P19544 (WT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Wilms tumor protein

Alternative name(s):
WT33

Gene names

Name:

WT1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	449 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transcription factor that plays an important role in cellular development and cell survival. Regulates the expression of numerous target genes, including EPO. Plays an essential role for development of the urogenital system. Recognizes and binds to the DNA sequence 5'-CGCCCCCGC-3'. 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. Isoforms containing the KTS motif may bind mRNA and play a role in mRNA metabolism or splicing. Isoform 1 has lower affinity for DNA, and can bind RNA. Ref.25 Ref.26
Subunit structure	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. Ref.16 Ref.17 Ref.18 Ref.24 Ref.26
Subcellular location	Nucleus. Nucleus › nucleolus. Cytoplasm By similarity. Note: Shuttles between nucleus and cytoplasm By similarity. Ref.23 Ref.24 Isoform 1: Nucleus speckle Ref.23 Ref.24. Isoform 4: Nucleus › nucleoplasm Ref.23 Ref.24.
Tissue specificity	Expressed in the kidney and a subset of hematopoietic cells.
Involvement in 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.43 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.29 Ref.39 Ref.40 Ref.48 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11 Ref.12 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.36 Ref.37 Ref.38 Ref.40 Ref.41 Ref.44 Ref.45 Ref.46 Ref.47 Ref.51 Nephrotic syndrome 4 (NPHS4) [MIM:256370]: A renal disease characterized clinically by proteinuria, 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.40 Ref.42 Ref.45 Ref.50 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.52 A chromosomal aberration involving WT1 may be a cause of desmoplastic small round cell tumor (DSRCT). Translocation t(11;22)(p13;q12) with EWSR1. 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. Note: The disease may be caused by mutations affecting the gene represented in this entry. Ref.35
Miscellaneous	Presence of the KTS motif hinders interactions between DNA and zinc-finger 4.
Sequence similarities	Belongs to the EGR C2H2-type zinc-finger protein family. Contains 4 C2H2-type zinc fingers.
RNA editing	Edited at position 281. Partially edited. Ref.14
Sequence caution	The sequence AAB33443.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part. The sequence CAA35956.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence CAA35956.1 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon. The sequence CAC39220.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence CAI95758.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence CAI95759.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative initiation Alternative splicing Chromosomal rearrangement RNA editing
Disease	Disease mutation Tumor suppressor
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding RNA-binding Zinc
PTM	Isopeptide bond Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA splicing Inferred from sequence or structural similarity. Source: UniProtKB adrenal cortex formation Inferred from sequence or structural similarity. Source: UniProtKB branching involved in ureteric bud morphogenesis Inferred from genetic interaction PubMed 10101119. Source: UniProtKB camera-type eye development Inferred from sequence or structural similarity. Source: UniProtKB cardiac muscle cell fate commitment Inferred from sequence or structural similarity. Source: BHF-UCL cellular response to cAMP Inferred from expression pattern PubMed 15961562. Source: UniProtKB cellular response to gonadotropin stimulus Inferred from direct assay PubMed 15961562. Source: UniProtKB diaphragm development Inferred from sequence or structural similarity. Source: UniProtKB germ cell development Inferred from sequence or structural similarity. Source: UniProtKB glomerular basement membrane development Inferred from mutant phenotype PubMed 19205749. Source: UniProtKB glomerular visceral epithelial cell differentiation Inferred from sequence or structural similarity. Source: UniProtKB induction of apoptosis Inferred from direct assay PubMed 7588596. Source: UniProtKB male genitalia development Inferred from sequence or structural similarity. Source: UniProtKB male gonad development Inferred from expression pattern PubMed 17848411. Source: UniProtKB mesenchymal to epithelial transition Inferred from sequence or structural similarity. Source: UniProtKB metanephric S-shaped body morphogenesis Inferred from genetic interaction PubMed 10101119. Source: UniProtKB metanephric epithelium development Inferred from expression pattern PubMed 7856737. Source: UniProtKB metanephric mesenchyme development Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of apoptotic process Inferred from genetic interaction PubMed 10101119. Source: UniProtKB negative regulation of cell growth Inferred from direct assay PubMed 9553041PubMed 9765217PubMed 7588596. Source: UniProtKB negative regulation of female gonad development Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of metanephric glomerular mesangial cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 7585606. Source: MGI negative regulation of transcription, DNA-dependent Inferred from direct assay PubMed 9815658PubMed 9815658PubMed 7588596PubMed 9815658PubMed 9815658. Source: UniProtKB negative regulation of translation Inferred from direct assay PubMed 7588596. Source: UniProtKB positive regulation of heart growth Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of male gonad development Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of metanephric ureteric bud development Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of transcription, DNA-dependent Inferred from direct assay PubMed 9815658PubMed 7588596PubMed 9815658. Source: UniProtKB posterior mesonephric tubule development Inferred from sequence or structural similarity. Source: UniProtKB regulation of organ formation Inferred from sequence or structural similarity. Source: UniProtKB sex determination Inferred from direct assay PubMed 9815658. Source: UniProtKB thorax and anterior abdomen determination Inferred from sequence or structural similarity. Source: UniProtKB vasculogenesis Inferred from sequence or structural similarity. Source: UniProtKB visceral serous pericardium development Inferred from genetic interaction PubMed 10101119. Source: UniProtKB
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB nuclear speck Inferred from direct assay Ref.24PubMed 9553041Ref.23. Source: UniProtKB nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Inferred from direct assay Ref.23. Source: UniProtKB
Molecular_function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Inferred from sequence or structural similarity. Source: UniProtKB sequence-specific DNA binding Inferred from direct assay PubMed 1662794PubMed 7720589PubMed 8119964. Source: UniProtKB transcription regulatory region DNA binding Inferred from direct assay PubMed 1332065PubMed 16467207PubMed 7585606PubMed 7588596PubMed 9815658. Source: UniProtKB zinc ion binding Inferred from direct assay Ref.27. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 8 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]

Isoform 1 (identifier: P19544-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: Detected in nucleus speckle, may bind mRNA.

