcripts and their tissue- RT specific alternative expression in human adult tissues."; RL Hum. Genet. 93:270-274(1994). RN [10] RP NUCLEOTIDE SEQUENCE OF 1-319 (ISOFORM 6/7), AND CHROMOSOMAL TRANSLOCATION RP WITH NCOA1. RX PubMed=15313887; DOI=10.1158/0008-5472.can-04-0844; RA Wachtel M., Dettling M., Koscielniak E., Stegmaier S., Treuner J., RA Simon-Klingenstein K., Buehlmann P., Niggli F.K., Schaefer B.W.; RT "Gene expression signatures identify rhabdomyosarcoma subtypes and detect a RT novel t(2;2)(q35;p23) translocation fusing PAX3 to NCOA1."; RL Cancer Res. 64:5539-5545(2004). RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 56-74, AND VARIANT WS1 63-ALA--ILE-67 RP DEL. RX PubMed=1347148; DOI=10.1038/355635a0; RA Tassabehji M., Read A.P., Newton V.E., Harris R., Balling R., Gruss P., RA Strachan T.; RT "Waardenburg's syndrome patients have mutations in the human homologue of RT the Pax-3 paired box gene."; RL Nature 355:635-636(1992). RN [12] RP NUCLEOTIDE SEQUENCE OF 265-319. RA Lalwani A.K., Ploplis B., Fex J., Grundfast K.M., San Agustin T.B., RA Wilcox E.R.; RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases. RN [13] RP INVOLVEMENT IN RMS2, AND CHROMOSOMAL TRANSLOCATION WITH FOXO1. RX PubMed=8275086; DOI=10.1038/ng1193-230; RA Galili N., Davis R.J., Fredericks W.J., Mukhopadhyay S., Rauscher F.J. III, RA Emanuel B.S., Rovera G., Barr F.G.; RT "Fusion of a fork head domain gene to PAX3 in the solid tumour alveolar RT rhabdomyosarcoma."; RL Nat. Genet. 5:230-235(1993). RN [14] RP INTERACTION WITH DAXX. RX PubMed=10393185; DOI=10.1093/emboj/18.13.3702; RA Hollenbach A.D., Sublett J.E., McPherson C.J., Grosveld G.; RT "The Pax3-FKHR oncoprotein is unresponsive to the Pax3-associated repressor RT hDaxx."; RL EMBO J. 18:3702-3711(1999). RN [15] RP INVOLVEMENT IN WS1. RX PubMed=1303193; DOI=10.1093/hmg/1.4.243; RA Morell R., Friedman T.B., Moeljopawiro S., Hartono S., Asher J.H. Jr.; RT "A frameshift mutation in the HuP2 paired domain of the probable human RT homolog of murine Pax-3 is responsible for Waardenburg syndrome type 1 in RT an Indonesian family."; RL Hum. Mol. Genet. 1:243-247(1992). RN [16] RP ALTERNATIVE SPLICING, AND FUNCTION. RX PubMed=16951170; DOI=10.1158/0008-5472.can-06-0947; RA Wang Q., Kumar S., Slevin M., Kumar P.; RT "Functional analysis of alternative isoforms of the transcription factor RT PAX3 in melanocytes in vitro."; RL Cancer Res. 66:8574-8580(2006). RN [17] RP PHOSPHORYLATION AT SER-201; SER-205 AND SER-209. RX PubMed=21440083; DOI=10.1016/j.biocel.2011.03.010; RA Dietz K.N., Miller P.J., Iyengar A.S., Loupe J.M., Hollenbach A.D.; RT "Identification of serines 201 and 209 as sites of Pax3 phosphorylation and RT the altered phosphorylation status of Pax3-FOXO1 during early myogenic RT differentiation."; RL Int. J. Biochem. Cell Biol. 43:936-945(2011). RN [18] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SOX10, AND RP CHARACTERIZATION OF VARIANT WS1 ASP-80. 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 [19] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 219-278 IN COMPLEX WITH DNA, AND RP SUBUNIT. RX PubMed=19199574; DOI=10.1021/bi802052y; RA Birrane G., Soni A., Ladias J.A.; RT "Structural basis for DNA recognition by the human PAX3 homeodomain."; RL Biochemistry 48:1148-1155(2009). RN [20] RP VARIANT WS1 LEU-50. RX PubMed=1347149; DOI=10.1038/355637a0; RA Baldwin C.T., Hoth C.F., Amos J.A., Da-Silva E.O., Milunsky A.; RT "An exonic mutation in the HuP2 paired domain gene causes Waardenburg's RT syndrome."; RL Nature 355:637-638(1992). RN [21] RP VARIANT WS1 ALA-81. RX PubMed=8490648; DOI=10.1038/ng0193-26; RA Tassabehji M., Read A.P., Newton V.E., Patton M., Gruss P., Harris R., RA Strachan T.; RT "Mutations in the PAX3 gene causing Waardenburg syndrome type 1 and type RT 2."; RL Nat. Genet. 