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Wilms tumor protein (WT33)

 WT1_HUMAN               Reviewed;         449 AA.
P19544; A8K6S1; B3KSA5; Q15881; Q16256; Q16575; Q4VXV4; Q4VXV5;
Q4VXV6; Q8IYZ5;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-AUG-1991, sequence version 2.
22-NOV-2017, entry version 216.
RecName: Full=Wilms tumor protein;
AltName: Full=WT33;
Name=WT1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7).
TISSUE=Fetal kidney;
PubMed=2154702; DOI=10.1038/343774a0;
Gessler M., Poustka A., Cavenee W., Neve R.L., Orkin S.H.,
Bruns G.A.P.;
"Homozygous deletion in Wilms tumours of a zinc-finger gene identified
by chromosome jumping.";
Nature 343:774-778(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS
1; 2; 3 AND 4).
TISSUE=Placenta;
PubMed=1658787; DOI=10.1073/pnas.88.21.9618;
Haber D.A., Sohn R.L., Buckler A.J., Pelletier J., Call K.M.,
Housman D.E.;
"Alternative splicing and genomic structure of the Wilms tumor gene
WT1.";
Proc. Natl. Acad. Sci. U.S.A. 88:9618-9622(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM
4).
PubMed=1572653; DOI=10.1016/0888-7543(92)90313-H;
Gessler M., Konig A., Bruns G.A.P.;
"The genomic organization and expression of the WT1 gene.";
Genomics 12:807-813(1992).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 9).
TISSUE=Placenta, and Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM
1).
NIEHS SNPs program;
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 85-449 (ISOFORM 2).
PubMed=2154335; DOI=10.1016/0092-8674(90)90601-A;
Call K.M., Glaser T., Ito C.Y., Buckler A.J., Pelletier J.,
Haber D.A., Rose E.A., Kral A., Yeger H., Lewis W.H., Jones C.,
Housman D.E.;
"Isolation and characterization of a zinc finger polypeptide gene at
the human chromosome 11 Wilms' tumor locus.";
Cell 60:509-520(1990).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 301-449 (ISOFORMS 2/4/6), AND FUNCTION.
TISSUE=Fetal kidney;
PubMed=7862533; DOI=10.1093/nar/23.2.277;
Hamilton T.B., Barilla K.C., Romaniuk P.J.;
"High affinity binding sites for the Wilms' tumour suppressor protein
WT1.";
Nucleic Acids Res. 23:277-284(1995).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 385-405, AND VARIANTS DDS.
PubMed=1655284; DOI=10.1016/0092-8674(91)90194-4;
Pelletier J., Bruening W., Kashtan C.E., Mauer S.M., Manivel J.C.,
Striegel J.E., Houghton D.C., Junien C., Habib R., Fouser L.,
Fine R.N., Silverman B.L., Haber D.A., Housman D.E.;
"Germline mutations in the Wilms' tumor suppressor gene are associated
with abnormal urogenital development in Denys-Drash syndrome.";
Cell 67:437-447(1991).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 385-405, AND VARIANTS DDS
TYR-330; PRO-394 AND TRP-394.
PubMed=1302008; DOI=10.1038/ng0592-144;
Bruening W., Bardeesy N., Silverman B.L., Cohn R.A., Machin G.A.,
Aronson A.J., Housman D., Pelletier J.;
"Germline intronic and exonic mutations in the Wilms' tumour gene
(WT1) affecting urogenital development.";
Nat. Genet. 1:144-148(1992).
[13]
IDENTIFICATION OF START CODON, AND ALTERNATIVE SPLICING.
PubMed=1671709; DOI=10.1128/MCB.11.3.1707;
Buckler A.J., Pelletier J., Haber D.A., Glaser T., Housman D.E.;
"Isolation, characterization, and expression of the murine Wilms'
tumor gene (WT1) during kidney development.";
Mol. Cell. Biol. 11:1707-1712(1991).
[14]
RNA EDITING OF POSITION 281.
PubMed=7926762; DOI=10.1101/gad.8.6.720;
Sharma P.M., Bowman M., Madden S.L., Rauscher F.J. III, Sukumar S.;
"RNA editing in the Wilms' tumor susceptibility gene, WT1.";
Genes Dev. 8:720-731(1994).
[15]
ALTERNATIVE INITIATION, AND ALTERNATIVE SPLICING (ISOFORMS 7 AND 8).
PubMed=8621495; DOI=10.1074/jbc.271.15.8646;
Bruening W., Pelletier J.;
"A non-AUG translational initiation event generates novel WT1
isoforms.";
J. Biol. Chem. 271:8646-8654(1996).
[16]
INTERACTION WITH WTAP.
PubMed=11001926; DOI=10.1093/oxfordjournals.hmg.a018914;
Little N.A., Hastie N.D., Davies R.C.;
"Identification of WTAP, a novel Wilms' tumour 1-associating
protein.";
Hum. Mol. Genet. 9:2231-2239(2000).
[17]
INTERACTION WITH ZNF224.
PubMed=12239212; DOI=10.1074/jbc.M205667200;
Lee T.H., Lwu S., Kim J., Pelletier J.;
"Inhibition of Wilms tumor 1 transactivation by bone marrow zinc
finger 2, a novel transcriptional repressor.";
J. Biol. Chem. 277:44826-44837(2002).
[18]
INTERACTION WITH SRY.
PubMed=12970737; DOI=10.1038/sj.onc.1206717;
Matsuzawa-Watanabe Y., Inoue J., Semba K.;
"Transcriptional activity of testis-determining factor SRY is
modulated by the Wilms' tumor 1 gene product, WT1.";
Oncogene 22:7900-7904(2003).
[19]
REVIEW.
PubMed=1313285;
Haber D.A., Buckler A.J.;
"WT1: a novel tumor suppressor gene inactivated in Wilms' tumor.";
New Biol. 4:97-106(1992).
[20]
REVIEW.
PubMed=8393820;
Rauscher F.J. III;
"The WT1 Wilms tumor gene product: a developmentally regulated
transcription factor in the kidney that functions as a tumor
suppressor.";
FASEB J. 7:896-903(1993).
[21]
INVOLVEMENT IN WILMS TUMOR.
PubMed=1654525; DOI=10.1038/353431a0;
Pelletier J., Bruening W., Li F.P., Haber D.A., Glaser T.,
Housman D.E.;
"WT1 mutations contribute to abnormal genital system development and
hereditary Wilms' tumour.";
Nature 353:431-434(1991).
[22]
REVIEW.
PubMed=17361230; DOI=10.1038/sj.leu.2404624;
Yang L., Han Y., Suarez Saiz F., Minden M.D.;
"A tumor suppressor and oncogene: the WT1 story.";
Leukemia 21:868-876(2007).
