WT1_HUMAN
ID WT1_HUMAN Reviewed; 449 AA.
AC P19544; A8K6S1; B3KSA5; Q15881; Q16256; Q16575; Q4VXV4; Q4VXV5; Q4VXV6;
AC Q8IYZ5;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 2.
DT 03-AUG-2022, entry version 250.
DE RecName: Full=Wilms tumor protein;
DE AltName: Full=WT33;
GN Name=WT1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7).
RC TISSUE=Fetal kidney;
RX PubMed=2154702; DOI=10.1038/343774a0;
RA Gessler M., Poustka A., Cavenee W., Neve R.L., Orkin S.H., Bruns G.A.P.;
RT "Homozygous deletion in Wilms tumours of a zinc-finger gene identified by
RT chromosome jumping.";
RL Nature 343:774-778(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS 1; 2;
RP 3 AND 4).
RC TISSUE=Placenta;
RX PubMed=1658787; DOI=10.1073/pnas.88.21.9618;
RA Haber D.A., Sohn R.L., Buckler A.J., Pelletier J., Call K.M., Housman D.E.;
RT "Alternative splicing and genomic structure of the Wilms tumor gene WT1.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:9618-9622(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM 4).
RX PubMed=1572653; DOI=10.1016/0888-7543(92)90313-h;
RA Gessler M., Konig A., Bruns G.A.P.;
RT "The genomic organization and expression of the WT1 gene.";
RL Genomics 12:807-813(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 9).
RC TISSUE=Placenta, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM 1).
RG NIEHS SNPs program;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [7]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 85-449 (ISOFORM 2).
RX PubMed=2154335; DOI=10.1016/0092-8674(90)90601-a;
RA Call K.M., Glaser T., Ito C.Y., Buckler A.J., Pelletier J., Haber D.A.,
RA Rose E.A., Kral A., Yeger H., Lewis W.H., Jones C., Housman D.E.;
RT "Isolation and characterization of a zinc finger polypeptide gene at the
RT human chromosome 11 Wilms' tumor locus.";
RL Cell 60:509-520(1990).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 301-449 (ISOFORMS 2/4/6), AND FUNCTION.
RC TISSUE=Fetal kidney;
RX PubMed=7862533; DOI=10.1093/nar/23.2.277;
RA Hamilton T.B., Barilla K.C., Romaniuk P.J.;
RT "High affinity binding sites for the Wilms' tumour suppressor protein
RT WT1.";
RL Nucleic Acids Res. 23:277-284(1995).
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 385-405, AND VARIANTS DDS.
RX PubMed=1655284; DOI=10.1016/0092-8674(91)90194-4;
RA Pelletier J., Bruening W., Kashtan C.E., Mauer S.M., Manivel J.C.,
RA Striegel J.E., Houghton D.C., Junien C., Habib R., Fouser L., Fine R.N.,
RA Silverman B.L., Haber D.A., Housman D.E.;
RT "Germline mutations in the Wilms' tumor suppressor gene are associated with
RT abnormal urogenital development in Denys-Drash syndrome.";
RL Cell 67:437-447(1991).
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 385-405, AND VARIANTS DDS TYR-330;
RP PRO-394 AND TRP-394.
RX PubMed=1302008; DOI=10.1038/ng0592-144;
RA Bruening W., Bardeesy N., Silverman B.L., Cohn R.A., Machin G.A.,
RA Aronson A.J., Housman D., Pelletier J.;
RT "Germline intronic and exonic mutations in the Wilms' tumour gene (WT1)
RT affecting urogenital development.";
RL Nat. Genet. 1:144-148(1992).
RN [13]
RP IDENTIFICATION OF START CODON, AND ALTERNATIVE SPLICING.
RX PubMed=1671709; DOI=10.1128/mcb.11.3.1707-1712.1991;
RA Buckler A.J., Pelletier J., Haber D.A., Glaser T., Housman D.E.;
RT "Isolation, characterization, and expression of the murine Wilms' tumor
RT gene (WT1) during kidney development.";
RL Mol. Cell. Biol. 11:1707-1712(1991).
RN [14]
RP RNA EDITING OF POSITION 281.
RX PubMed=7926762; DOI=10.1101/gad.8.6.720;
RA Sharma P.M., Bowman M., Madden S.L., Rauscher F.J. III, Sukumar S.;
RT "RNA editing in the Wilms' tumor susceptibility gene, WT1.";
RL Genes Dev. 8:720-731(1994).
RN [15]
RP ALTERNATIVE INITIATION, AND ALTERNATIVE SPLICING (ISOFORMS 7 AND 8).
RX PubMed=8621495; DOI=10.1074/jbc.271.15.8646;
RA Bruening W., Pelletier J.;
RT "A non-AUG translational initiation event generates novel WT1 isoforms.";
RL J. Biol. Chem. 271:8646-8654(1996).
RN [16]
RP INTERACTION WITH WTAP.
RX PubMed=11001926; DOI=10.1093/oxfordjournals.hmg.a018914;
RA Little N.A., Hastie N.D., Davies R.C.;
RT "Identification of WTAP, a novel Wilms' tumour 1-associating protein.";
RL Hum. Mol. Genet. 9:2231-2239(2000).
RN [17]
RP INTERACTION WITH ZNF224.
RX PubMed=12239212; DOI=10.1074/jbc.m205667200;
RA Lee T.H., Lwu S., Kim J., Pelletier J.;
RT "Inhibition of Wilms tumor 1 transactivation by bone marrow zinc finger 2,
RT a novel transcriptional repressor.";
RL J. Biol. Chem. 277:44826-44837(2002).
RN [18]
RP INTERACTION WITH SRY.
RX PubMed=12970737; DOI=10.1038/sj.onc.1206717;
RA Matsuzawa-Watanabe Y., Inoue J., Semba K.;
RT "Transcriptional activity of testis-determining factor SRY is modulated by
RT the Wilms' tumor 1 gene product, WT1.";
RL Oncogene 22:7900-7904(2003).
RN [19]
RP REVIEW.
RX PubMed=1313285;
RA Haber D.A., Buckler A.J.;
RT "WT1: a novel tumor suppressor gene inactivated in Wilms' tumor.";
RL New Biol. 4:97-106(1992).
RN [20]
RP REVIEW.
RX PubMed=8393820; DOI=10.1096/fasebj.7.10.8393820;
RA Rauscher F.J. III;
RT "The WT1 Wilms tumor gene product: a developmentally regulated
RT transcription factor in the kidney that functions as a tumor suppressor.";
RL FASEB J. 7:896-903(1993).
RN [21]
RP INVOLVEMENT IN WILMS TUMOR.
RX PubMed=1654525; DOI=10.1038/353431a0;
RA Pelletier J., Bruening W., Li F.P., Haber D.A., Glaser T., Housman D.E.;
RT "WT1 mutations contribute to abnormal genital system development and
RT hereditary Wilms' tumour.";
RL Nature 353:431-434(1991).
RN [22]
RP REVIEW.
RX PubMed=17361230; DOI=10.1038/sj.leu.2404624;
RA Yang L., Han Y., Suarez Saiz F., Minden M.D.;
RT "A tumor suppressor and oncogene: the WT1 story.";
RL Leukemia 21:868-876(2007).
RN [23]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-73 AND LYS-177, AND SUMOYLATION AT
RP LYS-73 AND LYS-177.
RX PubMed=15520190; DOI=10.1158/0008-5472.can-04-1502;
RA Smolen G.A., Vassileva M.T., Wells J., Matunis M.J., Haber D.A.;
RT "SUMO-1 modification of the Wilms' tumor suppressor WT1.";
RL Cancer Res. 64:7846-7851(2004).