Isoform 2 (identifier: P19544-2)

The sequence of this isoform differs from the canonical sequence as follows:
     250-266: Missing.
     408-410: Missing.

Isoform 3 (identifier: P19544-3)

The sequence of this isoform differs from the canonical sequence as follows:
     250-266: Missing.

Isoform 4 (identifier: P19544-4)

The sequence of this isoform differs from the canonical sequence as follows:
     408-410: Missing.

Isoform 6 (identifier: P19544-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-144: Missing.
     145-147: RNQ → MEK
     408-410: Missing.

Isoform 7 (identifier: P19544-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MDFLLLQDPASTCVPEPASQHTLRSGPGCLQQPEQQGVRDPGGIWAKLGAAEASAERLQGRRSRGASGSEPQQM

Note: Produced by alternative initiation of isoform 1. Extended N-terminus.

Isoform 8 (identifier: P19544-8)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MDFLLLQDPASTCVPEPASQHTLRSGPGCLQQPEQQGVRDPGGIWAKLGAAEASAERLQGRRSRGASGSEPQQM
     250-266: Missing.

Note: Produced by alternative initiation of isoform 1. Extended N-terminus.

Isoform 9 (identifier: P19544-9)

The sequence of this isoform differs from the canonical sequence as follows:
     1-144: Missing.
     145-147: RNQ → MEK
     250-266: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 449

449

Wilms tumor protein

PRO_0000047131

Regions

Zinc finger

323 – 347

25

C2H2-type 1

Zinc finger

353 – 377

25

C2H2-type 2

Zinc finger

383 – 405

23

C2H2-type 3

Zinc finger

414 – 438

25

C2H2-type 4

Region

367 – 381

15

Important for interaction with target DNA

Region

393 – 401

9

Important for interaction with target DNA

Motif

408 – 410

3

KTS motif

Compositional bias

27 – 83

57

Pro-rich

Sites

Site

424

1

Important for interaction with target DNA

Site

430

1

Important for interaction with target DNA

Amino acid modifications

Cross-link

73

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.23

Cross-link

177

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.23

Natural variations

Alternative sequence

1 – 144

144

Missing in isoform 6 and isoform 9.

VSP_037582

Alternative sequence

1

1

M → MDFLLLQDPASTCVPEPASQ HTLRSGPGCLQQPEQQGVRD PGGIWAKLGAAEASAERLQG RRSRGASGSEPQQM in isoform 7 and isoform 8.

VSP_037583

Alternative sequence

145 – 147

3

RNQ → MEK in isoform 6 and isoform 9.

VSP_037584

Alternative sequence

250 – 266

17

Missing in isoform 2, isoform 3, isoform 8 and isoform 9.

VSP_006866

Alternative sequence

408 – 410

3

Missing in isoform 2, isoform 4 and isoform 6.

VSP_006867

Natural variant

131

1

A → T in a patient with hypospadias. Ref.49

VAR_043798

Natural variant

181

1

P → S in WT1. Ref.39 Ref.48
Corresponds to variant rs2234584 [ dbSNP | Ensembl ].

VAR_007739

Natural variant

223

1

S → N in WT1. Ref.40

VAR_007740

Natural variant

253

1

G → A in WT1. Ref.39

VAR_007741

Natural variant

273

1

S → G Found in a mesothelioma sample; somatic mutation. Ref.35
Corresponds to variant rs121907908 [ dbSNP | Ensembl ].

VAR_007742

Natural variant

281

1

L → P in RNA edited version.

VAR_058021

Natural variant

312

1

R → Q in NPHS4. Ref.45

VAR_015053

Natural variant

330

1

C → Y in DDS. Ref.12

VAR_007743

Natural variant

342

1

M → R in DDS. Ref.45

VAR_015054

Natural variant

355

1

C → G in WT1. Ref.48

VAR_043799

Natural variant

355

1

C → Y in DDS. Ref.41 Ref.45

VAR_015055

Natural variant

360

1

C → G in DDS.

