Conclusion
Assessment
Binding Mode
Motif Status
Notes
Comments
Known motif
1 Monomer or homomultimer
High-throughput in vitro
Description
Description:
CXXC finger protein 5 [Source:HGNC Symbol;Acc:HGNC:26943]
Entrez Summary
TBA
Ensembl ID:
ENSG00000171604
External Link:
T074511_1.02
Interpro
IPR002857 ; ;
Protein Domain:
Protein: ENSP00000302543DBD: CxxCOther: Protein: ENSP00000424219DBD: CxxCOther: Protein: ENSP00000421057DBD: CxxCOther: Protein: ENSP00000425203DBD: CxxCOther: Protein: ENSP00000427440DBD: CxxCOther: Protein: ENSP00000427379DBD: CxxCOther: Protein: ENSP00000422883DBD: CxxCOther: Protein: ENSP00000430949DBD: CxxCOther: Protein: ENSP00000421866DBD: CxxCOther: Protein: ENSP00000423365DBD: CxxCOther: Protein: ENSP00000430522DBD: CxxCOther:
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.
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
1a1, Direct HQ evidence
TF has conditional DNA-binding requirements
DNA-Binding
Published Motif Data
Structure
Experimental History
{"regions": [{"startStyle": "curved", "end": 296, "endStyle": "curved", "aliStart": 257, "text": "zfCXXC", "colour": "#009900", "aliEnd": 296, "start": 255, "href": "http://pfam.xfam.org/family/PF02008.18", "type": "pfama", "display": "true", "metadata": {"end": 296, "description": "This domain contains eight conserved cysteine residues that bind to two zinc ions. The CXXC domain is found in a variety of chromatin-associated proteins. This domain binds to nonmethyl-CpG dinucleotides. The domain is characterised by two repeats [3], and shows a peculiar internal duplication in which the second unit is inserted into the first one [4]. Each of these units is characterised by four conserved cysteines, displaying a CXXCXXCX(n)C motif that chelate a Zn+2 ion. The DNA binding interface has been identified by NMR [3]. In eukaryotes, the CXXC domain is found in stramenopiles, plants and metazoans. Plants possess a mono-CXXC domain that is present in distinct chromatin proteins [4]. Structural comparisons show that the mono-CXXC is homologous to the structural-zinc binding domain of medium chain dehydrogenases [4].", "database": "PfamA", "aliStart": 257, "scoreName": "E-value", "accession": "PF02008.18", "start": 255, "score": 1.3e-07, "identifier": "CXXC zinc finger domain", "type": "DBD", "aliEnd": 296}}], "length": 323}
{"regions": [{"startStyle": "curved", "end": 296, "endStyle": "curved", "aliStart": 257, "text": "zfCXXC", "colour": "#009900", "aliEnd": 296, "start": 255, "href": "http://pfam.xfam.org/family/PF02008.18", "type": "pfama", "display": "true", "metadata": {"end": 296, "description": "This domain contains eight conserved cysteine residues that bind to two zinc ions. The CXXC domain is found in a variety of chromatin-associated proteins. This domain binds to nonmethyl-CpG dinucleotides. The domain is characterised by two repeats [3], and shows a peculiar internal duplication in which the second unit is inserted into the first one [4]. Each of these units is characterised by four conserved cysteines, displaying a CXXCXXCX(n)C motif that chelate a Zn+2 ion. The DNA binding interface has been identified by NMR [3]. In eukaryotes, the CXXC domain is found in stramenopiles, plants and metazoans. Plants possess a mono-CXXC domain that is present in distinct chromatin proteins [4]. Structural comparisons show that the mono-CXXC is homologous to the structural-zinc binding domain of medium chain dehydrogenases [4].", "database": "PfamA", "aliStart": 257, "scoreName": "E-value", "accession": "PF02008.18", "start": 255, "score": 1.3e-07, "identifier": "CXXC zinc finger domain", "type": "DBD", "aliEnd": 296}}], "length": 323}