RN [24]
RP INTERACTION WITH RBM4, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=16934801; DOI=10.1016/j.yexcr.2006.07.008;
RA Markus M.A., Heinrich B., Raitskin O., Adams D.J., Mangs H., Goy C.,
RA Ladomery M., Sperling R., Stamm S., Morris B.J.;
RT "WT1 interacts with the splicing protein RBM4 and regulates its ability to
RT modulate alternative splicing in vivo.";
RL Exp. Cell Res. 312:3379-3388(2006).
RN [25]
RP FUNCTION, AND MUTAGENESIS OF HIS-343; ARG-366; ARG-372; ARG-394 AND
RP HIS-434.
RX PubMed=19123921; DOI=10.1021/bi801586a;
RA Weiss T.C., Romaniuk P.J.;
RT "Contribution of individual amino acids to the RNA binding activity of the
RT Wilms' tumor suppressor protein WT1.";
RL Biochemistry 48:148-155(2009).
RN [26]
RP INTERACTION WITH AMER1, AND FUNCTION.
RX PubMed=19416806; DOI=10.1073/pnas.0811349106;
RA Rivera M.N., Kim W.J., Wells J., Stone A., Burger A., Coffman E.J.,
RA Zhang J., Haber D.A.;
RT "The tumor suppressor WTX shuttles to the nucleus and modulates WT1
RT activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8338-8343(2009).
RN [27]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-444, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [28]
RP 9AATAD MOTIF.
RX PubMed=31375868; DOI=10.1007/s00018-019-03251-w;
RA Piskacek M., Havelka M., Jendruchova K., Knight A., Keegan L.P.;
RT "The evolution of the 9aaTAD domain in Sp2 proteins: inactivation with
RT valines and intron reservoirs.";
RL Cell. Mol. Life Sci. 77:1793-1810(2020).
RN [29]
RP STRUCTURE BY NMR OF 381-407 IN COMPLEX WITH ZINC IONS.
RX PubMed=15518539; DOI=10.1021/bi0491999;
RA Lachenmann M.J., Ladbury J.E., Dong J., Huang K., Carey P., Weiss M.A.;
RT "Why zinc fingers prefer zinc: ligand-field symmetry and the hidden
RT thermodynamics of metal ion selectivity.";
RL Biochemistry 43:13910-13925(2004).
RN [30]
RP STRUCTURE BY NMR OF 318-438 IN COMPLEX WITH DNA AND ZINC IONS (ISOFORM 4),
RP X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 318-438 IN COMPLEX WITH DNA AND
RP ZINC IONS, AND FUNCTION.
RX PubMed=17716689; DOI=10.1016/j.jmb.2007.07.017;
RA Stoll R., Lee B.M., Debler E.W., Laity J.H., Wilson I.A., Dyson H.J.,
RA Wright P.E.;
RT "Structure of the Wilms tumor suppressor protein zinc finger domain bound
RT to DNA.";
RL J. Mol. Biol. 372:1227-1245(2007).
RN [31]
RP X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 350-440 IN COMPLEX WITH ZINC AND
RP TARGET DNA, FUNCTION, AND DOMAIN.
RX PubMed=25258363; DOI=10.1101/gad.250746.114;
RA Hashimoto H., Olanrewaju Y.O., Zheng Y., Wilson G.G., Zhang X., Cheng X.;
RT "Wilms tumor protein recognizes 5-carboxylcytosine within a specific DNA
RT sequence.";
RL Genes Dev. 28:2304-2313(2014).
RN [32]
RP VARIANT WT1 CYS-366.
RX PubMed=1317572; DOI=10.1073/pnas.89.11.4791;
RA Little M.H., Prosser J., Condie A., Smith P.J., van Heyningen V.,
RA Hastie N.D.;
RT "Zinc finger point mutations within the WT1 gene in Wilms tumor patients.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:4791-4795(1992).
RN [33]
RP VARIANTS DDS.
RX PubMed=1338906; DOI=10.1093/hmg/1.5.301;
RA Baird P.N., Santos A., Groves N., Jadresic L., Cowell J.K.;
RT "Constitutional mutations in the WT1 gene in patients with Denys-Drash
RT syndrome.";
RL Hum. Mol. Genet. 1:301-305(1992).
RN [34]
RP VARIANTS DDS.
RX PubMed=8388765; DOI=10.1093/hmg/2.3.259;
RA Little M.H., Williamson K.A., Mannens M., Kelsey A., Gosden C.,
RA Hastie N.D., van Heyningen V.;
RT "Evidence that WT1 mutations in Denys-Drash syndrome patients may act in a
RT dominant-negative fashion.";
RL Hum. Mol. Genet. 2:259-264(1993).
RN [35]
RP VARIANT DDS TYR-401.
RX PubMed=8111391; DOI=10.1093/hmg/2.12.2193;
RA Baird P.N., Cowell J.K.;
RT "A novel zinc finger mutation in a patient with Denys-Drash syndrome.";
RL Hum. Mol. Genet. 2:2193-2194(1993).
RN [36]
RP VARIANTS DDS TRP-394 AND PRO-398.
RX PubMed=8295405; DOI=10.1007/bf00714282;
RA Tsuda M., Sakiyama T., Kitagawa T., Watanabe S., Watanabe T., Takahashi S.,
RA Kawaguchi H., Ito K.;
RT "Molecular analysis of two Japanese cases of Denys-Drash syndrome.";
RL J. Inherit. Metab. Dis. 16:876-880(1993).
RN [37]
RP VARIANTS DDS TYR-360 AND TRP-394.
RX PubMed=8411073; DOI=10.1136/jmg.30.9.767;
RA Clarkson P.A., Davies H.R., Williams D.M., Chaudhary R., Hughes I.A.,
RA Patterson M.N.;
RT "Mutational screening of the Wilms's tumour gene, WT1, in males with
RT genital abnormalities.";
RL J. Med. Genet. 30:767-772(1993).
RN [38]
RP VARIANT GLY-273, AND INVOLVEMENT IN MESOM.
RX PubMed=8401592; DOI=10.1038/ng0893-415;
RA Park S., Schalling M., Bernard A., Maheswaran S., Shipley G.C., Roberts D.,
RA Fletcher J., Shipman R., Rheinwald J., Demetri G., Griffin J., Minden M.,
RA Housman D.E., Haber D.A.;
RT "The Wilms tumour gene WT1 is expressed in murine mesoderm-derived tissues
RT and mutated in a human mesothelioma.";
RL Nat. Genet. 4:415-420(1993).
RN [39]
RP VARIANT DDS ARG-377.
RX PubMed=8112732; DOI=10.1007/bf00210593;
RA Nordenskjold A., Friedman E., Anvret M.;
RT "WT1 mutations in patients with Denys-Drash syndrome: a novel mutation in
RT exon 8 and paternal allele origin.";
RL Hum. Genet. 93:115-120(1994).
RN [40]
RP VARIANT DDS LEU-366.
RX PubMed=8741319; DOI=10.1111/j.1442-200x.1996.tb03483.x;
RA Tsuda M., Sakiyama T., Owada M., Chiba Y.;
RT "A newly identified exonic mutation of the WT1 gene in a patient with
RT Denys-Drash syndrome.";
RL Acta Paediatr. Jpn. Overseas Ed. 38:265-266(1996).
RN [41]
RP VARIANT DDS TYR-373.