VAR_007744

Natural variant

360

1

C → Y in DDS. Ref.34

VAR_043800

Natural variant

364

1

F → L in NPHS4. Ref.42

VAR_043801

Natural variant

366

1

R → C in WT1, DDS and MEACHS. Ref.29 Ref.40 Ref.48 Ref.52

VAR_007745

Natural variant

366

1

R → H in DDS and WT1. Ref.41 Ref.42 Ref.45 Ref.48

VAR_007746

Natural variant

366

1

R → L in DDS. Ref.37

VAR_043802

Natural variant

369

1

Q → P in DDS. Ref.46

VAR_043803

Natural variant

373

1

H → Q in DDS and WT1. Ref.48

VAR_007747

Natural variant

373

1

H → Y in DDS. Ref.38

VAR_015056

Natural variant

377

1

H → R in DDS. Ref.36

VAR_015057

Natural variant

377

1

H → Y in NPHS4. Ref.40

VAR_007748

Natural variant

379

1

G → C in NPHS4. Ref.42

VAR_043804

Natural variant

383

1

F → L in NPHS4. Ref.40

VAR_007749

Natural variant

385

1

C → R in DDS. Ref.41 Ref.42 Ref.45

VAR_015058

Natural variant

388

1

C → F in DDS. Ref.45

VAR_015059

Natural variant

388

1

C → R in NPHS4. Ref.50

VAR_043805

Natural variant

388

1

C → Y in DDS. Ref.47

VAR_043806

Natural variant

392

1

F → L in FS. Ref.43

VAR_015060

Natural variant

394

1

R → L in WT1. Ref.48

VAR_043807

Natural variant

394

1

R → P in DDS. Ref.12

VAR_043808

Natural variant

394

1

R → Q in DDS. Ref.40 Ref.42

VAR_015061

Natural variant

394

1

R → W in DDS, WT1 and MEACHS. Ref.12 Ref.33 Ref.34 Ref.40 Ref.42 Ref.45 Ref.48 Ref.52

VAR_007750

Natural variant

396

1

D → G in DDS.

VAR_007752

Natural variant

396

1

D → N in DDS and NPHS4. Ref.40 Ref.42 Ref.45

VAR_007751

Natural variant

396

1

D → Y in DDS. Ref.44

VAR_043809

Natural variant

397

1

H → P in NPHS4. Ref.50

VAR_043810

Natural variant

398

1

L → P in DDS. Ref.33 Ref.40

VAR_015062

Natural variant

401

1

H → Y in DDS. Ref.32

VAR_043811

Natural variant

405

1

H → R in DDS. Ref.51

VAR_043812

Experimental info

Mutagenesis

73

1

K → R: Abolishes sumoylation; when associated with R-177. Ref.23

Mutagenesis

177

1

K → R: Abolishes sumoylation; when associated with R-77. Ref.23

Mutagenesis

343

1

H → A: Reduced RNA binding. Ref.25

Mutagenesis

366

1

R → A: Strongly reduced binding of DNA and RNA. Ref.25

Mutagenesis

372

1

R → A: Strongly reduced binding of DNA and RNA. Ref.25

Mutagenesis

394

1

R → A or S: Strongly reduced binding of DNA and RNA. Ref.25

Mutagenesis

434

1

H → A: Reduced RNA binding. Ref.25

Sequence conflict

288

1

I → M in AAH32861. Ref.8

Sequence conflict

365

1

S → F in AAA36810. Ref.9

Sequence conflict

365

1

S → F in AAB33443. Ref.10

Sequence conflict

387

1

T → A in CAA43819. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

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.

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.

.

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449

Helix Strand Turn

Details...