[23]
SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-73 AND LYS-177, AND
SUMOYLATION AT LYS-73 AND LYS-177.
PubMed=15520190; DOI=10.1158/0008-5472.CAN-04-1502;
Smolen G.A., Vassileva M.T., Wells J., Matunis M.J., Haber D.A.;
"SUMO-1 modification of the Wilms' tumor suppressor WT1.";
Cancer Res. 64:7846-7851(2004).
[24]
INTERACTION WITH RBM4, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=16934801; DOI=10.1016/j.yexcr.2006.07.008;
Markus M.A., Heinrich B., Raitskin O., Adams D.J., Mangs H., Goy C.,
Ladomery M., Sperling R., Stamm S., Morris B.J.;
"WT1 interacts with the splicing protein RBM4 and regulates its
ability to modulate alternative splicing in vivo.";
Exp. Cell Res. 312:3379-3388(2006).
[25]
FUNCTION, AND MUTAGENESIS OF HIS-343; ARG-366; ARG-372; ARG-394 AND
HIS-434.
PubMed=19123921; DOI=10.1021/bi801586a;
Weiss T.C., Romaniuk P.J.;
"Contribution of individual amino acids to the RNA binding activity of
the Wilms' tumor suppressor protein WT1.";
Biochemistry 48:148-155(2009).
[26]
INTERACTION WITH AMER1, AND FUNCTION.
PubMed=19416806; DOI=10.1073/pnas.0811349106;
Rivera M.N., Kim W.J., Wells J., Stone A., Burger A., Coffman E.J.,
Zhang J., Haber D.A.;
"The tumor suppressor WTX shuttles to the nucleus and modulates WT1
activity.";
Proc. Natl. Acad. Sci. U.S.A. 106:8338-8343(2009).
[27]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-444, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[28]
STRUCTURE BY NMR OF 381-407 IN COMPLEX WITH ZINC IONS.
PubMed=15518539; DOI=10.1021/bi0491999;
Lachenmann M.J., Ladbury J.E., Dong J., Huang K., Carey P.,
Weiss M.A.;
"Why zinc fingers prefer zinc: ligand-field symmetry and the hidden
thermodynamics of metal ion selectivity.";
Biochemistry 43:13910-13925(2004).
[29]
STRUCTURE BY NMR OF 318-438 IN COMPLEX WITH DNA AND ZINC IONS (ISOFORM
4), X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 318-438 IN COMPLEX WITH
DNA AND ZINC IONS, AND FUNCTION.
PubMed=17716689; DOI=10.1016/j.jmb.2007.07.017;
Stoll R., Lee B.M., Debler E.W., Laity J.H., Wilson I.A., Dyson H.J.,
Wright P.E.;
"Structure of the Wilms tumor suppressor protein zinc finger domain
bound to DNA.";
J. Mol. Biol. 372:1227-1245(2007).
[30]
X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 350-440 IN COMPLEX WITH ZINC
AND TARGET DNA, FUNCTION, AND DOMAIN.
PubMed=25258363; DOI=10.1101/gad.250746.114;
Hashimoto H., Olanrewaju Y.O., Zheng Y., Wilson G.G., Zhang X.,
Cheng X.;
"Wilms tumor protein recognizes 5-carboxylcytosine within a specific
DNA sequence.";
Genes Dev. 28:2304-2313(2014).
[31]
VARIANT WT1 CYS-366.
PubMed=1317572; DOI=10.1073/pnas.89.11.4791;
Little M.H., Prosser J., Condie A., Smith P.J., van Heyningen V.,
Hastie N.D.;
"Zinc finger point mutations within the WT1 gene in Wilms tumor
patients.";
Proc. Natl. Acad. Sci. U.S.A. 89:4791-4795(1992).
[32]
VARIANTS DDS.
PubMed=1338906; DOI=10.1093/hmg/1.5.301;
Baird P.N., Santos A., Groves N., Jadresic L., Cowell J.K.;
"Constitutional mutations in the WT1 gene in patients with Denys-Drash
syndrome.";
Hum. Mol. Genet. 1:301-305(1992).
[33]
VARIANTS DDS.
PubMed=8388765; DOI=10.1093/hmg/2.3.259;
Little M.H., Williamson K.A., Mannens M., Kelsey A., Gosden C.,
Hastie N.D., van Heyningen V.;
"Evidence that WT1 mutations in Denys-Drash syndrome patients may act
in a dominant-negative fashion.";
Hum. Mol. Genet. 2:259-264(1993).
[34]
VARIANT DDS TYR-401.
PubMed=8111391; DOI=10.1093/hmg/2.12.2193;
Baird P.N., Cowell J.K.;
"A novel zinc finger mutation in a patient with Denys-Drash
syndrome.";
Hum. Mol. Genet. 2:2193-2194(1993).
[35]
VARIANTS DDS TRP-394 AND PRO-398.
PubMed=8295405; DOI=10.1007/BF00714282;
Tsuda M., Sakiyama T., Kitagawa T., Watanabe S., Watanabe T.,
Takahashi S., Kawaguchi H., Ito K.;
"Molecular analysis of two Japanese cases of Denys-Drash syndrome.";
J. Inherit. Metab. Dis. 16:876-880(1993).
[36]
VARIANTS DDS TYR-360 AND TRP-394.
PubMed=8411073; DOI=10.1136/jmg.30.9.767;
Clarkson P.A., Davies H.R., Williams D.M., Chaudhary R., Hughes I.A.,
Patterson M.N.;
"Mutational screening of the Wilms's tumour gene, WT1, in males with
genital abnormalities.";
J. Med. Genet. 30:767-772(1993).
[37]
VARIANT GLY-273, AND INVOLVEMENT IN MESOM.
PubMed=8401592; DOI=10.1038/ng0893-415;
Park S., Schalling M., Bernard A., Maheswaran S., Shipley G.C.,
Roberts D., Fletcher J., Shipman R., Rheinwald J., Demetri G.,
Griffin J., Minden M., Housman D.E., Haber D.A.;
"The Wilms tumour gene WT1 is expressed in murine mesoderm-derived
tissues and mutated in a human mesothelioma.";
Nat. Genet. 4:415-420(1993).
[38]
VARIANT DDS ARG-377.
PubMed=8112732; DOI=10.1007/BF00210593;
Nordenskjold A., Friedman E., Anvret M.;
"WT1 mutations in patients with Denys-Drash syndrome: a novel mutation
in exon 8 and paternal allele origin.";
Hum. Genet. 93:115-120(1994).
[39]
VARIANT DDS LEU-366.