3:26-30(1993). RN [22] RP VARIANT WS3 HIS-47, AND VARIANT WS1 LEU-56. RX PubMed=8447316; RA Hoth C.F., Milunsky A., Lipsky N., Sheffer R., Clarren S.K., Baldwin C.T.; RT "Mutations in the paired domain of the human PAX3 gene cause Klein- RT Waardenburg syndrome (WS-III) as well as Waardenburg syndrome type I (WS- RT I)."; RL Am. J. Hum. Genet. 52:455-462(1993). RN [23] RP VARIANT WS1 VAL-62. RX PubMed=7833953; DOI=10.1002/humu.1380040310; RA Pierpont J.W., Doolan L.D., Amann K., Snead G.R., Erickson R.P.; RT "A single base pair substitution within the paired box of PAX3 in an RT individual with Waardenburg syndrome type 1 (WS1)."; RL Hum. Mutat. 4:227-228(1994). RN [24] RP VARIANTS WS1 PHE-265 AND GLY-271. RX PubMed=7825605; DOI=10.1016/s0003-3170(04)74851-8; RA Lalwani A.K., Brister J.R., Fex J., Grundfast K.M., Ploplis B., RA San Agustin T.B., Wilcox E.R.; RT "Further elucidation of the genomic structure of PAX3, and identification RT of two different point mutations within the PAX3 homeobox that cause RT Waardenburg syndrome type 1 in two families."; RL Am. J. Hum. Genet. 56:75-83(1995). RN [25] RP VARIANT WS3 PHE-84. RX PubMed=7726174; RA Zlotogora J., Lerer I., Bar-David S., Ergaz Z., Abeliovich D.; RT "Homozygosity for Waardenburg syndrome."; RL Am. J. Hum. Genet. 56:1173-1178(1995). RN [26] RP VARIANTS WS1 MET-60; GLU-85 AND SER-238. RX PubMed=8533800; DOI=10.1002/ajmg.1320580205; RA Baldwin C.T., Hoth C.F., Macina R.A., Milunsky A.; RT "Mutations in PAX3 that cause Waardenburg syndrome type I: ten new RT mutations and review of the literature."; RL Am. J. Med. Genet. 58:115-122(1995). RN [27] RP VARIANTS WS1 MET-78; ALA-81; ASP-99; CYS-266; CYS-270; CYS-271 AND HIS-271, RP AND VARIANT LYS-315. RX PubMed=8589691; DOI=10.1093/hmg/4.11.2131; RA Tassabehji M., Newton V.E., Liu X.-Z., Brady A., Donnai D., RA Krajewska-Walasek M., Murday V., Norman A., Obersztyn E., Reardon W., RA Rice J.C., Trembath R., Wieacker P., Whiteford M., Winter R., Read A.P.; RT "The mutational spectrum in Waardenburg syndrome."; RL Hum. Mol. Genet. 4:2131-2137(1995). RN [28] RP VARIANTS WS1 ARG-48; 223-ARG--PHE-479 DEL; CYS-270; HIS-271 AND LYS-273, RP AND VARIANT LYS-315. RX PubMed=8845842; DOI=10.1093/hmg/5.4.497; RA Pandya A., Xia X.-J., Landa B.L., Arnos K.S., Israel J., Lloyd J., RA James A.L., Diehl S.R., Blanton S.H., Nance W.E.; RT "Phenotypic variation in Waardenburg syndrome: mutational heterogeneity, RT modifier genes or polygenic background?"; RL Hum. Mol. Genet. 5:497-502(1996). RN [29] RP VARIANT CDHS LYS-47. RX PubMed=8664898; RX DOI=10.1002/(sici)1098-1004(1996)7:1<30::aid-humu4>3.0.co;2-t; RA Asher J.H. Jr., Sommer A., Morell R., Friedman T.B.; RT "Missense mutation in the paired domain of PAX3 causes craniofacial- RT deafness-hand syndrome."; RL Hum. Mutat. 7:30-35(1996). RN [30] RP VARIANT LYS-315. RX PubMed=8863157; DOI=10.1136/jmg.33.8.655; RA Hol F.A., Geurds M.P.A., Chatkupt S., Shugart Y.Y., Balling R., RA Schrander-Stumpel C.T.R.M., Johnson W.G., Hamel B.C.J., Mariman E.C.M.; RT "PAX genes and human neural tube defects: an amino acid substitution in RT PAX1 in a patient with spina bifida."; RL J. Med. Genet. 33:655-660(1996). RN [31] RP VARIANT WS1 PHE-59. RX PubMed=9067759; RX DOI=10.1002/(sici)1098-1004(1997)9:2<177::aid-humu11>3.0.co;2-#; RA Soejima H., Fujimoto M., Tsukamoto K., Matsumoto N., Yoshiura K., RA Fukushima Y., Jinno Y., Niikawa N.; RT "Three novel PAX3 mutations observed in patients with Waardenburg syndrome RT type 1."; RL Hum. Mutat. 9:177-180(1997). RN [32] RP VARIANT WS1 VAL-62. RX PubMed=9452070; DOI=10.1002/humu.1380110149; RA Hol F.A., Geurds M.P.A., Cremers C.W.R.J., Hamel B.C.J., Mariman E.C.M.; RT "Identification of two PAX3 mutations causing Waardenburg syndrome, one RT within the paired domain (M62V) and the other downstream of the homeodomain RT (Q282X)."; RL Hum. Mutat. Suppl. 