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Protein

Wilms tumor protein

Gene

WT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transcription factor that plays an important role in cellular development and cell survival (PubMed:7862533). Recognizes and binds to the DNA sequence 5'-GCG(T/G)GGGCG-3' (PubMed:7862533, PubMed:17716689, PubMed:25258363). Regulates the expression of numerous target genes, including EPO. Plays an essential role for development of the urogenital system. It has a tumor suppressor as well as an oncogenic role in tumor formation. Function may be isoform-specific: isoforms lacking the KTS motif may act as transcription factors (PubMed:15520190). Isoforms containing the KTS motif may bind mRNA and play a role in mRNA metabolism or splicing (PubMed:16934801). Isoform 1 has lower affinity for DNA, and can bind RNA (PubMed:19123921).7 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei424Important for interaction with target DNA1
Sitei430Important for interaction with target DNA1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri323 – 347C2H2-type 1PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri353 – 377C2H2-type 2PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri383 – 405C2H2-type 3PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri414 – 438C2H2-type 4PROSITE-ProRule annotationAdd BLAST25

GO - Molecular functioni

  • C2H2 zinc finger domain binding Source: UniProtKB
  • double-stranded methylated DNA binding Source: UniProtKB
  • hemi-methylated DNA-binding Source: UniProtKB
  • RNA binding Source: UniProtKB-KW
  • sequence-specific DNA binding Source: UniProtKB
  • transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: UniProtKB
  • transcription factor activity, sequence-specific DNA binding Source: UniProtKB
  • transcription regulatory region DNA binding Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • adrenal cortex formation Source: UniProtKB
  • adrenal gland development Source: UniProtKB
  • branching involved in ureteric bud morphogenesis Source: UniProtKB
  • camera-type eye development Source: UniProtKB
  • cardiac muscle cell fate commitment Source: BHF-UCL
  • cellular response to cAMP Source: UniProtKB
  • cellular response to gonadotropin stimulus Source: UniProtKB
  • diaphragm development Source: UniProtKB
  • epithelial cell differentiation Source: UniProtKB
  • germ cell development Source: UniProtKB
  • glomerular basement membrane development Source: UniProtKB
  • glomerular visceral epithelial cell differentiation Source: UniProtKB
  • glomerulus development Source: UniProtKB
  • gonad development Source: UniProtKB
  • heart development Source: UniProtKB
  • kidney development Source: UniProtKB
  • male genitalia development Source: UniProtKB
  • male gonad development Source: UniProtKB
  • mesenchymal to epithelial transition Source: UniProtKB
  • metanephric epithelium development Source: UniProtKB
  • metanephric mesenchyme development Source: UniProtKB
  • metanephric S-shaped body morphogenesis Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of cell growth Source: UniProtKB
  • negative regulation of cell proliferation Source: UniProtKB
  • negative regulation of female gonad development Source: UniProtKB
  • negative regulation of metanephric glomerular mesangial cell proliferation Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • negative regulation of translation Source: UniProtKB
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of heart growth Source: UniProtKB
  • positive regulation of male gonad development Source: UniProtKB
  • positive regulation of metanephric ureteric bud development Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • posterior mesonephric tubule development Source: UniProtKB
  • regulation of animal organ formation Source: UniProtKB
  • regulation of transcription, DNA-templated Source: UniProtKB
  • regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • RNA splicing Source: UniProtKB
  • sex determination Source: UniProtKB
  • thorax and anterior abdomen determination Source: UniProtKB
  • tissue development Source: UniProtKB
  • ureteric bud development Source: UniProtKB
  • vasculogenesis Source: UniProtKB
  • visceral serous pericardium development Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, RNA-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:G66-33724-MONOMER.
SignaLinkiP19544.
SIGNORiP19544.

Names & Taxonomyi

Protein namesi
Recommended name:
Wilms tumor protein
Alternative name(s):
WT33
Gene namesi
Name:WT1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:12796. WT1.

