The Human Transcription Factors

Conclusion

Assessment	Binding Mode	Motif Status	Notes	Comments
Known motif	1 Monomer or homomultimer	High-throughput in vitro		Based on Newman et al 2003 (PMID: 12805554), the protein has strong preference for forming heterodimers with MAFG and MAFK over homo-dimerisation. The Homer ChIP-seq motif appears to be a MAF-BACH2 heterodimer.

Description

Description:	BTB domain and CNC homolog 2 [Source:HGNC Symbol;Acc:HGNC:14078]
Entrez Summary	TBA
Ensembl ID:	ENSG00000112182
External Link:	T025274_1.02
Interpro	IPR000210; IPR004826; IPR004827; IPR008917; IPR011333; IPR013069;
Protein Domain:
Protein: ENSP00000257749	DBD: bZIP	Other: BTB
Protein: ENSP00000437473	DBD: bZIP	Other: BTB
Protein: ENSP00000384145	DBD: bZIP	Other: BTB

Previous Annotations

Source	Annotation
TF-CAT classification	TF Gene_DNA-Binding sequence-specific_DNA Binding Transactivation_ PMIDS:8887638 10949928
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:0001206 RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity involv IEA - GO_REF:0000019 GO:0003700 sequence-specific DNA binding transcription factor activity IBA - GO_REF:0000033
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

Source	Annotation	Motif	Evidence
HT-SELEX	Yin2017		Direct
HT-SELEX	Yin2017		Direct
Methyl-HT-SELEX	Yin2017		Direct
Transfac	Transfac	License required	Direct
Misc	HOMER		Direct
ChIP-seq	modENCODE		Inferred - BACH1 (68% AA Identity, Homo sapiens)
ChIP-seq	modENCODE		Inferred - BACH1 (68% AA Identity, Homo sapiens)
ChIP-seq	modENCODE		Inferred - BACH1 (68% AA Identity, Homo sapiens)
Transfac	Transfac	License required	Inferred - BACH1 (68% AA Identity, Homo sapiens)
Transfac	Transfac	License required	Inferred - BACH1 (68% AA Identity, Homo sapiens)
Misc	HocoMoco		Inferred - BACH1 (68% AA Identity, Homo sapiens)
Misc	HOMER		Inferred - BACH1 (68% AA Identity, Homo sapiens)

Structure

Structure	PDB	Not_Covered

Experimental History

Method	Constructs
Tried in PBM? (Whether the protein was tried in PBM or not)
Tried in HT-SELEX (Whether the protein was tried in HT-SELEX or not, and if so, then what kind of clones were tested)
Other Information? (Tried with another method and failed?)

External Contribution

Name
Email
Comment
Reference

{"regions": [{"startStyle": "curved", "end": 709, "endStyle": "jagged", "aliStart": 618, "text": "MAF", "colour": "#FFD800", "aliEnd": 696, "start": 617, "href": "http://pfam.xfam.org/family/PF03131.15", "type": "pfama", "display": "true", "metadata": {"end": 709, "description": "Maf transcription factors contain a conserved basic region leucine zipper (bZIP) domain, which mediates their dimerisation and DNA binding property [1]. Thus, this family is probably related to Pfam:PF00170. This family also includes the DNA_binding domain of Skn-1 (Swiss:P34707), this domain lacks the leucine zipper found in other bZip domains, and binds DNA is a monomer [2,3].", "database": "PfamA", "aliStart": 618, "scoreName": "E-value", "accession": "PF03131.15", "start": 617, "score": 4.8e-13, "identifier": "bZIP Maf transcription factor", "type": "DBD", "aliEnd": 696}}, {"startStyle": "jagged", "end": 707, "endStyle": "curved", "aliStart": 651, "text": "bZIP", "colour": "#009900", "aliEnd": 704, "start": 647, "href": "http://pfam.xfam.org/family/PF00170.19", "type": "pfama", "display": "true", "metadata": {"end": 707, "description": "The Pfam entry includes the basic region and the leucine zipper region.", "database": "PfamA", "aliStart": 651, "scoreName": "E-value", "accession": "PF00170.19", "start": 647, "score": 2.0999999999999998e-09, "identifier": "bZIP transcription factor", "type": "DBD", "aliEnd": 704}}, {"startStyle": "straight", "end": 133, "endStyle": "straight", "aliStart": 27, "text": "BTB", "colour": "#9999ff", "aliEnd": 132, "start": 27, "href": "http://pfam.xfam.org/family/PF00651.29", "type": "pfama", "display": "true", "metadata": {"end": 133, "description": "The BTB (for BR-C, ttk and bab) [1] or POZ (for Pox virus and Zinc finger) [2] domain is present near the N-terminus of a fraction of zinc finger (Pfam:PF00096) proteins and in proteins that contain the Pfam:PF01344 motif such as Kelch and a family of pox virus proteins. The BTB/POZ domain mediates homomeric dimerisation and in some instances heteromeric dimerisation [2]. The structure of the dimerised PLZF BTB/POZ domain has been solved and consists of a tightly intertwined homodimer.  The central scaffolding of the protein is made up of a cluster of alpha-helices flanked by short beta-sheets at both the top and bottom of the molecule [3]. POZ domains from several zinc finger proteins have been shown to mediate transcriptional repression and to interact with components of histone deacetylase co-repressor complexes including N-CoR and SMRT [4,5,6]. The POZ or BTB domain is also known as BR-C/Ttk or ZiN.", "database": "PfamA", "aliStart": 27, "scoreName": "E-value", "accession": "PF00651.29", "start": 27, "score": 1.7e-27, "identifier": "BTB/POZ domain", "type": "DBD", "aliEnd": 132}}], "length": 842}

{"regions": [{"startStyle": "straight", "end": 81, "endStyle": "jagged", "aliStart": 27, "text": "BTB", "colour": "#9999ff", "aliEnd": 73, "start": 27, "href": "http://pfam.xfam.org/family/PF00651.29", "type": "pfama", "display": "true", "metadata": {"end": 81, "description": "The BTB (for BR-C, ttk and bab) [1] or POZ (for Pox virus and Zinc finger) [2] domain is present near the N-terminus of a fraction of zinc finger (Pfam:PF00096) proteins and in proteins that contain the Pfam:PF01344 motif such as Kelch and a family of pox virus proteins. The BTB/POZ domain mediates homomeric dimerisation and in some instances heteromeric dimerisation [2]. The structure of the dimerised PLZF BTB/POZ domain has been solved and consists of a tightly intertwined homodimer.  The central scaffolding of the protein is made up of a cluster of alpha-helices flanked by short beta-sheets at both the top and bottom of the molecule [3]. POZ domains from several zinc finger proteins have been shown to mediate transcriptional repression and to interact with components of histone deacetylase co-repressor complexes including N-CoR and SMRT [4,5,6]. The POZ or BTB domain is also known as BR-C/Ttk or ZiN.", "database": "PfamA", "aliStart": 27, "scoreName": "E-value", "accession": "PF00651.29", "start": 27, "score": 5.3e-15, "identifier": "BTB/POZ domain", "type": "DBD", "aliEnd": 73}}], "length": 81}

TF Info Page for BACH2 (bZIP)