Conclusion
Assessment
Binding Mode
Motif Status
Notes
Comments
Likely to be sequence specific TF
1 Monomer or homomultimer
No motif
Description
Description:
zinc fingers and homeoboxes 3 [Source:HGNC Symbol;Acc:HGNC:15935]
Entrez Summary
TBA
Ensembl ID:
ENSG00000174306
External Link:
Interpro
IPR001356 ; IPR009057 ; IPR015880 ; IPR024578 ;
Protein Domain:
Protein: ENSP00000405421DBD: HomeodomainOther: Protein: ENSP00000443783DBD: HomeodomainOther: HomezProtein: ENSP00000452965DBD: HomeodomainOther: Protein: ENSP00000454006DBD: HomeodomainOther: Protein: ENSP00000362358DBD: HomeodomainOther: Protein: ENSP00000415498DBD: HomeodomainOther: Protein: ENSP00000401852DBD: HomeodomainOther: Protein: ENSP00000399433DBD: HomeodomainOther: zf-Di19Protein: ENSP00000453310DBD: HomeodomainOther: HomezProtein: ENSP00000403048DBD: HomeodomainOther:
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.
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:0003700 sequence-specific DNA binding transcription factor activity IDA - PMID:12659632
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
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{"regions": [{"startStyle": "straight", "end": 117, "endStyle": "jagged", "aliStart": 77, "text": "zf-Di19", "colour": "#9999ff", "aliEnd": 115, "start": 76, "href": "http://pfam.xfam.org/family/PF05605.10", "type": "pfama", "display": "true", "metadata": {"end": 117, "description": "This family consists of several drought induced 19 (Di19) like proteins. Di19 has been found to be strongly expressed in both the roots and leaves of Arabidopsis thaliana during progressive drought [1]. This domain is a zinc-binding domain.", "database": "PfamA", "aliStart": 77, "scoreName": "E-value", "accession": "PF05605.10", "start": 76, "score": 0.00088, "identifier": "Drought induced 19 protein (Di19), zinc-binding", "type": "DBD", "aliEnd": 115}}], "length": 118}
{"regions": [{"startStyle": "jagged", "end": 50, "endStyle": "jagged", "aliStart": 10, "text": "Homez", "colour": "#9999ff", "aliEnd": 38, "start": 6, "href": "http://pfam.xfam.org/family/PF11569.6", "type": "pfama", "display": "true", "metadata": {"end": 50, "description": "Homez contains two leucine zipper-like motifs and an acidic domain and belongs to the superfamily of homeobox-containing proteins. The presence of leucine zippers suggests that Homez can function as a homo or heterodimer in the nucleus [1]. It is thought that the first leucine zipper and homeodomain 1 (HD1)of Homez is responsible for dimerisation and HD2 has a specific DNA-binding activity. Homez is also thought to function as a transcriptional repressor due to the acidic region in its C-terminal domain [1]. Homez is involved in a complex regulatory network [1].", "database": "PfamA", "aliStart": 10, "scoreName": "E-value", "accession": "PF11569.6", "start": 6, "score": 1.6e-07, "identifier": "Homeodomain leucine-zipper encoding, Homez", "type": "DBD", "aliEnd": 38}}], "length": 128}