Conclusion
Assessment
Binding Mode
Motif Status
Notes
Comments
Known motif
1 Monomer or homomultimer
High-throughput in vitro
Description
Description:
DNA (cytosine-5-)-methyltransferase 1 [Source:HGNC Symbol;Acc:HGNC:2976]
Entrez Summary
TBA
Ensembl ID:
ENSG00000130816
External Link:
T074507_1.02
Interpro
IPR001025 ; IPR001525 ; IPR002857 ; IPR010506 ; IPR017198 ; IPR018117 ; IPR022702 ; IPR029063 ;
Protein Domain:
Protein: ENSP00000345739DBD: CxxCOther: BAH, DMAP_binding, DNA_methylase, DNMT1-RFDProtein: ENSP00000352516DBD: CxxCOther: BAH, DMAP_binding, DNA_methylase, DNMT1-RFDProtein: ENSP00000468062DBD: CxxCOther: Protein: ENSP00000465555DBD: CxxCOther: Protein: ENSP00000465993DBD: 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?
Yes
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": 691, "endStyle": "curved", "aliStart": 646, "text": "zfCXXC", "colour": "#009900", "aliEnd": 691, "start": 645, "href": "http://pfam.xfam.org/family/PF02008.18", "type": "pfama", "display": "true", "metadata": {"end": 691, "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": 646, "scoreName": "E-value", "accession": "PF02008.18", "start": 645, "score": 4.9e-15, "identifier": "CXXC zinc finger domain", "type": "DBD", "aliEnd": 691}}, {"startStyle": "straight", "end": 534, "endStyle": "straight", "aliStart": 400, "text": "DNMT1-RFD", "colour": "#9999ff", "aliEnd": 533, "start": 399, "href": "http://pfam.xfam.org/family/PF12047.6", "type": "pfama", "display": "true", "metadata": {"end": 534, "description": "This domain is part of a cytosine specific DNA methyltransferase enzyme. It functions non-catalytically to target the protein towards replication foci. This allows the DNMT1 protein to methylate the correct residues. This domain targets DMAP1 and HDAC2 to the replication foci during the S phase of mitosis. They are thought to have some importance in conversion of critical histone lysine moieties. [1]", "database": "PfamA", "aliStart": 400, "scoreName": "E-value", "accession": "PF12047.6", "start": 399, "score": 6e-48, "identifier": "Cytosine specific DNA methyltransferase replication foci domain", "type": "DBD", "aliEnd": 533}}, {"startStyle": "straight", "end": 1594, "endStyle": "straight", "aliStart": 1140, "text": "DNA_methylase", "colour": "#9999ff", "aliEnd": 1593, "start": 1139, "href": "http://pfam.xfam.org/family/PF00145.15", "type": "pfama", "display": "true", "metadata": {"end": 1594, "description": NaN, "database": "PfamA", "aliStart": 1140, "scoreName": "E-value", "accession": "PF00145.15", "start": 1139, "score": 2.9999999999999997e-47, "identifier": "C-5 cytosine-specific DNA methylase", "type": "DBD", "aliEnd": 1593}}, {"startStyle": "straight", "end": 880, "endStyle": "straight", "aliStart": 755, "text": "BAH", "colour": "#9999ff", "aliEnd": 879, "start": 755, "href": "http://pfam.xfam.org/family/PF01426.16", "type": "pfama", "display": "true", "metadata": {"end": 880, "description": "This domain has been called BAH (Bromo adjacent homology) domain and has also been called ELM1 and BAM (Bromo adjacent motif) domain. The function of this domain is unknown but may be involved in protein-protein interaction [3].", "database": "PfamA", "aliStart": 755, "scoreName": "E-value", "accession": "PF01426.16", "start": 755, "score": 4.299999999999999e-46, "identifier": "BAH domain", "type": "DBD", "aliEnd": 879}}, {"startStyle": "straight", "end": 1100, "endStyle": "straight", "aliStart": 932, "text": "BAH", "colour": "#9999ff", "aliEnd": 1099, "start": 931, "href": "http://pfam.xfam.org/family/PF01426.16", "type": "pfama", "display": "true", "metadata": {"end": 1100, "description": "This domain has been called BAH (Bromo adjacent homology) domain and has also been called ELM1 and BAM (Bromo adjacent motif) domain. The function of this domain is unknown but may be involved in protein-protein interaction [3].", "database": "PfamA", "aliStart": 932, "scoreName": "E-value", "accession": "PF01426.16", "start": 931, "score": 4.299999999999999e-46, "identifier": "BAH domain", "type": "DBD", "aliEnd": 1099}}, {"startStyle": "straight", "end": 105, "endStyle": "straight", "aliStart": 18, "text": "DMAP_binding", "colour": "#9999ff", "aliEnd": 103, "start": 16, "href": "http://pfam.xfam.org/family/PF06464.9", "type": "pfama", "display": "true", "metadata": {"end": 105, "description": "This domain binds DMAP1, a transcriptional co-repressor.", "database": "PfamA", "aliStart": 18, "scoreName": "E-value", "accession": "PF06464.9", "start": 16, "score": 8.000000000000001e-21, "identifier": "DMAP1-binding Domain", "type": "DBD", "aliEnd": 103}}], "length": 1617}
