The Human Transcription Factors

Conclusion

Assessment	Binding Mode	Motif Status	Notes	Comments
Likely to be sequence specific TF	1 Monomer or homomultimer	No motif	Single C2H2 domain	Based on (PMID: 20534488), the protein has a C2H2 ZF domain; but it uses the domain for contacting RAB5A rather than for binding DNA.

Description

Description:	early endosome antigen 1 [Source:HGNC Symbol;Acc:HGNC:3185]
Entrez Summary	TBA
Ensembl ID:	ENSG00000102189
External Link:
Interpro	IPR000306; IPR007087; IPR011011; IPR017455;
Protein Domain:
Protein: ENSP00000317955	DBD: Other	Other: Atg14, FYVE
Protein: ENSP00000446785	DBD: Other	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.	x
CisBP considers it as a TF?	No
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	5a, one of the source datasets predicts is as a TF
TF has conditional DNA-binding requirements

DNA-Binding

Published Motif Data

Source	Annotation	Motif	Evidence

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": "straight", "end": 1411, "endStyle": "straight", "aliStart": 1348, "text": "FYVE", "colour": "#9999ff", "aliEnd": 1410, "start": 1347, "href": "http://pfam.xfam.org/family/PF01363.19", "type": "pfama", "display": "true", "metadata": {"end": 1411, "description": "The FYVE zinc finger is named after four proteins that it has been found in: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn++ ions [1]. The FYVE finger has eight potential zinc coordinating cysteine positions.  Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue.  We have included members which do not conserve these histidine residues but are clearly related.", "database": "PfamA", "aliStart": 1348, "scoreName": "E-value", "accession": "PF01363.19", "start": 1347, "score": 3.6000000000000003e-20, "identifier": "FYVE zinc finger", "type": "DBD", "aliEnd": 1410}}, {"startStyle": "straight", "end": 238, "endStyle": "jagged", "aliStart": 37, "text": "Atg14", "colour": "#9999ff", "aliEnd": 217, "start": 34, "href": "http://pfam.xfam.org/family/PF10186.7", "type": "pfama", "display": "true", "metadata": {"end": 238, "description": "The Atg14 or Apg14 proteins are hydrophilic proteins with a predicted molecular mass of 40.5 kDa, and have a coiled-coil motif at the N terminus region. Yeast cells with mutant Atg14 are defective not only in autophagy but also in sorting of carboxypeptidase Y (CPY), a vacuolar-soluble hydrolase, to the vacuole. Subcellular fractionation indicate that Apg14p and Apg6p are peripherally associated with a membrane structure(s). Apg14p was co-immunoprecipitated with Apg6p, suggesting that they form a stable protein complex. These results imply that Apg6/Vps30p has two distinct functions: in the autophagic process and in the vacuolar protein sorting pathway. Apg14p may be a component specifically required for the function of Apg6/Vps30p through the autophagic pathway [1]. There are 17 auto-phagosomal component proteins which are categorized into six functional units, one of which is the AS-PI3K complex (Vps30/Atg6 and Atg14). The AS-PI3K complex and the Atg2-Atg18 complex are essential for nucleation, and the specific function of the AS-PI3K apparently is to produce phosphatidylinositol 3-phosphate (PtdIns(3)P) at the pre-autophagosomal structure (PAS). The localisation of this complex at the PAS is controlled by Atg14 [2]. Autophagy mediates the cellular response to nutrient deprivation, protein aggregation, and pathogen invasion in humans, and malfunction of autophagy has been implicated in multiple human diseases including cancer. This effect seems to be mediated through direct interaction of the human Atg14 with Beclin 1 in the human phosphatidylinositol 3-kinase class III complex [3].", "database": "PfamA", "aliStart": 37, "scoreName": "E-value", "accession": "PF10186.7", "start": 34, "score": 0.00043, "identifier": "Vacuolar sorting 38 and autophagy-related subunit 14", "type": "DBD", "aliEnd": 217}}, {"startStyle": "straight", "end": 555, "endStyle": "jagged", "aliStart": 447, "text": "Atg14", "colour": "#9999ff", "aliEnd": 545, "start": 437, "href": "http://pfam.xfam.org/family/PF10186.7", "type": "pfama", "display": "true", "metadata": {"end": 