Conclusion
Assessment
Binding Mode
Motif Status
Notes
Comments
Known motif
1 Monomer or homomultimer
High-throughput in vitro
Description
Description:
early growth response 1 [Source:HGNC Symbol;Acc:HGNC:3238]
Entrez Summary
TBA
Ensembl ID:
ENSG00000120738
External Link:
T044306_1.02
Interpro
IPR007087 ; IPR015880 ; IPR021839 ; IPR021849 ;
Protein Domain:
Protein: ENSP00000239938DBD: C2H2 ZF Containing ProteinsOther: Cornifin, DUF3432, DUF3446
Previous Annotations
Source
Annotation
TF-CAT classification
TF Gene_DNA-Binding sequence-specific_DNA Binding Transactivation_ PMIDS:8336701 9858508 10049687
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:0001077 RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor a IEA - GO_REF:0000019 GO:0003700 sequence-specific DNA binding transcription factor activity IDA - PMID:12560508
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
{"regions": [{"startStyle": "curved", "end": 362, "endStyle": "curved", "aliStart": 338, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 362, "start": 338, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 362, "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": 338, "scoreName": "E-value", "accession": "PF00096.24", "start": 338, "score": 9.4e-15, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 362}}, {"startStyle": "curved", "end": 390, "endStyle": "curved", "aliStart": 368, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 390, "start": 368, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 390, "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": 368, "scoreName": "E-value", "accession": "PF00096.24", "start": 368, "score": 9.4e-15, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 390}}, {"startStyle": "curved", "end": 418, "endStyle": "curved", "aliStart": 396, "text": "zfC2H2", "colour": "#228B22", "aliEnd": 418, "start": 396, "href": "http://pfam.xfam.org/family/PF00096.24", "type": "pfama", "display": "true", "metadata": {"end": 418, "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": 396, "scoreName": "E-value", "accession": "PF00096.24", "start": 396, "score": 9.4e-15, "identifier": "Zinc finger, C2H2 type", "type": "DBD", "aliEnd": 418}}, {"startStyle": "straight", "end": 466, "endStyle": "jagged", "aliStart": 429, "text": "DUF3432", "colour": "#9999ff", "aliEnd": 466, "start": 421, "href": "http://pfam.xfam.org/family/PF11914.6", "type": "pfama", "display": "true", "metadata": {"end": 466, "description": "This presumed domain is functionally uncharacterised. This domain is found in eukaryotes. This domain is about 100 amino acids in length. This domain is found associated with Pfam:PF00096. This domain has two conserved sequence motifs: YPSPV and PSP.", "database": "PfamA", "aliStart": 429, "scoreName": "E-value", "accession": "PF11914.6", "start": 421, "score": 2.7e-34, "identifier": "Domain of unknown function (DUF3432)", "type": "DBD", "aliEnd": 466}}, {"startStyle": "jagged", "end": 530, "endStyle": "straight", "aliStart": 453, "text": "DUF3432", "colour": "#9999ff", "aliEnd": 530, "start": 453, "href": "http://pfam.xfam.org/family/PF11914.6", "type": "pfama", "display": "true", "metadata": {"end": 530, "description": "This presumed domain is functionally uncharacterised. This domain is found in eukaryotes. This domain is about 100 amino acids in length. This domain is found associated with Pfam:PF00096. This domain has two conserved sequence motifs: YPSPV and PSP.", "database": "PfamA", "aliStart": 453, "scoreName": "E-value", "accession": "PF11914.6", "start": 453, "score": 2.7e-34, "identifier": "Domain of unknown function (DUF3432)", "type": "DBD", "aliEnd": 530}}, {"startStyle": "straight", "end": 219, "endStyle": "straight", "aliStart": 135, "text": "DUF3446", "colour": "#9999ff", "aliEnd": 219, "start": 135, "href": "http://pfam.xfam.org/family/PF11928.6", "type": "pfama", "display": "true", "metadata": {"end": 219, "description": "This presumed domain is functionally uncharacterised. This domain is found in eukaryotes. This domain is typically between 80 to 99 amino acids in length. This domain is found associated with Pfam:PF00096. This domain has a single completely conserved residue P that may be functionally important.", "database": "PfamA", "aliStart": 135, "scoreName": "E-value", "accession": "PF11928.6", "start": 135, "score": 1.1e-24, "identifier": "Domain of unknown function (DUF3446)", "type": "DBD", "aliEnd": 219}}, {"startStyle": "jagged", "end": 523, "endStyle": "jagged", "aliStart": 441, "text": "Cornifin", "colour": "#9999ff", "aliEnd": 496, "start": 418, "href": "http://pfam.xfam.org/family/PF02389.13", "type": "pfama", "display": "true", "metadata": {"end": 523, "description": "SPRR genes (formerly SPR) encode a novel class of polypeptides (small proline rich proteins) that are strongly induced during differentiation of human epidermal keratinocytes in vitro and in vivo. The most characteristic feature of the SPRR gene family resides in the structure of the central segments of the encoded polypeptides that are built up from tandemly repeated units of either eight (SPRR1 and SPRR3) or nine (SPRR2) amino acids with the general consensus XKXPEPXX where X is any amino acid [1]. In order to avoid bacterial contamination due to the high polar-nature of the HMM the threshold has been set very high.", "database": "PfamA", "aliStart": 441, "scoreName": "E-value", "accession": "PF02389.13", "start": 418, "score": 0.0047, "identifier": "Cornifin (SPRR) family", "type": "DBD", "aliEnd": 496}}], "length": 544}