Subcellular locationi

Isoform 1 :
Isoform 4 :

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • nuclear speck Source: UniProtKB
  • nucleolus Source: UniProtKB-SubCell
  • nucleoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Frasier syndrome (FS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionCharacterized 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.
See also OMIM:136680
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_015060392F → L in FS. 1 Publication1
Wilms tumor 1 (WT1)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionEmbryonal malignancy of the kidney that affects approximately 1 in 10'000 infants and young children. It occurs both in sporadic and hereditary forms.
See also OMIM:194070
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_007739181P → S in WT1. 2 PublicationsCorresponds to variant rs2234584dbSNPEnsembl.1
Natural variantiVAR_007740223S → N in WT1. 1 Publication1
Natural variantiVAR_007741253G → A in WT1. 1 Publication1
Natural variantiVAR_043799355C → G in WT1. 1 Publication1
Natural variantiVAR_007745366R → C in WT1, DDS and MEACHS. 4 Publications1
Natural variantiVAR_007746366R → H in DDS and WT1. 4 Publications1
Natural variantiVAR_007747373H → Q in DDS and WT1. 1 Publication1
Natural variantiVAR_043807394R → L in WT1. 1 Publication1
Natural variantiVAR_007750394R → W in DDS, WT1 and MEACHS. 8 Publications1
Denys-Drash syndrome (DDS)17 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionTypical 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.
See also OMIM:194080
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_007743330C → Y in DDS. 1 Publication1
Natural variantiVAR_015054342M → R in DDS. 1 Publication1
Natural variantiVAR_015055355C → Y in DDS. 2 Publications1
Natural variantiVAR_007744360C → G in DDS. 1
Natural variantiVAR_043800360C → Y in DDS. 1 Publication1
Natural variantiVAR_007745366R → C in WT1, DDS and MEACHS. 4 Publications1
Natural variantiVAR_007746366R → H in DDS and WT1. 4 Publications1
Natural variantiVAR_043802366R → L in DDS. 1 Publication1
Natural variantiVAR_043803369Q → P in DDS. 1 Publication1
Natural variantiVAR_007747373H → Q in DDS and WT1. 1 Publication1
Natural variantiVAR_015056373H → Y in DDS. 1 Publication1
Natural variantiVAR_015057377H → R in DDS. 1 Publication1
Natural variantiVAR_015058385C → R in DDS. 3 Publications1
Natural variantiVAR_015059388C → F in DDS. 1 Publication1
Natural variantiVAR_043806388C → Y in DDS. 1 Publication1
Natural variantiVAR_043808394R → P in DDS. 1 Publication1
Natural variantiVAR_015061394R → Q in DDS. 2 Publications1
Natural variantiVAR_007750394R → W in DDS, WT1 and MEACHS. 8 Publications1
Natural variantiVAR_007752396D → G in DDS. 1
Natural variantiVAR_007751396D → N in DDS and NPHS4. 3 Publications1
Natural variantiVAR_043809396D → Y in DDS. 1 Publication1
Natural variantiVAR_015062398L → P in DDS. 2 Publications1
Natural variantiVAR_043811401H → Y in DDS. 1 Publication1
Natural variantiVAR_043812405H → R in DDS. 1 Publication1
Nephrotic syndrome 4 (NPHS4)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of nephrotic syndrome, a renal disease clinically characterized by severe proteinuria, resulting in complications such as hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show non-specific histologic changes such as focal segmental glomerulosclerosis and diffuse mesangial proliferation. Some affected individuals have an inherited steroid-resistant form and progress to end-stage renal failure. Most patients with NPHS4 show diffuse mesangial sclerosis on renal biopsy, which is a pathologic entity characterized by mesangial matrix expansion with no mesangial hypercellularity, hypertrophy of the podocytes, vacuolized podocytes, thickened basement membranes, and diminished patency of the capillary lumen.
See also OMIM:256370
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_015053312R → Q in NPHS4. 1 Publication1
Natural variantiVAR_043801364F → L in NPHS4. 1 Publication1
Natural variantiVAR_007748377H → Y in NPHS4. 1 Publication1
Natural variantiVAR_043804379G → C in NPHS4. 1 Publication1
Natural variantiVAR_007749383F → L in NPHS4. 1 Publication1
Natural variantiVAR_043805388C → R in NPHS4. 1 Publication1
Natural variantiVAR_007751396D → N in DDS and NPHS4. 3 Publications1
Natural variantiVAR_043810397H → P in NPHS4. 1 Publication1
Meacham syndrome (MEACHS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionRare 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.
See also OMIM:608978
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_007745366R → C in WT1, DDS and MEACHS. 4 Publications1
Natural variantiVAR_007750394R → W in DDS, WT1 and MEACHS. 8 Publications1