Beta strand

322 – 324

3

Turn

328 – 330

3

Beta strand

333 – 337

5

Helix

338 – 344

7

Helix

345 – 349

5

Beta strand

363 – 366

4

Helix

367 – 378

12

Turn

386 – 388

3

Beta strand

391 – 393

3

Helix

395 – 406

12

Beta strand

418 – 420

3

Beta strand

424 – 427

4

Helix

428 – 435

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 1, 1991. Version 2. Checksum: 11C7FA3D485096B2	FASTA	449	49,188
	10 20 30 40 50 60 MGSDVRDLNA LLPAVPSLGG GGGCALPVSG AAQWAPVLDF APPGASAYGS LGGPAPPPAP 70 80 90 100 110 120 PPPPPPPPHS FIKQEPSWGG AEPHEEQCLS AFTVHFSGQF TGTAGACRYG PFGPPPPSQA 130 140 150 160 170 180 SSGQARMFPN APYLPSCLES QPAIRNQGYS TVTFDGTPSY GHTPSHHAAQ FPNHSFKHED 190 200 210 220 230 240 PMGQQGSLGE QQYSVPPPVY GCHTPTDSCT GSQALLLRTP YSSDNLYQMT SQLECMTWNQ 250 260 270 280 290 300 MNLGATLKGV AAGSSSSVKW TEGQSNHSTG YESDNHTTPI LCGAQYRIHT HGVFRGIQDV 310 320 330 340 350 360 RRVPGVAPTL VRSASETSEK RPFMCAYPGC NKRYFKLSHL QMHSRKHTGE KPYQCDFKDC 370 380 390 400 410 420 ERRFSRSDQL KRHQRRHTGV KPFQCKTCQR KFSRSDHLKT HTRTHTGKTS EKPFSCRWPS 430 440 CQKKFARSDE LVRHHNMHQR NMTKLQLAL
	Isoform 2 [UniParc]. Checksum: C2F9912E0A4DA3DB	FASTA	429	47,195
	10 20 30 40 50 60 MGSDVRDLNA LLPAVPSLGG GGGCALPVSG AAQWAPVLDF APPGASAYGS LGGPAPPPAP 70 80 90 100 110 120 PPPPPPPPHS FIKQEPSWGG AEPHEEQCLS AFTVHFSGQF TGTAGACRYG PFGPPPPSQA 130 140 150 160 170 180 SSGQARMFPN APYLPSCLES QPAIRNQGYS TVTFDGTPSY GHTPSHHAAQ FPNHSFKHED 190 200 210 220 230 240 PMGQQGSLGE QQYSVPPPVY GCHTPTDSCT GSQALLLRTP YSSDNLYQMT SQLECMTWNQ 250 260 270 280 290 300 MNLGATLKGH STGYESDNHT TPILCGAQYR IHTHGVFRGI QDVRRVPGVA PTLVRSASET 310 320 330 340 350 360 SEKRPFMCAY PGCNKRYFKL SHLQMHSRKH TGEKPYQCDF KDCERRFSRS DQLKRHQRRH 370 380 390 400 410 420 TGVKPFQCKT CQRKFSRSDH LKTHTRTHTG EKPFSCRWPS CQKKFARSDE LVRHHNMHQR NMTKLQLAL
	Isoform 3 [UniParc]. Checksum: 1ACA6CE3563DA9D2	FASTA	432	47,511
	10 20 30 40 50 60 MGSDVRDLNA LLPAVPSLGG GGGCALPVSG AAQWAPVLDF APPGASAYGS LGGPAPPPAP 70 80 90 100 110 120 PPPPPPPPHS FIKQEPSWGG AEPHEEQCLS AFTVHFSGQF TGTAGACRYG PFGPPPPSQA 130 140 150 160 170 180 SSGQARMFPN APYLPSCLES QPAIRNQGYS TVTFDGTPSY GHTPSHHAAQ FPNHSFKHED 190 200 210 220 230 240 PMGQQGSLGE QQYSVPPPVY GCHTPTDSCT GSQALLLRTP YSSDNLYQMT SQLECMTWNQ 250 260 270 280 290 300 MNLGATLKGH STGYESDNHT TPILCGAQYR IHTHGVFRGI QDVRRVPGVA PTLVRSASET 310 320 330 340 350 360 SEKRPFMCAY PGCNKRYFKL SHLQMHSRKH TGEKPYQCDF KDCERRFSRS DQLKRHQRRH 370 380 390 400 410 420 TGVKPFQCKT CQRKFSRSDH LKTHTRTHTG KTSEKPFSCR WPSCQKKFAR SDELVRHHNM 430 HQRNMTKLQL AL
	Isoform 4 [UniParc]. Checksum: 8CE7FC116A41DA04	FASTA	446	48,872
	10 20 30 40 50 60 MGSDVRDLNA LLPAVPSLGG GGGCALPVSG AAQWAPVLDF APPGASAYGS LGGPAPPPAP 70 80 90 100 110 120 PPPPPPPPHS FIKQEPSWGG AEPHEEQCLS AFTVHFSGQF TGTAGACRYG PFGPPPPSQA 130 140 150 160 170 180 SSGQARMFPN APYLPSCLES QPAIRNQGYS TVTFDGTPSY GHTPSHHAAQ FPNHSFKHED 190 200 210 220 230 240 PMGQQGSLGE QQYSVPPPVY GCHTPTDSCT GSQALLLRTP YSSDNLYQMT SQLECMTWNQ 250 260 270 280 290 300 MNLGATLKGV AAGSSSSVKW TEGQSNHSTG YESDNHTTPI LCGAQYRIHT HGVFRGIQDV 310 320 330 340 350 360 RRVPGVAPTL VRSASETSEK RPFMCAYPGC NKRYFKLSHL QMHSRKHTGE KPYQCDFKDC 370 380 390 400 410 420 ERRFSRSDQL KRHQRRHTGV KPFQCKTCQR KFSRSDHLKT HTRTHTGEKP FSCRWPSCQK 430 440 KFARSDELVR HHNMHQRNMT KLQLAL
	Isoform 6 [UniParc]. Checksum: 715B121077C0991D	FASTA	302	34,447
	10 20 30 40 50 60 MEKGYSTVTF DGTPSYGHTP SHHAAQFPNH SFKHEDPMGQ QGSLGEQQYS VPPPVYGCHT 70 80 90 100 110 120 PTDSCTGSQA LLLRTPYSSD NLYQMTSQLE CMTWNQMNLG ATLKGVAAGS SSSVKWTEGQ 130 140 150 160 170 180 SNHSTGYESD NHTTPILCGA QYRIHTHGVF RGIQDVRRVP GVAPTLVRSA SETSEKRPFM 190 200 210 220 230 240 CAYPGCNKRY FKLSHLQMHS RKHTGEKPYQ CDFKDCERRF SRSDQLKRHQ RRHTGVKPFQ 250 260 270 280 290 300 CKTCQRKFSR SDHLKTHTRT HTGEKPFSCR WPSCQKKFAR SDELVRHHNM HQRNMTKLQL AL
	Isoform 7 [UniParc]. Checksum: FB30F6E34A60EC04	FASTA	522	56,883
	10 20 30 40 50 60 MDFLLLQDPA STCVPEPASQ HTLRSGPGCL QQPEQQGVRD PGGIWAKLGA AEASAERLQG 70 80 90 100 110 120 RRSRGASGSE PQQMGSDVRD LNALLPAVPS LGGGGGCALP VSGAAQWAPV LDFAPPGASA 130 140 150 160 170 180 YGSLGGPAPP PAPPPPPPPP PHSFIKQEPS WGGAEPHEEQ CLSAFTVHFS GQFTGTAGAC 190 200 210 220 230 240 RYGPFGPPPP SQASSGQARM FPNAPYLPSC LESQPAIRNQ GYSTVTFDGT PSYGHTPSHH 250 260 270 280 290 300 AAQFPNHSFK HEDPMGQQGS LGEQQYSVPP PVYGCHTPTD SCTGSQALLL RTPYSSDNLY 310 320 330 340 350 360 QMTSQLECMT WNQMNLGATL KGVAAGSSSS VKWTEGQSNH STGYESDNHT TPILCGAQYR 370 380 390 400 410 420 IHTHGVFRGI QDVRRVPGVA PTLVRSASET SEKRPFMCAY PGCNKRYFKL SHLQMHSRKH 430 440 450 460 470 480 TGEKPYQCDF KDCERRFSRS DQLKRHQRRH TGVKPFQCKT CQRKFSRSDH LKTHTRTHTG 490 500 510 520 KTSEKPFSCR WPSCQKKFAR SDELVRHHNM HQRNMTKLQL AL
	Isoform 8 [UniParc]. Checksum: C7CE98CE8B83C250	FASTA	505	55,206
	10 20 30 40 50 60 MDFLLLQDPA STCVPEPASQ HTLRSGPGCL QQPEQQGVRD PGGIWAKLGA AEASAERLQG 70 80 90 100 110 120 RRSRGASGSE PQQMGSDVRD LNALLPAVPS LGGGGGCALP VSGAAQWAPV LDFAPPGASA 130 140 150 160 170 180 YGSLGGPAPP PAPPPPPPPP PHSFIKQEPS WGGAEPHEEQ CLSAFTVHFS GQFTGTAGAC 190 200 210 220 230 240 RYGPFGPPPP SQASSGQARM FPNAPYLPSC LESQPAIRNQ GYSTVTFDGT PSYGHTPSHH 250 260 270 280 290 300 AAQFPNHSFK HEDPMGQQGS LGEQQYSVPP PVYGCHTPTD SCTGSQALLL RTPYSSDNLY 310 320 330 340 350 360 QMTSQLECMT WNQMNLGATL KGHSTGYESD NHTTPILCGA QYRIHTHGVF RGIQDVRRVP 370 380 390 400 410 420 GVAPTLVRSA SETSEKRPFM CAYPGCNKRY FKLSHLQMHS RKHTGEKPYQ CDFKDCERRF 430 440 450 460 470 480 SRSDQLKRHQ RRHTGVKPFQ CKTCQRKFSR SDHLKTHTRT HTGKTSEKPF SCRWPSCQKK 490 500 FARSDELVRH HNMHQRNMTK LQLAL