RX PubMed=8956030; DOI=10.1159/000154374;
RA Ghahremani M., Chan C.B., Bistritzer T., Aladjem M.M., Tieder M.,
RA Pelletier J.;
RT "A novel mutation H373Y in the Wilms' tumor suppressor gene, WT1,
RT associated with Denys-Drash syndrome.";
RL Hum. Hered. 46:336-338(1996).
RN [42]
RP VARIANTS WT1 SER-181 AND ALA-253.
RX PubMed=9108089; DOI=10.1073/pnas.94.8.3972;
RA Schumacher V., Schneider S., Figge A., Wildhardt G., Harms D., Schmidt D.,
RA Weirich A., Ludwig R., Royer-Pokora B.;
RT "Correlation of germ-line mutations and two-hit inactivation of the WT1
RT gene with Wilms tumors of stromal-predominant histology.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:3972-3977(1997).
RN [43]
RP VARIANTS NPHS4 TYR-377; LEU-383 AND ASN-396, VARIANTS DDS CYS-366; GLN-394;
RP TRP-394 AND PRO-398, AND VARIANT WT1 ASN-223.
RX PubMed=9529364; DOI=10.1086/301806;
RA Jeanpierre C., Denamur E., Henry I., Cabanis M.-O., Luce S., Cecille A.,
RA Elion J., Peuchmaur M., Loirat C., Niaudet P., Gubler M.-C., Junien C.;
RT "Identification of constitutional WT1 mutations, in patients with isolated
RT diffuse mesangial sclerosis, and analysis of genotype/phenotype
RT correlations by use of a computerized mutation database.";
RL Am. J. Hum. Genet. 62:824-833(1998).
RN [44]
RP VARIANTS DDS TYR-355; HIS-366 AND ARG-385.
RX PubMed=9475094; DOI=10.1136/jmg.35.1.45;
RA Kikuchi H., Takata A., Akasaka Y., Fukuzawa R., Yoneyama H., Kurosawa Y.,
RA Honda M., Kamiyama Y., Hata J.;
RT "Do intronic mutations affecting splicing of WT1 exon 9 cause Frasier
RT syndrome?";
RL J. Med. Genet. 35:45-48(1998).
RN [45]
RP VARIANTS NPHS4 LEU-364; HIS-366; CYS-379; ARG-385; GLN-394; TRP-394 AND
RP ASN-396.
RX PubMed=9607189; DOI=10.1046/j.1523-1755.1998.00948.x;
RA Schumacher V., Schaerer K., Wuehl E., Altrogge H., Bonzel K.-E.,
RA Guschmann M., Neuhaus T.J., Pollastro R.M., Kuwertz-Broeking E., Bulla M.,
RA Tondera A.-M., Mundel P., Helmchen U., Waldherr R., Weirich A.,
RA Royer-Pokora B.;
RT "Spectrum of early onset nephrotic syndrome associated with WT1 missense
RT mutations.";
RL Kidney Int. 53:1594-1600(1998).
RN [46]
RP VARIANT FS LEU-392.
RX PubMed=10571943;
RX DOI=10.1002/(sici)1098-1004(199912)14:6<466::aid-humu4>3.0.co;2-6;
RA Kohsaka T., Tagawa M., Takekoshi Y., Yanagisawa H., Tadokoro K., Yamada M.;
RT "Exon 9 mutations in the WT1 gene, without influencing KTS splice isoforms,
RT are also responsible for Frasier syndrome.";
RL Hum. Mutat. 14:466-470(1999).
RN [47]
RP VARIANT DDS TYR-396.
RX PubMed=10738002;
RX DOI=10.1002/(sici)1098-1004(200004)15:4<389::aid-humu29>3.0.co;2-e;
RA Little M., Carman G., Donaldson E.;
RT "Novel WT1 exon 9 mutation (D396Y) in a patient with early onset Denys
RT Drash syndrome.";
RL Hum. Mutat. 15:389-389(2000).
RN [48]
RP VARIANTS DDS ARG-342; TYR-355; HIS-366; ARG-385; PHE-388; TRP-394 AND
RP ASN-396, AND VARIANT NPHS4 GLN-312.
RX PubMed=11182928; DOI=10.1136/jmg.37.9.698;
RA Takata A., Kikuchi H., Fukuzawa R., Ito S., Honda M., Hata J.;
RT "Constitutional WT1 correlate with clinical features in children with
RT progressive nephropathy.";
RL J. Med. Genet. 37:698-701(2000).
RN [49]
RP VARIANT DDS PRO-369.
RX PubMed=10799199; DOI=10.1016/s0022-5347(05)67560-x;
RA Ohta S., Ozawa T., Izumino K., Sakuragawa N., Fuse H.;
RT "A novel missense mutation of the WT1 gene causing Denys-Drash syndrome
RT with exceptionally mild renal manifestations.";
RL J. Urol. 163:1857-1858(2000).
RN [50]
RP VARIANT DDS TYR-388.
RX PubMed=11519891; DOI=10.1007/s004670100626;
RA Swiatecka-Urban A., Mokrzycki M.H., Kaskel F., Da Silva F., Denamur E.;
RT "Novel WT1 mutation (C388Y) in a female child with Denys-Drash syndrome.";
RL Pediatr. Nephrol. 16:627-630(2001).
RN [51]
RP VARIANTS WT1 SER-181; GLY-355; CYS-366; HIS-366; GLN-373; TRP-394 AND
RP LEU-394.
RX PubMed=15150775; DOI=10.1002/ajmg.a.30015;
RA Royer-Pokora B., Beier M., Henzler M., Alam R., Schumacher V., Weirich A.,
RA Huff V.;
RT "Twenty-four new cases of WT1 germline mutations and review of the
RT literature: genotype/phenotype correlations for Wilms tumor development.";
RL Am. J. Med. Genet. A 127:249-257(2004).
RN [52]
RP VARIANT THR-131.
RX PubMed=15266301; DOI=10.1038/sj.ejhg.5201232;
RA Wang Y., Li Q., Xu J., Liu Q., Wang W., Lin Y., Ma F., Chen T., Li S.,
RA Shen Y.;
RT "Mutation analysis of five candidate genes in Chinese patients with
RT hypospadias.";
RL Eur. J. Hum. Genet. 12:706-712(2004).
RN [53]
RP VARIANTS NPHS4 ARG-388 AND PRO-397.
RX PubMed=15253707; DOI=10.1111/j.1523-1755.2004.00775.x;
RG Members of the APN study group;
RA Ruf R.G., Schultheiss M., Lichtenberger A., Karle S.M., Zalewski I.,
RA Mucha B., Everding A.S., Neuhaus T., Patzer L., Plank C., Haas J.P.,
RA Ozaltin F., Imm A., Fuchshuber A., Bakkaloglu A., Hildebrandt F.;
RT "Prevalence of WT1 mutations in a large cohort of patients with steroid-
RT resistant and steroid-sensitive nephrotic syndrome.";
RL Kidney Int. 66:564-570(2004).
RN [54]
RP VARIANT DDS ARG-405.
RX PubMed=15349765; DOI=10.1007/s00467-004-1564-3;
RA Hu M., Craig J., Howard N., Kan A., Chaitow J., Little D., Alexander S.I.;
RT "A novel mutation of WT1 exon 9 in a patient with Denys-Drash syndrome and
RT pyloric stenosis.";
RL Pediatr. Nephrol. 19:1160-1163(2004).
RN [55]
RP VARIANTS MEACHS CYS-366 AND TRP-394.
RX PubMed=17853480; DOI=10.1002/ajmg.a.31924;
RA Suri M., Kelehan P., O'neill D., Vadeyar S., Grant J., Ahmed S.F.,
RA Tolmie J., McCann E., Lam W., Smith S., FitzPatrick D., Hastie N.D.,
RA Reardon W.;
RT "WT1 mutations in Meacham syndrome suggest a coelomic mesothelial origin of
RT the cardiac and diaphragmatic malformations.";
RL Am. J. Med. Genet. A 143:2312-2320(2007).
