Conclusion
Assessment
Binding Mode
Motif Status
Notes
Comments
Known motif
1 Monomer or homomultimer
High-throughput in vitro
X-ray structure (PDB:3QMI) indicates sequence specific binding through base contacts (PMID: 21407193).
Description
Description:
CXXC finger protein 1 [Source:HGNC Symbol;Acc:HGNC:24343]
Entrez Summary
TBA
Ensembl ID:
ENSG00000154832
External Link:
Interpro
IPR001965 ; IPR002857 ; IPR011011 ; IPR019786 ; IPR019787 ; IPR022056 ;
Protein Domain:
Protein: ENSP00000285106DBD: CxxCOther: PHD, zf-CpG_bind_CProtein: ENSP00000390475DBD: CxxCOther: PHD, zf-CpG_bind_CProtein: ENSP00000467634DBD: CxxCOther: PHD, zf-CpG_bind_CProtein: ENSP00000468038DBD: CxxCOther: PHD, PHD_2Protein: ENSP00000465849DBD: 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.
other
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": 208, "endStyle": "curved", "aliStart": 163, "text": "zfCXXC", "colour": "#009900", "aliEnd": 208, "start": 160, "href": "http://pfam.xfam.org/family/PF02008.18", "type": "pfama", "display": "true", "metadata": {"end": 208, "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": 163, "scoreName": "E-value", "accession": "PF02008.18", "start": 160, "score": 1.3999999999999998e-16, "identifier": "CXXC zinc finger domain", "type": "DBD", "aliEnd": 208}}, {"startStyle": "straight", "end": 636, "endStyle": "straight", "aliStart": 400, "text": "zf-CpG_bind_C", "colour": "#9999ff", "aliEnd": 636, "start": 400, "href": "http://pfam.xfam.org/family/PF12269.6", "type": "pfama", "display": "true", "metadata": {"end": 636, "description": "This domain family is found in eukaryotes, and is approximately 240 amino acids in length. This domain is the zinc finger domain of a CpG binding DNA methyltransferase protein. It contains a CxxC motif which forms the zinc finger and binds to DNA.", "database": "PfamA", "aliStart": 400, "scoreName": "E-value", "accession": "PF12269.6", "start": 400, "score": 1.5999999999999996e-104, "identifier": "CpG binding protein zinc finger C terminal domain", "type": "DBD", "aliEnd": 636}}, {"startStyle": "straight", "end": 76, "endStyle": "straight", "aliStart": 28, "text": "PHD", "colour": "#9999ff", "aliEnd": 75, "start": 28, "href": "http://pfam.xfam.org/family/PF00628.27", "type": "pfama", "display": "true", "metadata": {"end": 76, "description": "PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar manner to that of the RING and FYVE domains [2]. Several PHD fingers have been identified as binding modules of methylated histone H3 [3].", "database": "PfamA", "aliStart": 28, "scoreName": "E-value", "accession": "PF00628.27", "start": 28, "score": 7.2e-11, "identifier": "PHD-finger", "type": "DBD", "aliEnd": 75}}], "length": 657}
{"regions": [{"startStyle": "curved", "end": 208, "endStyle": "curved", "aliStart": 163, "text": "zfCXXC", "colour": "#009900", "aliEnd": 208, "start": 160, "href": "http://pfam.xfam.org/family/PF02008.18", "type": "pfama", "display": "true", "metadata": {"end": 208, "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": 163, "scoreName": "E-value", "accession": "PF02008.18", "start": 160, "score": 1.3999999999999998e-16, "identifier": "CXXC zinc finger domain", "type": "DBD", "aliEnd": 208}}, {"startStyle": "straight", "end": 640, "endStyle": "straight", "aliStart": 404, "text": "zf-CpG_bind_C", "colour": "#9999ff", "aliEnd": 640, "start": 404, "href": "http://pfam.xfam.org/family/PF12269.6", "type": "pfama", "display": "true", "metadata": {"end": 640, "description": "This domain family is found in eukaryotes, and is approximately 240 amino acids in length. This domain is the zinc finger domain of a CpG binding DNA methyltransferase protein. It contains a CxxC motif which forms the zinc finger and binds to DNA.", "database": "PfamA", "aliStart": 404, "scoreName": "E-value", "accession": "PF12269.6", "start": 404, "score": 1.6999999999999998e-104, "identifier": "CpG binding protein zinc finger C terminal domain", "type": "DBD", "aliEnd": 640}}, {"startStyle": "straight", "end": 76, "endStyle": "straight", "aliStart": 28, "text": "PHD", "colour": "#9999ff", "aliEnd": 75, "start": 28, "href": "http://pfam.xfam.org/family/PF00628.27", "type": "pfama", "display": "true", "metadata": {"end": 76, "description": "PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar manner to that of the RING and FYVE domains [2]. Several PHD fingers have been identified as binding modules of methylated histone H3 [3].", "database": "PfamA", "aliStart": 28, "scoreName": "E-value", "accession": "PF00628.27", "start": 28, "score": 7.2e-11, "identifier": "PHD-finger", "type": "DBD", "aliEnd": 75}}], "length": 661}