	Isoform 9 [UniParc]. Checksum: 9526D02081619728	FASTA	288	33,086
	10 20 30 40 50 60 MEKGYSTVTF DGTPSYGHTP SHHAAQFPNH SFKHEDPMGQ QGSLGEQQYS VPPPVYGCHT 70 80 90 100 110 120 PTDSCTGSQA LLLRTPYSSD NLYQMTSQLE CMTWNQMNLG ATLKGHSTGY ESDNHTTPIL 130 140 150 160 170 180 CGAQYRIHTH GVFRGIQDVR RVPGVAPTLV RSASETSEKR PFMCAYPGCN KRYFKLSHLQ 190 200 210 220 230 240 MHSRKHTGEK PYQCDFKDCE RRFSRSDQLK RHQRRHTGVK PFQCKTCQRK FSRSDHLKTH 250 260 270 280 TRTHTGKTSE KPFSCRWPSC QKKFARSDEL VRHHNMHQRN MTKLQLAL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Homozygous deletion in Wilms tumours of a zinc-finger gene identified by chromosome jumping." Gessler M., Poustka A., Cavenee W., Neve R.L., Orkin S.H., Bruns G.A.P. Nature 343:774-778(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7). Tissue: Fetal kidney.
[2]	"Alternative splicing and genomic structure of the Wilms tumor gene WT1." Haber D.A., Sohn R.L., Buckler A.J., Pelletier J., Call K.M., Housman D.E. Proc. Natl. Acad. Sci. U.S.A. 88:9618-9622(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3 AND 4). Tissue: Placenta.
[3]	"The genomic organization and expression of the WT1 gene." Gessler M., Konig A., Bruns G.A.P. Genomics 12:807-813(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 4).
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 9). Tissue: Placenta and Testis.
[5]	NIEHS SNPs program Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1).
[6]	"Human chromosome 11 DNA sequence and analysis including novel gene identification." 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. Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6). Tissue: Testis.
[9]	"Isolation and characterization of a zinc finger polypeptide gene at the human chromosome 11 Wilms' tumor locus." 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. Cell 60:509-520(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 85-449 (ISOFORM 2).
[10]	"High affinity binding sites for the Wilms' tumour suppressor protein WT1." Hamilton T.B., Barilla K.C., Romaniuk P.J. Nucleic Acids Res. 23:277-284(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 301-449 (ISOFORMS 2/4/6). Tissue: Fetal kidney.
[11]	"Germline mutations in the Wilms' tumor suppressor gene are associated with abnormal urogenital development in Denys-Drash syndrome." 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. Cell 67:437-447(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 385-405, VARIANTS DDS.
[12]	"Germline intronic and exonic mutations in the Wilms' tumour gene (WT1) affecting urogenital development." Bruening W., Bardeesy N., Silverman B.L., Cohn R.A., Machin G.A., Aronson A.J., Housman D., Pelletier J. Nat. Genet. 1:144-148(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 385-405, VARIANTS DDS TYR-330; PRO-394 AND TRP-394.
[13]	"Isolation, characterization, and expression of the murine Wilms' tumor gene (WT1) during kidney development." Buckler A.J., Pelletier J., Haber D.A., Glaser T., Housman D.E. Mol. Cell. Biol. 11:1707-1712(1991) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION OF START CODON, ALTERNATIVE SPLICING.
[14]	"RNA editing in the Wilms' tumor susceptibility gene, WT1." Sharma P.M., Bowman M., Madden S.L., Rauscher F.J. III, Sukumar S. Genes Dev. 8:720-731(1994) [PubMed] [Europe PMC] [Abstract] Cited for: RNA EDITING OF POSITION 281.
[15]	"A non-AUG translational initiation event generates novel WT1 isoforms." Bruening W., Pelletier J. J. Biol. Chem. 271:8646-8654(1996) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE INITIATION, ALTERNATIVE SPLICING (ISOFORMS 7 AND 8).
[16]	"Identification of WTAP, a novel Wilms' tumour 1-associating protein." Little N.A., Hastie N.D., Davies R.C. Hum. Mol. Genet. 9:2231-2239(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH WTAP.
[17]	"Inhibition of Wilms tumor 1 transactivation by bone marrow zinc finger 2, a novel transcriptional repressor." Lee T.H., Lwu S., Kim J., Pelletier J. J. Biol. Chem. 277:44826-44837(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ZNF224.
[18]	"Transcriptional activity of testis-determining factor SRY is modulated by the Wilms' tumor 1 gene product, WT1." Matsuzawa-Watanabe Y., Inoue J., Semba K. Oncogene 22:7900-7904(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SRY.
[19]	"WT1: a novel tumor suppressor gene inactivated in Wilms' tumor." Haber D.A., Buckler A.J. New Biol. 4:97-106(1992) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[20]	"The WT1 Wilms tumor gene product: a developmentally regulated transcription factor in the kidney that functions as a tumor suppressor." Rauscher F.J. III FASEB J. 7:896-903(1993) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[21]	"WT1 mutations contribute to abnormal genital system development and hereditary Wilms' tumour." Pelletier J., Bruening W., Li F.P., Haber D.A., Glaser T., Housman D.E. Nature 353:431-434(1991) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN WILMS TUMOR.
