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	Binds to TTATTA and tandem repeats of ATTGGTTA (PMID: 11533054)

Description

Description:	autoimmune regulator [Source:HGNC Symbol;Acc:HGNC:360]
Entrez Summary	TBA
Ensembl ID:	ENSG00000160224
External Link:
Interpro	IPR000770; IPR001965; IPR004865; IPR008087; IPR010919; IPR011011; IPR019786; IPR019787;
Protein Domain:
Protein: ENSP00000291582	DBD: SAND	Other: HSR, PHD, PHD_2, zf-HC5HC2H

Previous Annotations

Source	Annotation
TF-CAT classification	TF Gene Candidate_DNA-Binding sequence-specific_DNA Binding_ PMIDS:10022980 10049735 12376594 10748110 11274163 11533054 10748110 15649436 10677297 15649436
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.	a
CisBP considers it as a TF?	Yes
TFclass considers it as a TF?	Yes
Has GO:0003700 "transcription factor activity, sequence-specific DNA binding"	Yes
GO-Info	GO:0001228 RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor IC - GO_REF:0000036
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
Transfac	Transfac	License required	Direct
Misc	HocoMoco		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

{"regions": [{"startStyle": "jagged", "end": 249, "endStyle": "jagged", "aliStart": 204, "text": "SAND", "colour": "#2cb42c", "aliEnd": 244, "start": 197, "href": "http://pfam.xfam.org/family/PF01342.19", "type": "pfama", "display": "true", "metadata": {"end": 249, "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": 204, "scoreName": "E-value", "accession": "PF01342.19", "start": 197, "score": 4.1e-06, "identifier": "SAND domain", "type": "DBD", "aliEnd": 244}}, {"startStyle": "straight", "end": 103, "endStyle": "straight", "aliStart": 4, "text": "HSR", "colour": "#9999ff", "aliEnd": 102, "start": 3, "href": "http://pfam.xfam.org/family/PF03172.11", "type": "pfama", "display": "true", "metadata": {"end": 103, "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": 4, "scoreName": "E-value", "accession": "PF03172.11", "start": 3, "score": 8e-25, "identifier": "HSR domain", "type": "DBD", "aliEnd": 102}}, {"startStyle": "straight", "end": 343, "endStyle": "straight", "aliStart": 299, "text": "PHD", "colour": "#9999ff", "aliEnd": 342, "start": 298, "href": "http://pfam.xfam.org/family/PF00628.27", "type": "pfama", "display": "true", "metadata": {"end": 343, "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": 299, "scoreName": "E-value", "accession": "PF00628.27", "start": 298, "score": 4.8e-15, "identifier": "PHD-finger", "type": "DBD", "aliEnd": 342}}, {"startStyle": "straight", "end": 478, "endStyle": "straight", "aliStart": 433, "text": "PHD", "colour": "#9999ff", "aliEnd": 476, "start": 433, "href": "http://pfam.xfam.org/family/PF00628.27", "type": "pfama", "display": "true", "metadata": {"end": 478, "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": 433, "scoreName": "E-value", "accession": "PF00628.27", "start": 433, "score": 4.8e-15, "identifier": "PHD-finger", "type": "DBD", "aliEnd": 476}}, {"startStyle": "jagged", "end": 326, "endStyle": "jagged", "aliStart": 292, "text": "zf-HC5HC2H", "colour": "#9999ff", "aliEnd": 323, "start": 287, "href": "http://pfam.xfam.org/family/PF13771.4", "type": "pfama", "display": "true", "metadata": {"end": 326, "description": "The members of this family are annotated as containing PHD domain, but the zinc-binding region here is not typical of PHD domains.  The conformation here is a well-conserved cysteine-histidine rich region spanning 90 residues, where the Cys and His are arranged as HxxC(31)CxxC(6)CxxCxxxxCxxxxHxxC (21)CxxH.", "database": "PfamA", "aliStart": 292, "scoreName": "E-value", "accession": "PF13771.4", "start": 287, "score": 0.0009, "identifier": "PHD-like zinc-binding domain", "type": "DBD", "aliEnd": 323}}, {"startStyle": "jagged", "end": 468, "endStyle": "jagged", "aliStart": 432, "text": "zf-HC5HC2H", "colour": "#9999ff", "aliEnd": 462, "start": 423, "href": "http://pfam.xfam.org/family/PF13771.4", "type": "pfama", "display": "true", "metadata": {"end": 468, "description": "The members of this family are annotated as containing PHD domain, but the zinc-binding region here is not typical of PHD domains.  The conformation here is a well-conserved cysteine-histidine rich region spanning 90 residues, where the Cys and His are arranged as HxxC(31)CxxC(6)CxxCxxxxCxxxxHxxC (21)CxxH.", "database": "PfamA", "aliStart": 432, "scoreName": "E-value", "accession": "PF13771.4", "start": 423, "score": 0.0009, "identifier": "PHD-like zinc-binding domain", "type": "DBD", "aliEnd": 462}}, {"startStyle": "straight", "end": 341, "endStyle": "straight", "aliStart": 307, "text": "PHD_2", "colour": "#9999ff", "aliEnd": 340, "start": 306, "href": "http://pfam.xfam.org/family/PF13831.4", "type": "pfama", "display": "true", "metadata": {"end": 341, "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": 307, "scoreName": "E-value", "accession": "PF13831.4", "start": 306, "score": 0.003, "identifier": "PHD-finger", "type": "DBD", "aliEnd": 340}}, {"startStyle": "jagged", "end": 476, "endStyle": "straight", "aliStart": 443, "text": "PHD_2", "colour": "#9999ff", "aliEnd": 475, "start": 442, "href": "http://pfam.xfam.org/family/PF13831.4", "type": "pfama", "display": "true", "metadata": {"end": 476, "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": 443, "scoreName": "E-value", "accession": "PF13831.4", "start": 442, "score": 0.003, "identifier": "PHD-finger", "type": "DBD", "aliEnd": 475}}], "length": 546}

TF Info Page for AIRE (SAND)