Conclusion
Assessment
Binding Mode
Motif Status
Notes
Comments
Likely to be sequence specific TF
1 Monomer or homomultimer
No motif
Description
Description:
tet methylcytosine dioxygenase 3 [Source:HGNC Symbol;Acc:HGNC:28313]
Entrez Summary
TBA
Ensembl ID:
ENSG00000187605
External Link:
Interpro
IPR002857 ; IPR024779 ;
Protein Domain:
Protein: ENSP00000386869DBD: CxxCOther: Tet_JBPProtein: ENSP00000307803DBD: CxxCOther: Tet_JBP
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
3a, decent circumstantial evidence for its role as
TF has conditional DNA-binding requirements
DNA-Binding
Published Motif Data
Structure
Experimental History
{"regions": [{"startStyle": "curved", "end": 89, "endStyle": "curved", "aliStart": 51, "text": "zfCXXC", "colour": "#009900", "aliEnd": 89, "start": 49, "href": "http://pfam.xfam.org/family/PF02008.18", "type": "pfama", "display": "true", "metadata": {"end": 89, "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": 51, "scoreName": "E-value", "accession": "PF02008.18", "start": 49, "score": 1e-06, "identifier": "CXXC zinc finger domain", "type": "DBD", "aliEnd": 89}}, {"startStyle": "straight", "end": 1697, "endStyle": "straight", "aliStart": 985, "text": "Tet_JBP", "colour": "#9999ff", "aliEnd": 1697, "start": 985, "href": "http://pfam.xfam.org/family/PF12851.5", "type": "pfama", "display": "true", "metadata": {"end": 1697, "description": "A double-stranded beta helix (DSBH) fold domain of the 2-oxoglutarate (2OG)-Fe(II)-dependent dioxygenase (2OGFeDO) superfamily found in various eukaryotes, bacteria and bacteriophages [1]. Members of this family catalyze nucleic acid modifications, such as thymidine hydroxylation during base J synthesis in kinetoplastids [2], and the conversion of 5 methyl-cytosine (5-mC) to 5-hydroxymethyl-cytosine (hmC) [3], or further oxidation to 5-formylcytosine (5fC) and 5-carboxylcytosine (5caC) [4]. Metazoan TET proteins contain a cysteine-rich region inserted into the core of the DSBH fold. Vertebrate TET proteins are oncogenes that are mutated in various myeloid cancers [5]. Fungal and algal versions of this family are linked to a predicted transposase and show lineage-specific expansions [1].", "database": "PfamA", "aliStart": 985, "scoreName": "E-value", "accession": "PF12851.5", "start": 985, "score": 1.0999999999999999e-104, "identifier": "Oxygenase domain of the 2OGFeDO superfamily ", "type": "DBD", "aliEnd": 1697}}], "length": 1796}
{"regions": [{"startStyle": "straight", "end": 1604, "endStyle": "straight", "aliStart": 892, "text": "Tet_JBP", "colour": "#9999ff", "aliEnd": 1604, "start": 892, "href": "http://pfam.xfam.org/family/PF12851.5", "type": "pfama", "display": "true", "metadata": {"end": 1604, "description": "A double-stranded beta helix (DSBH) fold domain of the 2-oxoglutarate (2OG)-Fe(II)-dependent dioxygenase (2OGFeDO) superfamily found in various eukaryotes, bacteria and bacteriophages [1]. Members of this family catalyze nucleic acid modifications, such as thymidine hydroxylation during base J synthesis in kinetoplastids [2], and the conversion of 5 methyl-cytosine (5-mC) to 5-hydroxymethyl-cytosine (hmC) [3], or further oxidation to 5-formylcytosine (5fC) and 5-carboxylcytosine (5caC) [4]. Metazoan TET proteins contain a cysteine-rich region inserted into the core of the DSBH fold. Vertebrate TET proteins are oncogenes that are mutated in various myeloid cancers [5]. Fungal and algal versions of this family are linked to a predicted transposase and show lineage-specific expansions [1].", "database": "PfamA", "aliStart": 892, "scoreName": "E-value", "accession": "PF12851.5", "start": 892, "score": 9.999999999999998e-105, "identifier": "Oxygenase domain of the 2OGFeDO superfamily ", "type": "DBD", "aliEnd": 1604}}], "length": 1703}