[22]	"A tumor suppressor and oncogene: the WT1 story." Yang L., Han Y., Suarez Saiz F., Minden M.D. Leukemia 21:868-876(2007) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[23]	"SUMO-1 modification of the Wilms' tumor suppressor WT1." Smolen G.A., Vassileva M.T., Wells J., Matunis M.J., Haber D.A. Cancer Res. 64:7846-7851(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-73 AND LYS-177, SUMOYLATION AT LYS-73 AND LYS-177.
[24]	"WT1 interacts with the splicing protein RBM4 and regulates its ability to modulate alternative splicing in vivo." Markus M.A., Heinrich B., Raitskin O., Adams D.J., Mangs H., Goy C., Ladomery M., Sperling R., Stamm S., Morris B.J. Exp. Cell Res. 312:3379-3388(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RBM4, SUBCELLULAR LOCATION.
[25]	"Contribution of individual amino acids to the RNA binding activity of the Wilms' tumor suppressor protein WT1." Weiss T.C., Romaniuk P.J. Biochemistry 48:148-155(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF HIS-343; ARG-366; ARG-372; ARG-394 AND HIS-434.
[26]	"The tumor suppressor WTX shuttles to the nucleus and modulates WT1 activity." Rivera M.N., Kim W.J., Wells J., Stone A., Burger A., Coffman E.J., Zhang J., Haber D.A. Proc. Natl. Acad. Sci. U.S.A. 106:8338-8343(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH AMER1, FUNCTION.
[27]	"Why zinc fingers prefer zinc: ligand-field symmetry and the hidden thermodynamics of metal ion selectivity." Lachenmann M.J., Ladbury J.E., Dong J., Huang K., Carey P., Weiss M.A. Biochemistry 43:13910-13925(2004) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 381-407 IN COMPLEX WITH ZINC IONS.
[28]	"Structure of the Wilms tumor suppressor protein zinc finger domain bound to DNA." Stoll R., Lee B.M., Debler E.W., Laity J.H., Wilson I.A., Dyson H.J., Wright P.E. J. Mol. Biol. 372:1227-1245(2007) [PubMed] [Europe PMC] [Abstract] Cited for: 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.
[29]	"Zinc finger point mutations within the WT1 gene in Wilms tumor patients." Little M.H., Prosser J., Condie A., Smith P.J., van Heyningen V., Hastie N.D. Proc. Natl. Acad. Sci. U.S.A. 89:4791-4795(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT WT1 CYS-366.
[30]	"Constitutional mutations in the WT1 gene in patients with Denys-Drash syndrome." Baird P.N., Santos A., Groves N., Jadresic L., Cowell J.K. Hum. Mol. Genet. 1:301-305(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS DDS.
[31]	"Evidence that WT1 mutations in Denys-Drash syndrome patients may act in a dominant-negative fashion." Little M.H., Williamson K.A., Mannens M., Kelsey A., Gosden C., Hastie N.D., van Heyningen V. Hum. Mol. Genet. 2:259-264(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS DDS.
[32]	"A novel zinc finger mutation in a patient with Denys-Drash syndrome." Baird P.N., Cowell J.K. Hum. Mol. Genet. 2:2193-2194(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT DDS TYR-401.
[33]	"Molecular analysis of two Japanese cases of Denys-Drash syndrome." Tsuda M., Sakiyama T., Kitagawa T., Watanabe S., Watanabe T., Takahashi S., Kawaguchi H., Ito K. J. Inherit. Metab. Dis. 16:876-880(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS DDS TRP-394 AND PRO-398.
[34]	"Mutational screening of the Wilms's tumour gene, WT1, in males with genital abnormalities." Clarkson P.A., Davies H.R., Williams D.M., Chaudhary R., Hughes I.A., Patterson M.N. J. Med. Genet. 30:767-772(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS DDS TYR-360 AND TRP-394.
[35]	"The Wilms tumour gene WT1 is expressed in murine mesoderm-derived tissues and mutated in a human mesothelioma." 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. Nat. Genet. 4:415-420(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GLY-273, INVOLVEMENT IN MESOM.
[36]	"WT1 mutations in patients with Denys-Drash syndrome: a novel mutation in exon 8 and paternal allele origin." Nordenskjold A., Friedman E., Anvret M. Hum. Genet. 93:115-120(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT DDS ARG-377.
[37]	"A newly identified exonic mutation of the WT1 gene in a patient with Denys-Drash syndrome." Tsuda M., Sakiyama T., Owada M., Chiba Y. Acta Paediatr. Jpn. Overseas Ed. 38:265-266(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT DDS LEU-366.
[38]	"A novel mutation H373Y in the Wilms' tumor suppressor gene, WT1, associated with Denys-Drash syndrome." Ghahremani M., Chan C.B., Bistritzer T., Aladjem M.M., Tieder M., Pelletier J. Hum. Hered. 46:336-338(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT DDS TYR-373.
[39]	"Correlation of germ-line mutations and two-hit inactivation of the WT1 gene with Wilms tumors of stromal-predominant histology." Schumacher V., Schneider S., Figge A., Wildhardt G., Harms D., Schmidt D., Weirich A., Ludwig R., Royer-Pokora B. Proc. Natl. Acad. Sci. U.S.A. 94:3972-3977(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS WT1 SER-181 AND ALA-253.
