Conclusion
Assessment
Binding Mode
Motif Status
Notes
Comments
Likely to be sequence specific TF
3 Low specificity DNA-binding protein
No motif
Component of the silencing nucleolar remodelling complex (NoRC) (PMID: 22368283)
Description
Description:
bromodomain adjacent to zinc finger domain 2A [Source:HGNC Symbol;Acc:HGNC:962]
Entrez Summary
TBA
Ensembl ID:
ENSG00000076108
External Link:
T113536_1.02
Interpro
IPR001487 ; IPR001739 ; IPR001965 ; IPR004022 ; IPR011011 ; IPR016177 ; IPR017956 ; IPR018359 ; IPR018500 ; IPR018501 ; IPR019787 ; ;
Protein Domain:
Protein: ENSP00000368754DBD: Methyl-CpG DNA-bindingOther: Bromodomain, DDT, PHD, WHIM1, WSDProtein: ENSP00000448760DBD: Methyl-CpG DNA-bindingOther: Bromodomain, PHD, WSDProtein: ENSP00000446880DBD: Methyl-CpG DNA-bindingOther: Bromodomain, DDT, PHD, WHIM1, WSDProtein: ENSP00000447248DBD: Methyl-CpG DNA-bindingOther: Protein: ENSP00000447941DBD: Methyl-CpG DNA-bindingOther: Bromodomain, DDT, PHD, WHIM1, WSDProtein: ENSP00000449496DBD: Methyl-CpG DNA-bindingOther: Protein: ENSP00000449473DBD: Methyl-CpG DNA-bindingOther:
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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The acidic residue from the GxD signature at the N-terminus is a major determinant of the interaction between the ISWI and WHIM motifs. The N-terminal portion also contacts the inter-nucleosomal linker DNA. The module shows a great domain architectural diversity and is often combined with other modified histone peptide recognizing and DNA binding domains, some of which discriminate methylated DNA. 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Based on the Ioc3 structure, the N-terminus of this module is inferred to interact with nucleosomal linker DNA and the SLIDE domain of ISWI proteins [1,2]. The resulting complex forms a protein ruler that measures out the spacing between two adjacent nucleosomes [2]. The acidic residue from the GxD signature at the N-terminus is a major determinant of the interaction between the ISWI and WHIM motifs. The N-terminal portion also contacts the inter-nucleosomal linker DNA. The module shows a great domain architectural diversity and is often combined with other modified histone peptide recognizing and DNA binding domains, some of which discriminate methylated DNA. The WSD module constitutes the inter-nucleosomal linker DNA binding site in the major groove of DNA [1], and was first identified as WSD [3], the D-TOX E motif of plant homeodomains homologous with the mutant transcription factor causing Williams-Beuren syndrome in association with the DDT-domain.", "database": "PfamA", "aliStart": 1433, "scoreName": "E-value", "accession": "PF15613.4", "start": 1384, "score": 1.3999999999999999e-14, "identifier": "Williams-Beuren syndrome DDT (WSD), D-TOX E motif", "type": "DBD", "aliEnd": 1470}}, {"startStyle": "straight", "end": 1724, "endStyle": "straight", "aliStart": 1677, "text": "PHD", "colour": "#9999ff", "aliEnd": 1722, "start": 1676, "href": "http://pfam.xfam.org/family/PF00628.27", "type": "pfama", "display": "true", "metadata": {"end": 1724, "description": "PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar manner to that of the RING and FYVE domains [2]. Several PHD fingers have been identified as binding modules of methylated histone H3 [3].", "database": "PfamA", "aliStart": 1677, "scoreName": "E-value", "accession": "PF00628.27", "start": 1676, "score": 1.1000000000000001e-10, "identifier": "PHD-finger", "type": "DBD", "aliEnd": 1722}}, {"startStyle": "straight", "end": 908, "endStyle": "straight", "aliStart": 848, "text": "DDT", "colour": "#9999ff", "aliEnd": 908, "start": 847, "href": "http://pfam.xfam.org/family/PF02791.15", "type": "pfama", "display": "true", "metadata": {"end": 908, "description": "The DDT domain is named after (DNA binding homeobox and Different Transcription factors) and is approximately 