Conclusion
Assessment
Binding Mode
Motif Status
Notes
Comments
Likely to be sequence specific TF
1 Monomer or homomultimer
No motif
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.
b
CisBP considers it as a TF?
Yes
TFclass considers it as a TF?
Yes
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": "jagged", "end": 313, "endStyle": "curved", "aliStart": 260, "text": "SAND", "colour": "#2cb42c", "aliEnd": 313, "start": 255, "href": "http://pfam.xfam.org/family/PF01342.19", "type": "pfama", "display": "true", "metadata": {"end": 313, "description": "The DNA binding activity of two proteins has been mapped to the SAND domain. The conserved KDWK motif is necessary for DNA binding, and it appears to be important for dimerisation [2]. This region is also found in the putative transcription factor RegA from the multicellular green alga Volvox cateri. This region of RegA is known as the VARL domain [3].", "database": "PfamA", "aliStart": 260, "scoreName": "E-value", "accession": "PF01342.19", "start": 255, "score": 4.0000000000000004e-20, "identifier": "SAND domain", "type": "DBD", "aliEnd": 313}}, {"startStyle": "straight", "end": 122, "endStyle": "straight", "aliStart": 25, "text": "HSR", "colour": "#9999ff", "aliEnd": 121, "start": 24, "href": "http://pfam.xfam.org/family/PF03172.11", "type": "pfama", "display": "true", "metadata": {"end": 122, "description": "The Sp100 protein is a constituent of nuclear domains, also known as nuclear dots (NDs). An ND-targeting region that coincides with a homodimerization domain was mapped in Sp100. Sequences similar to the Sp100 homodimerization/ND-targeting region occur in several other proteins and constitute a novel protein motif, termed HSR domain (for homogeneously-staining region) [2]. The HSR domain has also been named ASS (AIRE, Sp-100 and Sp140) [3]. This domain is usually found at the amino terminus of proteins that contain a SAND domain Pfam:PF01342.", "database": "PfamA", "aliStart": 25, "scoreName": "E-value", "accession": "PF03172.11", "start": 24, "score": 1.0999999999999999e-44, "identifier": "HSR domain", "type": "DBD", "aliEnd": 121}}, {"startStyle": "jagged", "end": 495, "endStyle": "jagged", "aliStart": 446, "text": "Bromodomain", "colour": "#9999ff", "aliEnd": 488, "start": 417, "href": "http://pfam.xfam.org/family/PF00439.23", "type": "pfama", "display": "true", "metadata": {"end": 495, "description": "Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine [3].", "database": "PfamA", "aliStart": 446, "scoreName": "E-value", "accession": "PF00439.23", "start": 417, "score": 6.900000000000001e-08, "identifier": "Bromodomain", "type": "DBD", "aliEnd": 488}}, {"startStyle": "straight", "end": 389, "endStyle": "straight", "aliStart": 346, "text": "PHD", "colour": "#9999ff", "aliEnd": 388, "start": 345, "href": "http://pfam.xfam.org/family/PF00628.27", "type": "pfama", "display": "true", "metadata": {"end": 389, "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": 346, "scoreName": "E-value", "accession": "PF00628.27", "start": 345, "score": 1.6e-07, "identifier": "PHD-finger", "type": "DBD", "aliEnd": 388}}], "length": 521}
{"regions": [{"startStyle": "jagged", "end": 60, "endStyle": "straight", "aliStart": 1, "text": "HSR", "colour": "#9999ff", "aliEnd": 59, "start": 1, "href": "http://pfam.xfam.org/family/PF03172.11", "type": "pfama", "display": "true", "metadata": {"end": 60, "description": "The Sp100 protein is a constituent of nuclear domains, also known as nuclear dots (NDs). An ND-targeting region that coincides with a homodimerization domain was mapped in Sp100. Sequences similar to the Sp100 homodimerization/ND-targeting region occur in several other proteins and constitute a novel protein motif, termed HSR domain (for homogeneously-staining region) [2]. The HSR domain has also been named ASS (AIRE, Sp-100 and Sp140) [3]. This domain is usually found at the amino terminus of proteins that contain a SAND domain Pfam:PF01342.", "database": "PfamA", "aliStart": 1, "scoreName": "E-value", "accession": "PF03172.11", "start": 1, "score": 7.299999999999999e-24, "identifier": "HSR domain", "type": "DBD", "aliEnd": 59}}], "length": 130}