Conclusion
Assessment
Binding Mode
Motif Status
Notes
Comments
Likely to be sequence specific TF
1 Monomer or homomultimer
No motif
Binds DNA as a homodimer, recognizing a TGTCRSWWYYGWC consensus based on SELEX experiments (PMID: 22926524)
Description
Description:
NACC family member 2 [Source:HGNC Symbol;Acc:HGNC:23846];Nucleus accumbens-associated protein 2
Entrez Summary
TBA
Ensembl ID:
ENSG00000148411
External Link:
Interpro
IPR000210 ; IPR011333 ; IPR013069 ; IPR018379 ;
Protein Domain:
Protein: ENSP00000277554DBD: OtherOther: BEN, BTBProtein: ENSP00000360818DBD: OtherOther: BEN, BTB
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.
No
CisBP considers it as a TF?
No
TFclass considers it as a TF?
No
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:22926524
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
5a, one of the source datasets predicts is as a TF
TF has conditional DNA-binding requirements
DNA-Binding
Published Motif Data
Structure
Experimental History
{"regions": [{"startStyle": "straight", "end": 122, "endStyle": "straight", "aliStart": 20, "text": "BTB", "colour": "#9999ff", "aliEnd": 116, "start": 20, "href": "http://pfam.xfam.org/family/PF00651.29", "type": "pfama", "display": "true", "metadata": {"end": 122, "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": 20, "scoreName": "E-value", "accession": "PF00651.29", "start": 20, "score": 2e-23, "identifier": "BTB/POZ domain", "type": "DBD", "aliEnd": 116}}, {"startStyle": "straight", "end": 458, "endStyle": "jagged", "aliStart": 376, "text": "BEN", "colour": "#9999ff", "aliEnd": 431, "start": 375, "href": "http://pfam.xfam.org/family/PF10523.7", "type": "pfama", "display": "true", "metadata": {"end": 458, "description": "The BEN domain is found in diverse animal proteins such as BANP/SMAR1, NAC1 and the Drosophila mod(mdg4) isoform C, in the chordopoxvirus virosomal protein E5R and in several proteins of polydnaviruses. Computational analysis suggests that the BEN domain mediates protein-DNA and protein-protein interactions during chromatin organisation and transcription [1].", "database": "PfamA", "aliStart": 376, "scoreName": "E-value", "accession": "PF10523.7", "start": 375, "score": 1e-09, "identifier": "BEN domain", "type": "DBD", "aliEnd": 431}}], "length": 588}
{"regions": [{"startStyle": "straight", "end": 122, "endStyle": "straight", "aliStart": 20, "text": "BTB", "colour": "#9999ff", "aliEnd": 116, "start": 20, "href": "http://pfam.xfam.org/family/PF00651.29", "type": "pfama", "display": "true", "metadata": {"end": 122, "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": 20, "scoreName": "E-value", "accession": "PF00651.29", "start": 20, "score": 2e-23, "identifier": "BTB/POZ domain", "type": "DBD", "aliEnd": 116}}, {"startStyle": "straight", "end": 458, "endStyle": "jagged", "aliStart": 376, "text": "BEN", "colour": "#9999ff", "aliEnd": 431, "start": 375, "href": "http://pfam.xfam.org/family/PF10523.7", "type": "pfama", "display": "true", "metadata": {"end": 458, "description": "The BEN domain is found in diverse animal proteins such as BANP/SMAR1, NAC1 and the Drosophila mod(mdg4) isoform C, in the chordopoxvirus virosomal protein E5R and in several proteins of polydnaviruses. Computational analysis suggests that the BEN domain mediates protein-DNA and protein-protein interactions during chromatin organisation and transcription [1].", "database": "PfamA", "aliStart": 376, "scoreName": "E-value", "accession": "PF10523.7", "start": 375, "score": 1e-09, "identifier": "BEN domain", "type": "DBD", "aliEnd": 431}}], "length": 588}