Conclusion
Assessment
Binding Mode
Motif Status
Notes
Comments
Known motif
1 Monomer or homomultimer
High-throughput in vitro
Crystal structure (PDB:2JP9) is with dsDNA GCGCAGACGCCCCCGCG, which is consistent with the PWMs
Description
Description:
Wilms tumor 1 [Source:HGNC Symbol;Acc:HGNC:12796]
Entrez Summary
#!usr/local/bin/perl
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This gene encodes a transcription factor that contains four
zinc-finger motifs at the C-terminus and a proline/glutamine-rich DNA-binding
domain at the N-terminus. It has an essential role in the normal development
of the urogenital system, and it is mutated in a small subset of patients
with Wilms tumor. This gene exhibits complex tissue-specific and polymorphic
imprinting pattern, with biallelic, and monoallelic expression from the
maternal and paternal alleles in different tissues. Multiple transcript
variants have been described. In several variants, there is evidence for the
use of a non-AUG (CUG) translation initiation codon upstream of, and in-frame
with the first AUG. Authors of PMID:7926762 also provide evidence that WT1
mRNA undergoes RNA editing in human and rat, and that this process is
tissue-restricted and developmentally regulated. [provided by RefSeq, Mar
2015]
Ensembl ID:
ENSG00000184937
External Link:
CisBP
Interpro
IPR000976 ; IPR007087 ; IPR015880 ; IPR017987 ;
Protein Domain:
ENSP00000331327
Protein Domain:
ENSP00000368370
Protein Domain:
ENSP00000415516
Protein Domain:
ENSP00000413452
Protein Domain:
ENSP00000435307
Domain:
Protein: ENSP00000331327DBD: C2H2 ZF Containing ProteinsOther: WT1Protein: ENSP00000368370DBD: C2H2 ZF Containing ProteinsOther: WT1Protein: ENSP00000415516DBD: C2H2 ZF Containing ProteinsOther: WT1Protein: ENSP00000413452DBD: C2H2 ZF Containing ProteinsOther: WT1Protein: ENSP00000435307DBD: C2H2 ZF Containing ProteinsOther: WT1
Previous Annotations
Source
Annotation
TF-CAT classification
No PMIDS:
Vaquerizas 2009 TF classification
"a " Has direct evidence of TF function;
"b " Has evidence for an orthologous TF;
"c " contains likely DBDs, but has no functional evidence;
"x " is an unlikely TF such as predicted gene, genes with likely non-specific DBDs or that have function outside transcription;
"other " category contains proteins without clear DBDs they curated from external sources.
a
CisBP considers it as a TF?
Yes
TFclass considers it as a TF?
Yes
Has GO:0003700 "transcription factor activity, sequence-specific DNA binding"
No
GO-Info
GO:0001077 RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor a ISS - GO_REF:0000024 GO:0003700 sequence-specific DNA binding transcription factor activity ISS - GO_REF:0000024 | NAS - PMID:7862533, PMID:83
Initial Assessment
1a1 Protein has a high confidence PWM (HT-SELEX, PBM or B1H model) or there is a crystal structure that supports sequence specific DNA binding;
1a2 There is high confidence data for a close ortholog (as defined in CisBP);
2a1 There is lower confidence direct evidence, such as a Jaspar, Hocomoco or Transfac model;
2a2 There is lower confidence evidence for an close ortholog;
3a There is decent circumstantial evidence for its role as a TF or not;
4a Two or more datasets predict it as a TF;
5a One of the source datasets predicts is as a TF
1a1, Direct HQ evidence
TF has conditional DNA-binding requirements
DNA-Binding
Published Motif Data
Structure
Experimental History
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The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter [2].", "database": "PfamA", "aliStart": 451, "scoreName": "E-value", "accession": "PF00096.24", "start": 451, "score": 2.5e-14, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 473}}, {"startStyle": "curved", "end": 503, "endStyle": "curved", "aliStart": 479, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 503, "start": 479, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 503, "description": "The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter [2].", "database": "PfamA", "aliStart": 479, "scoreName": "E-value", "accession": "PF00096.24", "start": 479, "score": 2.5e-14, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 503}}, {"startStyle": "straight", "end": 331, "endStyle": "jagged", "aliStart": 69, "text": "WT1", "colour": "#9999ff", "aliEnd": 325, "start": 69, "href": "http://pfam.xfam.org/family/PF02165.13", "type": "pfama", "display": "true", "metadata": {"end": 331, "description": NaN, "database": "PfamA", "aliStart": 69, "scoreName": "E-value", "accession": "PF02165.13", "start": 69, "score": 1.8999999999999998e-149, "identifier": "Wilm's tumour protein", "type": "DBD", "aliEnd": 325}}, {"startStyle": "jagged", "end": 389, "endStyle": "straight", "aliStart": 334, "text": "WT1", "colour": "#9999ff", "aliEnd": 389, "start": 326, "href": "http://pfam.xfam.org/family/PF02165.13", "type": "pfama", "display": "true", "metadata": {"end": 389, "description": NaN, "database": "PfamA", "aliStart": 334, "scoreName": "E-value", "accession": "PF02165.13", "start": 326, "score": 1.8999999999999998e-149, "identifier": "Wilm's tumour protein", "type": "DBD", "aliEnd": 389}}], "length": 515}
{"regions": [{"startStyle": "curved", "end": 186, "endStyle": "curved", "aliStart": 162, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 186, "start": 162, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 186, "description": "The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter [2].", "database": "PfamA", "aliStart": 162, "scoreName": "E-value", "accession": "PF00096.24", "start": 162, "score": 1.4e-15, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 186}}, {"startStyle": "curved", "end": 216, "endStyle": "curved", "aliStart": 192, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 216, "start": 192, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 216, "description": "The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter [2].", "database": "PfamA", "aliStart": 192, "scoreName": "E-value", "accession": "PF00096.24", "start": 192, "score": 1.4e-15, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 216}}, {"startStyle": "curved", "end": 244, "endStyle": "curved", "aliStart": 222, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 244, "start": 222, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 244, "description": "The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter [2].", "database": "PfamA", "aliStart": 222, "scoreName": "E-value", "accession": "PF00096.24", "start": 222, "score": 1.4e-15, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 244}}, {"startStyle": "curved", "end": 277, "endStyle": "curved", "aliStart": 253, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 277, "start": 253, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 277, "description": "The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter [2].", "database": "PfamA", "aliStart": 253, "scoreName": "E-value", "accession": "PF00096.24", "start": 253, "score": 1.4e-15, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 277}}, {"startStyle": "jagged", "end": 160, "endStyle": "straight", "aliStart": 3, "text": "WT1", "colour": "#9999ff", "aliEnd": 160, "start": 1, "href": "http://pfam.xfam.org/family/PF02165.13", "type": "pfama", "display": "true", "metadata": {"end": 160, "description": NaN, "database": "PfamA", "aliStart": 3, "scoreName": "E-value", "accession": "PF02165.13", "start": 1, "score": 1.5999999999999997e-91, "identifier": "Wilm's tumour protein", "type": "DBD", "aliEnd": 160}}], "length": 289}