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)1 Publication
The disease may be caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:156240

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi73K → R: Abolishes sumoylation; when associated with R-177. 1 Publication1
Mutagenesisi177K → R: Abolishes sumoylation; when associated with R-77. 1 Publication1
Mutagenesisi343H → A: Reduced RNA binding. 1 Publication1
Mutagenesisi366R → A: Strongly reduced binding of DNA and RNA. 1 Publication1
Mutagenesisi372R → A: Strongly reduced binding of DNA and RNA. 1 Publication1
Mutagenesisi394R → A or S: Strongly reduced binding of DNA and RNA. 1 Publication1
Mutagenesisi434H → A: Reduced RNA binding. 1 Publication1

Keywords - Diseasei

Disease mutation, Tumor suppressor

Organism-specific databases

DisGeNETi7490.
MalaCardsiWT1.
MIMi136680. phenotype.
156240. phenotype.
194070. phenotype.
194080. phenotype.
256370. phenotype.
608978. phenotype.
OpenTargetsiENSG00000184937.
Orphaneti251510. 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.
PharmGKBiPA37395.

Polymorphism and mutation databases

BioMutaiWT1.
DMDMi139778.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000471311 – 449Wilms tumor proteinAdd BLAST449

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki73Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Cross-linki177Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP19544.
PaxDbiP19544.
PeptideAtlasiP19544.
PRIDEiP19544.

PTM databases

iPTMnetiP19544.
PhosphoSitePlusiP19544.

Expressioni

Tissue specificityi

Expressed in the kidney and a subset of hematopoietic cells.

Gene expression databases

BgeeiENSG00000184937.
CleanExiHS_WT1.
ExpressionAtlasiP19544. baseline and differential.
GenevisibleiP19544. HS.

Organism-specific databases

HPAiCAB000327.

Interactioni

Subunit structurei

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.By similarity7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
KRT40Q6A1623EBI-2320534,EBI-10171697
KRTAP10-8P604103EBI-2320534,EBI-10171774

GO - Molecular functioni

  • C2H2 zinc finger domain binding Source: UniProtKB

Protein-protein interaction databases

BioGridi113327. 28 interactors.
IntActiP19544. 23 interactors.
MINTiMINT-105556.
STRINGi9606.ENSP00000331327.