RN [56]
RP VARIANTS NPHS4 ARG-388; GLN-394; TRP-394 AND PRO-397.
RX PubMed=20798252; DOI=10.2215/cjn.01190210;
RA Buescher A.K., Kranz B., Buescher R., Hildebrandt F., Dworniczak B.,
RA Pennekamp P., Kuwertz-Broeking E., Wingen A.M., John U., Kemper M.,
RA Monnens L., Hoyer P.F., Weber S., Konrad M.;
RT "Immunosuppression and renal outcome in congenital and pediatric steroid-
RT resistant nephrotic syndrome.";
RL Clin. J. Am. Soc. Nephrol. 5:2075-2084(2010).
CC -!- FUNCTION: Transcription factor that plays an important role in cellular
CC development and cell survival (PubMed:7862533). Recognizes and binds to
CC the DNA sequence 5'-GCG(T/G)GGGCG-3' (PubMed:7862533, PubMed:17716689,
CC PubMed:25258363). Regulates the expression of numerous target genes,
CC including EPO. Plays an essential role for development of the
CC urogenital system. It has a tumor suppressor as well as an oncogenic
CC role in tumor formation. Function may be isoform-specific: isoforms
CC lacking the KTS motif may act as transcription factors
CC (PubMed:15520190). Isoforms containing the KTS motif may bind mRNA and
CC play a role in mRNA metabolism or splicing (PubMed:16934801). Isoform 1
CC has lower affinity for DNA, and can bind RNA (PubMed:19123921).
CC {ECO:0000269|PubMed:15520190, ECO:0000269|PubMed:16934801,
CC ECO:0000269|PubMed:17716689, ECO:0000269|PubMed:19123921,
CC ECO:0000269|PubMed:19416806, ECO:0000269|PubMed:25258363,
CC ECO:0000269|PubMed:7862533}.
CC -!- SUBUNIT: Homodimer. Interacts with WTIP. Interacts with actively
CC translating polysomes. Detected in nuclear ribonucleoprotein (mRNP)
CC particles. Interacts with HNRNPU via the zinc-finger region. Interacts
CC with U2AF2. Interacts with CITED2 (By similarity). Interacts with
CC ZNF224 via the zinc-finger region. Interacts with WTAP and SRY.
CC Interacts with AMER1. Interacts with RBM4. {ECO:0000250,
CC ECO:0000269|PubMed:11001926, ECO:0000269|PubMed:12239212,
CC ECO:0000269|PubMed:12970737, ECO:0000269|PubMed:15518539,
CC ECO:0000269|PubMed:16934801, ECO:0000269|PubMed:17716689,
CC ECO:0000269|PubMed:19416806}.
CC -!- INTERACTION:
CC P19544; Q92997: DVL3; NbExp=3; IntAct=EBI-2320534, EBI-739789;
CC P19544; Q6A162: KRT40; NbExp=4; IntAct=EBI-2320534, EBI-10171697;
CC P19544; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-2320534, EBI-10171774;
CC P19544; Q6N021: TET2; NbExp=9; IntAct=EBI-2320534, EBI-310727;
CC P19544-6; P05067: APP; NbExp=3; IntAct=EBI-11745701, EBI-77613;
CC P19544-6; O14503: BHLHE40; NbExp=3; IntAct=EBI-11745701, EBI-711810;
CC P19544-6; P28329-3: CHAT; NbExp=3; IntAct=EBI-11745701, EBI-25837549;
CC P19544-6; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-11745701, EBI-3867333;
CC P19544-6; P25685: DNAJB1; NbExp=3; IntAct=EBI-11745701, EBI-357034;
CC P19544-6; P22607: FGFR3; NbExp=3; IntAct=EBI-11745701, EBI-348399;
CC P19544-6; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-11745701, EBI-2549423;
CC P19544-6; P01112: HRAS; NbExp=3; IntAct=EBI-11745701, EBI-350145;
CC P19544-6; O15397: IPO8; NbExp=3; IntAct=EBI-11745701, EBI-358808;
CC P19544-6; P60371: KRTAP10-6; NbExp=3; IntAct=EBI-11745701, EBI-12012928;
CC P19544-6; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-11745701, EBI-10172290;
CC P19544-6; Q9H4L5: OSBPL3; NbExp=3; IntAct=EBI-11745701, EBI-1051317;
CC P19544-6; P16284: PECAM1; NbExp=3; IntAct=EBI-11745701, EBI-716404;
CC P19544-6; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-11745701, EBI-79165;
CC P19544-6; Q13501: SQSTM1; NbExp=3; IntAct=EBI-11745701, EBI-307104;
CC P19544-6; P37173: TGFBR2; NbExp=3; IntAct=EBI-11745701, EBI-296151;
CC P19544-6; Q15007: WTAP; NbExp=3; IntAct=EBI-11745701, EBI-751647;
CC P19544-6; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-11745701, EBI-527853;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15520190}. Nucleus,
CC nucleolus. Cytoplasm {ECO:0000250}. Note=Isoforms lacking the KTS motif
CC have a diffuse nuclear location (PubMed:15520190). Shuttles between
CC nucleus and cytoplasm. {ECO:0000250, ECO:0000269|PubMed:15520190}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus speckle
CC {ECO:0000269|PubMed:15520190}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:15520190}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=8;
CC Name=1;
CC IsoId=P19544-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P19544-2; Sequence=VSP_006866, VSP_006867;
CC Name=3;
CC IsoId=P19544-3; Sequence=VSP_006866;
CC Name=4;
CC IsoId=P19544-4; Sequence=VSP_006867;
CC Name=6;
CC IsoId=P19544-6; Sequence=VSP_037582, VSP_037584, VSP_006867;
CC Name=7;
CC IsoId=P19544-7; Sequence=VSP_037583;
CC Name=8;
CC IsoId=P19544-8; Sequence=VSP_037583, VSP_006866;
CC Name=9;
CC IsoId=P19544-9; Sequence=VSP_037582, VSP_037584, VSP_006866;
CC -!- TISSUE SPECIFICITY: Expressed in the kidney and a subset of
CC hematopoietic cells.
CC -!- DOMAIN: Binds to DNA motifs with the sequence 5'-GCG(T/G)GGGCG-3' via
CC its C2H2-type zinc fingers. Starting from the N-terminus, the second
CC zinc finger binds to the 3'-GCG motif, the middle zinc finger interacts
CC with the central TGG motif, and the C-terminal zinc finger binds to the
CC 5'-GCG motif. Binds double-stranded target DNA, irrespective of the
CC cytosine methylation status. Has reduced affinity for target DNA where
CC the cytosines have been oxidized to 5-hydroxymethylcytosine, 5-
CC formylcytosine or 5-carboxylcytosine. {ECO:0000269|PubMed:25258363}.
CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors.
CC {ECO:0000269|PubMed:31375868}.
CC -!- RNA EDITING: Modified_positions=281 {ECO:0000269|PubMed:7926762};
CC Note=Partially edited.;
CC -!- DISEASE: Frasier syndrome (FS) [MIM:136680]: Characterized by a slowly
CC progressing nephropathy leading to renal failure in adolescence or
CC early adulthood, male pseudohermaphroditism, and no Wilms tumor. As for
CC histological findings of the kidneys, focal glomerular sclerosis is
CC often observed. There is phenotypic overlap with Denys-Drash syndrome.