[40]	"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." 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. Am. J. Hum. Genet. 62:824-833(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS NPHS4 TYR-377; LEU-383 AND ASN-396, VARIANTS DDS CYS-366; GLN-394; TRP-394 AND PRO-398, VARIANT WT1 ASN-223.
[41]	"Do intronic mutations affecting splicing of WT1 exon 9 cause Frasier syndrome?" Kikuchi H., Takata A., Akasaka Y., Fukuzawa R., Yoneyama H., Kurosawa Y., Honda M., Kamiyama Y., Hata J. J. Med. Genet. 35:45-48(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS DDS TYR-355; HIS-366 AND ARG-385.
[42]	"Spectrum of early onset nephrotic syndrome associated with WT1 missense mutations." 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. Kidney Int. 53:1594-1600(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS NPHS4 LEU-364; HIS-366; CYS-379; ARG-385; GLN-394; TRP-394 AND ASN-396.
[43]	"Exon 9 mutations in the WT1 gene, without influencing KTS splice isoforms, are also responsible for Frasier syndrome." Kohsaka T., Tagawa M., Takekoshi Y., Yanagisawa H., Tadokoro K., Yamada M. Hum. Mutat. 14:466-470(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FS LEU-392.
[44]	"Novel WT1 exon 9 mutation (D396Y) in a patient with early onset Denys Drash syndrome." Little M., Carman G., Donaldson E. Hum. Mutat. 15:389-389(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT DDS TYR-396.
[45]	"Constitutional WT1 correlate with clinical features in children with progressive nephropathy." Takata A., Kikuchi H., Fukuzawa R., Ito S., Honda M., Hata J. J. Med. Genet. 37:698-701(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS DDS ARG-342; TYR-355; HIS-366; ARG-385; PHE-388; TRP-394 AND ASN-396, VARIANT NPHS4 GLN-312.
[46]	"A novel missense mutation of the WT1 gene causing Denys-Drash syndrome with exceptionally mild renal manifestations." Ohta S., Ozawa T., Izumino K., Sakuragawa N., Fuse H. J. Urol. 163:1857-1858(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT DDS PRO-369.
[47]	"Novel WT1 mutation (C388Y) in a female child with Denys-Drash syndrome." Swiatecka-Urban A., Mokrzycki M.H., Kaskel F., Da Silva F., Denamur E. Pediatr. Nephrol. 16:627-630(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT DDS TYR-388.
[48]	"Twenty-four new cases of WT1 germline mutations and review of the literature: genotype/phenotype correlations for Wilms tumor development." Royer-Pokora B., Beier M., Henzler M., Alam R., Schumacher V., Weirich A., Huff V. Am. J. Med. Genet. A 127:249-257(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS WT1 SER-181; GLY-355; CYS-366; HIS-366; GLN-373; TRP-394 AND LEU-394.
[49]	"Mutation analysis of five candidate genes in Chinese patients with hypospadias." Wang Y., Li Q., Xu J., Liu Q., Wang W., Lin Y., Ma F., Chen T., Li S., Shen Y. Eur. J. Hum. Genet. 12:706-712(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT THR-131.
[50]	"Prevalence of WT1 mutations in a large cohort of patients with steroid-resistant and steroid-sensitive nephrotic syndrome." 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. Kidney Int. 66:564-570(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS NPHS4 ARG-388 AND PRO-397.
[51]	"A novel mutation of WT1 exon 9 in a patient with Denys-Drash syndrome and pyloric stenosis." Hu M., Craig J., Howard N., Kan A., Chaitow J., Little D., Alexander S.I. Pediatr. Nephrol. 19:1160-1163(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT DDS ARG-405.
[52]	"WT1 mutations in Meacham syndrome suggest a coelomic mesothelial origin of the cardiac and diaphragmatic malformations." 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. Am. J. Med. Genet. A 143:2312-2320(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MEACHS CYS-366 AND TRP-394.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X51630 mRNA. Translation: CAA35956.1. Sequence problems.
M80232 , M80217, M80218, M80219, M80220, M80221, M80228, M80229, M80231 Genomic DNA. Translation: AAA61299.1.
X61631 , X61632, X61633, X61634, X61635, X61636, X61637, X61638 Genomic DNA. Translation: CAA43819.1.
AK093168 mRNA. Translation: BAG52667.1.
AK291736 mRNA. Translation: BAF84425.1.
AY245105 Genomic DNA. Translation: AAO61088.1.
AL049692 Genomic DNA. Translation: CAC39220.3. Different initiation.
AL049692 Genomic DNA. Translation: CAI95758.2. Different initiation.
AL049692 Genomic DNA. Translation: CAI95759.2. Different initiation.
AL049692 Genomic DNA. Translation: CAI95760.1.
CH471064 Genomic DNA. Translation: EAW68220.1.
CH471064 Genomic DNA. Translation: EAW68223.1.
CH471064 Genomic DNA. Translation: EAW68224.1.
BC032861 mRNA. Translation: AAH32861.1.
M30393 mRNA. Translation: AAA36810.1.
S75264 mRNA. Translation: AAB33443.1. Sequence problems.
S61515 Genomic DNA. Translation: AAB20110.1.
S61522 Genomic DNA. Translation: AAB20111.1.
S61524 Genomic DNA. Translation: AAB20112.1.
S60755 Genomic DNA. Translation: AAC60605.1.

