Conclusion
Assessment
Binding Mode
Motif Status
Notes
Comments
Likely to be sequence specific TF
1 Monomer or homomultimer
No motif
Description
Description:
chromosome 11 open reading frame 95 [Source:HGNC Symbol;Acc:HGNC:28449]
Entrez Summary
TBA
Ensembl ID:
ENSG00000188070
External Link:
Interpro
IPR015880 ; ;
Protein Domain:
Protein: ENSP00000483097DBD: BED ZFOther: Protein: ENSP00000482857DBD: BED ZFOther: Protein: ENSP00000482180DBD: BED ZFOther: DUF678, Trm112pProtein: ENSP00000478462DBD: BED ZFOther:
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?
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
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": 150, "endStyle": "curved", "aliStart": 121, "text": "zfBED", "colour": "#2cb42c", "aliEnd": 150, "start": 111, "href": "http://pfam.xfam.org/family/PF02892.13", "type": "pfama", "display": "true", "metadata": {"end": 150, "description": "The BED finger, which was named after the Drosophila proteins BEAF and DREF, is found in one or more copies in cellular regulatory factors and transposases from plants, animals and fungi. The BED finger is an about 50 to 60 amino acid residues domain that contains a characteristic motif with two highly conserved aromatic positions, as well as a shared pattern of cysteines and histidines that is predicted to form a zinc finger. As diverse BED fingers are able to bind DNA, it has been suggested that DNA-binding is the general function of this domain [PUBMED:10973053].", "database": "PfamA", "aliStart": 121, "scoreName": "E-value", "accession": "PF02892.13", "start": 111, "score": 1.9e-10, "identifier": "BED zinc finger", "type": "DBD", "aliEnd": 150}}, {"startStyle": "jagged", "end": 463, "endStyle": "curved", "aliStart": 428, "text": "zfBED", "colour": "#2cb42c", "aliEnd": 463, "start": 422, "href": "http://pfam.xfam.org/family/PF02892.13", "type": "pfama", "display": "true", "metadata": {"end": 463, "description": "The BED finger, which was named after the Drosophila proteins BEAF and DREF, is found in one or more copies in cellular regulatory factors and transposases from plants, animals and fungi. The BED finger is an about 50 to 60 amino acid residues domain that contains a characteristic motif with two highly conserved aromatic positions, as well as a shared pattern of cysteines and histidines that is predicted to form a zinc finger. As diverse BED fingers are able to bind DNA, it has been suggested that DNA-binding is the general function of this domain [PUBMED:10973053].", "database": "PfamA", "aliStart": 428, "scoreName": "E-value", "accession": "PF02892.13", "start": 422, "score": 1.9e-10, "identifier": "BED zinc finger", "type": "DBD", "aliEnd": 463}}, {"startStyle": "jagged", "end": 626, "endStyle": "curved", "aliStart": 596, "text": "zfBED", "colour": "#2cb42c", "aliEnd": 626, "start": 588, "href": "http://pfam.xfam.org/family/PF02892.13", "type": "pfama", "display": "true", "metadata": {"end": 626, "description": "The BED finger, which was named after the Drosophila proteins BEAF and DREF, is found in one or more copies in cellular regulatory factors and transposases from plants, animals and fungi. The BED finger is an about 50 to 60 amino acid residues domain that contains a characteristic motif with two highly conserved aromatic positions, as well as a shared pattern of cysteines and histidines that is predicted to form a zinc finger. As diverse BED fingers are able to bind DNA, it has been suggested that DNA-binding is the general function of this domain [PUBMED:10973053].", "database": "PfamA", "aliStart": 596, "scoreName": "E-value", "accession": "PF02892.13", "start": 588, "score": 1.9e-10, "identifier": "BED zinc finger", "type": "DBD", "aliEnd": 626}}, {"startStyle": "jagged", "end": 299, "endStyle": "straight", "aliStart": 278, "text": "DUF678", "colour": "#9999ff", "aliEnd": 295, "start": 267, "href": "http://pfam.xfam.org/family/PF05077.10", "type": "pfama", "display": "true", "metadata": {"end": 299, "description": "This family contains several poxvirus proteins of unknown function.", "database": "PfamA", "aliStart": 278, "scoreName": "E-value", "accession": "PF05077.10", "start": 267, "score": 0.0004, "identifier": "Protein of unknown function (DUF678)", "type": "DBD", "aliEnd": 295}}, {"startStyle": "jagged", "end": 293, "endStyle": "straight", "aliStart": 257, "text": "Trm112p", "colour": "#9999ff", "aliEnd": 293, "start": 206, "href": "http://pfam.xfam.org/family/PF03966.14", "type": "pfama", "display": "true", "metadata": {"end": 293, "description": "The function of this family is uncertain. The bacterial members are about 60-70 amino acids in length and the eukaryotic examples are about 120 amino acids in length. The C terminus contains the strongest conservation. Trm112p is required for tRNA methylation in S. cerevisiae and is found in complexes with 2 tRNA methylases (TRM9 and TRM11) also with putative methyltransferase YDR140W [1]. The zinc-finger protein Ynr046w is plurifunctional and a component of the eRF1 methyltransferase in yeast [2]. The crystal structure of Ynr046w has been determined to 1.7 A resolution. It comprises a zinc-binding domain built from both the N- and C-terminal sequences and an inserted domain, absent from bacterial and archaeal orthologs of the protein, composed of three alpha-helices [2].", "database": "PfamA", "aliStart": 257, "scoreName": "E-value", "accession": "PF03966.14", "start": 206, "score": 0.0023, "identifier": "Trm112p-like protein", "type": "DBD", "aliEnd": 293}}], "length": 679}