CC Inheritance is autosomal dominant. {ECO:0000269|PubMed:10571943}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- DISEASE: Wilms tumor 1 (WT1) [MIM:194070]: Embryonal malignancy of the
CC kidney that affects approximately 1 in 10'000 infants and young
CC children. It occurs both in sporadic and hereditary forms.
CC {ECO:0000269|PubMed:1317572, ECO:0000269|PubMed:15150775,
CC ECO:0000269|PubMed:9108089, ECO:0000269|PubMed:9529364}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Denys-Drash syndrome (DDS) [MIM:194080]: Typical nephropathy
CC characterized by diffuse mesangial sclerosis, genital abnormalities,
CC and/or Wilms tumor. There is phenotypic overlap with WAGR syndrome and
CC Frasier syndrome. Inheritance is autosomal dominant, but most cases are
CC sporadic. {ECO:0000269|PubMed:10738002, ECO:0000269|PubMed:10799199,
CC ECO:0000269|PubMed:11182928, ECO:0000269|PubMed:11519891,
CC ECO:0000269|PubMed:1302008, ECO:0000269|PubMed:1338906,
CC ECO:0000269|PubMed:15349765, ECO:0000269|PubMed:1655284,
CC ECO:0000269|PubMed:8111391, ECO:0000269|PubMed:8112732,
CC ECO:0000269|PubMed:8295405, ECO:0000269|PubMed:8388765,
CC ECO:0000269|PubMed:8411073, ECO:0000269|PubMed:8741319,
CC ECO:0000269|PubMed:8956030, ECO:0000269|PubMed:9475094,
CC ECO:0000269|PubMed:9529364}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Nephrotic syndrome 4 (NPHS4) [MIM:256370]: A form of nephrotic
CC syndrome, a renal disease clinically characterized by severe
CC proteinuria, resulting in complications such as hypoalbuminemia,
CC hyperlipidemia and edema. Kidney biopsies show non-specific histologic
CC changes such as focal segmental glomerulosclerosis and diffuse
CC mesangial proliferation. Some affected individuals have an inherited
CC steroid-resistant form and progress to end-stage renal failure. Most
CC patients with NPHS4 show diffuse mesangial sclerosis on renal biopsy,
CC which is a pathologic entity characterized by mesangial matrix
CC expansion with no mesangial hypercellularity, hypertrophy of the
CC podocytes, vacuolized podocytes, thickened basement membranes, and
CC diminished patency of the capillary lumen.
CC {ECO:0000269|PubMed:11182928, ECO:0000269|PubMed:15253707,
CC ECO:0000269|PubMed:20798252, ECO:0000269|PubMed:9529364,
CC ECO:0000269|PubMed:9607189}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Meacham syndrome (MEACHS) [MIM:608978]: Rare sporadically
CC occurring multiple malformation syndrome characterized by male
CC pseudohermaphroditism with abnormal internal female genitalia
CC comprising a uterus and double or septate vagina, complex congenital
CC heart defect and diaphragmatic abnormalities.
CC {ECO:0000269|PubMed:17853480}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Note=A chromosomal aberration involving WT1 may be a cause of
CC desmoplastic small round cell tumor (DSRCT). Translocation
CC t(11;22)(p13;q12) with EWSR1.
CC -!- DISEASE: Mesothelioma, malignant (MESOM) [MIM:156240]: An aggressive
CC neoplasm of the serosal lining of the chest. It appears as broad sheets
CC of cells, with some regions containing spindle-shaped, sarcoma-like
CC cells and other regions showing adenomatous patterns. Pleural
CC mesotheliomas have been linked to exposure to asbestos.
CC {ECO:0000269|PubMed:8401592}. Note=The disease may be caused by
CC variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: Presence of the KTS motif hinders interactions between
CC DNA and zinc-finger 4.
CC -!- MISCELLANEOUS: [Isoform 1]: Detected in nucleus speckle, may bind mRNA.
CC -!- MISCELLANEOUS: [Isoform 7]: Produced by alternative initiation of
CC isoform 1. Extended N-terminus. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 8]: Produced by alternative initiation of
CC isoform 1. Extended N-terminus. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the EGR C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB33443.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
CC Sequence=CAA35956.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA35956.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
CC Sequence=CAC39220.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAI95758.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAI95759.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/WT1ID78.html";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/wt1/";
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
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DR EMBL; X51630; CAA35956.1; ALT_SEQ; mRNA.
DR EMBL; M80232; AAA61299.1; -; Genomic_DNA.
DR EMBL; M80217; AAA61299.1; JOINED; Genomic_DNA.
DR EMBL; M80218; AAA61299.1; JOINED; Genomic_DNA.
DR EMBL; M80219; AAA61299.1; JOINED; Genomic_DNA.
DR EMBL; M80220; AAA61299.1; JOINED; Genomic_DNA.
DR EMBL; M80221; AAA61299.1; JOINED; Genomic_DNA.
DR EMBL; M80228; AAA61299.1; JOINED; Genomic_DNA.
DR EMBL; M80229; AAA61299.1; JOINED; Genomic_DNA.
DR EMBL; M80231; AAA61299.1; JOINED; Genomic_DNA.
DR EMBL; X61631; CAA43819.1; -; Genomic_DNA.
DR EMBL; X61632; CAA43819.1; JOINED; Genomic_DNA.
DR EMBL; X61633; CAA43819.1; JOINED; Genomic_DNA.
DR EMBL; X61634; CAA43819.1; JOINED; Genomic_DNA.
DR EMBL; X61635; CAA43819.1; JOINED; Genomic_DNA.
DR EMBL; X61636; CAA43819.1; JOINED; Genomic_DNA.
DR EMBL; X61637; CAA43819.1; JOINED; Genomic_DNA.
DR EMBL; X61638; CAA43819.1; JOINED; Genomic_DNA.
DR EMBL; AK093168; BAG52667.1; -; mRNA.
DR EMBL; AK291736; BAF84425.1; -; mRNA.
DR EMBL; AY245105; AAO61088.1; -; Genomic_DNA.
DR EMBL; AL049692; CAC39220.3; ALT_INIT; Genomic_DNA.
DR EMBL; AL049692; CAI95758.2; ALT_INIT; Genomic_DNA.
DR EMBL; AL049692; CAI95759.2; ALT_INIT; Genomic_DNA.
DR EMBL; AL049692; CAI95760.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68220.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68223.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68224.1; -; Genomic_DNA.
DR EMBL; BC032861; AAH32861.1; -; mRNA.
DR EMBL; M30393; AAA36810.1; -; mRNA.
DR EMBL; S75264; AAB33443.1; ALT_SEQ; mRNA.
DR EMBL; S61515; AAB20110.1; -; Genomic_DNA.
DR EMBL; S61522; AAB20111.1; -; Genomic_DNA.
DR EMBL; S61524; AAB20112.1; -; Genomic_DNA.
DR EMBL; S60755; AAC60605.1; -; Genomic_DNA.
DR CCDS; CCDS55750.1; -. [P19544-9]
DR CCDS; CCDS55751.1; -. [P19544-6]
DR CCDS; CCDS7878.2; -. [P19544-7]
DR PIR; A38080; A38080.
DR RefSeq; NP_000369.3; NM_000378.4.
DR RefSeq; NP_001185480.1; NM_001198551.1. [P19544-6]
DR RefSeq; NP_001185481.1; NM_001198552.1. [P19544-9]
DR RefSeq; NP_077742.2; NM_024424.3.
DR RefSeq; NP_077744.3; NM_024426.4. [P19544-7]
DR PDB; 1XF7; NMR; -; A=381-407.