1:S145-S147(1998). RN [33] RP VARIANT WS1 HIS-391. RX PubMed=9541113; DOI=10.1136/jmg.35.3.248; RA Carey M.L., Friedman T.B., Asher J.H. Jr., Innis J.W.; RT "Septo-optic dysplasia and WS1 in the proband of a WS1 family segregating RT for a novel mutation in PAX3 exon 7."; RL J. Med. Genet. 35:248-250(1998). RN [34] RP VARIANT LYS-315. RX PubMed=9584079; DOI=10.1006/mcpr.1997.0149; RA Wang C., Kim E., Attaie A., Smith T.N., Wilcox E.R., Lalwani A.K.; RT "A PAX3 polymorphism (T315K) in a family exhibiting Waardenburg syndrome RT type 2."; RL Mol. Cell. Probes 12:55-57(1998). RN [35] RP VARIANT WS1 ASN-59. RA Markova T.G., Shevtsov S.P., Moskolenko L.N., Lantsov A.A., Schwartz E.I.; RT "A novel missense mutation Ile59Asn in the PAX3 gene in a family with RT Waardenburg syndrome type I."; RL Hum. Mutat. 13:85-85(1999). RN [36] RP VARIANT WS3 CYS-270. RA Bottani A., Antonarakis S.E., Blouin J.-L.; RL Submitted (MAY-1999) to UniProtKB. RN [37] RP VARIANT WS1 LEU-73. RX PubMed=10779847; DOI=10.1076/1381-6810(200003)21:1;1-i;ft025; RA Sotirova V.N., Rezaie T.M., Khoshsorour M.M., Sarfarazi M.; RT "Identification of a novel mutation in the paired domain of PAX3 in an RT Iranian family with Waardenburg syndrome type I."; RL Ophthalmic Genet. 21:25-28(2000). RN [38] RP VARIANT WS1 MET-60, AND VARIANT WS3 HIS-90. RX PubMed=12949970; DOI=10.1002/ajmg.a.20260; RA Wollnik B., Tukel T., Uyguner O., Ghanbari A., Kayserili H., Emiroglu M., RA Yuksel-Apak M.; RT "Homozygous and heterozygous inheritance of PAX3 mutations causes different RT types of Waardenburg syndrome."; RL Am. J. Med. Genet. A 122:42-45(2003). RN [39] RP VARIANT WS1 PRO-234. RX PubMed=16971891; RA Qin W., Shu A., Qian X., Gao J., Xing Q., Zhang J., Zheng Y., Li X., Li S., RA Feng G., He L.; RT "A novel mutation of PAX3 in a Chinese family with Waardenburg syndrome."; RL Mol. Vis. 12:1001-1008(2006). RN [40] RP VARIANTS WS1 ASP-80; 223-ARG--PHE-479 DEL; PRO-234 AND HIS-271. RX PubMed=20478267; DOI=10.1016/j.bbrc.2010.05.066; RA Chen H., Jiang L., Xie Z., Mei L., He C., Hu Z., Xia K., Feng Y.; RT "Novel mutations of PAX3, MITF, and SOX10 genes in Chinese patients with RT type I or type II Waardenburg syndrome."; RL Biochem. Biophys. Res. Commun. 397:70-74(2010). CC -!- FUNCTION: Transcription factor that may regulate cell proliferation, CC migration and apoptosis. Involved in neural development and myogenesis. CC Transcriptional activator of MITF, acting synergistically with SOX10 CC (PubMed:21965087). {ECO:0000269|PubMed:16951170, CC ECO:0000269|PubMed:21965087}. CC -!- SUBUNIT: Can bind to DNA as a homodimer or a heterodimer with PAX7. CC Interacts with PAXBP1; the interaction links PAX3 to a WDR5-containing CC histone methyltransferase complex. Interacts with DAXX. Interacts with CC TBX18. Interacts with SOX10 (PubMed:21965087). CC {ECO:0000250|UniProtKB:P24610, ECO:0000269|PubMed:10393185, CC ECO:0000269|PubMed:19199574, ECO:0000269|PubMed:21965087}. CC -!- INTERACTION: CC P23760; P20265: POU3F2; NbExp=2; IntAct=EBI-1167564, EBI-1167176; CC P23760; P56693: SOX10; NbExp=2; IntAct=EBI-1167564, EBI-1167533; CC P23760-8; O94829: IPO13; NbExp=3; IntAct=EBI-12105196, EBI-747310; CC P23760-8; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-12105196, EBI-11962084; CC P23760-8; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-12105196, EBI-10261141; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21965087}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=8; CC Name=Pax3; Synonyms=Pax3C; CC IsoId=P23760-1; Sequence=Displayed; CC Name=Pax3A; CC IsoId=P23760-2; Sequence=VSP_002355, VSP_002356; CC Name=Pax3B; CC IsoId=P23760-3; Sequence=VSP_002357, VSP_002358; CC Name=Pax3G; CC IsoId=P23760-4; Sequence=VSP_042004; CC Name=Pax3H; CC IsoId=P23760-5; Sequence=VSP_042005; CC Name=6; CC IsoId=P23760-6; Sequence=VSP_043634, VSP_043635; CC Name=7; CC IsoId=P23760-7; Sequence=VSP_043635; CC Name=Pax3E; CC IsoId=P23760-8; Sequence=VSP_044915; CC -!