PubMed=8741319;
Tsuda M., Sakiyama T., Owada M., Chiba Y.;
"A newly identified exonic mutation of the WT1 gene in a patient with
Denys-Drash syndrome.";
Acta Paediatr. Jpn. Overseas Ed. 38:265-266(1996).
[40]
VARIANT DDS TYR-373.
PubMed=8956030; DOI=10.1159/000154374;
Ghahremani M., Chan C.B., Bistritzer T., Aladjem M.M., Tieder M.,
Pelletier J.;
"A novel mutation H373Y in the Wilms' tumor suppressor gene, WT1,
associated with Denys-Drash syndrome.";
Hum. Hered. 46:336-338(1996).
[41]
VARIANTS WT1 SER-181 AND ALA-253.
PubMed=9108089; DOI=10.1073/pnas.94.8.3972;
Schumacher V., Schneider S., Figge A., Wildhardt G., Harms D.,
Schmidt D., Weirich A., Ludwig R., Royer-Pokora B.;
"Correlation of germ-line mutations and two-hit inactivation of the
WT1 gene with Wilms tumors of stromal-predominant histology.";
Proc. Natl. Acad. Sci. U.S.A. 94:3972-3977(1997).
[42]
VARIANTS NPHS4 TYR-377; LEU-383 AND ASN-396, VARIANTS DDS CYS-366;
GLN-394; TRP-394 AND PRO-398, AND VARIANT WT1 ASN-223.
PubMed=9529364; DOI=10.1086/301806;
Jeanpierre C., Denamur E., Henry I., Cabanis M.-O., Luce S.,
Cecille A., Elion J., Peuchmaur M., Loirat C., Niaudet P.,
Gubler M.-C., Junien C.;
"Identification of constitutional WT1 mutations, in patients with
isolated diffuse mesangial sclerosis, and analysis of
genotype/phenotype correlations by use of a computerized mutation
database.";
Am. J. Hum. Genet. 62:824-833(1998).
[43]
VARIANTS DDS TYR-355; HIS-366 AND ARG-385.
PubMed=9475094; DOI=10.1136/jmg.35.1.45;
Kikuchi H., Takata A., Akasaka Y., Fukuzawa R., Yoneyama H.,
Kurosawa Y., Honda M., Kamiyama Y., Hata J.;
"Do intronic mutations affecting splicing of WT1 exon 9 cause Frasier
syndrome?";
J. Med. Genet. 35:45-48(1998).
[44]
VARIANTS NPHS4 LEU-364; HIS-366; CYS-379; ARG-385; GLN-394; TRP-394
AND ASN-396.
PubMed=9607189; DOI=10.1046/j.1523-1755.1998.00948.x;
Schumacher V., Schaerer K., Wuehl E., Altrogge H., Bonzel K.-E.,
Guschmann M., Neuhaus T.J., Pollastro R.M., Kuwertz-Broeking E.,
Bulla M., Tondera A.-M., Mundel P., Helmchen U., Waldherr R.,
Weirich A., Royer-Pokora B.;
"Spectrum of early onset nephrotic syndrome associated with WT1
missense mutations.";
Kidney Int. 53:1594-1600(1998).
[45]
VARIANT FS LEU-392.
PubMed=10571943;
DOI=10.1002/(SICI)1098-1004(199912)14:6<466::AID-HUMU4>3.0.CO;2-6;
Kohsaka T., Tagawa M., Takekoshi Y., Yanagisawa H., Tadokoro K.,
Yamada M.;
"Exon 9 mutations in the WT1 gene, without influencing KTS splice
isoforms, are also responsible for Frasier syndrome.";
Hum. Mutat. 14:466-470(1999).
[46]
VARIANT DDS TYR-396.
PubMed=10738002;
DOI=10.1002/(SICI)1098-1004(200004)15:4<389::AID-HUMU29>3.3.CO;2-5;
Little M., Carman G., Donaldson E.;
"Novel WT1 exon 9 mutation (D396Y) in a patient with early onset Denys
Drash syndrome.";
Hum. Mutat. 15:389-389(2000).
[47]
VARIANTS DDS ARG-342; TYR-355; HIS-366; ARG-385; PHE-388; TRP-394 AND
ASN-396, AND VARIANT NPHS4 GLN-312.
PubMed=11182928; DOI=10.1136/jmg.37.9.698;
Takata A., Kikuchi H., Fukuzawa R., Ito S., Honda M., Hata J.;
"Constitutional WT1 correlate with clinical features in children with
progressive nephropathy.";
J. Med. Genet. 37:698-701(2000).
[48]
VARIANT DDS PRO-369.
PubMed=10799199; DOI=10.1016/S0022-5347(05)67560-X;
Ohta S., Ozawa T., Izumino K., Sakuragawa N., Fuse H.;
"A novel missense mutation of the WT1 gene causing Denys-Drash
syndrome with exceptionally mild renal manifestations.";
J. Urol. 163:1857-1858(2000).
[49]
VARIANT DDS TYR-388.
PubMed=11519891; DOI=10.1007/s004670100626;
Swiatecka-Urban A., Mokrzycki M.H., Kaskel F., Da Silva F.,
Denamur E.;
"Novel WT1 mutation (C388Y) in a female child with Denys-Drash
syndrome.";
Pediatr. Nephrol. 16:627-630(2001).
[50]
VARIANTS WT1 SER-181; GLY-355; CYS-366; HIS-366; GLN-373; TRP-394 AND
LEU-394.
PubMed=15150775; DOI=10.1002/ajmg.a.30015;
Royer-Pokora B., Beier M., Henzler M., Alam R., Schumacher V.,
Weirich A., Huff V.;
"Twenty-four new cases of WT1 germline mutations and review of the
literature: genotype/phenotype correlations for Wilms tumor
development.";
Am. J. Med. Genet. A 127:249-257(2004).
[51]
VARIANT THR-131.
PubMed=15266301; DOI=10.1038/sj.ejhg.5201232;
Wang Y., Li Q., Xu J., Liu Q., Wang W., Lin Y., Ma F., Chen T., Li S.,
Shen Y.;
"Mutation analysis of five candidate genes in Chinese patients with
hypospadias.";
Eur. J. Hum. Genet. 12:706-712(2004).
[52]
VARIANTS NPHS4 ARG-388 AND PRO-397.
PubMed=15253707; DOI=10.1111/j.1523-1755.2004.00775.x;
Members of the APN study group;
Ruf R.G., Schultheiss M., Lichtenberger A., Karle S.M., Zalewski I.,
Mucha B., Everding A.S., Neuhaus T., Patzer L., Plank C., Haas J.P.,
Ozaltin F., Imm A., Fuchshuber A., Bakkaloglu A., Hildebrandt F.;
"Prevalence of WT1 mutations in a large cohort of patients with
steroid-resistant and steroid-sensitive nephrotic syndrome.";
Kidney Int. 66:564-570(2004).