DR PDB; 2JP9; NMR; -; A=318-438.
DR PDB; 2JPA; NMR; -; A=318-438.
DR PDB; 2PRT; X-ray; 3.15 A; A=318-438.
DR PDB; 3HPJ; X-ray; 2.00 A; C/F=126-134.
DR PDB; 3MYJ; X-ray; 1.89 A; C/F=126-134.
DR PDB; 4R2E; X-ray; 1.84 A; A=350-440.
DR PDB; 4R2P; X-ray; 1.79 A; A=350-440.
DR PDB; 4R2Q; X-ray; 1.54 A; A=350-440.
DR PDB; 4R2R; X-ray; 2.09 A; A=350-440.
DR PDB; 4R2S; X-ray; 2.49 A; A=350-440.
DR PDB; 4WUU; X-ray; 3.05 A; C=126-134.
DR PDB; 5KL2; X-ray; 1.69 A; A=350-440.
DR PDB; 5KL3; X-ray; 1.45 A; A=350-440.
DR PDB; 5KL4; X-ray; 1.78 A; A/D=350-440.
DR PDB; 5KL5; X-ray; 2.29 A; A=350-440.
DR PDB; 5KL6; X-ray; 1.64 A; A=350-440.
DR PDB; 5KL7; X-ray; 1.58 A; A=350-440.
DR PDB; 6B0O; X-ray; 1.55 A; A/D=321-440.
DR PDB; 6B0P; X-ray; 2.08 A; A/D=321-440.
DR PDB; 6B0Q; X-ray; 2.79 A; A/D=321-440.
DR PDB; 6B0R; X-ray; 1.82 A; A/D=321-440.
DR PDB; 6BLW; X-ray; 1.83 A; A=319-440.
DR PDB; 6RSY; X-ray; 2.95 A; C/H=126-134.
DR PDB; 6WLH; NMR; -; A=318-438.
DR PDBsum; 1XF7; -.
DR PDBsum; 2JP9; -.
DR PDBsum; 2JPA; -.
DR PDBsum; 2PRT; -.
DR PDBsum; 3HPJ; -.
DR PDBsum; 3MYJ; -.
DR PDBsum; 4R2E; -.
DR PDBsum; 4R2P; -.
DR PDBsum; 4R2Q; -.
DR PDBsum; 4R2R; -.
DR PDBsum; 4R2S; -.
DR PDBsum; 4WUU; -.
DR PDBsum; 5KL2; -.
DR PDBsum; 5KL3; -.
DR PDBsum; 5KL4; -.
DR PDBsum; 5KL5; -.
DR PDBsum; 5KL6; -.
DR PDBsum; 5KL7; -.
DR PDBsum; 6B0O; -.
DR PDBsum; 6B0P; -.
DR PDBsum; 6B0Q; -.
DR PDBsum; 6B0R; -.
DR PDBsum; 6BLW; -.
DR PDBsum; 6RSY; -.
DR PDBsum; 6WLH; -.
DR AlphaFoldDB; P19544; -.
DR BMRB; P19544; -.
DR SMR; P19544; -.
DR BioGRID; 113327; 66.
DR IntAct; P19544; 58.
DR MINT; P19544; -.
DR STRING; 9606.ENSP00000331327; -.
DR ChEMBL; CHEMBL4662942; -.
DR iPTMnet; P19544; -.
DR PhosphoSitePlus; P19544; -.
DR BioMuta; WT1; -.
DR DMDM; 139778; -.
DR jPOST; P19544; -.
DR MassIVE; P19544; -.
DR MaxQB; P19544; -.
DR PaxDb; P19544; -.
DR PeptideAtlas; P19544; -.
DR PRIDE; P19544; -.
DR ProteomicsDB; 53673; -. [P19544-1]
DR ProteomicsDB; 53674; -. [P19544-2]
DR ProteomicsDB; 53675; -. [P19544-3]
DR ProteomicsDB; 53676; -. [P19544-4]
DR ProteomicsDB; 53677; -. [P19544-6]
DR ProteomicsDB; 53678; -. [P19544-7]
DR ProteomicsDB; 53679; -. [P19544-8]
DR ProteomicsDB; 53680; -. [P19544-9]
DR ABCD; P19544; 1 sequenced antibody.
DR Antibodypedia; 3523; 1129 antibodies from 45 providers.
DR DNASU; 7490; -.
DR Ensembl; ENST00000379079.8; ENSP00000368370.2; ENSG00000184937.16. [P19544-6]
DR Ensembl; ENST00000452863.10; ENSP00000415516.5; ENSG00000184937.16. [P19544-7]
DR Ensembl; ENST00000530998.5; ENSP00000435307.1; ENSG00000184937.16. [P19544-9]
DR Ensembl; ENST00000639563.3; ENSP00000492269.3; ENSG00000184937.16. [P19544-8]
DR GeneID; 7490; -.
DR KEGG; hsa:7490; -.
DR MANE-Select; ENST00000452863.10; ENSP00000415516.5; NM_024426.6; NP_077744.4. [P19544-7]
DR UCSC; uc001mtl.3; human. [P19544-1]
DR CTD; 7490; -.
DR DisGeNET; 7490; -.
DR GeneCards; WT1; -.
DR GeneReviews; WT1; -.
DR HGNC; HGNC:12796; WT1.
DR HPA; ENSG00000184937; Tissue enhanced (endometrium, fallopian tube, ovary).
DR MalaCards; WT1; -.
DR MIM; 136680; phenotype.
DR MIM; 156240; phenotype.
DR MIM; 194070; phenotype.
DR MIM; 194080; phenotype.
DR MIM; 256370; phenotype.
DR MIM; 607102; gene.
DR MIM; 608978; phenotype.
DR neXtProt; NX_P19544; -.
DR OpenTargets; ENSG00000184937; -.
DR Orphanet; 242; 46,XY complete gonadal dysgenesis.
DR Orphanet; 251510; 46,XY partial gonadal dysgenesis.
DR Orphanet; 220; Denys-Drash syndrome.
DR Orphanet; 83469; Desmoplastic small round cell tumor.
DR Orphanet; 347; Frasier syndrome.
DR Orphanet; 656; Genetic steroid-resistant nephrotic syndrome.
DR Orphanet; 3097; Meacham syndrome.
DR Orphanet; 654; Nephroblastoma.
DR Orphanet; 893; WAGR syndrome.
DR PharmGKB; PA37395; -.
DR VEuPathDB; HostDB:ENSG00000184937; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000156734; -.
DR InParanoid; P19544; -.
DR OMA; LDADPHC; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; P19544; -.
DR PathwayCommons; P19544; -.
DR Reactome; R-HSA-9690406; Transcriptional regulation of testis differentiation.
DR SignaLink; P19544; -.
DR SIGNOR; P19544; -.
DR BioGRID-ORCS; 7490; 20 hits in 1108 CRISPR screens.
DR ChiTaRS; WT1; human.
DR EvolutionaryTrace; P19544; -.
DR GeneWiki; WT1; -.
DR GenomeRNAi; 7490; -.
DR Pharos; P19544; Tbio.
DR PRO; PR:P19544; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P19544; protein.
DR Bgee; ENSG00000184937; Expressed in germinal epithelium of ovary and 126 other tissues.
DR ExpressionAtlas; P19544; baseline and differential.
DR Genevisible; P19544; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0070742; F:C2H2 zinc finger domain binding; IPI:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:ARUK-UCL.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0010385; F:double-stranded methylated DNA binding; IDA:UniProtKB.
