The Human Transcription Factors

Conclusion

Assessment	Binding Mode	Motif Status	Notes	Comments
Known motif	1 Monomer or homomultimer	In vivo/Misc source		Likely binds as a homodimer

Description

Description:	THAP domain containing 1 [Source:HGNC Symbol;Acc:HGNC:20856]
Entrez Summary	TBA
Ensembl ID:	ENSG00000131931
External Link:
Interpro	IPR006612; ;
Protein Domain:
Protein: ENSP00000254250	DBD: THAP	Other: ADIP, APG6, ATG16, CENP-Q, Cep57_CLD, DUF4391, MPS
Protein: ENSP00000344966	DBD: THAP	Other:
Protein: ENSP00000433912	DBD: THAP	Other:

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	1a1, Direct HQ evidence
TF has conditional DNA-binding requirements

DNA-Binding

Published Motif Data

Source	Annotation	Motif	Evidence
ChIP-seq	ENCODE		Direct
ChIP-seq	JASPAR		Direct
Transfac	Transfac	License required	Direct
Transfac	Transfac	License required	Direct

Structure

Structure	PDB	2KO0

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": 81, "endStyle": "curved", "aliStart": 5, "text": "THAP", "colour": "#009900", "aliEnd": 81, "start": 5, "href": "http://pfam.xfam.org/family/PF05485.10", "type": "pfama", "display": "true", "metadata": {"end": 81, "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": 2.4e-17, "identifier": "THAP domain", "type": "DBD", "aliEnd": 81}}, {"startStyle": "jagged", "end": 204, "endStyle": "jagged", "aliStart": 139, "text": "Cep57_CLD", "colour": "#9999ff", "aliEnd": 195, "start": 129, "href": "http://pfam.xfam.org/family/PF14073.4", "type": "pfama", "display": "true", "metadata": {"end": 204, "description": "The CLD or centrosome localisation domain of Cep57 is found at the N-terminus, and lies approximately between residues 58 and 239. This region lies within the first alpha-helical coiled-coil segment of Cep57, and localises to the centrosome internally to gamma-tubulin, suggesting that it is either on both centrioles or on a centromatrix component.  This N-terminal region can also multimerise with the N-terminus of other Cep57 molecules.  The C-terminal part, Family Cep57_MT_bd, Pfam:PF06657, is the microtubule-binding region of Cep57.", "database": "PfamA", "aliStart": 139, "scoreName": "E-value", "accession": "PF14073.4", "start": 129, "score": 1.1e-05, "identifier": "Centrosome localisation domain of Cep57", "type": "DBD", "aliEnd": 195}}, {"startStyle": "jagged", "end": 196, "endStyle": "straight", "aliStart": 144, "text": "Sec2p", "colour": "#9999ff", "aliEnd": 193, "start": 130, "href": "http://pfam.xfam.org/family/PF06428.9", "type": "pfama", "display": "true", "metadata": {"end": 196, "description": "In Saccharomyces cerevisiae,  Sec2p is a GDP/GTP exchange factor for Sec4p, which is required for vesicular transport at the post-Golgi stage of yeast secretion [1].", "database": "PfamA", "aliStart": 144, "scoreName": "E-value", "accession": "PF06428.9", "start": 130, "score": 0.00023999999999999998, "identifier": "GDP/GTP exchange factor Sec2p", "type": "DBD", "aliEnd": 193}}, {"startStyle": "jagged", "end": 197, "endStyle": "jagged", "aliStart": 141, "text": "ATG16", "colour": "#9999ff", "aliEnd": 191, "start": 79, "href": "http://pfam.xfam.org/family/PF08614.9", "type": "pfama", "display": "true", "metadata": {"end": 197, "description": "Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells.                                During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway [1].", "database": "PfamA", "aliStart": 141, "scoreName": "E-value", "accession": "PF08614.9", "start": 79, "score": 0.00045, "identifier": "Autophagy protein 16 (ATG16)", "type": "DBD", "aliEnd": 191}}, {"startStyle": "jagged", "end": 204, "endStyle": "jagged", "aliStart": 143, "text": "MPS2", "colour": "#9999ff", "aliEnd": 198, "start": 125, "href": "http://pfam.xfam.org/family/PF17060.3", "type": "pfama", "display": "true", "metadata": {"end": 204, "description": "Is a fungal transmembrane protein which is part of the component of the spindle pole body (SPB) required for the insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication [1,2,3,4,5,7,8]. It seems that Mps2-Spc24 interaction may contribute to the localisation of Spc24 and other kinetochore components to the inner plaque of the SPB [6].", "database": "PfamA", "aliStart": 