The Human Transcription Factors

Conclusion

Assessment	Binding Mode	Motif Status	Notes	Comments
Known motif	1 Monomer or homomultimer	In vivo/Misc source	Only known motifs are from Transfac or HocoMoco - origin is uncertain

Description

Description:	TOP1 binding arginine/serine rich protein [Source:HGNC Symbol;Acc:HGNC:21653]
Entrez Summary	TBA
Ensembl ID:	ENSG00000197579
External Link:	T153711_1.02
Interpro	IPR001841; IPR017907; IPR018957;
Protein Domain:
Protein: ENSP00000353735	DBD: Other	Other: Prok-RING_4, zf-ANAPC11, zf-C3HC4, zf-C3HC4_2, zf-
Protein: ENSP00000369187	DBD: Other	Other: Prok-RING_4, zf-ANAPC11, zf-C3HC4, zf-C3HC4_2, zf-

Previous Annotations

Source	Annotation
TF-CAT classification	TF Gene_Single stranded RNA/DNA binding_DNA Binding_ PMIDS:11278651 15735665
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?	Yes
TFclass considers it as a TF?	No
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	2a1, Lower confidence direct evidence
TF has conditional DNA-binding requirements

DNA-Binding

Published Motif Data

Source	Annotation	Motif	Evidence
Transfac	Transfac	License required	Direct

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

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The protein, of which this domain is the conserved region, participates in diverse functions relevant to chromosome metabolism and cell cycle control [1].", "database": "PfamA", "aliStart": 101, "scoreName": "E-value", "accession": "PF12678.5", "start": 94, "score": 1.3000000000000001e-05, "identifier": "RING-H2 zinc finger domain", "type": "DBD", "aliEnd": 142}}, {"startStyle": "straight", "end": 143, "endStyle": "straight", "aliStart": 102, "text": "zf-RING_5", "colour": "#9999ff", "aliEnd": 143, "start": 102, "href": "http://pfam.xfam.org/family/PF14634.4", "type": "pfama", "display": "true", "metadata": {"end": 143, "description": NaN, "database": "PfamA", "aliStart": 102, "scoreName": "E-value", "accession": "PF14634.4", "start": 102, "score": 5e-05, "identifier": "zinc-RING finger domain", "type": "DBD", "aliEnd": 143}}, {"startStyle": "straight", "end": 141, "endStyle": "straight", "aliStart": 103, "text": "zf-C3HC4_4", "colour": "#9999ff", "aliEnd": 141, "start": 103, "href": "http://pfam.xfam.org/family/PF15227.4", "type": "pfama", "display": "true", "metadata": {"end": 141, "description": "This is a family of primate-specific Ret finger protein-like (RFPL) zinc-fingers of the C3HC4 type. Ret finger protein-like proteins are primate-specific target genes of Pax6, a key transcription factor for pancreas, eye and neocortex development [1]. This domain is likely to be DNA-binding [2]. This zinc-finger domain together with the RDM domain, Pfam:PF11002, forms a large zinc-finger structure of the RING/U-Box superfamily. RING-containing proteins are known to exert an E3 ubiquitin protein ligase activity with the zinc-finger structure being mandatory for binding to the E2 ubiquitin-conjugating enzyme [3].", "database": "PfamA", "aliStart": 103, "scoreName": "E-value", "accession": "PF15227.4", "start": 103, "score": 5.9e-05, "identifier": "zinc finger of C3HC4-type, RING", "type": "DBD", "aliEnd": 141}}, {"startStyle": "jagged", "end": 148, "endStyle": "straight", "aliStart": 100, "text": "zf-ANAPC11", "colour": "#9999ff", "aliEnd": 145, "start": 91, "href": "http://pfam.xfam.org/family/PF12861.5", "type": "pfama", "display": "true", "metadata": {"end": 148, "description": "Apc11 is one of the subunits of the anaphase-promoting complex or cyclosome [1]. The APC subunits are cullin family proteins with ubiquitin ligase activity [2]. Polyubiquitination marks proteins for degradation by the 26S proteasome and is carried out by a cascade of enzymes that includes ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s), and ubiquitin ligases (E3s). Apc11 acts as an E3 enzyme and is responsible for recruiting E2s to the APC and for mediating the subsequent transfer of ubiquitin to APC substrates in vivo. In Saccharomyces cerevisiae this RING-H2 finger protein defines the minimal ubiquitin ligase activity of the APC, and the integrity of the RING-H2 finger is essential for budding yeast cell viability [3].", "database": "PfamA", "aliStart": 100, "scoreName": "E-value", "accession": "PF12861.5", "start": 91, "score": 0.0033, "identifier": "Anaphase-promoting complex subunit 11 RING-H2 finger", "type": "DBD", "aliEnd": 145}}, {"startStyle": "straight", "end": 149, "endStyle": "jagged", "aliStart": 103, "text": "Prok-RING_4", "colour": "#9999ff", "aliEnd": 145, "start": 103, "href": "http://pfam.xfam.org/family/PF14447.4", "type": "pfama", "display": "true", "metadata": {"end": 149, "description": "RING finger family domain found sporadically in bacteria. The finger is fused to an N-terminal alpha-helical domain, ROT/Trove-like repeats and a C-terminal TerD domain [1]. The architecture suggests a possible role in an RNA-processing complex [1].", "database": "PfamA", "aliStart": 103, "scoreName": "E-value", "accession": "PF14447.4", "start": 103, "score": 0.0045, "identifier": "Prokaryotic RING finger family 4", "type": "DBD", "aliEnd": 145}}], "length": 1046}

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Polyubiquitination marks proteins for degradation by the 26S proteasome and is carried out by a cascade of enzymes that includes ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s), and ubiquitin ligases (E3s). Apc11 acts as an E3 enzyme and is responsible for recruiting E2s to the APC and for mediating the subsequent transfer of ubiquitin to APC substrates in vivo. In Saccharomyces cerevisiae this RING-H2 finger protein defines the minimal ubiquitin ligase activity of the APC, and the integrity of the RING-H2 finger is essential for budding yeast cell viability [3].", "database": "PfamA", "aliStart": 35, "scoreName": "E-value", "accession": "PF12861.5", "start": 27, "score": 0.0028, "identifier": "Anaphase-promoting complex subunit 11 RING-H2 finger", "type": "DBD", "aliEnd": 80}}, {"startStyle": "straight", "end": 84, "endStyle": "jagged", "aliStart": 38, "text": "Prok-RING_4", "colour": "#9999ff", "aliEnd": 80, "start": 38, "href": "http://pfam.xfam.org/family/PF14447.4", "type": "pfama", "display": "true", "metadata": {"end": 84, "description": "RING finger family domain found sporadically in bacteria. The finger is fused to an N-terminal alpha-helical domain, ROT/Trove-like repeats and a C-terminal TerD domain [1]. 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TF Info Page for TOPORS (Unknown)