DR GO; GO:0044729; F:hemi-methylated DNA-binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:ARUK-UCL.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0035802; P:adrenal cortex formation; ISS:UniProtKB.
DR GO; GO:0030325; P:adrenal gland development; IGI:UniProtKB.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IGI:UniProtKB.
DR GO; GO:0043010; P:camera-type eye development; ISS:UniProtKB.
DR GO; GO:0060923; P:cardiac muscle cell fate commitment; ISS:BHF-UCL.
DR GO; GO:0071320; P:cellular response to cAMP; IEP:UniProtKB.
DR GO; GO:0071371; P:cellular response to gonadotropin stimulus; IDA:UniProtKB.
DR GO; GO:0060539; P:diaphragm development; ISS:UniProtKB.
DR GO; GO:0030855; P:epithelial cell differentiation; ISS:UniProtKB.
DR GO; GO:0007281; P:germ cell development; ISS:UniProtKB.
DR GO; GO:0032836; P:glomerular basement membrane development; IMP:UniProtKB.
DR GO; GO:0032835; P:glomerulus development; IGI:UniProtKB.
DR GO; GO:0008406; P:gonad development; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; IGI:UniProtKB.
DR GO; GO:0001822; P:kidney development; IGI:UniProtKB.
DR GO; GO:0030539; P:male genitalia development; ISS:UniProtKB.
DR GO; GO:0008584; P:male gonad development; IEP:UniProtKB.
DR GO; GO:0060231; P:mesenchymal to epithelial transition; ISS:UniProtKB.
DR GO; GO:0072207; P:metanephric epithelium development; IEP:UniProtKB.
DR GO; GO:0072075; P:metanephric mesenchyme development; ISS:UniProtKB.
DR GO; GO:0072284; P:metanephric S-shaped body morphogenesis; IGI:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IGI:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:2000195; P:negative regulation of female gonad development; ISS:UniProtKB.
DR GO; GO:0072302; P:negative regulation of metanephric glomerular mesangial cell proliferation; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB.
DR GO; GO:0072112; P:podocyte differentiation; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:1905643; P:positive regulation of DNA methylation; IMP:ARUK-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:0060421; P:positive regulation of heart growth; ISS:UniProtKB.
DR GO; GO:2000020; P:positive regulation of male gonad development; ISS:UniProtKB.
DR GO; GO:2001076; P:positive regulation of metanephric ureteric bud development; ISS:UniProtKB.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; IMP:ARUK-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ARUK-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0072166; P:posterior mesonephric tubule development; ISS:UniProtKB.
DR GO; GO:0003156; P:regulation of animal organ formation; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; ISS:UniProtKB.
DR GO; GO:0007530; P:sex determination; IDA:UniProtKB.
DR GO; GO:0007356; P:thorax and anterior abdomen determination; ISS:UniProtKB.
DR GO; GO:0009888; P:tissue development; ISS:UniProtKB.
DR GO; GO:0001657; P:ureteric bud development; ISS:UniProtKB.
DR GO; GO:0001570; P:vasculogenesis; ISS:UniProtKB.
DR GO; GO:0061032; P:visceral serous pericardium development; IGI:UniProtKB.
DR InterPro; IPR017987; Wilms_tumour.
DR InterPro; IPR000976; Wilms_tumour_N.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR23235:SF49; PTHR23235:SF49; 1.
DR Pfam; PF02165; WT1; 1.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Alternative splicing;
KW Chromosomal rearrangement; Cytoplasm; Disease variant; DNA-binding;
KW Isopeptide bond; Metal-binding; Nucleus; Reference proteome; Repeat;
KW RNA editing; RNA-binding; Transcription; Transcription regulation;
KW Tumor suppressor; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..449
FT /note="Wilms tumor protein"
FT /id="PRO_0000047131"
FT ZN_FING 323..347
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 353..377
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 383..405
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 414..438
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 48..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..381
FT /note="Important for interaction with target DNA"
FT REGION 393..401
FT /note="Important for interaction with target DNA"
FT MOTIF 236..244
FT /note="9aaTAD"
FT /evidence="ECO:0000269|PubMed:31375868"
FT MOTIF 408..410
FT /note="KTS motif"
FT COMPBIAS 53..72
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 424
FT /note="Important for interaction with target DNA"
FT SITE 430
FT /note="Important for interaction with target DNA"
FT CROSSLNK 73
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:15520190"
FT CROSSLNK 177
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:15520190"
FT CROSSLNK 444
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..144
FT /note="Missing (in isoform 6 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_037582"
FT VAR_SEQ 1
FT /note="M -> MDFLLLQDPASTCVPEPASQHTLRSGPGCLQQPEQQGVRDPGGIWAK
FT LGAAEASAERLQGRRSRGASGSEPQQM (in isoform 7 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:2154702"
FT /id="VSP_037583"
FT VAR_SEQ 145..147
FT /note="RNQ -> MEK (in isoform 6 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_037584"
FT VAR_SEQ 250..266
FT /note="Missing (in isoform 2, isoform 3, isoform 8 and
FT isoform 9)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:2154335"
FT /id="VSP_006866"
FT VAR_SEQ 408..410
FT /note="Missing (in isoform 2, isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:2154335"
FT /id="VSP_006867"
FT VARIANT 131
FT /note="A -> T (in a patient with hypospadias)"
FT /evidence="ECO:0000269|PubMed:15266301"
FT /id="VAR_043798"
FT VARIANT 181
FT /note="P -> S (in WT1; dbSNP:rs2234584)"
FT /evidence="ECO:0000269|PubMed:15150775,
FT ECO:0000269|PubMed:9108089"
FT /id="VAR_007739"
FT VARIANT 223
FT /note="S -> N (in WT1)"
FT /evidence="ECO:0000269|PubMed:9529364"
FT /id="VAR_007740"
FT VARIANT 253
FT /note="G -> A (in WT1)"
FT /evidence="ECO:0000269|PubMed:9108089"
FT /id="VAR_007741"
FT VARIANT 273
FT /note="S -> G (found in a mesothelioma sample; somatic
FT mutation; dbSNP:rs121907908)"
FT /evidence="ECO:0000269|PubMed:8401592"
FT /id="VAR_007742"
FT VARIANT 281
FT /note="L -> P (in RNA edited version)"
FT /id="VAR_058021"
FT VARIANT 312
FT /note="R -> Q (in NPHS4)"