Structurei

Secondary structure

1449
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi322 – 324Combined sources3
Turni328 – 330Combined sources3
Beta strandi333 – 337Combined sources5
Helixi338 – 344Combined sources7
Helixi345 – 349Combined sources5
Beta strandi363 – 366Combined sources4
Helixi367 – 378Combined sources12
Turni386 – 388Combined sources3
Beta strandi391 – 393Combined sources3
Helixi395 – 401Combined sources7
Helixi403 – 406Combined sources4
Turni419 – 421Combined sources3
Beta strandi424 – 427Combined sources4
Helixi428 – 438Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LU6model-A310-449[»]
1XF7NMR-A381-407[»]
2G7Tmodel-A310-449[»]
2G7Vmodel-A310-449[»]
2G7Wmodel-A310-449[»]
2G7Xmodel-A310-449[»]
2JP9NMR-A318-438[»]
2JPANMR-A318-438[»]
2PRTX-ray3.15A318-438[»]
3HPJX-ray2.00C/F126-134[»]
3MYJX-ray1.89C/F126-134[»]
4R2EX-ray1.84A350-440[»]
4R2PX-ray1.79A350-440[»]
4R2QX-ray1.54A350-440[»]
4R2RX-ray2.09A350-440[»]
4R2SX-ray2.49A350-440[»]
4WUUX-ray3.05C126-134[»]
5KL2X-ray1.69A350-440[»]
5KL3X-ray1.45A350-440[»]
5KL4X-ray1.78A/D350-440[»]
5KL5X-ray2.29A350-440[»]
5KL6X-ray1.64A350-440[»]
5KL7X-ray1.58A350-440[»]
ProteinModelPortaliP19544.
SMRiP19544.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19544.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni367 – 381Important for interaction with target DNAAdd BLAST15
Regioni393 – 401Important for interaction with target DNA9

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi408 – 410KTS motif3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi27 – 83Pro-richAdd BLAST57

Domaini

Binds to DNA motifs with the sequence 5'-GCG(T/G)GGGCG-3' via its C2H2-type zinc fingers. Starting from the N-terminus, the second zinc finger binds to the 3'-GCG motif, the middle zinc finger interacts with the central TGG motif, and the C-terminal zinc finger binds to the 5'-GCG motif. Binds double-stranded target DNA, irrespective of the cytosine methylation status. Has reduced affinity for target DNA where the cytosines have been oxidized to 5-hydroxymethylcytosine, 5-formylcytosine or 5-carboxylcytosine.1 Publication

Sequence similaritiesi

Contains 4 C2H2-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri323 – 347C2H2-type 1PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri353 – 377C2H2-type 2PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri383 – 405C2H2-type 3PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri414 – 438C2H2-type 4PROSITE-ProRule annotationAdd BLAST25

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00550000074455.
HOVERGENiHBG006960.
InParanoidiP19544.
KOiK09234.
PhylomeDBiP19544.

Family and domain databases

Gene3Di3.30.160.60. 4 hits.
InterProiIPR017987. Wilms_tumour.
IPR000976. Wilms_tumour_N.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF02165. WT1. 1 hit.
PF00096. zf-C2H2. 1 hit.
[Graphical view]
PRINTSiPR00049. WILMSTUMOUR.
SMARTiSM00355. ZnF_C2H2. 4 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 4 hits.
PS50157. ZINC_FINGER_C2H2_2. 4 hits.
[Graphical view]

Sequences (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative splicing and alternative initiation. AlignAdd to basket

Isoform 1 (identifier: P19544-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MGSDVRDLNA LLPAVPSLGG GGGCALPVSG AAQWAPVLDF APPGASAYGS
60 70 80 90 100
LGGPAPPPAP PPPPPPPPHS FIKQEPSWGG AEPHEEQCLS AFTVHFSGQF
110 120 130 140 150
TGTAGACRYG PFGPPPPSQA SSGQARMFPN APYLPSCLES QPAIRNQGYS
160 170 180 190 200
TVTFDGTPSY GHTPSHHAAQ FPNHSFKHED PMGQQGSLGE QQYSVPPPVY
210 220 230 240 250
GCHTPTDSCT GSQALLLRTP YSSDNLYQMT SQLECMTWNQ MNLGATLKGV
260 270 280 290 300
AAGSSSSVKW TEGQSNHSTG YESDNHTTPI LCGAQYRIHT HGVFRGIQDV
310 320 330 340 350
RRVPGVAPTL VRSASETSEK RPFMCAYPGC NKRYFKLSHL QMHSRKHTGE
360 370 380 390 400
KPYQCDFKDC ERRFSRSDQL KRHQRRHTGV KPFQCKTCQR KFSRSDHLKT
410 420 430 440
HTRTHTGKTS EKPFSCRWPS CQKKFARSDE LVRHHNMHQR NMTKLQLAL
Note: Detected in nucleus speckle, may bind mRNA.
Length:449
Mass (Da):49,188
Last modified:August 1, 1991 - v2
Checksum:i11C7FA3D485096B2
GO
Isoform 2 (identifier: P19544-2) [UniParc]FASTAAdd to basket

