Conclusion
Assessment
Binding Mode
Motif Status
Notes
Comments
Likely to be sequence specific TF
1 Monomer or homomultimer
No motif
Description
Description:
THAP domain containing 5 [Source:HGNC Symbol;Acc:HGNC:23188]
Entrez Summary
TBA
Ensembl ID:
ENSG00000177683
External Link:
T152767_1.02
Interpro
IPR006612 ; ;
Protein Domain:
Protein: ENSP00000322440DBD: THAPOther: ADIPProtein: ENSP00000400500DBD: THAPOther: ADIPProtein: ENSP00000415841DBD: THAPOther:
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.
c
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
{"regions": [{"startStyle": "jagged", "end": 42, "endStyle": "curved", "aliStart": 3, "text": "THAP", "colour": "#009900", "aliEnd": 42, "start": 1, "href": "http://pfam.xfam.org/family/PF05485.10", "type": "pfama", "display": "true", "metadata": {"end": 42, "description": "The THAP domain is a putative DNA-binding domain (DBD) and probably also binds a zinc ion. It features the conserved C2CH architecture (consensus sequence: Cys - 2-4 residues - Cys - 35-50 residues - Cys - 2 residues - His). Other universal features include the location of the domain at the N-termini of proteins, its size of about 90 residues, a C-terminal AVPTIF box and several other conserved residues. Orthologues of the human THAP domain have been identified in other vertebrates and probably worms and flies, but not in other eukaryotes or any prokaryotes [1].", "database": "PfamA", "aliStart": 3, "scoreName": "E-value", "accession": "PF05485.10", "start": 1, "score": 9.6e-05, "identifier": "THAP domain", "type": "DBD", "aliEnd": 42}}, {"startStyle": "jagged", "end": 348, "endStyle": "jagged", "aliStart": 273, "text": "ADIP", "colour": "#9999ff", "aliEnd": 345, "start": 269, "href": "http://pfam.xfam.org/family/PF11559.6", "type": "pfama", "display": "true", "metadata": {"end": 348, "description": "This family is found in mammals where it is localised at cell-cell adherens junctions [1], and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules [2]. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins Localised at Cell-Cell Adherens Junctions.", "database": "PfamA", "aliStart": 273, "scoreName": "E-value", "accession": "PF11559.6", "start": 269, "score": 0.0014, "identifier": "Afadin- and alpha -actinin-Binding", "type": "DBD", "aliEnd": 345}}], "length": 354}
{"regions": [{"startStyle": "curved", "end": 84, "endStyle": "curved", "aliStart": 5, "text": "THAP", "colour": "#009900", "aliEnd": 84, "start": 5, "href": "http://pfam.xfam.org/family/PF05485.10", "type": "pfama", "display": "true", "metadata": {"end": 84, "description": "The THAP domain is a putative DNA-binding domain (DBD) and probably also binds a zinc ion. It features the conserved C2CH architecture (consensus sequence: Cys - 2-4 residues - Cys - 35-50 residues - Cys - 2 residues - His). Other universal features include the location of the domain at the N-termini of proteins, its size of about 90 residues, a C-terminal AVPTIF box and several other conserved residues. Orthologues of the human THAP domain have been identified in other vertebrates and probably worms and flies, but not in other eukaryotes or any prokaryotes [1].", "database": "PfamA", "aliStart": 5, "scoreName": "E-value", "accession": "PF05485.10", "start": 5, "score": 1.1e-15, "identifier": "THAP domain", "type": "DBD", "aliEnd": 84}}, {"startStyle": "jagged", "end": 390, "endStyle": "jagged", "aliStart": 315, "text": "ADIP", "colour": "#9999ff", "aliEnd": 387, "start": 311, "href": "http://pfam.xfam.org/family/PF11559.6", "type": "pfama", "display": "true", "metadata": {"end": 390, "description": "This family is found in mammals where it is localised at cell-cell adherens junctions [1], and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules [2]. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins Localised at Cell-Cell Adherens Junctions.", "database": "PfamA", "aliStart": 315, "scoreName": "E-value", "accession": "PF11559.6", "start": 311, "score": 0.0017, "identifier": "Afadin- and alpha -actinin-Binding", "type": "DBD", "aliEnd": 387}}], "length": 396}
{"regions": [{"startStyle": "curved", "end": 54, "endStyle": "jagged", "aliStart": 5, "text": "THAP", "colour": "#009900", "aliEnd": 52, "start": 5, "href": "http://pfam.xfam.org/family/PF05485.10", "type": "pfama", "display": "true", "metadata": {"end": 54, "description": "The THAP domain is a putative DNA-binding domain (DBD) and probably also binds a zinc ion. It features the conserved C2CH architecture (consensus sequence: Cys - 2-4 residues - Cys - 35-50 residues - Cys - 2 residues - His). Other universal features include the location of the domain at the N-termini of proteins, its size of about 90 residues, a C-terminal AVPTIF box and several other conserved residues. Orthologues of the human THAP domain have been identified in other vertebrates and probably worms and flies, but not in other eukaryotes or any prokaryotes [1].", "database": "PfamA", "aliStart": 5, "scoreName": "E-value", "accession": "PF05485.10", "start": 5, "score": 5.7999999999999997e-08, "identifier": "THAP domain", "type": "DBD", "aliEnd": 52}}], "length": 56}