FT /evidence="ECO:0000269|PubMed:11182928"
FT /id="VAR_015053"
FT VARIANT 330
FT /note="C -> Y (in DDS)"
FT /evidence="ECO:0000269|PubMed:1302008"
FT /id="VAR_007743"
FT VARIANT 342
FT /note="M -> R (in DDS)"
FT /evidence="ECO:0000269|PubMed:11182928"
FT /id="VAR_015054"
FT VARIANT 355
FT /note="C -> G (in WT1)"
FT /evidence="ECO:0000269|PubMed:15150775"
FT /id="VAR_043799"
FT VARIANT 355
FT /note="C -> Y (in DDS)"
FT /evidence="ECO:0000269|PubMed:11182928,
FT ECO:0000269|PubMed:9475094"
FT /id="VAR_015055"
FT VARIANT 360
FT /note="C -> G (in DDS)"
FT /id="VAR_007744"
FT VARIANT 360
FT /note="C -> Y (in DDS)"
FT /evidence="ECO:0000269|PubMed:8411073"
FT /id="VAR_043800"
FT VARIANT 364
FT /note="F -> L (in NPHS4)"
FT /evidence="ECO:0000269|PubMed:9607189"
FT /id="VAR_043801"
FT VARIANT 366
FT /note="R -> C (in WT1, DDS and MEACHS)"
FT /evidence="ECO:0000269|PubMed:1317572,
FT ECO:0000269|PubMed:15150775, ECO:0000269|PubMed:17853480,
FT ECO:0000269|PubMed:9529364"
FT /id="VAR_007745"
FT VARIANT 366
FT /note="R -> H (in DDS and WT1)"
FT /evidence="ECO:0000269|PubMed:11182928,
FT ECO:0000269|PubMed:15150775, ECO:0000269|PubMed:9475094,
FT ECO:0000269|PubMed:9607189"
FT /id="VAR_007746"
FT VARIANT 366
FT /note="R -> L (in DDS)"
FT /evidence="ECO:0000269|PubMed:8741319"
FT /id="VAR_043802"
FT VARIANT 369
FT /note="Q -> P (in DDS)"
FT /evidence="ECO:0000269|PubMed:10799199"
FT /id="VAR_043803"
FT VARIANT 373
FT /note="H -> Q (in DDS and WT1)"
FT /evidence="ECO:0000269|PubMed:15150775"
FT /id="VAR_007747"
FT VARIANT 373
FT /note="H -> Y (in DDS)"
FT /evidence="ECO:0000269|PubMed:8956030"
FT /id="VAR_015056"
FT VARIANT 377
FT /note="H -> R (in DDS)"
FT /evidence="ECO:0000269|PubMed:8112732"
FT /id="VAR_015057"
FT VARIANT 377
FT /note="H -> Y (in NPHS4)"
FT /evidence="ECO:0000269|PubMed:9529364"
FT /id="VAR_007748"
FT VARIANT 379
FT /note="G -> C (in NPHS4)"
FT /evidence="ECO:0000269|PubMed:9607189"
FT /id="VAR_043804"
FT VARIANT 383
FT /note="F -> L (in NPHS4)"
FT /evidence="ECO:0000269|PubMed:9529364"
FT /id="VAR_007749"
FT VARIANT 385
FT /note="C -> R (in DDS)"
FT /evidence="ECO:0000269|PubMed:11182928,
FT ECO:0000269|PubMed:9475094, ECO:0000269|PubMed:9607189"
FT /id="VAR_015058"
FT VARIANT 388
FT /note="C -> F (in DDS)"
FT /evidence="ECO:0000269|PubMed:11182928"
FT /id="VAR_015059"
FT VARIANT 388
FT /note="C -> R (in NPHS4)"
FT /evidence="ECO:0000269|PubMed:15253707,
FT ECO:0000269|PubMed:20798252"
FT /id="VAR_043805"
FT VARIANT 388
FT /note="C -> Y (in DDS)"
FT /evidence="ECO:0000269|PubMed:11519891"
FT /id="VAR_043806"
FT VARIANT 392
FT /note="F -> L (in FS)"
FT /evidence="ECO:0000269|PubMed:10571943"
FT /id="VAR_015060"
FT VARIANT 394
FT /note="R -> L (in WT1)"
FT /evidence="ECO:0000269|PubMed:15150775"
FT /id="VAR_043807"
FT VARIANT 394
FT /note="R -> P (in DDS)"
FT /evidence="ECO:0000269|PubMed:1302008"
FT /id="VAR_043808"
FT VARIANT 394
FT /note="R -> Q (in DDS and NPHS4)"
FT /evidence="ECO:0000269|PubMed:20798252,
FT ECO:0000269|PubMed:9529364, ECO:0000269|PubMed:9607189"
FT /id="VAR_015061"
FT VARIANT 394
FT /note="R -> W (in DDS, WT1, MEACHS and NPHS4)"
FT /evidence="ECO:0000269|PubMed:11182928,
FT ECO:0000269|PubMed:1302008, ECO:0000269|PubMed:15150775,
FT ECO:0000269|PubMed:17853480, ECO:0000269|PubMed:20798252,
FT ECO:0000269|PubMed:8295405, ECO:0000269|PubMed:8411073,
FT ECO:0000269|PubMed:9529364, ECO:0000269|PubMed:9607189"
FT /id="VAR_007750"
FT VARIANT 396
FT /note="D -> G (in DDS)"
FT /id="VAR_007752"
FT VARIANT 396
FT /note="D -> N (in DDS and NPHS4)"
FT /evidence="ECO:0000269|PubMed:11182928,
FT ECO:0000269|PubMed:9529364, ECO:0000269|PubMed:9607189"
FT /id="VAR_007751"
FT VARIANT 396
FT /note="D -> Y (in DDS)"
FT /evidence="ECO:0000269|PubMed:10738002"
FT /id="VAR_043809"
FT VARIANT 397
FT /note="H -> P (in NPHS4)"
FT /evidence="ECO:0000269|PubMed:15253707,
FT ECO:0000269|PubMed:20798252"
FT /id="VAR_043810"
FT VARIANT 398
FT /note="L -> P (in DDS)"
FT /evidence="ECO:0000269|PubMed:8295405,
FT ECO:0000269|PubMed:9529364"
FT /id="VAR_015062"
FT VARIANT 401
FT /note="H -> Y (in DDS)"
FT /evidence="ECO:0000269|PubMed:8111391"
FT /id="VAR_043811"
FT VARIANT 405
FT /note="H -> R (in DDS)"
FT /evidence="ECO:0000269|PubMed:15349765"
FT /id="VAR_043812"
FT MUTAGEN 73
FT /note="K->R: Abolishes sumoylation; when associated with R-
FT 177."
FT /evidence="ECO:0000269|PubMed:15520190"
FT MUTAGEN 177
FT /note="K->R: Abolishes sumoylation; when associated with R-
FT 77."
FT /evidence="ECO:0000269|PubMed:15520190"
FT MUTAGEN 343
FT /note="H->A: Reduced RNA binding."
FT /evidence="ECO:0000269|PubMed:19123921"
FT MUTAGEN 366
FT /note="R->A: Strongly reduced binding of DNA and RNA."
FT /evidence="ECO:0000269|PubMed:19123921"
FT MUTAGEN 372
FT /note="R->A: Strongly reduced binding of DNA and RNA."
FT /evidence="ECO:0000269|PubMed:19123921"
FT MUTAGEN 394
FT /note="R->A,S: Strongly reduced binding of DNA and RNA."
FT /evidence="ECO:0000269|PubMed:19123921"
FT MUTAGEN 434
FT /note="H->A: Reduced RNA binding."
FT /evidence="ECO:0000269|PubMed:19123921"
FT CONFLICT 288
FT /note="I -> M (in Ref. 8; AAH32861)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="S -> F (in Ref. 9; AAA36810 and 10; AAB33443)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="T -> A (in Ref. 3; CAA43819)"
FT /evidence="ECO:0000305"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:6B0Q"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:6B0R"
FT STRAND 333..336
FT /evidence="ECO:0007829|PDB:6B0O"
FT HELIX 337..348
FT /evidence="ECO:0007829|PDB:6B0O"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:6WLH"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:6B0R"
FT STRAND 363..366
FT /evidence="ECO:0007829|PDB:5KL3"
FT HELIX 367..378
FT /evidence="ECO:0007829|PDB:5KL3"
FT TURN 386..388
FT /evidence="ECO:0007829|PDB:5KL3"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:5KL3"
FT HELIX 395..401
FT /evidence="ECO:0007829|PDB:5KL3"
FT HELIX 403..406
FT /evidence="ECO:0007829|PDB:5KL3"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:6BLW"
FT STRAND 424..427
FT /evidence="ECO:0007829|PDB:5KL3"
FT HELIX 428..438
FT /evidence="ECO:0007829|PDB:5KL3"
SQ 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