IPI

IPI00019517.
IPI00374173.
IPI00550100.
IPI00853526.
IPI00935507.
IPI00935900.
IPI00936595.
IPI01009246.

PIR

A38080.

RefSeq

NP_000369.3. NM_000378.4.
NP_001185480.1. NM_001198551.1.
NP_001185481.1. NM_001198552.1.
NP_077742.2. NM_024424.3.
NP_077744.3. NM_024426.4.

UniGene

Hs.591980.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LU6	model	-	A	310-449	[»]
1XF7	NMR	-	A	381-407	[»]
2G7T	model	-	A	310-449	[»]
2G7V	model	-	A	310-449	[»]
2G7W	model	-	A	310-449	[»]
2G7X	model	-	A	310-449	[»]
2JP9	NMR	-	A	318-438	[»]
2JPA	NMR	-	A	318-438	[»]
2PRT	X-ray	3.15	A	318-438	[»]
3HPJ	X-ray	2.00	C/F	126-134	[»]
3MYJ	X-ray	1.89	C/F	127-134	[»]

ProteinModelPortal

P19544.

ModBase

Search...

Protein-protein interaction databases

IntAct

P19544. 2 interactions.

PTM databases

PhosphoSite

P19544.

Polymorphism databases

DMDM

139778.

Proteomic databases

PaxDb

P19544.

PRIDE

P19544.

Protocols and materials databases

DNASU

7490.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000379079; ENSP00000368370; ENSG00000184937.
ENST00000452863; ENSP00000415516; ENSG00000184937.
ENST00000530998; ENSP00000435307; ENSG00000184937.

GeneID

7490.

KEGG

hsa:7490.

UCSC

uc001mtl.2. human.
uc001mtn.2. human.

Organism-specific databases

CTD

7490.

GeneCards

GC11M032365.

H-InvDB

HIX0009531.

HGNC

HGNC:12796. WT1.

HPA

CAB000327.

MIM

136680. phenotype.
156240. phenotype.
194070. phenotype.
194080. phenotype.
256370. phenotype.
607102. gene.
608978. phenotype.

neXtProt

NX_P19544.

Orphanet

251510. 46,XY partial gonadal dysgenesis.
220. Denys-Drash syndrome.
83469. Desmoplastic small round cell tumor.
93217. Familial idiopathic steroid-resistant nephrotic syndrome with diffuse mesangial sclerosis.
93213. Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis.
347. Frasier syndrome.
3097. Meacham syndrome.
654. Nephroblastoma.
93220. Sporadic idiopathic steroid-resistant nephrotic syndrome with diffuse mesangial sclerosis.
893. WAGR syndrome.

PharmGKB

PA37395.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5048.

HOVERGEN

HBG006960.

InParanoid

P19544.

KO

K09234.

PhylomeDB

P19544.

Enzyme and pathway databases

Pathway_Interaction_DB

telomerasepathway. Regulation of Telomerase.

Gene expression databases

ArrayExpress

P19544.

Bgee

P19544.

CleanEx

HS_WT1.

Genevestigator

P19544.

GermOnline

ENSG00000184937. Homo sapiens.

Family and domain databases

Gene3D

3.30.160.60. 4 hits.

InterPro

IPR017987. Wilms_tumour.
IPR000976. Wilms_tumour_N.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]

Pfam

PF02165. WT1. 1 hit.
[Graphical view]

PRINTS

PR00049. WILMSTUMOUR.

SMART

SM00355. ZnF_C2H2. 4 hits.
[Graphical view]

PROSITE

PS00028. ZINC_FINGER_C2H2_1. 4 hits.
PS50157. ZINC_FINGER_C2H2_2. 4 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P19544.

GenomeRNAi

7490.

NextBio

29336.

SOURCE

Search...

Entry information

Entry name

WT1_HUMAN

Accession

Primary (citable) accession number: P19544
Secondary accession number(s): A8K6S1 , B3KSA5, Q15881, Q16256, Q16575, Q4VXV4, Q4VXV5, Q4VXV6, Q8IYZ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	August 1, 1991
Last modified:	May 1, 2013
This is version 173 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.