Conclusion
Assessment
Binding Mode
Motif Status
Notes
Comments
Likely to be sequence specific TF
1 Monomer or homomultimer
No motif
Description
Description:
pogo transposable element with KRAB domain [Source:HGNC Symbol;Acc:HGNC:18800]
Entrez Summary
TBA
Ensembl ID:
ENSG00000143157
External Link:
Interpro
IPR001909 ; IPR004875 ; IPR006600 ; IPR009057 ; IPR018586 ; ;
Protein Domain:
Protein: ENSP00000356850DBD: BrinkerOther: DDE_1, HTH_Tnp_Tc5, KRABProtein: ENSP00000404402DBD: BrinkerOther: KRABProtein: ENSP00000356849DBD: BrinkerOther: DDE_1, HTH_Tnp_Tc5, KRAB
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.
x
CisBP considers it as a TF?
Yes
TFclass considers it as a TF?
No
Has GO:0003700 "transcription factor activity, sequence-specific DNA binding"
No
GO-Info
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
4a, two or more datasets predict it as a TF
TF has conditional DNA-binding requirements
DNA-Binding
Published Motif Data
Structure
Experimental History
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{"regions": [{"startStyle": "curved", "end": 209, "endStyle": "jagged", "aliStart": 195, "text": "BrkDBD", "colour": "#228B22", "aliEnd": 209, "start": 195, "href": "http://pfam.xfam.org/family/PF09607.8", "type": "pfama", "display": "true", "metadata": {"end": 209, "description": "This DNA-binding domain is the first approx. 100 residues of the N-terminal end of Brinker. The structure of this domain in complex with DNA consists of four alpha-helices that contain a helix-turn-helix DNA recognition motif specific for GC-rich DNA. The Brinker nuclear repressor is a major element of the Drosophila Decapentaplegic morphogen signalling pathway [1].", "database": "PfamA", "aliStart": 195, "scoreName": "E-value", "accession": "PF09607.8", "start": 195, "score": 0.0035, "identifier": "Brinker DNA-binding domain", "type": "DBD", "aliEnd": 209}}, {"startStyle": "straight", "end": 87, "endStyle": "straight", "aliStart": 49, "text": "KRAB", "colour": "#9999ff", "aliEnd": 86, "start": 46, "href": "http://pfam.xfam.org/family/PF01352.25", "type": "pfama", "display": "true", "metadata": {"end": 87, "description": "The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions [2,3]. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation [4].", "database": "PfamA", "aliStart": 49, "scoreName": "E-value", "accession": "PF01352.25", "start": 46, "score": 1.8999999999999998e-16, "identifier": "KRAB box", "type": "DBD", "aliEnd": 86}}], "length": 209}
{"regions": [{"startStyle": "curved", "end": 247, "endStyle": "curved", "aliStart": 195, "text": "BrkDBD", "colour": "#228B22", "aliEnd": 247, "start": 195, "href": "http://pfam.xfam.org/family/PF09607.8", "type": "pfama", "display": "true", "metadata": {"end": 247, "description": "This DNA-binding domain is the first approx. 100 residues of the N-terminal end of Brinker. The structure of this domain in complex with DNA consists of four alpha-helices that contain a helix-turn-helix DNA recognition motif specific for GC-rich DNA. The Brinker nuclear repressor is a major element of the Drosophila Decapentaplegic morphogen signalling pathway [1].", "database": "PfamA", "aliStart": 195, "scoreName": "E-value", "accession": "PF09607.8", "start": 195, "score": 7.9e-26, "identifier": "Brinker DNA-binding domain", "type": "DBD", "aliEnd": 247}}, {"startStyle": "straight", "end": 567, "endStyle": "straight", "aliStart": 396, "text": "DDE_1", "colour": "#9999ff", "aliEnd": 567, "start": 395, "href": "http://pfam.xfam.org/family/PF03184.17", "type": "pfama", "display": "true", "metadata": {"end": 567, "description": "This family of proteins are related to Pfam:PF00665 and are probably endonucleases of the DDE superfamily. Transposase proteins are necessary for efficient DNA transposition. This domain is a member of the DDE superfamily, which contain three carboxylate residues that are believed to be responsible for coordinating metal ions needed for catalysis. The catalytic activity of this enzyme involves DNA cleavage at a specific site followed by a strand transfer reaction. Interestingly this family also includes the CENP-B protein. This domain in that protein appears to have lost the metal binding residues and is unlikely to have endonuclease activity. Centromere Protein B (CENP-B) is a DNA-binding protein localised to the centromere.", "database": "PfamA", "aliStart": 396, "scoreName": "E-value", "accession": "PF03184.17", "start": 395, "score": 2.6000000000000003e-44, "identifier": "DDE superfamily endonuclease", "type": "DBD", "aliEnd": 567}}, {"startStyle": "straight", "end": 87, "endStyle": "straight", "aliStart": 49, "text": "KRAB", "colour": "#9999ff", "aliEnd": 86, "start": 46, "href": "http://pfam.xfam.org/family/PF01352.25", "type": "pfama", "display": "true", "metadata": {"end": 87, "description": "The KRAB domain (or Kruppel-associated box) is present in about a third of zinc finger proteins containing C2H2 fingers. The KRAB domain is found to be involved in protein-protein interactions [2,3]. The KRAB domain is generally encoded by two exons. The regions coded by the two exons are known as KRAB-A and KRAB-B. The A box plays an important role in repression by binding to corepressors, while the B box is thought to enhance this repression brought about by the A box. KRAB-containing proteins are thought to have critical functions in cell proliferation and differentiation, apoptosis and neoplastic transformation [4].", "database": "PfamA", "aliStart": 49, "scoreName": "E-value", "accession": "PF01352.25", "start": 46, "score": 4e-16, "identifier": "KRAB box", "type": "DBD", "aliEnd": 86}}, {"startStyle": "straight", "end": 323, "endStyle": "straight", "aliStart": 260, "text": "HTH_Tnp_Tc5", "colour": "#9999ff", "aliEnd": 322, "start": 259, "href": "http://pfam.xfam.org/family/PF03221.14", "type": "pfama", "display": "true", "metadata": {"end": 323, "description": NaN, "database": "PfamA", "aliStart": 260, "scoreName": "E-value", "accession": "PF03221.14", "start": 259, "score": 1.3e-13, "identifier": "Tc5 transposase DNA-binding domain", "type": "DBD", "aliEnd": 322}}], "length": 610}