555, "description": "The Atg14 or Apg14 proteins are hydrophilic proteins with a predicted molecular mass of 40.5 kDa, and have a coiled-coil motif at the N terminus region. Yeast cells with mutant Atg14 are defective not only in autophagy but also in sorting of carboxypeptidase Y (CPY), a vacuolar-soluble hydrolase, to the vacuole. Subcellular fractionation indicate that Apg14p and Apg6p are peripherally associated with a membrane structure(s). Apg14p was co-immunoprecipitated with Apg6p, suggesting that they form a stable protein complex. These results imply that Apg6/Vps30p has two distinct functions: in the autophagic process and in the vacuolar protein sorting pathway. Apg14p may be a component specifically required for the function of Apg6/Vps30p through the autophagic pathway [1]. There are 17 auto-phagosomal component proteins which are categorized into six functional units, one of which is the AS-PI3K complex (Vps30/Atg6 and Atg14). The AS-PI3K complex and the Atg2-Atg18 complex are essential for nucleation, and the specific function of the AS-PI3K apparently is to produce phosphatidylinositol 3-phosphate (PtdIns(3)P) at the pre-autophagosomal structure (PAS). The localisation of this complex at the PAS is controlled by Atg14 [2]. Autophagy mediates the cellular response to nutrient deprivation, protein aggregation, and pathogen invasion in humans, and malfunction of autophagy has been implicated in multiple human diseases including cancer. This effect seems to be mediated through direct interaction of the human Atg14 with Beclin 1 in the human phosphatidylinositol 3-kinase class III complex [3].", "database": "PfamA", "aliStart": 447, "scoreName": "E-value", "accession": "PF10186.7", "start": 437, "score": 0.00043, "identifier": "Vacuolar sorting 38 and autophagy-related subunit 14", "type": "DBD", "aliEnd": 545}}, {"startStyle": "straight", "end": 709, "endStyle": "jagged", "aliStart": 563, "text": "Atg14", "colour": "#9999ff", "aliEnd": 706, "start": 559, "href": "http://pfam.xfam.org/family/PF10186.7", "type": "pfama", "display": "true", "metadata": {"end": 709, "description": "The Atg14 or Apg14 proteins are hydrophilic proteins with a predicted molecular mass of 40.5 kDa, and have a coiled-coil motif at the N terminus region. Yeast cells with mutant Atg14 are defective not only in autophagy but also in sorting of carboxypeptidase Y (CPY), a vacuolar-soluble hydrolase, to the vacuole. Subcellular fractionation indicate that Apg14p and Apg6p are peripherally associated with a membrane structure(s). Apg14p was co-immunoprecipitated with Apg6p, suggesting that they form a stable protein complex. These results imply that Apg6/Vps30p has two distinct functions: in the autophagic process and in the vacuolar protein sorting pathway. Apg14p may be a component specifically required for the function of Apg6/Vps30p through the autophagic pathway [1]. There are 17 auto-phagosomal component proteins which are categorized into six functional units, one of which is the AS-PI3K complex (Vps30/Atg6 and Atg14). The AS-PI3K complex and the Atg2-Atg18 complex are essential for nucleation, and the specific function of the AS-PI3K apparently is to produce phosphatidylinositol 3-phosphate (PtdIns(3)P) at the pre-autophagosomal structure (PAS). The localisation of this complex at the PAS is controlled by Atg14 [2]. Autophagy mediates the cellular response to nutrient deprivation, protein aggregation, and pathogen invasion in humans, and malfunction of autophagy has been implicated in multiple human diseases including cancer. This effect seems to be mediated through direct interaction of the human Atg14 with Beclin 1 in the human phosphatidylinositol 3-kinase class III complex [3].", "database": "PfamA", "aliStart": 563, "scoreName": "E-value", "accession": "PF10186.7", "start": 559, "score": 0.00043, "identifier": "Vacuolar sorting 38 and autophagy-related subunit 14", "type": "DBD", "aliEnd": 706}}, {"startStyle": "straight", "end": 797, "endStyle": "jagged", "aliStart": 704, "text": "Atg14", "colour": "#9999ff", "aliEnd": 