[53]
VARIANT DDS ARG-405.
PubMed=15349765; DOI=10.1007/s00467-004-1564-3;
Hu M., Craig J., Howard N., Kan A., Chaitow J., Little D.,
Alexander S.I.;
"A novel mutation of WT1 exon 9 in a patient with Denys-Drash syndrome
and pyloric stenosis.";
Pediatr. Nephrol. 19:1160-1163(2004).
[54]
VARIANTS MEACHS CYS-366 AND TRP-394.
PubMed=17853480; DOI=10.1002/ajmg.a.31924;
Suri M., Kelehan P., O'neill D., Vadeyar S., Grant J., Ahmed S.F.,
Tolmie J., McCann E., Lam W., Smith S., FitzPatrick D., Hastie N.D.,
Reardon W.;
"WT1 mutations in Meacham syndrome suggest a coelomic mesothelial
origin of the cardiac and diaphragmatic malformations.";
Am. J. Med. Genet. A 143:2312-2320(2007).
-!- FUNCTION: Transcription factor that plays an important role in
cellular development and cell survival (PubMed:7862533).
Recognizes and binds to the DNA sequence 5'-GCG(T/G)GGGCG-3'
(PubMed:7862533, PubMed:17716689, PubMed:25258363). Regulates the
expression of numerous target genes, including EPO. Plays an
essential role for development of the urogenital system. It has a
tumor suppressor as well as an oncogenic role in tumor formation.
Function may be isoform-specific: isoforms lacking the KTS motif
may act as transcription factors (PubMed:15520190). Isoforms
containing the KTS motif may bind mRNA and play a role in mRNA
metabolism or splicing (PubMed:16934801). Isoform 1 has lower
affinity for DNA, and can bind RNA (PubMed:19123921).
{ECO:0000269|PubMed:15520190, ECO:0000269|PubMed:16934801,
ECO:0000269|PubMed:17716689, ECO:0000269|PubMed:19123921,
ECO:0000269|PubMed:19416806, ECO:0000269|PubMed:25258363,
ECO:0000269|PubMed:7862533}.
-!- SUBUNIT: Homodimer. Interacts with WTIP. Interacts with actively
translating polysomes. Detected in nuclear ribonucleoprotein
(mRNP) particles. Interacts with HNRNPU via the zinc-finger
region. Interacts with U2AF2. Interacts with CITED2 (By
similarity). Interacts with ZNF224 via the zinc-finger region.
Interacts with WTAP and SRY. Interacts with AMER1. Interacts with
RBM4. {ECO:0000250, ECO:0000269|PubMed:11001926,
ECO:0000269|PubMed:12239212, ECO:0000269|PubMed:12970737,
ECO:0000269|PubMed:15518539, ECO:0000269|PubMed:16934801,
ECO:0000269|PubMed:17716689, ECO:0000269|PubMed:19416806}.
-!- INTERACTION:
Q6A162:KRT40; NbExp=3; IntAct=EBI-2320534, EBI-10171697;
P60410:KRTAP10-8; NbExp=3; IntAct=EBI-2320534, EBI-10171774;
Q9NRD5:PICK1; NbExp=4; IntAct=EBI-11745701, EBI-79165;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15520190}.
Nucleus, nucleolus. Cytoplasm {ECO:0000250}. Note=Isoforms lacking
the KTS motif have a diffuse nuclear location (PubMed:15520190).
Shuttles between nucleus and cytoplasm. {ECO:0000250,
ECO:0000269|PubMed:15520190}.
-!- SUBCELLULAR LOCATION: Isoform 1: Nucleus speckle
{ECO:0000269|PubMed:15520190}.
-!- SUBCELLULAR LOCATION: Isoform 4: Nucleus, nucleoplasm
{ECO:0000269|PubMed:15520190}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=8;
Name=1;
IsoId=P19544-1; Sequence=Displayed;
Note=Detected in nucleus speckle, may bind mRNA.;
Name=2;
IsoId=P19544-2; Sequence=VSP_006866, VSP_006867;
Name=3;
IsoId=P19544-3; Sequence=VSP_006866;
Name=4;
IsoId=P19544-4; Sequence=VSP_006867;
Name=6;
IsoId=P19544-6; Sequence=VSP_037582, VSP_037584, VSP_006867;
Name=7;
IsoId=P19544-7; Sequence=VSP_037583;
Note=Produced by alternative initiation of isoform 1. Extended
N-terminus.;
Name=8;
IsoId=P19544-8; Sequence=VSP_037583, VSP_006866;
Note=Produced by alternative initiation of isoform 1. Extended
N-terminus.;
Name=9;
IsoId=P19544-9; Sequence=VSP_037582, VSP_037584, VSP_006866;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in the kidney and a subset of
hematopoietic cells.
-!- DOMAIN: Binds to DNA motifs with the sequence 5'-GCG(T/G)GGGCG-3'
via its C2H2-type zinc fingers. Starting from the N-terminus, the
second zinc finger binds to the 3'-GCG motif, the middle zinc
finger interacts with the central TGG motif, and the C-terminal
zinc finger binds to the 5'-GCG motif. Binds double-stranded
target DNA, irrespective of the cytosine methylation status. Has
reduced affinity for target DNA where the cytosines have been
oxidized to 5-hydroxymethylcytosine, 5-formylcytosine or 5-
carboxylcytosine. {ECO:0000269|PubMed:25258363}.
-!- RNA EDITING: Modified_positions=281 {ECO:0000269|PubMed:7926762};
Note=Partially edited.;
-!- DISEASE: Frasier syndrome (FS) [MIM:136680]: Characterized by a
slowly progressing nephropathy leading to renal failure in
adolescence or early adulthood, male pseudohermaphroditism, and no
Wilms tumor. As for histological findings of the kidneys, focal
glomerular sclerosis is often observed. There is phenotypic
overlap with Denys-Drash syndrome. Inheritance is autosomal
dominant. {ECO:0000269|PubMed:10571943}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- DISEASE: Wilms tumor 1 (WT1) [MIM:194070]: Embryonal malignancy of
the kidney that affects approximately 1 in 10'000 infants and
young children. It occurs both in sporadic and hereditary forms.
{ECO:0000269|PubMed:1317572, ECO:0000269|PubMed:15150775,
ECO:0000269|PubMed:9108089, ECO:0000269|PubMed:9529364}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Denys-Drash syndrome (DDS) [MIM:194080]: Typical
nephropathy characterized by diffuse mesangial sclerosis, genital
abnormalities, and/or Wilms tumor. There is phenotypic overlap
with WAGR syndrome and Frasier syndrome. Inheritance is autosomal
dominant, but most cases are sporadic.