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

Show »
Length:429
Mass (Da):47,195
Checksum:iC2F9912E0A4DA3DB
GO
Isoform 3 (identifier: P19544-3) [UniParc]FASTAAdd to basket

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

Show »
Length:432
Mass (Da):47,511
Checksum:i1ACA6CE3563DA9D2
GO
Isoform 4 (identifier: P19544-4) [UniParc]FASTAAdd to basket

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

Show »
Length:446
Mass (Da):48,872
Checksum:i8CE7FC116A41DA04
GO
Isoform 6 (identifier: P19544-6) [UniParc]FASTAAdd to basket

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

Show »
Length:302
Mass (Da):34,447
Checksum:i715B121077C0991D
GO
Isoform 7 (identifier: P19544-7) [UniParc]FASTAAdd to basket

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.
Show »
Length:522
Mass (Da):56,883
Checksum:iFB30F6E34A60EC04
GO
Isoform 8 (identifier: P19544-8) [UniParc]FASTAAdd to basket

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.
Show »
Length:505
Mass (Da):55,206
Checksum:iC7CE98CE8B83C250
GO
Isoform 9 (identifier: P19544-9) [UniParc]FASTAAdd to basket

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.
Show »
Length:288
Mass (Da):33,086
Checksum:i9526D02081619728
GO

Sequence cautioni

The sequence AAB33443 differs from that shown. Contaminating sequence. Sequence of unknown origin in the N-terminal part.Curated
The sequence CAA35956 differs from that shown. Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated
The sequence CAA35956 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAC39220 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAI95758 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAI95759 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti288I → M in AAH32861 (PubMed:15489334).Curated1
Sequence conflicti365S → F in AAA36810 (PubMed:2154335).Curated1
Sequence conflicti365S → F in AAB33443 (PubMed:7862533).Curated1
Sequence conflicti387T → A in CAA43819 (PubMed:1572653).Curated1

RNA editingi

Edited at position 281.1 Publication
Partially edited.