{"regions": [{"startStyle": "curved", "end": 707, "endStyle": "curved", "aliStart": 662, "text": "zfCXXC", "colour": "#009900", "aliEnd": 707, "start": 661, "href": "http://pfam.xfam.org/family/PF02008.18", "type": "pfama", "display": "true", "metadata": {"end": 707, "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": 662, "scoreName": "E-value", "accession": "PF02008.18", "start": 661, "score": 5e-15, "identifier": "CXXC zinc finger domain", "type": "DBD", "aliEnd": 707}}, {"startStyle": "straight", "end": 550, "endStyle": "straight", "aliStart": 416, "text": "DNMT1-RFD", "colour": "#9999ff", "aliEnd": 549, "start": 415, "href": "http://pfam.xfam.org/family/PF12047.6", "type": "pfama", "display": "true", "metadata": {"end": 550, "description": "This domain is part of a cytosine specific DNA methyltransferase enzyme. It functions non-catalytically to target the protein towards replication foci. This allows the DNMT1 protein to methylate the correct residues. This domain targets DMAP1 and HDAC2 to the replication foci during the S phase of mitosis. They are thought to have some importance in conversion of critical histone lysine moieties. [1]", "database": "PfamA", "aliStart": 416, "scoreName": "E-value", "accession": "PF12047.6", "start": 415, "score": 6.2e-48, "identifier": "Cytosine specific DNA methyltransferase replication foci domain", "type": "DBD", "aliEnd": 549}}, {"startStyle": "straight", "end": 1610, "endStyle": "straight", "aliStart": 1156, "text": "DNA_methylase", "colour": "#9999ff", "aliEnd": 1609, "start": 1155, "href": "http://pfam.xfam.org/family/PF00145.15", "type": "pfama", "display": "true", "metadata": {"end": 1610, "description": NaN, "database": "PfamA", "aliStart": 1156, "scoreName": "E-value", "accession": "PF00145.15", "start": 1155, "score": 3.1e-47, "identifier": "C-5 cytosine-specific DNA methylase", "type": "DBD", "aliEnd": 1609}}, {"startStyle": "straight", "end": 896, "endStyle": "straight", "aliStart": 771, "text": "BAH", "colour": "#9999ff", "aliEnd": 895, "start": 771, "href": "http://pfam.xfam.org/family/PF01426.16", "type": "pfama", "display": "true", "metadata": {"end": 896, "description": "This domain has been called BAH (Bromo adjacent homology) domain and has also been called ELM1 and BAM (Bromo adjacent motif) domain. The function of this domain is unknown but may be involved in protein-protein interaction [3].", "database": "PfamA", "aliStart": 771, "scoreName": "E-value", "accession": "PF01426.16", "start": 771, "score": 4.5e-46, "identifier": "BAH domain", "type": "DBD", "aliEnd": 895}}, {"startStyle": "straight", "end": 1116, "endStyle": "straight", "aliStart": 948, "text": "BAH", "colour": "#9999ff", "aliEnd": 1115, "start": 947, "href": "http://pfam.xfam.org/family/PF01426.16", "type": "pfama", "display": "true", "metadata": {"end": 1116, "description": "This domain has been called BAH (Bromo adjacent homology) domain and has also been called ELM1 and BAM (Bromo adjacent motif) domain. The function of this domain is unknown but may be involved in protein-protein interaction [3].", "database": "PfamA", "aliStart": 948, "scoreName": "E-value", "accession": "PF01426.16", "start": 947, "score": 4.5e-46, "identifier": "BAH domain", "type": "DBD", "aliEnd": 1115}}, {"startStyle": "straight", "end": 105, "endStyle": "straight", "aliStart": 18, "text": "DMAP_binding", "colour": "#9999ff", "aliEnd": 103, "start": 16, "href": "http://pfam.xfam.org/family/PF06464.9", "type": "pfama", "display": "true", "metadata": {"end": 105, "description": "This domain binds DMAP1, a transcriptional co-repressor.", "database": "PfamA", "aliStart": 18, "scoreName": "E-value", "accession": "PF06464.9", "start": 16, "score": 8.100000000000001e-21, "identifier": "DMAP1-binding Domain", "type": "DBD", "aliEnd": 103}}], "length": 1633}