- DISEASE: Waardenburg syndrome 1 (WS1) [MIM:193500]: WS1 is an autosomal CC dominant disorder characterized by non-progressive sensorineural CC deafness, pigmentary disturbances such as frontal white blaze of hair, CC heterochromia of irides, white eyelashes, leukoderma, and wide bridge CC of nose owing to lateral displacement of the inner canthus of each eye CC (dystopia canthorum). WS1 shows variable clinical expression and some CC affected individuals do not manifest hearing impairment or iris CC pigmentation disturbances. Dystopia canthorum is the most consistent CC sign and is found in 98% of the patients. {ECO:0000269|PubMed:10779847, CC ECO:0000269|PubMed:12949970, ECO:0000269|PubMed:1303193, CC ECO:0000269|PubMed:1347148, ECO:0000269|PubMed:1347149, CC ECO:0000269|PubMed:16971891, ECO:0000269|PubMed:20478267, CC ECO:0000269|PubMed:21965087, ECO:0000269|PubMed:7825605, CC ECO:0000269|PubMed:7833953, ECO:0000269|PubMed:7981674, CC ECO:0000269|PubMed:8447316, ECO:0000269|PubMed:8490648, CC ECO:0000269|PubMed:8533800, ECO:0000269|PubMed:8589691, CC ECO:0000269|PubMed:8845842, ECO:0000269|PubMed:9067759, CC ECO:0000269|PubMed:9452070, ECO:0000269|PubMed:9541113, CC ECO:0000269|Ref.35}. Note=The disease is caused by variants affecting CC the gene represented in this entry. CC -!- DISEASE: Waardenburg syndrome 3 (WS3) [MIM:148820]: WS3 is an autosomal CC dominant disorder characterized by sensorineural deafness, pigmentary CC disturbances, dystopia canthorum and limb anomalies such as hypoplasia CC of the musculoskeletal system, flexion contractures, fusion of the CC carpal bones, syndactylies. {ECO:0000269|PubMed:12949970, CC ECO:0000269|PubMed:7726174, ECO:0000269|PubMed:8447316, CC ECO:0000269|Ref.36}. Note=The disease is caused by variants affecting CC the gene represented in this entry. CC -!- DISEASE: Craniofacial-deafness-hand syndrome (CDHS) [MIM:122880]: CC Thought to be an autosomal dominant disease which comprises absence or CC hypoplasia of the nasal bones, hypoplastic maxilla, small and short CC nose with thin nares, limited movement of the wrist, short palpebral CC fissures, ulnar deviation of the fingers, hypertelorism and profound CC sensory-neural deafness. {ECO:0000269|PubMed:8664898}. Note=The disease CC is caused by variants affecting the gene represented in this entry. CC -!- DISEASE: Rhabdomyosarcoma 2 (RMS2) [MIM:268220]: A form of CC rhabdomyosarcoma, a highly malignant tumor of striated muscle derived CC from primitive mesenchymal cells and exhibiting differentiation along CC rhabdomyoblastic lines. Rhabdomyosarcoma is one of the most frequently CC occurring soft tissue sarcomas and the most common in children. It CC occurs in four forms: alveolar, pleomorphic, embryonal and botryoidal CC rhabdomyosarcomas. {ECO:0000269|PubMed:8275086}. Note=The gene CC represented in this entry is involved in disease pathogenesis. A CC chromosomal aberration involving PAX3 is found in rhabdomyosarcoma. CC Translocation (2;13)(q35;q14) with FOXO1. The resulting protein is a CC transcriptional activator. {ECO:0000269|PubMed:8275086}. CC -!- DISEASE: Note=A chromosomal aberration involving PAX3 is a cause of CC rhabdomyosarcoma. Translocation t(2;2)(q35;p23) with NCOA1 generates CC the NCOA1-PAX3 oncogene consisting of the N-terminus part of PAX3 and CC the C-terminus part of NCOA1. The fusion protein acts as a CC transcriptional activator. Rhabdomyosarcoma is the most common soft CC tissue carcinoma in childhood, representing 5-8% of all malignancies in CC children. {ECO:0000269|PubMed:15313887}. CC -!