{ECO:0000269|PubMed:10738002, ECO:0000269|PubMed:10799199,
ECO:0000269|PubMed:11182928, ECO:0000269|PubMed:11519891,
ECO:0000269|PubMed:1302008, ECO:0000269|PubMed:1338906,
ECO:0000269|PubMed:15349765, ECO:0000269|PubMed:1655284,
ECO:0000269|PubMed:8111391, ECO:0000269|PubMed:8112732,
ECO:0000269|PubMed:8295405, ECO:0000269|PubMed:8388765,
ECO:0000269|PubMed:8411073, ECO:0000269|PubMed:8741319,
ECO:0000269|PubMed:8956030, ECO:0000269|PubMed:9475094,
ECO:0000269|PubMed:9529364}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Nephrotic syndrome 4 (NPHS4) [MIM:256370]: A form of
nephrotic syndrome, a renal disease clinically characterized by
severe proteinuria, resulting in complications such as
hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show
non-specific histologic changes such as focal segmental
glomerulosclerosis and diffuse mesangial proliferation. Some
affected individuals have an inherited steroid-resistant form and
progress to end-stage renal failure. Most patients with NPHS4 show
diffuse mesangial sclerosis on renal biopsy, which is a pathologic
entity characterized by mesangial matrix expansion with no
mesangial hypercellularity, hypertrophy of the podocytes,
vacuolized podocytes, thickened basement membranes, and diminished
patency of the capillary lumen. {ECO:0000269|PubMed:11182928,
ECO:0000269|PubMed:15253707, ECO:0000269|PubMed:9529364,
ECO:0000269|PubMed:9607189}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Meacham syndrome (MEACHS) [MIM:608978]: Rare sporadically
occurring multiple malformation syndrome characterized by male
pseudohermaphroditism with abnormal internal female genitalia
comprising a uterus and double or septate vagina, complex
congenital heart defect and diaphragmatic abnormalities.
{ECO:0000269|PubMed:17853480}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Note=A chromosomal aberration involving WT1 may be a
cause of desmoplastic small round cell tumor (DSRCT).
Translocation t(11;22)(p13;q12) with EWSR1.
-!- DISEASE: Mesothelioma, malignant (MESOM) [MIM:156240]: An
aggressive neoplasm of the serosal lining of the chest. It appears
as broad sheets of cells, with some regions containing spindle-
shaped, sarcoma-like cells and other regions showing adenomatous
patterns. Pleural mesotheliomas have been linked to exposure to
asbestos. {ECO:0000269|PubMed:8401592}. Note=The disease may be
caused by mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: Presence of the KTS motif hinders interactions
between DNA and zinc-finger 4.
-!- SIMILARITY: Belongs to the EGR C2H2-type zinc-finger protein
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB33443.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
Sequence=CAA35956.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAA35956.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
Sequence=CAC39220.3; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAI95758.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAI95759.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/WT1ID78.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/wt1/";
-----------------------------------------------------------------------
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EMBL; X51630; CAA35956.1; ALT_SEQ; mRNA.
EMBL; M80232; AAA61299.1; -; Genomic_DNA.
EMBL; M80217; AAA61299.1; JOINED; Genomic_DNA.
EMBL; M80218; AAA61299.1; JOINED; Genomic_DNA.
EMBL; M80219; AAA61299.1; JOINED; Genomic_DNA.
EMBL; M80220; AAA61299.1; JOINED; Genomic_DNA.
EMBL; M80221; AAA61299.1; JOINED; Genomic_DNA.
EMBL; M80228; AAA61299.1; JOINED; Genomic_DNA.
EMBL; M80229; AAA61299.1; JOINED; Genomic_DNA.
EMBL; M80231; AAA61299.1; JOINED; Genomic_DNA.
EMBL; X61631; CAA43819.1; -; Genomic_DNA.
EMBL; X61632; CAA43819.1; JOINED; Genomic_DNA.
EMBL; X61633; CAA43819.1; JOINED; Genomic_DNA.
EMBL; X61634; CAA43819.1; JOINED; Genomic_DNA.
EMBL; X61635; CAA43819.1; JOINED; Genomic_DNA.
EMBL; X61636; CAA43819.1; JOINED; Genomic_DNA.
EMBL; X61637; CAA43819.1; JOINED; Genomic_DNA.
EMBL; X61638; CAA43819.1; JOINED; Genomic_DNA.
EMBL; AK093168; BAG52667.1; -; mRNA.
EMBL; AK291736; BAF84425.1; -; mRNA.
EMBL; AY245105; AAO61088.1; -; Genomic_DNA.
EMBL; AL049692; CAC39220.3; ALT_INIT; Genomic_DNA.
EMBL; AL049692; CAI95758.2; ALT_INIT; Genomic_DNA.
EMBL; AL049692; CAI95759.2; ALT_INIT; Genomic_DNA.
EMBL; AL049692; CAI95760.1; -; Genomic_DNA.
EMBL; CH471064; EAW68220.1; -; Genomic_DNA.
EMBL; CH471064; EAW68223.1; -; Genomic_DNA.
EMBL; CH471064; EAW68224.1; -; Genomic_DNA.
EMBL; BC032861; AAH32861.1; -; mRNA.
EMBL; M30393; AAA36810.1; -; mRNA.
EMBL; S75264; AAB33443.1; ALT_SEQ; mRNA.
EMBL; S61515; AAB20110.1; -; Genomic_DNA.
EMBL; S61522; AAB20111.1; -; Genomic_DNA.
EMBL; S61524; AAB20112.1; -; Genomic_DNA.
EMBL; S60755; AAC60605.1; -; Genomic_DNA.
CCDS; CCDS55750.1; -. [P19544-9]
CCDS; CCDS55751.1; -. [P19544-6]
PIR; A38080; A38080.
RefSeq; NP_000369.3; NM_000378.4.
RefSeq; NP_001185480.1; NM_001198551.1. [P19544-6]
RefSeq; NP_001185481.1; NM_001198552.1. [P19544-9]
RefSeq; NP_077742.2; NM_024424.3.
RefSeq; NP_077744.3; NM_024426.4.
UniGene; Hs.591980; -.
PDB; 1LU6; Model; -; A=310-449.
PDB; 1XF7; NMR; -; A=381-407.
PDB; 2G7T; Model; -; A=310-449.
PDB; 2G7V; Model; -; A=310-449.
PDB; 2G7W; Model; -; A=310-449.
PDB; 2G7X; Model; -; A=310-449.
PDB; 2JP9; NMR; -; A=318-438.
PDB; 2JPA; NMR; -; A=318-438.
PDB; 2PRT; X-ray; 3.15 A; A=318-438.
