PAX3_HUMAN
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 03-AUG-2022, entry version 228.
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 VARIANTS WS3 HIS-47 AND 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;
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)2111-ift025;
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="http://atlasgeneticsoncology.org/Genes/PAX3ID70ch2q35.html";
CC ---------------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
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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_000438.5. [P23760-2]
DR RefSeq; NP_001120838.1; NM_001127366.2. [P23760-6]
DR RefSeq; NP_039230.1; NM_013942.4. [P23760-3]
DR RefSeq; NP_852122.1; NM_181457.3. [P23760-1]
DR RefSeq; NP_852123.1; NM_181458.3. [P23760-7]
DR RefSeq; NP_852124.1; NM_181459.3. [P23760-8]
DR RefSeq; NP_852125.1; NM_181460.3. [P23760-5]
DR RefSeq; NP_852126.1; NM_181461.3. [P23760-4]
DR PDB; 3CMY; X-ray; 1.95 A; A=219-278.
DR PDBsum; 3CMY; -.
DR AlphaFoldDB; P23760; -.
DR SMR; P23760; -.
DR BioGRID; 111111; 37.
DR CORUM; P23760; -.
DR IntAct; P23760; 22.
DR MINT; P23760; -.
DR STRING; 9606.ENSP00000375921; -.
DR iPTMnet; P23760; -.
DR PhosphoSitePlus; P23760; -.
DR BioMuta; PAX3; -.
DR DMDM; 1172022; -.
DR MassIVE; P23760; -.
DR MaxQB; P23760; -.
DR PaxDb; P23760; -.
DR PeptideAtlas; P23760; -.
DR PRIDE; 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 Antibodypedia; 4602; 547 antibodies from 45 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 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 neXtProt; NX_P23760; -.
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 PharmGKB; PA32957; -.
DR VEuPathDB; HostDB:ENSG00000135903; -.
DR eggNOG; KOG0849; Eukaryota.
DR GeneTree; ENSGT00940000156504; -.
DR HOGENOM; CLU_019281_8_0_1; -.
DR InParanoid; P23760; -.
DR OMA; VSISHVH; -.
DR OrthoDB; 1126858at2759; -.
DR PhylomeDB; P23760; -.
DR TreeFam; TF351610; -.
DR PathwayCommons; P23760; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR SignaLink; P23760; -.
DR SIGNOR; P23760; -.
DR BioGRID-ORCS; 5077; 18 hits in 1091 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 80 other tissues.
DR Genevisible; P23760; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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:0071837; F:HMG box domain binding; IEA:Ensembl.
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:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0009887; P:animal organ morphogenesis; TAS:ProtInc.
DR GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; 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 Gene3D; 1.10.10.10; -; 2.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR043182; PAIRED_DNA-bd_dom.
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; PTHR45636; 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; SSF46689; 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.
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; Proto-oncogene;
KW Reference proteome; Transcription; Transcription regulation;
KW 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 165..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..228
FT /note="Basic and acidic 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; important hearing loss;
FT dbSNP:rs104893650)"
FT /evidence="ECO:0000269|PubMed:1347149"
FT /id="VAR_003793"
FT VARIANT 56
FT /note="R -> L (in WS1; associated with meningomyelocele;
FT 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)"
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)"
FT /evidence="ECO:0000269|PubMed:8533800"
FT /id="VAR_003804"
FT VARIANT 265
FT /note="V -> F (in WS1)"
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; associated with K-273 in one family;
FT 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; associated with H-271 in one family;
FT unknown pathological significance; 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 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