795, "start": 701, "href": "http://pfam.xfam.org/family/PF10186.7", "type": "pfama", "display": "true", "metadata": {"end": 797, "description": "The Atg14 or Apg14 proteins are hydrophilic proteins with a predicted molecular mass of 40.5 kDa, and have a coiled-coil motif at the N terminus region. Yeast cells with mutant Atg14 are defective not only in autophagy but also in sorting of carboxypeptidase Y (CPY), a vacuolar-soluble hydrolase, to the vacuole. Subcellular fractionation indicate that Apg14p and Apg6p are peripherally associated with a membrane structure(s). Apg14p was co-immunoprecipitated with Apg6p, suggesting that they form a stable protein complex. These results imply that Apg6/Vps30p has two distinct functions: in the autophagic process and in the vacuolar protein sorting pathway. Apg14p may be a component specifically required for the function of Apg6/Vps30p through the autophagic pathway [1]. There are 17 auto-phagosomal component proteins which are categorized into six functional units, one of which is the AS-PI3K complex (Vps30/Atg6 and Atg14). The AS-PI3K complex and the Atg2-Atg18 complex are essential for nucleation, and the specific function of the AS-PI3K apparently is to produce phosphatidylinositol 3-phosphate (PtdIns(3)P) at the pre-autophagosomal structure (PAS). The localisation of this complex at the PAS is controlled by Atg14 [2]. Autophagy mediates the cellular response to nutrient deprivation, protein aggregation, and pathogen invasion in humans, and malfunction of autophagy has been implicated in multiple human diseases including cancer. This effect seems to be mediated through direct interaction of the human Atg14 with Beclin 1 in the human phosphatidylinositol 3-kinase class III complex [3].", "database": "PfamA", "aliStart": 704, "scoreName": "E-value", "accession": "PF10186.7", "start": 701, "score": 0.00043, "identifier": "Vacuolar sorting 38 and autophagy-related subunit 14", "type": "DBD", "aliEnd": 795}}, {"startStyle": "straight", "end": 902, "endStyle": "jagged", "aliStart": 784, "text": "Atg14", "colour": "#9999ff", "aliEnd": 892, "start": 781, "href": "http://pfam.xfam.org/family/PF10186.7", "type": "pfama", "display": "true", "metadata": {"end": 902, "description": "The Atg14 or Apg14 proteins are hydrophilic proteins with a predicted molecular mass of 40.5 kDa, and have a coiled-coil motif at the N terminus region. Yeast cells with mutant Atg14 are defective not only in autophagy but also in sorting of carboxypeptidase Y (CPY), a vacuolar-soluble hydrolase, to the vacuole. Subcellular fractionation indicate that Apg14p and Apg6p are peripherally associated with a membrane structure(s). Apg14p was co-immunoprecipitated with Apg6p, suggesting that they form a stable protein complex. These results imply that Apg6/Vps30p has two distinct functions: in the autophagic process and in the vacuolar protein sorting pathway. Apg14p may be a component specifically required for the function of Apg6/Vps30p through the autophagic pathway [1]. There are 17 auto-phagosomal component proteins which are categorized into six functional units, one of which is the AS-PI3K complex (Vps30/Atg6 and Atg14). The AS-PI3K complex and the Atg2-Atg18 complex are essential for nucleation, and the specific function of the AS-PI3K apparently is to produce phosphatidylinositol 3-phosphate (PtdIns(3)P) at the pre-autophagosomal structure (PAS). The localisation of this complex at the PAS is controlled by Atg14 [2]. Autophagy mediates the cellular response to nutrient deprivation, protein aggregation, and pathogen invasion in humans, and malfunction of autophagy has been implicated in multiple human diseases including cancer. This effect seems to be mediated through direct interaction of the human Atg14 with Beclin 1 in the human phosphatidylinositol 3-kinase class III complex [3].", "database": "PfamA", "aliStart": 784, "scoreName": "E-value", "accession": "PF10186.7", "start": 781, "score": 0.00043, "identifier": "Vacuolar sorting 38 and autophagy-related subunit 14", "type": "DBD", "aliEnd": 892}}], "length": 1412}

TF Info Page for EEA1 (C2H2 ZF(non-KRAB))