143, "scoreName": "E-value", "accession": "PF17060.3", "start": 125, "score": 0.0012, "identifier": "Monopolar spindle protein 2", "type": "DBD", "aliEnd": 198}}, {"startStyle": "jagged", "end": 204, "endStyle": "jagged", "aliStart": 130, "text": "CENP-Q", "colour": "#9999ff", "aliEnd": 190, "start": 97, "href": "http://pfam.xfam.org/family/PF13094.4", "type": "pfama", "display": "true", "metadata": {"end": 204, "description": "CENP-Q is one of the components that assembles onto the CENPA-nucleosome distal (CAD) centromere. The centromere, which is the basic element of chromosome inheritance, is epigenetically determined in mammals. CENP-A, the centromere-specific histone H3 variant, assembles an array of nucleosomes and it is this that seems to be the prime candidate for specifying centromere identity. CENPA nucleosomes directly recruit a proximal CENPA-nucleosome-associated complex (NAC) comprised of CENP-M, CENP-N and CENP-T, CENP-U(50), CENP-C and CENP-H. Assembly of the CENPA NAC at centromeres is dependent on CENP-M, CENP-N and CENP-T. Additionally, there are seven other subunits which make up the CENPA-nucleosome distal (CAD) centromere, CENP-K, CENP-L, CENP-O, CENP-P, CENP-Q, CENP-R and CENP-S, also assembling on the CENP-A NAC [2]. Fta7 is the equivalent component of the fission yeast Sim4 complex [1].", "database": "PfamA", "aliStart": 130, "scoreName": "E-value", "accession": "PF13094.4", "start": 97, "score": 0.0048, "identifier": "CENP-Q, a CENPA-CAD centromere complex subunit", "type": "DBD", "aliEnd": 190}}, {"startStyle": "jagged", "end": 199, "endStyle": "jagged", "aliStart": 140, "text": "APG6", "colour": "#9999ff", "aliEnd": 188, "start": 103, "href": "http://pfam.xfam.org/family/PF04111.10", "type": "pfama", "display": "true", "metadata": {"end": 199, "description": "In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in  eukaryotic cells [1]. Apg6/Vps30p has two distinct functions in the autophagic process, either associated with the membrane or in a retrieval step of the  carboxypeptidase Y sorting pathway [2].", "database": "PfamA", "aliStart": 140, "scoreName": "E-value", "accession": "PF04111.10", "start": 103, "score": 0.0058, "identifier": "Autophagy protein Apg6", "type": "DBD", "aliEnd": 188}}, {"startStyle": "jagged", "end": 196, "endStyle": "jagged", "aliStart": 141, "text": "ADIP", "colour": "#9999ff", "aliEnd": 189, "start": 134, "href": "http://pfam.xfam.org/family/PF11559.6", "type": "pfama", "display": "true", "metadata": {"end": 196, "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": 141, "scoreName": "E-value", "accession": "PF11559.6", "start": 134, "score": 0.0059, "identifier": "Afadin- and alpha -actinin-Binding", "type": "DBD", "aliEnd": 189}}, {"startStyle": "jagged", "end": 185, "endStyle": "straight", "aliStart": 131, "text": "DUF4391", "colour": "#9999ff", "aliEnd": 181, "start": 122, "href": "http://pfam.xfam.org/family/PF14335.4", "type": "pfama", "display": "true", "metadata": {"end": 185, "description": "This family of proteins is functionally uncharacterised. This family of proteins is found in bacteria and archaea. Proteins in this family are typically between 220 and 257 amino acids in length.", "database": "PfamA", "aliStart": 131, "scoreName": "E-value", "accession": "PF14335.4", "start": 122, "score": 0.0068, "identifier": "Domain of unknown function (DUF4391)", "type": "DBD", "aliEnd": 181}}, {"startStyle": "jagged", "end": 196, "endStyle": "straight", "aliStart": 143, "text": "PI3K_P85_iSH2", "colour": "#9999ff", "aliEnd": 195, "start": 134, "href": "http://pfam.xfam.org/family/PF16454.3", "type": "pfama", "display": "true", "metadata": {"end": 196, "description": "This domain is found between the two SH2 domains in phosphatidylinositol 3-kinase regulatory subunit P85. It forms a complex with the adaptor-binding domain of phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha [1].", "database": "PfamA", "aliStart": 143, "scoreName": "E-value", "accession": "PF16454.3", "start": 134, "score": 0.0083, "identifier": "Phosphatidylinositol 3-kinase regulatory subunit P85 inter-SH2 domain", "type": "DBD", "aliEnd": 195}}], "length": 214}

TF Info Page for THAP1 (THAP finger)