PDB; 3HPJ; X-ray; 2.00 A; C/F=126-134.
PDB; 3MYJ; X-ray; 1.89 A; C/F=126-134.
PDB; 4R2E; X-ray; 1.84 A; A=350-440.
PDB; 4R2P; X-ray; 1.79 A; A=350-440.
PDB; 4R2Q; X-ray; 1.54 A; A=350-440.
PDB; 4R2R; X-ray; 2.09 A; A=350-440.
PDB; 4R2S; X-ray; 2.49 A; A=350-440.
PDB; 4WUU; X-ray; 3.05 A; C=126-134.
PDB; 5KL2; X-ray; 1.69 A; A=350-440.
PDB; 5KL3; X-ray; 1.45 A; A=350-440.
PDB; 5KL4; X-ray; 1.78 A; A/D=350-440.
PDB; 5KL5; X-ray; 2.29 A; A=350-440.
PDB; 5KL6; X-ray; 1.64 A; A=350-440.
PDB; 5KL7; X-ray; 1.58 A; A=350-440.
PDBsum; 1LU6; -.
PDBsum; 1XF7; -.
PDBsum; 2G7T; -.
PDBsum; 2G7V; -.
PDBsum; 2G7W; -.
PDBsum; 2G7X; -.
PDBsum; 2JP9; -.
PDBsum; 2JPA; -.
PDBsum; 2PRT; -.
PDBsum; 3HPJ; -.
PDBsum; 3MYJ; -.
PDBsum; 4R2E; -.
PDBsum; 4R2P; -.
PDBsum; 4R2Q; -.
PDBsum; 4R2R; -.
PDBsum; 4R2S; -.
PDBsum; 4WUU; -.
PDBsum; 5KL2; -.
PDBsum; 5KL3; -.
PDBsum; 5KL4; -.
PDBsum; 5KL5; -.
PDBsum; 5KL6; -.
PDBsum; 5KL7; -.
ProteinModelPortal; P19544; -.
SMR; P19544; -.
BioGrid; 113327; 28.
IntAct; P19544; 24.
MINT; MINT-105556; -.
STRING; 9606.ENSP00000331327; -.
iPTMnet; P19544; -.
PhosphoSitePlus; P19544; -.
BioMuta; WT1; -.
DMDM; 139778; -.
MaxQB; P19544; -.
PaxDb; P19544; -.
PeptideAtlas; P19544; -.
PRIDE; P19544; -.
DNASU; 7490; -.
Ensembl; ENST00000379079; ENSP00000368370; ENSG00000184937. [P19544-6]
Ensembl; ENST00000530998; ENSP00000435307; ENSG00000184937. [P19544-9]
GeneID; 7490; -.
KEGG; hsa:7490; -.
UCSC; uc001mtl.3; human. [P19544-1]
CTD; 7490; -.
DisGeNET; 7490; -.
EuPathDB; HostDB:ENSG00000184937.12; -.
GeneCards; WT1; -.
GeneReviews; WT1; -.
H-InvDB; HIX0009531; -.
HGNC; HGNC:12796; WT1.
HPA; CAB000327; -.
HPA; HPA035717; -.
HPA; HPA053848; -.
MalaCards; WT1; -.
MIM; 136680; phenotype.
MIM; 156240; phenotype.
MIM; 194070; phenotype.
MIM; 194080; phenotype.
MIM; 256370; phenotype.
MIM; 607102; gene.
MIM; 608978; phenotype.
neXtProt; NX_P19544; -.
OpenTargets; ENSG00000184937; -.
Orphanet; 251510; 46,XY partial gonadal dysgenesis.
Orphanet; 220; Denys-Drash syndrome.
Orphanet; 83469; Desmoplastic small round cell tumor.
Orphanet; 93217; Familial idiopathic steroid-resistant nephrotic syndrome with diffuse mesangial sclerosis.
Orphanet; 93213; Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis.
Orphanet; 347; Frasier syndrome.
Orphanet; 3097; Meacham syndrome.
Orphanet; 654; Nephroblastoma.
Orphanet; 93220; Sporadic idiopathic steroid-resistant nephrotic syndrome with diffuse mesangial sclerosis.
Orphanet; 893; WAGR syndrome.
PharmGKB; PA37395; -.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
GeneTree; ENSGT00550000074455; -.
HOVERGEN; HBG006960; -.
InParanoid; P19544; -.
KO; K09234; -.
PhylomeDB; P19544; -.
SignaLink; P19544; -.
SIGNOR; P19544; -.
ChiTaRS; WT1; human.
EvolutionaryTrace; P19544; -.
GeneWiki; WT1; -.
GenomeRNAi; 7490; -.
PRO; PR:P19544; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000184937; -.
CleanEx; HS_WT1; -.
ExpressionAtlas; P19544; baseline and differential.
Genevisible; P19544; HS.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0070742; F:C2H2 zinc finger domain binding; IPI:UniProtKB.
GO; GO:0010385; F:double-stranded methylated DNA binding; IDA:UniProtKB.
GO; GO:0044729; F:hemi-methylated DNA-binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0035802; P:adrenal cortex formation; ISS:UniProtKB.
GO; GO:0030325; P:adrenal gland development; IGI:UniProtKB.
GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IGI:UniProtKB.
GO; GO:0043010; P:camera-type eye development; ISS:UniProtKB.
GO; GO:0060923; P:cardiac muscle cell fate commitment; ISS:BHF-UCL.
GO; GO:0071320; P:cellular response to cAMP; IEP:UniProtKB.
GO; GO:0071371; P:cellular response to gonadotropin stimulus; IDA:UniProtKB.
GO; GO:0060539; P:diaphragm development; ISS:UniProtKB.
GO; GO:0030855; P:epithelial cell differentiation; ISS:UniProtKB.
GO; GO:0007281; P:germ cell development; ISS:UniProtKB.
GO; GO:0032836; P:glomerular basement membrane development; IMP:UniProtKB.
GO; GO:0072112; P:glomerular visceral epithelial cell differentiation; ISS:UniProtKB.
GO; GO:0032835; P:glomerulus development; IGI:UniProtKB.
GO; GO:0008406; P:gonad development; ISS:UniProtKB.
GO; GO:0007507; P:heart development; IGI:UniProtKB.
GO; GO:0001822; P:kidney development; IGI:UniProtKB.
GO; GO:0030539; P:male genitalia development; ISS:UniProtKB.
GO; GO:0008584; P:male gonad development; IEP:UniProtKB.
GO; GO:0060231; P:mesenchymal to epithelial transition; ISS:UniProtKB.
GO; GO:0072207; P:metanephric epithelium development; IEP:UniProtKB.