- SIMILARITY: Belongs to the paired homeobox family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/70/PAX3"; 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; AY251279; AAP13872.1; -; mRNA. DR EMBL; AY251280; AAP13873.1; -; mRNA. DR EMBL; AK291278; BAF83967.1; -; mRNA. DR EMBL; AC010980; AAY14900.1; -; Genomic_DNA. DR EMBL; AC012591; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471063; EAW70789.1; -; Genomic_DNA. DR EMBL; CH471063; EAW70791.1; -; Genomic_DNA. DR EMBL; CH471063; EAW70794.1; -; Genomic_DNA. DR EMBL; CH471063; EAW70796.1; -; Genomic_DNA. DR EMBL; BC063547; AAH63547.1; -; mRNA. DR EMBL; BC101299; AAI01300.1; -; mRNA. DR EMBL; BC101300; AAI01301.1; -; mRNA. DR EMBL; BC101301; AAI01302.1; -; mRNA. DR EMBL; BC101302; AAI01303.1; -; mRNA. DR EMBL; BC114363; AAI14364.1; -; mRNA. DR EMBL; U12263; AAA80573.1; -; Genomic_DNA. DR EMBL; U12259; AAA80574.1; -; Genomic_DNA. DR EMBL; U12258; AAA80574.1; JOINED; Genomic_DNA. DR EMBL; U12260; AAA80574.1; JOINED; Genomic_DNA. DR EMBL; U12262; AAA80574.1; JOINED; Genomic_DNA. DR EMBL; X15043; CAA33145.1; -; Genomic_DNA. DR EMBL; X15252; CAA33145.1; JOINED; Genomic_DNA. DR EMBL; X15253; CAA33145.1; JOINED; Genomic_DNA. DR EMBL; Z29972; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z29973; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z29974; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; S69369; AAB30167.1; -; mRNA. DR EMBL; S69370; AAB30168.1; -; mRNA. DR EMBL; AY633656; AAT47737.1; -; mRNA. DR EMBL; S83614; AAB21476.1; -; Genomic_DNA. DR EMBL; L10614; AAA91849.1; -; Genomic_DNA. DR CCDS; CCDS2448.1; -. [P23760-8] DR CCDS; CCDS2449.1; -. [P23760-5] DR CCDS; CCDS2450.1; -. [P23760-4] DR CCDS; CCDS2451.1; -. [P23760-3] DR CCDS; CCDS42825.1; -. [P23760-7] DR CCDS; CCDS42826.1; -. [P23760-1] DR CCDS; CCDS46522.1; -. [P23760-6] DR CCDS; CCDS46523.1; -. [P23760-2] DR PIR; I54276; I54276. DR PIR; I68547; I68547. DR PIR; S06960; S06960. DR RefSeq; NP_000429.2; NM_000438.6. [P23760-2] DR RefSeq; NP_001120838.1; NM_001127366.3. [P23760-6] DR RefSeq; NP_039230.1; NM_013942.5. [P23760-3] DR RefSeq; NP_852122.1; NM_181457.4. [P23760-1] DR RefSeq; NP_852123.1; NM_181458.4. [P23760-7] DR RefSeq; NP_852124.1; NM_181459.4. [P23760-8] DR RefSeq; NP_852125.1; NM_181460.4. [P23760-5] DR RefSeq; NP_852126.1; NM_181461.4. [P23760-4] DR PDB; 3CMY; X-ray; 1.95 A; A=219-278. DR AlphaFoldDB; P23760; -. DR SMR; P23760; -. DR BioGRID; 111111; 37. DR CORUM; P23760; -. DR FunCoup; P23760; 906. DR IntAct; P23760; 25. DR MINT; P23760; -. DR NDEx; IQUERY-CP-PAX3; 7 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000375921; -. DR BindingDB; P23760; -. DR iPTMnet; P23760; -. DR PhosphoSitePlus; P23760; -. DR BioMuta; PAX3; -. DR DMDM; 1172022; -. DR jPOST; P23760; -. DR MassIVE; P23760; -. DR PaxDb; 9606-ENSP00000375921; -. DR PeptideAtlas; P23760; -. DR ProteomicsDB; 33896; -. DR ProteomicsDB; 54150; -. [P23760-1] DR ProteomicsDB; 54151; -. [P23760-2] DR ProteomicsDB; 54152; -. [P23760-3] DR ProteomicsDB; 54153; -. [P23760-4] DR ProteomicsDB; 54154; -. [P23760-5] DR ProteomicsDB; 54155; -. [P23760-6] DR ProteomicsDB; 54156; -. [P23760-7] DR Pumba; P23760; -. DR Antibodypedia; 4602; 573 antibodies from 46 providers. DR DNASU; 5077; -. DR Ensembl; ENST00000258387.6; ENSP00000258387.5; ENSG00000135903.20. [P23760-3] DR Ensembl; ENST00000336840.11; ENSP00000338767.5; ENSG00000135903.20. [P23760-5] DR Ensembl; ENST00000344493.9; ENSP00000342092.4; ENSG00000135903.20. [P23760-4] DR Ensembl; ENST00000350526.9; ENSP00000343052.4; ENSG00000135903.20. [P23760-1] DR Ensembl; ENST00000392069.6; ENSP00000375921.2; ENSG00000135903.20. [P23760-8] DR Ensembl; ENST00000392070.7; ENSP00000375922.3; ENSG00000135903.20. [P23760-7] DR Ensembl; ENST00000409551.7; ENSP00000386750.3; ENSG00000135903.20. [P23760-6] DR Ensembl; ENST00000409828.7; ENSP00000386817.3; ENSG00000135903.20. [P23760-2] DR