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_043798131A → T in a patient with hypospadias. 1 Publication1
Natural variantiVAR_007739181P → S in WT1. 2 PublicationsCorresponds to variant rs2234584dbSNPEnsembl.1
Natural variantiVAR_007740223S → N in WT1. 1 Publication1
Natural variantiVAR_007741253G → A in WT1. 1 Publication1
Natural variantiVAR_007742273S → G Found in a mesothelioma sample; somatic mutation. 1 PublicationCorresponds to variant rs121907908dbSNPEnsembl.1
Natural variantiVAR_058021281L → P in RNA edited version. 1
Natural variantiVAR_015053312R → Q in NPHS4. 1 Publication1
Natural variantiVAR_007743330C → Y in DDS. 1 Publication1
Natural variantiVAR_015054342M → R in DDS. 1 Publication1
Natural variantiVAR_043799355C → G in WT1. 1 Publication1
Natural variantiVAR_015055355C → Y in DDS. 2 Publications1
Natural variantiVAR_007744360C → G in DDS. 1
Natural variantiVAR_043800360C → Y in DDS. 1 Publication1
Natural variantiVAR_043801364F → L in NPHS4. 1 Publication1
Natural variantiVAR_007745366R → C in WT1, DDS and MEACHS. 4 Publications1
Natural variantiVAR_007746366R → H in DDS and WT1. 4 Publications1
Natural variantiVAR_043802366R → L in DDS. 1 Publication1
Natural variantiVAR_043803369Q → P in DDS. 1 Publication1
Natural variantiVAR_007747373H → Q in DDS and WT1. 1 Publication1
Natural variantiVAR_015056373H → Y in DDS. 1 Publication1
Natural variantiVAR_015057377H → R in DDS. 1 Publication1
Natural variantiVAR_007748377H → Y in NPHS4. 1 Publication1
Natural variantiVAR_043804379G → C in NPHS4. 1 Publication1
Natural variantiVAR_007749383F → L in NPHS4. 1 Publication1
Natural variantiVAR_015058385C → R in DDS. 3 Publications1
Natural variantiVAR_015059388C → F in DDS. 1 Publication1
Natural variantiVAR_043805388C → R in NPHS4. 1 Publication1
Natural variantiVAR_043806388C → Y in DDS. 1 Publication1
Natural variantiVAR_015060392F → L in FS. 1 Publication1
Natural variantiVAR_043807394R → L in WT1. 1 Publication1
Natural variantiVAR_043808394R → P in DDS. 1 Publication1
Natural variantiVAR_015061394R → Q in DDS. 2 Publications1
Natural variantiVAR_007750394R → W in DDS, WT1 and MEACHS. 8 Publications1
Natural variantiVAR_007752396D → G in DDS. 1
Natural variantiVAR_007751396D → N in DDS and NPHS4. 3 Publications1
Natural variantiVAR_043809396D → Y in DDS. 1 Publication1
Natural variantiVAR_043810397H → P in NPHS4. 1 Publication1
Natural variantiVAR_015062398L → P in DDS. 2 Publications1
Natural variantiVAR_043811401H → Y in DDS. 1 Publication1
Natural variantiVAR_043812405H → R in DDS. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0375821 – 144Missing in isoform 6 and isoform 9. 2 PublicationsAdd BLAST144
Alternative sequenceiVSP_0375831M → MDFLLLQDPASTCVPEPASQ HTLRSGPGCLQQPEQQGVRD PGGIWAKLGAAEASAERLQG RRSRGASGSEPQQM in isoform 7 and isoform 8. 1 Publication1
Alternative sequenceiVSP_037584145 – 147RNQ → MEK in isoform 6 and isoform 9. 2 Publications3
Alternative sequenceiVSP_006866250 – 266Missing in isoform 2, isoform 3, isoform 8 and isoform 9. 2 PublicationsAdd BLAST17
Alternative sequenceiVSP_006867408 – 410Missing in isoform 2, isoform 4 and isoform 6. 3 Publications3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS55750.1. [P19544-9]
CCDS55751.1. [P19544-6]
PIRiA38080.
RefSeqiNP_000369.3. NM_000378.4.
NP_001185480.1. NM_001198551.1. [P19544-6]
NP_001185481.1. NM_001198552.1. [P19544-9]
NP_077742.2. NM_024424.3.
NP_077744.3. NM_024426.4.
UniGeneiHs.591980.

Genome annotation databases

EnsembliENST00000379079; ENSP00000368370; ENSG00000184937. [P19544-6]
ENST00000530998; ENSP00000435307; ENSG00000184937. [P19544-9]
GeneIDi7490.
KEGGihsa:7490.
UCSCiuc001mtl.3. human. [P19544-1]