GO; GO:0072075; P:metanephric mesenchyme development; ISS:UniProtKB.
GO; GO:0072284; P:metanephric S-shaped body morphogenesis; IGI:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IGI:UniProtKB.
GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO; GO:2000195; P:negative regulation of female gonad development; ISS:UniProtKB.
GO; GO:0072302; P:negative regulation of metanephric glomerular mesangial cell proliferation; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0060421; P:positive regulation of heart growth; ISS:UniProtKB.
GO; GO:2000020; P:positive regulation of male gonad development; ISS:UniProtKB.
GO; GO:2001076; P:positive regulation of metanephric ureteric bud development; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0072166; P:posterior mesonephric tubule development; ISS:UniProtKB.
GO; GO:0003156; P:regulation of animal organ formation; ISS:UniProtKB.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0008380; P:RNA splicing; ISS:UniProtKB.
GO; GO:0007530; P:sex determination; IDA:UniProtKB.
GO; GO:0007356; P:thorax and anterior abdomen determination; ISS:UniProtKB.
GO; GO:0009888; P:tissue development; ISS:UniProtKB.
GO; GO:0001657; P:ureteric bud development; ISS:UniProtKB.
GO; GO:0001570; P:vasculogenesis; ISS:UniProtKB.
GO; GO:0061032; P:visceral serous pericardium development; IGI:UniProtKB.
InterPro; IPR017987; Wilms_tumour.
InterPro; IPR000976; Wilms_tumour_N.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
Pfam; PF02165; WT1; 1.
PRINTS; PR00049; WILMSTUMOUR.
SMART; SM00355; ZnF_C2H2; 4.
SUPFAM; SSF57667; SSF57667; 2.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
1: Evidence at protein level;
3D-structure; Alternative initiation; Alternative splicing;
Chromosomal rearrangement; Complete proteome; Cytoplasm;
Disease mutation; DNA-binding; Isopeptide bond; Metal-binding;
Nucleus; Reference proteome; Repeat; RNA editing; RNA-binding;
Transcription; Transcription regulation; Tumor suppressor;
Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 449 Wilms tumor protein.
/FTId=PRO_0000047131.
ZN_FING 323 347 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 353 377 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 383 405 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 414 438 C2H2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
REGION 367 381 Important for interaction with target
DNA.
REGION 393 401 Important for interaction with target
DNA.
MOTIF 408 410 KTS motif.
COMPBIAS 27 83 Pro-rich.
SITE 424 424 Important for interaction with target
DNA.
SITE 430 430 Important for interaction with target
DNA.
CROSSLNK 73 73 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:15520190}.
CROSSLNK 177 177 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:15520190}.
CROSSLNK 444 444 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 144 Missing (in isoform 6 and isoform 9).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_037582.
VAR_SEQ 1 1 M -> MDFLLLQDPASTCVPEPASQHTLRSGPGCLQQPEQQ
GVRDPGGIWAKLGAAEASAERLQGRRSRGASGSEPQQM
(in isoform 7 and isoform 8).
{ECO:0000303|PubMed:2154702}.
/FTId=VSP_037583.
VAR_SEQ 145 147 RNQ -> MEK (in isoform 6 and isoform 9).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_037584.
VAR_SEQ 250 266 Missing (in isoform 2, isoform 3, isoform
8 and isoform 9).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:2154335}.
/FTId=VSP_006866.
VAR_SEQ 408 410 Missing (in isoform 2, isoform 4 and
isoform 6). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:2154335}.
/FTId=VSP_006867.
VARIANT 131 131 A -> T (in a patient with hypospadias).
{ECO:0000269|PubMed:15266301}.
/FTId=VAR_043798.
VARIANT 181 181 P -> S (in WT1; dbSNP:rs2234584).
{ECO:0000269|PubMed:15150775,
ECO:0000269|PubMed:9108089}.
/FTId=VAR_007739.
VARIANT 223 223 S -> N (in WT1).
{ECO:0000269|PubMed:9529364}.
/FTId=VAR_007740.
VARIANT 253 253 G -> A (in WT1).
{ECO:0000269|PubMed:9108089}.
/FTId=VAR_007741.
VARIANT 273 273 S -> G (found in a mesothelioma sample;
somatic mutation; dbSNP:rs121907908).
{ECO:0000269|PubMed:8401592}.
/FTId=VAR_007742.
VARIANT 281 281 L -> P (in RNA edited version).
/FTId=VAR_058021.
VARIANT 312 312 R -> Q (in NPHS4).
{ECO:0000269|PubMed:11182928}.
/FTId=VAR_015053.
VARIANT 330 330 C -> Y (in DDS).
{ECO:0000269|PubMed:1302008}.
/FTId=VAR_007743.
VARIANT 342 342 M -> R (in DDS).
{ECO:0000269|PubMed:11182928}.
/FTId=VAR_015054.
VARIANT 355 355 C -> G (in WT1).
{ECO:0000269|PubMed:15150775}.
/FTId=VAR_043799.
VARIANT 355 355 C -> Y (in DDS).
{ECO:0000269|PubMed:11182928,
ECO:0000269|PubMed:9475094}.
/FTId=VAR_015055.
VARIANT 360 360 C -> G (in DDS).
/FTId=VAR_007744.
VARIANT 360 360 C -> Y (in DDS).
{ECO:0000269|PubMed:8411073}.
/FTId=VAR_043800.
VARIANT 364 364 F -> L (in NPHS4).
{ECO:0000269|PubMed:9607189}.
/FTId=VAR_043801.
VARIANT 366 366 R -> C (in WT1, DDS and MEACHS).
{ECO:0000269|PubMed:1317572,
ECO:0000269|PubMed:15150775,
ECO:0000269|PubMed:17853480,
ECO:0000269|PubMed:9529364}.
/FTId=VAR_007745.
VARIANT 366 366 R -> H (in DDS and WT1).
{ECO:0000269|PubMed:11182928,
ECO:0000269|PubMed:15150775,
ECO:0000269|PubMed:9475094,
ECO:0000269|PubMed:9607189}.
/FTId=VAR_007746.
VARIANT 366 366 R -> L (in DDS).
{ECO:0000269|PubMed:8741319}.
/FTId=VAR_043802.
VARIANT 369 369 Q -> P (in DDS).
{ECO:0000269|PubMed:10799199}.
/FTId=VAR_043803.
VARIANT 373 373 H -> Q (in DDS and WT1).
{ECO:0000269|PubMed:15150775}.
/FTId=VAR_007747.
VARIANT 373 373 H -> Y (in DDS).
{ECO:0000269|PubMed:8956030}.
/FTId=VAR_015056.
VARIANT 377 377 H -> R (in DDS).
{ECO:0000269|PubMed:8112732}.