GeneID; 5077; -. DR KEGG; hsa:5077; -. DR MANE-Select; ENST00000392070.7; ENSP00000375922.3; NM_181458.4; NP_852123.1. [P23760-7] DR UCSC; uc002vmt.3; human. [P23760-1] DR AGR; HGNC:8617; -. DR ClinPGx; PA32957; -. DR CTD; 5077; -. DR DisGeNET; 5077; -. DR GeneCards; PAX3; -. DR GeneReviews; PAX3; -. DR HGNC; HGNC:8617; PAX3. DR HPA; ENSG00000135903; Tissue enhanced (brain, salivary gland, skeletal muscle, skin). DR MalaCards; PAX3; -. DR MIM; 122880; phenotype. DR MIM; 148820; phenotype. DR MIM; 193500; phenotype. DR MIM; 268220; phenotype. DR MIM; 606597; gene. DR OpenTargets; ENSG00000135903; -. DR Orphanet; 99756; Alveolar rhabdomyosarcoma. DR Orphanet; 1529; Craniofacial-deafness-hand syndrome. DR Orphanet; 894; Waardenburg syndrome type 1. DR Orphanet; 896; Waardenburg syndrome type 3. DR VEuPathDB; HostDB:ENSG00000135903; -. DR eggNOG; KOG0849; Eukaryota. DR GeneTree; ENSGT00940000156504; -. DR HOGENOM; CLU_019281_8_0_1; -. DR InParanoid; P23760; -. DR OMA; PDIACFQ; -. DR OrthoDB; 6159439at2759; -. DR PAN-GO; P23760; 4 GO annotations based on evolutionary models. DR PhylomeDB; P23760; -. DR PathwayCommons; P23760; -. DR Reactome; R-HSA-3214847; HATs acetylate histones. DR Reactome; R-HSA-9834899; Specification of the neural plate border. DR Reactome; R-HSA-9856649; Transcriptional and post-translational regulation of MITF-M expression and activity. DR SignaLink; P23760; -. DR SIGNOR; P23760; -. DR Agora; ENSG00000135903; -. DR BioGRID-ORCS; 5077; 18 hits in 1167 CRISPR screens. DR ChiTaRS; PAX3; human. DR EvolutionaryTrace; P23760; -. DR GeneWiki; PAX3; -. DR GenomeRNAi; 5077; -. DR Pharos; P23760; Tbio. DR PRO; PR:P23760; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; P23760; protein. DR Bgee; ENSG00000135903; Expressed in olfactory segment of nasal mucosa and 82 other cell types or tissues. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; EXP:UniProtKB. DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL. DR GO; GO:0009887; P:animal organ morphogenesis; TAS:ProtInc. DR GO; GO:0006915; P:apoptotic process; TAS:ProtInc. DR GO; GO:0007399; P:nervous system development; IBA:GO_Central. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0007605; P:sensory perception of sound; TAS:ProtInc. DR CDD; cd00086; homeodomain; 1. DR CDD; cd00131; PAX; 1. DR FunFam; 1.10.10.10:FF:000080; paired box protein Pax-3 isoform X2; 1. DR FunFam; 1.10.10.60:FF:000035; paired box protein Pax-3 isoform X2; 1. DR FunFam; 1.10.10.10:FF:000031; Paired box protein Pax-7; 1. DR Gene3D; 1.10.10.60; Homeodomain-like; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2. DR InterPro; IPR001356; HD. DR InterPro; IPR017970; Homeobox_CS. DR InterPro; IPR009057; Homeodomain-like_sf. DR InterPro; IPR043182; PAIRED_DNA-bd_site. DR InterPro; IPR001523; Paired_dom. DR InterPro; IPR022106; Pax7_C. DR InterPro; IPR043565; PAX_fam. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR PANTHER; PTHR45636:SF17; PAIRED BOX PROTEIN PAX-3; 1. DR PANTHER; PTHR45636; PAIRED BOX PROTEIN PAX-6-RELATED-RELATED; 1. DR Pfam; PF00046; Homeodomain; 1. DR Pfam; PF00292; PAX; 1. DR Pfam; PF12360; Pax7; 1. DR PRINTS; PR00027; PAIREDBOX. DR SMART; SM00389; HOX; 1. DR SMART; SM00351; PAX; 1. DR SUPFAM; SSF46689; Homeodomain-like; 2. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. DR PROSITE; PS00034; PAIRED_1; 1. DR PROSITE; PS51057; PAIRED_2; 1. DR PDBsum; 3CMY; -. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Chromosomal rearrangement; Deafness; KW Developmental protein; Disease variant; DNA-binding; Homeobox; Myogenesis; KW Neurogenesis; Nucleus; Paired box; Phosphoprotein; KW Proteomics identification; Proto-oncogene; Reference proteome; KW Transcription; Transcription regulation; Waardenburg syndrome. FT CHAIN 1..479 FT /note="Paired box protein Pax-3" FT /id="PRO_0000050178" FT DNA_BIND 34..161 FT /note="Paired" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00381" FT DNA_BIND 219..278 FT /note="Homeobox" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108" FT REGION 1..21 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 37..93 FT /note="PAI subdomain" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00381" FT REGION 113..161 FT /note="RED subdomain" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00381" FT REGION 165..228 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 309..351 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 172..188 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 309..329 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 338..351 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 319..320 FT /note="Breakpoint for translocation to form PAX3-NCOA1 FT oncogene" FT MOD_RES 201 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:21440083" FT MOD_RES 205 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:21440083" FT MOD_RES 209 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:21440083" FT VAR_SEQ 108 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_043634" FT VAR_SEQ 196..215 FT /note="ASAPQSDEGSDIDSEPDLPL -> GKRWRLGRRTCWVTWRASAS (in FT isoform Pax3A)" FT /evidence="ECO:0000303|PubMed:7545913" FT /id="VSP_002355" FT VAR_SEQ 196..206 FT /note="ASAPQSDEGSD -> GKALVSGVSSH (in isoform Pax3B)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:7545913" FT /id="VSP_002357" FT VAR_SEQ 207..479 FT /note="Missing (in isoform Pax3B)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:7545913" FT /id="VSP_002358" FT VAR_SEQ 216..479 FT /note="Missing (in isoform Pax3A)" FT /evidence="ECO:0000303|PubMed:7545913" FT /id="VSP_002356" FT VAR_SEQ 393..479 FT /note="MGLLTNHGGVPHQPQTDYALSPLTGGLEPTTTVSASCSQRLDHMKSLDSLPT FT SQSYCPPTYSTTGYSMDPVTGYQYGQYGQSKPWTF -> PFIISSQISRK (in FT isoform Pax3G)" FT /evidence="ECO:0000303|PubMed:14639621" FT /id="VSP_042004" FT VAR_SEQ 393..479 FT /note="MGLLTNHGGVPHQPQTDYALSPLTGGLEPTTTVSASCSQRLDHMKSLDSLPT FT SQSYCPPTYSTTGYSMDPVTGYQYGQYGQSKPWTF -> PFIISSQISLGFKSF (in FT isoform Pax3H)" FT /evidence="ECO:0000303|PubMed:14639621" FT /id="VSP_042005" FT VAR_SEQ 475..479 FT /note="KPWTF -> AFHYLKPDIA (in isoform 6 and isoform 7)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_043635" FT VAR_SEQ 475..479 FT /note="KPWTF -> AFHYLKPDIAWFQILLNTFDKSSGEEEDLEQ (in isoform FT Pax3E)" FT /evidence="ECO:0000305" FT /id="VSP_044915" FT VARIANT 45 FT /note="F -> L (in WS1)" FT /evidence="ECO:0000269|PubMed:7981674" FT /id="VAR_003790" FT VARIANT 47 FT /note="N -> H (in WS3; dbSNP:rs104893653)" FT /evidence="ECO:0000269|PubMed:8447316" FT /id="VAR_003791" FT VARIANT 47 FT /note="N -> K (in CDHS; dbSNP:rs104893652)" FT /evidence="ECO:0000269|PubMed:8664898" FT /id="VAR_003792" FT VARIANT 48 FT /note="G -> R (in WS1; dbSNP:rs1419548558)" FT /evidence="ECO:0000269|PubMed:8845842" FT /id="VAR_017533" FT VARIANT 50 FT /note="P -> L (in WS1; dbSNP:rs104893650)" FT /evidence="ECO:0000269|PubMed:1347149" FT /id="VAR_003793" FT VARIANT 56 FT /note="R -> L (in WS1; dbSNP:rs267606931)" FT /evidence="ECO:0000269|PubMed:8447316" FT /id="VAR_003794" FT VARIANT 59 FT /note="I -> F (in WS1)" FT /evidence="ECO:0000269|PubMed:9067759" FT /id="VAR_003795" FT VARIANT 59 FT /note="I -> N (in WS1)" FT /evidence="ECO:0000269|Ref.35" FT /id="VAR_003796" FT VARIANT 60 FT /note="V -> M (in WS1)" FT /evidence="ECO:0000269|PubMed:12949970, FT ECO:0000269|PubMed:8533800" FT /id="VAR_003797" FT VARIANT 62 FT /note="M -> V (in WS1; dbSNP:rs2106203978)" FT /evidence="ECO:0000269|PubMed:7833953, FT ECO:0000269|PubMed:9452070" FT /id="VAR_003798" FT VARIANT 63..67 FT /note="Missing (in WS1)" FT /evidence="ECO:0000269|PubMed:1347148" FT /id="VAR_003799" FT VARIANT 73 FT /note="S -> L (in WS1; dbSNP:rs1553593928)" FT /evidence="ECO:0000269|PubMed:10779847" FT /id="VAR_013640" FT VARIANT 78 FT /note="V -> M (in WS1)" FT /evidence="ECO:0000269|PubMed:8589691" FT /id="VAR_017534" FT VARIANT 80 FT /note="H -> D (in WS1; results in decreased transcriptional FT activation of MITF; no effect on localization to nucleus; FT no effect on interaction with SOX10; dbSNP:rs387906947)" FT /evidence="ECO:0000269|PubMed:20478267, FT ECO:0000269|PubMed:21965087" FT /id="VAR_079619" FT VARIANT 81 FT /note="G -> A (in WS1; originally classified as Waardenburg FT syndrome type 2; dbSNP:rs587776586)" FT /evidence="ECO:0000269|PubMed:8490648, FT ECO:0000269|PubMed:8589691" FT /id="VAR_003800" FT VARIANT 84 FT /note="S -> F (in WS3; dbSNP:rs104893651)" FT /evidence="ECO:0000269|PubMed:7726174" FT /id="VAR_003801" FT VARIANT 85 FT /note="K -> E (in WS1)" FT /evidence="ECO:0000269|PubMed:8533800" FT /id="VAR_003802" FT VARIANT 90 FT /note="Y -> H (in WS3; dbSNP:rs104893654)" FT /evidence="ECO:0000269|PubMed:12949970" FT /id="VAR_017535" FT VARIANT 99 FT /note="G -> D (in WS1; dbSNP:rs1189463428)" FT /evidence="ECO:0000269|PubMed:7981674, FT ECO:0000269|PubMed:8589691" FT /id="VAR_003803" FT VARIANT 223..479 FT /note="Missing (in WS1)" FT /evidence="ECO:0000269|PubMed:20478267, FT ECO:0000269|PubMed:8845842" FT /id="VAR_079620" FT VARIANT 234 FT /note="L -> P (in WS1)" FT /evidence="ECO:0000269|PubMed:16971891, FT ECO:0000269|PubMed:20478267" FT /id="VAR_079621" FT VARIANT 238 FT /note="F -> S (in WS1; dbSNP:rs2106095147)" FT /evidence="ECO:0000269|PubMed:8533800" FT /id="VAR_003804" FT VARIANT 265 FT /note="V -> F (in WS1; dbSNP:rs1210072810)" FT /evidence="ECO:0000269|PubMed:7825605" FT /id="VAR_003805" FT VARIANT 266 FT /note="W -> C (in WS1)" FT /evidence="ECO:0000269|PubMed:8589691" FT /id="VAR_017536" FT VARIANT 270 FT /note="R -> C (in WS1 and WS3; dbSNP:rs1228590199)" FT /evidence="ECO:0000269|PubMed:8589691, FT ECO:0000269|PubMed:8845842, ECO:0000269|Ref.36" FT /id="VAR_013619" FT VARIANT 271 FT /note="R -> C (in WS1; dbSNP:rs1380858784)" FT /evidence="ECO:0000269|PubMed:8589691" FT /id="VAR_017537" FT VARIANT 271 FT /note="R -> G (in WS1)" FT /evidence="ECO:0000269|PubMed:7825605" FT /id="VAR_003806" FT VARIANT 271 FT /note="R -> H (in WS1; dbSNP:rs774528745)" FT /evidence="ECO:0000269|PubMed:20478267, FT ECO:0000269|PubMed:8589691, ECO:0000269|PubMed:8845842" FT /id="VAR_017538" FT VARIANT 273 FT /note="R -> K (in WS1; uncertain significance; FT dbSNP:rs1020175890)" FT /evidence="ECO:0000269|PubMed:8845842" FT /id="VAR_017539" FT VARIANT 315 FT /note="T -> K (in dbSNP:rs2234675)" FT /evidence="ECO:0000269|PubMed:8589691, FT ECO:0000269|PubMed:8845842, ECO:0000269|PubMed:8863157, FT ECO:0000269|PubMed:9584079" FT /id="VAR_003807" FT VARIANT 391 FT /note="Q -> H (in WS1)" FT /evidence="ECO:0000269|PubMed:9541113" FT /id="VAR_013641" FT CONFLICT 358 FT /note="S -> R (in Ref. 1; AAP13872/AAP13873)" FT /evidence="ECO:0000305" FT HELIX 221..224 FT /evidence="ECO:0007829|PDB:3CMY" FT HELIX 228..240 FT /evidence="ECO:0007829|PDB:3CMY" FT HELIX 246..256 FT /evidence="ECO:0007829|PDB:3CMY" FT HELIX 260..276 FT /evidence="ECO:0007829|PDB:3CMY" SQ SEQUENCE 479 AA; 52968 MW; 8AFCA674E3ACB4FE CRC64; MTTLAGAVPR MMRPGPGQNY PRSGFPLEVS TPLGQGRVNQ LGGVFINGRP LPNHIRHKIV EMAHHGIRPC VISRQLRVSH GCVSKILCRY QETGSIRPGA IGGSKPKQVT TPDVEKKIEE YKRENPGMFS WEIRDKLLKD AVCDRNTVPS VSSISRILRS KFGKGEEEEA DLERKEAEES EKKAKHSIDG ILSERASAPQ SDEGSDIDSE PDLPLKRKQR RSRTTFTAEQ LEELERAFER THYPDIYTRE ELAQRAKLTE ARVQVWFSNR RARWRKQAGA NQLMAFNHLI PGGFPPTAMP TLPTYQLSET SYQPTSIPQA VSDPSSTVHR PQPLPPSTVH QSTIPSNPDS SSAYCLPSTR HGFSSYTDSF VPPSGPSNPM NPTIGNGLSP QVMGLLTNHG GVPHQPQTDY ALSPLTGGLE PTTTVSASCS QRLDHMKSLD SLPTSQSYCP PTYSTTGYSM DPVTGYQYGQ YGQSKPWTF //