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing, Chromosomal rearrangement, RNA editing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS55750.1. [P19544-9]
CCDS55751.1. [P19544-6]
PIRiA38080.
RefSeqiNP_000369.3. NM_000378.4.
NP_001185480.1. NM_001198551.1. [P19544-6]
NP_001185481.1. NM_001198552.1. [P19544-9]
NP_077742.2. NM_024424.3.
NP_077744.3. NM_024426.4.
UniGeneiHs.591980.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LU6model-A310-449[»]
1XF7NMR-A381-407[»]
2G7Tmodel-A310-449[»]
2G7Vmodel-A310-449[»]
2G7Wmodel-A310-449[»]
2G7Xmodel-A310-449[»]
2JP9NMR-A318-438[»]
2JPANMR-A318-438[»]
2PRTX-ray3.15A318-438[»]
3HPJX-ray2.00C/F126-134[»]
3MYJX-ray1.89C/F126-134[»]
4R2EX-ray1.84A350-440[»]
4R2PX-ray1.79A350-440[»]
4R2QX-ray1.54A350-440[»]
4R2RX-ray2.09A350-440[»]
4R2SX-ray2.49A350-440[»]
4WUUX-ray3.05C126-134[»]
5KL2X-ray1.69A350-440[»]
5KL3X-ray1.45A350-440[»]
5KL4X-ray1.78A/D350-440[»]
5KL5X-ray2.29A350-440[»]
5KL6X-ray1.64A350-440[»]
5KL7X-ray1.58A350-440[»]
ProteinModelPortaliP19544.
SMRiP19544.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113327. 28 interactors.
IntActiP19544. 23 interactors.
MINTiMINT-105556.
STRINGi9606.ENSP00000331327.

PTM databases

iPTMnetiP19544.
PhosphoSitePlusiP19544.

Polymorphism and mutation databases

BioMutaiWT1.
DMDMi139778.

Proteomic databases

MaxQBiP19544.
PaxDbiP19544.
PeptideAtlasiP19544.
PRIDEiP19544.

Protocols and materials databases

DNASUi7490.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000379079; ENSP00000368370; ENSG00000184937. [P19544-6]
ENST00000530998; ENSP00000435307; ENSG00000184937. [P19544-9]
GeneIDi7490.
KEGGihsa:7490.
UCSCiuc001mtl.3. human. [P19544-1]

Organism-specific databases

CTDi7490.
DisGeNETi7490.
GeneCardsiWT1.
GeneReviewsiWT1.
H-InvDBHIX0009531.
HGNCiHGNC:12796. WT1.
HPAiCAB000327.
MalaCardsiWT1.
MIMi136680. phenotype.
156240. phenotype.
194070. phenotype.
194080. phenotype.
256370. phenotype.
607102. gene.
608978. phenotype.
neXtProtiNX_P19544.
OpenTargetsiENSG00000184937.
Orphaneti251510. 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.
PharmGKBiPA37395.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00550000074455.
HOVERGENiHBG006960.
InParanoidiP19544.
KOiK09234.
PhylomeDBiP19544.

Enzyme and pathway databases

BioCyciZFISH:G66-33724-MONOMER.
SignaLinkiP19544.
SIGNORiP19544.

Miscellaneous databases

ChiTaRSiWT1. human.
EvolutionaryTraceiP19544.
GeneWikiiWT1.
GenomeRNAii7490.
PROiP19544.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000184937.
CleanExiHS_WT1.
ExpressionAtlasiP19544. baseline and differential.
GenevisibleiP19544. HS.

Family and domain databases

Gene3Di3.30.160.60. 4 hits.
InterProiIPR017987. Wilms_tumour.
IPR000976. Wilms_tumour_N.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF02165. WT1. 1 hit.
PF00096. zf-C2H2. 1 hit.
[Graphical view]
PRINTSiPR00049. WILMSTUMOUR.
SMARTiSM00355. ZnF_C2H2. 4 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 4 hits.
PS50157. ZINC_FINGER_C2H2_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiWT1_HUMAN
AccessioniPrimary (citable) accession number: P19544
Secondary accession number(s): A8K6S1
, B3KSA5, Q15881, Q16256, Q16575, Q4VXV4, Q4VXV5, Q4VXV6, Q8IYZ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: August 1, 1991
Last modified: November 30, 2016
This is version 207 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Miscellaneous

Presence of the KTS motif hinders interactions between DNA and zinc-finger 4.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.