60 residues in length [1]. Along with the WHIM motifs, it comprises an entirely alpha helical module found in diverse eukaryotic chromatin proteins [2]. Based on the structure of Ioc3, this module is inferred to interact with nucleosomal linker DNA and the SLIDE domain of ISWI proteins [2][3]. The resulting complex forms a protein ruler that measures out the spacing between two adjacent nucleosomes [2]. In particular, the DDT domain, in combination with the WHIM1 and WHIM2 motifs form the SLIDE domain binding pocket [2].", "database": "PfamA", "aliStart": 848, "scoreName": "E-value", "accession": "PF02791.15", "start": 847, "score": 1.6e-09, "identifier": "DDT domain", "type": "DBD", "aliEnd": 908}}, {"startStyle": "jagged", "end": 991, "endStyle": "straight", "aliStart": 950, "text": "WHIM1", "colour": "#9999ff", "aliEnd": 991, "start": 948, "href": "http://pfam.xfam.org/family/PF15612.4", "type": "pfama", "display": "true", "metadata": {"end": 991, "description": "A conserved alpha helical motif that along with the WHIM2 and WHIM3 motifs, and the DDT domain comprise an alpha helical module found in diverse eukaryotic chromatin proteins [1].Based on the Ioc3 structure, this module is inferred to interact with nucleosomal linker DNA and the SLIDE domain of ISWI proteins [1][2]. The resulting complex forms a protein ruler that measures out the spacing between two adjacent nucleosomes [2]. The conserved basic residue in WHIM1 is involved in packing with the DDT motif. The module shows a great domain architectural diversity and is often combined with other modified histone peptide recognising and DNA binding domains, some of which discriminate methylated DNA [1].", "database": "PfamA", "aliStart": 950, "scoreName": "E-value", "accession": "PF15612.4", "start": 948, "score": 1.8e-05, "identifier": "WSTF, HB1, Itc1p, MBD9 motif 1", "type": "DBD", "aliEnd": 991}}], "length": 1904}
{"regions": [{"startStyle": "jagged", "end": 49, "endStyle": "curved", "aliStart": 2, "text": "MBD", "colour": "#2cb42c", "aliEnd": 47, "start": 1, "href": "http://pfam.xfam.org/family/PF01429.17", "type": "pfama", "display": "true", "metadata": {"end": 49, "description": "The Methyl-CpG binding domain (MBD) binds to DNA that contains one or more symmetrically methylated CpGs [1]. DNA methylation in animals is associated with alterations in chromatin structure and silencing of gene expression. MBD has negligible non-specific affinity for DNA. In vitro foot-printing with MeCP2 showed the MBD can protect a 12 nucleotide region surrounding a methyl CpG pair [1]. MBDs are found in several Methyl-CpG binding proteins and also DNA demethylase [2].", "database": "PfamA", "aliStart": 2, "scoreName": "E-value", "accession": "PF01429.17", "start": 1, "score": 1.4e-11, "identifier": "Methyl-CpG binding domain", "type": "DBD", "aliEnd": 47}}, {"startStyle": "curved", "end": 87, "endStyle": "curved", "aliStart": 75, "text": "AThook", "colour": "#2cb42c", "aliEnd": 86, "start": 75, "href": "http://pfam.xfam.org/family/PF02178.17", "type": "pfama", "display": "true", "metadata": {"end": 87, "description": "At hooks are DNA binding motifs with a preference for A/T rich regions.", "database": "PfamA", "aliStart": 75, "scoreName": "E-value", "accession": "PF02178.17", "start": 75, "score": 0.0022, "identifier": "AT hook motif", "type": "DBD", "aliEnd": 86}}, {"startStyle": "curved", "end": 106, "endStyle": "jagged", "aliStart": 96, "text": "AThook", "colour": "#2cb42c", "aliEnd": 105, "start": 96, "href": "http://pfam.xfam.org/family/PF02178.17", "type": "pfama", "display": "true", "metadata": {"end": 106, "description": "At hooks are DNA binding motifs with a preference for A/T rich regions.", "database": "PfamA", "aliStart": 96, "scoreName": "E-value", "accession": "PF02178.17", "start": 96, "score": 0.0022, "identifier": "AT hook motif", "type": "DBD", "aliEnd": 105}}], "length": 205}