Conclusion
Assessment
Binding Mode
Motif Status
Notes
Comments
Known motif
1 Monomer or homomultimer
In vivo/Misc source
Description
Description:
RE1 silencing transcription factor [Source:HGNC Symbol;Acc:HGNC:9966]
Entrez Summary
#!usr/local/bin/perl
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This gene was initially identified as a transcriptional repressor
that represses neuronal genes in non-neuronal tissues. However, depending on
the cellular context, this gene can act as either an oncogene or a tumor
suppressor. The encoded protein is a member of the Kruppel-type zinc finger
transcription factor family. It represses transcription by binding a DNA
sequence element called the neuron-restrictive silencer element. The protein
is also found in undifferentiated neuronal progenitor cells and it is thought
that this repressor may act as a master negative regulator of neurogenesis.
Alternatively spliced transcript variants have been described. [provided by
RefSeq, May 2018]
Ensembl ID:
ENSG00000084093
External Link:
CisBP
Interpro
IPR007087 ; IPR015880 ;
Protein Domain:
ENSP00000311816
Protein Domain:
ENSP00000479151
Protein Domain:
ENSP00000484836
Protein Domain:
ENSP00000481650
Domain:
Protein: ENSP00000311816DBD: C2H2 ZF Containing ProteinsOther: zf-C2H2_4, zf-H2C2_5Protein: ENSP00000479151DBD: C2H2 ZF Containing ProteinsOther: Protein: ENSP00000484836DBD: C2H2 ZF Containing ProteinsOther: zf-C2H2_4, zf-H2C2_5Protein: ENSP00000481650DBD: C2H2 ZF Containing ProteinsOther:
Previous Annotations
Source
Annotation
TF-CAT classification
TF Gene_DNA-Binding sequence-specific_DNA Binding_ PMIDS:15240883
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"
Yes
GO-Info
GO:0001078 RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor a IDA - PMID:10449787, PMID:10734093, PMID:21284946 GO:0001228 RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor IEA - GO_REF:0000019 GO:0003700 sequence-specific DNA binding transcription factor activity IDA - PMID:19342457
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
2a1, Lower confidence direct evidence
TF has conditional DNA-binding requirements
DNA-Binding
Published Motif Data
Structure
Experimental History
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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. 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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. 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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": 304, "scoreName": "E-value", "accession": "PF00096.24", "start": 304, "score": 6.8e-11, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 326}}], "length": 341}
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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": 276, "scoreName": "E-value", "accession": "PF00096.24", "start": 276, "score": 3.2e-13, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 298}}, {"startStyle": "curved", "end": 326, "endStyle": "curved", "aliStart": 304, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 326, "start": 304, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 326, "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": 304, "scoreName": "E-value", "accession": "PF00096.24", "start": 304, "score": 3.2e-13, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 326}}, {"startStyle": "curved", "end": 355, "endStyle": "curved", "aliStart": 332, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 355, "start": 332, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 355, "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": 332, "scoreName": "E-value", "accession": "PF00096.24", "start": 332, "score": 3.2e-13, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 355}}, {"startStyle": "curved", "end": 383, "endStyle": "curved", "aliStart": 362, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 383, "start": 361, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 383, "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": 362, "scoreName": "E-value", "accession": "PF00096.24", "start": 361, "score": 3.2e-13, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 383}}, {"startStyle": "curved", "end": 412, "endStyle": "curved", "aliStart": 389, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 412, "start": 389, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 412, "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": 389, "scoreName": "E-value", "accession": "PF00096.24", "start": 389, "score": 3.2e-13, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 412}}, {"startStyle": "curved", "end": 1082, "endStyle": "curved", "aliStart": 1060, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 1082, "start": 1060, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 1082, "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": 1060, "scoreName": "E-value", "accession": "PF00096.24", "start": 1060, "score": 3.2e-13, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 1082}}, {"startStyle": "straight", "end": 183, "endStyle": "straight", "aliStart": 159, "text": "zf-H2C2_5", "colour": "#9999ff", "aliEnd": 182, "start": 159, "href": "http://pfam.xfam.org/family/PF13909.4", "type": "pfama", "display": "true", "metadata": {"end": 183, "description": NaN, "database": "PfamA", "aliStart": 159, "scoreName": "E-value", "accession": "PF13909.4", "start": 159, "score": 9.2e-22, "identifier": "C2H2-type zinc-finger domain", "type": "DBD", "aliEnd": 182}}, {"startStyle": "straight", "end": 182, "endStyle": "straight", "aliStart": 159, "text": "zf-C2H2_4", "colour": "#9999ff", "aliEnd": 181, "start": 159, "href": "http://pfam.xfam.org/family/PF13894.4", "type": "pfama", "display": "true", "metadata": {"end": 182, "description": "This family contains a number of divergent C2H2 type zinc fingers.", "database": "PfamA", "aliStart": 159, "scoreName": "E-value", "accession": "PF13894.4", "start": 159, "score": 1e-09, "identifier": "C2H2-type zinc finger", "type": "DBD", "aliEnd": 181}}], "length": 1098}
{"regions": [{"startStyle": "curved", "end": 138, "endStyle": "curved", "aliStart": 116, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 138, "start": 116, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 138, "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": 116, "scoreName": "E-value", "accession": "PF00096.24", "start": 116, "score": 2.0999999999999998e-09, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 138}}, {"startStyle": "curved", "end": 166, "endStyle": "curved", "aliStart": 144, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 166, "start": 144, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 166, "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": 144, "scoreName": "E-value", "accession": "PF00096.24", "start": 144, "score": 2.0999999999999998e-09, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 166}}, {"startStyle": "curved", "end": 194, "endStyle": "curved", "aliStart": 172, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 194, "start": 172, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 194, "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": 172, "scoreName": "E-value", "accession": "PF00096.24", "start": 172, "score": 2.0999999999999998e-09, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 194}}, {"startStyle": "curved", "end": 299, "endStyle": "curved", "aliStart": 277, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 299, "start": 277, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 299, "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": 277, "scoreName": "E-value", "accession": "PF00096.24", "start": 277, "score": 2.0999999999999998e-09, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 299}}], "length": 315}