/FTId=VAR_015057.
VARIANT 377 377 H -> Y (in NPHS4).
{ECO:0000269|PubMed:9529364}.
/FTId=VAR_007748.
VARIANT 379 379 G -> C (in NPHS4).
{ECO:0000269|PubMed:9607189}.
/FTId=VAR_043804.
VARIANT 383 383 F -> L (in NPHS4).
{ECO:0000269|PubMed:9529364}.
/FTId=VAR_007749.
VARIANT 385 385 C -> R (in DDS).
{ECO:0000269|PubMed:11182928,
ECO:0000269|PubMed:9475094,
ECO:0000269|PubMed:9607189}.
/FTId=VAR_015058.
VARIANT 388 388 C -> F (in DDS).
{ECO:0000269|PubMed:11182928}.
/FTId=VAR_015059.
VARIANT 388 388 C -> R (in NPHS4).
{ECO:0000269|PubMed:15253707}.
/FTId=VAR_043805.
VARIANT 388 388 C -> Y (in DDS).
{ECO:0000269|PubMed:11519891}.
/FTId=VAR_043806.
VARIANT 392 392 F -> L (in FS).
{ECO:0000269|PubMed:10571943}.
/FTId=VAR_015060.
VARIANT 394 394 R -> L (in WT1).
{ECO:0000269|PubMed:15150775}.
/FTId=VAR_043807.
VARIANT 394 394 R -> P (in DDS).
{ECO:0000269|PubMed:1302008}.
/FTId=VAR_043808.
VARIANT 394 394 R -> Q (in DDS).
{ECO:0000269|PubMed:9529364,
ECO:0000269|PubMed:9607189}.
/FTId=VAR_015061.
VARIANT 394 394 R -> W (in DDS, WT1 and MEACHS).
{ECO:0000269|PubMed:11182928,
ECO:0000269|PubMed:1302008,
ECO:0000269|PubMed:15150775,
ECO:0000269|PubMed:17853480,
ECO:0000269|PubMed:8295405,
ECO:0000269|PubMed:8411073,
ECO:0000269|PubMed:9529364,
ECO:0000269|PubMed:9607189}.
/FTId=VAR_007750.
VARIANT 396 396 D -> G (in DDS).
/FTId=VAR_007752.
VARIANT 396 396 D -> N (in DDS and NPHS4).
{ECO:0000269|PubMed:11182928,
ECO:0000269|PubMed:9529364,
ECO:0000269|PubMed:9607189}.
/FTId=VAR_007751.
VARIANT 396 396 D -> Y (in DDS).
{ECO:0000269|PubMed:10738002}.
/FTId=VAR_043809.
VARIANT 397 397 H -> P (in NPHS4).
{ECO:0000269|PubMed:15253707}.
/FTId=VAR_043810.
VARIANT 398 398 L -> P (in DDS).
{ECO:0000269|PubMed:8295405,
ECO:0000269|PubMed:9529364}.
/FTId=VAR_015062.
VARIANT 401 401 H -> Y (in DDS).
{ECO:0000269|PubMed:8111391}.
/FTId=VAR_043811.
VARIANT 405 405 H -> R (in DDS).
{ECO:0000269|PubMed:15349765}.
/FTId=VAR_043812.
MUTAGEN 73 73 K->R: Abolishes sumoylation; when
associated with R-177.
{ECO:0000269|PubMed:15520190}.
MUTAGEN 177 177 K->R: Abolishes sumoylation; when
associated with R-77.
{ECO:0000269|PubMed:15520190}.
MUTAGEN 343 343 H->A: Reduced RNA binding.
{ECO:0000269|PubMed:19123921}.
MUTAGEN 366 366 R->A: Strongly reduced binding of DNA and
RNA. {ECO:0000269|PubMed:19123921}.
MUTAGEN 372 372 R->A: Strongly reduced binding of DNA and
RNA. {ECO:0000269|PubMed:19123921}.
MUTAGEN 394 394 R->A,S: Strongly reduced binding of DNA
and RNA. {ECO:0000269|PubMed:19123921}.
MUTAGEN 434 434 H->A: Reduced RNA binding.
{ECO:0000269|PubMed:19123921}.
CONFLICT 288 288 I -> M (in Ref. 8; AAH32861).
{ECO:0000305}.
CONFLICT 365 365 S -> F (in Ref. 9; AAA36810 and 10;
AAB33443). {ECO:0000305}.
CONFLICT 387 387 T -> A (in Ref. 3; CAA43819).
{ECO:0000305}.
STRAND 322 324 {ECO:0000244|PDB:2JPA}.
TURN 328 330 {ECO:0000244|PDB:2JPA}.
STRAND 333 337 {ECO:0000244|PDB:2PRT}.
HELIX 338 344 {ECO:0000244|PDB:2PRT}.
HELIX 345 349 {ECO:0000244|PDB:2PRT}.
STRAND 363 366 {ECO:0000244|PDB:5KL3}.
HELIX 367 378 {ECO:0000244|PDB:5KL3}.
TURN 386 388 {ECO:0000244|PDB:5KL3}.
STRAND 391 393 {ECO:0000244|PDB:5KL3}.
HELIX 395 401 {ECO:0000244|PDB:5KL3}.
HELIX 403 406 {ECO:0000244|PDB:5KL3}.
TURN 419 421 {ECO:0000244|PDB:5KL5}.
STRAND 424 427 {ECO:0000244|PDB:5KL3}.
HELIX 428 438 {ECO:0000244|PDB:5KL3}.
SEQUENCE 449 AA; 49188 MW; 11C7FA3D485096B2 CRC64;
MGSDVRDLNA LLPAVPSLGG GGGCALPVSG AAQWAPVLDF APPGASAYGS LGGPAPPPAP
PPPPPPPPHS FIKQEPSWGG AEPHEEQCLS AFTVHFSGQF TGTAGACRYG PFGPPPPSQA
SSGQARMFPN APYLPSCLES QPAIRNQGYS TVTFDGTPSY GHTPSHHAAQ FPNHSFKHED
PMGQQGSLGE QQYSVPPPVY GCHTPTDSCT GSQALLLRTP YSSDNLYQMT SQLECMTWNQ
MNLGATLKGV AAGSSSSVKW TEGQSNHSTG YESDNHTTPI LCGAQYRIHT HGVFRGIQDV
RRVPGVAPTL VRSASETSEK RPFMCAYPGC NKRYFKLSHL QMHSRKHTGE KPYQCDFKDC
ERRFSRSDQL KRHQRRHTGV KPFQCKTCQR KFSRSDHLKT HTRTHTGKTS EKPFSCRWPS
CQKKFARSDE LVRHHNMHQR NMTKLQLAL


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