{"regions": [{"startStyle": "curved", "end": 208, "endStyle": "curved", "aliStart": 163, "text": "zfCXXC", "colour": "#009900", "aliEnd": 208, "start": 160, "href": "http://pfam.xfam.org/family/PF02008.18", "type": "pfama", "display": "true", "metadata": {"end": 208, "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": 163, "scoreName": "E-value", "accession": "PF02008.18", "start": 160, "score": 1.2e-16, "identifier": "CXXC zinc finger domain", "type": "DBD", "aliEnd": 208}}, {"startStyle": "straight", "end": 529, "endStyle": "jagged", "aliStart": 400, "text": "zf-CpG_bind_C", "colour": "#9999ff", "aliEnd": 526, "start": 400, "href": "http://pfam.xfam.org/family/PF12269.6", "type": "pfama", "display": "true", "metadata": {"end": 529, "description": "This domain family is found in eukaryotes, and is approximately 240 amino acids in length. This domain is the zinc finger domain of a CpG binding DNA methyltransferase protein. It contains a CxxC motif which forms the zinc finger and binds to DNA.", "database": "PfamA", "aliStart": 400, "scoreName": "E-value", "accession": "PF12269.6", "start": 400, "score": 5.200000000000001e-44, "identifier": "CpG binding protein zinc finger C terminal domain", "type": "DBD", "aliEnd": 526}}, {"startStyle": "straight", "end": 76, "endStyle": "straight", "aliStart": 28, "text": "PHD", "colour": "#9999ff", "aliEnd": 75, "start": 28, "href": "http://pfam.xfam.org/family/PF00628.27", "type": "pfama", "display": "true", "metadata": {"end": 76, "description": "PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar manner to that of the RING and FYVE domains [2]. Several PHD fingers have been identified as binding modules of methylated histone H3 [3].", "database": "PfamA", "aliStart": 28, "scoreName": "E-value", "accession": "PF00628.27", "start": 28, "score": 6.6e-11, "identifier": "PHD-finger", "type": "DBD", "aliEnd": 75}}], "length": 614}
{"regions": [{"startStyle": "curved", "end": 208, "endStyle": "curved", "aliStart": 163, "text": "zfCXXC", "colour": "#009900", "aliEnd": 208, "start": 160, "href": "http://pfam.xfam.org/family/PF02008.18", "type": "pfama", "display": "true", "metadata": {"end": 208, "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": 163, "scoreName": "E-value", "accession": "PF02008.18", "start": 160, "score": 3.4999999999999996e-17, "identifier": "CXXC zinc finger domain", "type": "DBD", "aliEnd": 208}}, {"startStyle": "straight", "end": 76, "endStyle": "straight", "aliStart": 28, "text": "PHD", "colour": "#9999ff", "aliEnd": 75, "start": 28, "href": "http://pfam.xfam.org/family/PF00628.27", "type": "pfama", "display": "true", "metadata": {"end": 76, "description": "PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar manner to that of the RING and FYVE domains [2]. Several PHD fingers have been identified as binding modules of methylated histone H3 [3].", "database": "PfamA", "aliStart": 28, "scoreName": "E-value", "accession": "PF00628.27", "start": 28, "score": 1.9e-11, "identifier": "PHD-finger", "type": "DBD", "aliEnd": 75}}, {"startStyle": "jagged", "end": 74, "endStyle": "straight", "aliStart": 40, "text": "PHD_2", "colour": "#9999ff", "aliEnd": 74, "start": 37, "href": "http://pfam.xfam.org/family/PF13831.4", "type": "pfama", "display": "true", "metadata": {"end": 74, "description": "PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar manner to that of the RING and FYVE domains [2]. Several PHD fingers have been identified as binding modules of methylated histone H3 [3].", "database": "PfamA", "aliStart": 40, "scoreName": "E-value", "accession": "PF13831.4", "start": 37, "score": 0.0043, "identifier": "PHD-finger", "type": "DBD", "aliEnd": 74}}], "length": 253}
{"regions": [{"startStyle": "curved", "end": 56, "endStyle": "curved", "aliStart": 11, "text": "zfCXXC", "colour": "#009900", "aliEnd": 56, "start": 8, "href": "http://pfam.xfam.org/family/PF02008.18", "type": "pfama", "display": "true", "metadata": {"end": 56, "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": 11, "scoreName": "E-value", "accession": "PF02008.18", "start": 8, "score": 1.2e-17, "identifier": "CXXC zinc finger domain", "type": "DBD", "aliEnd": 56}}], "length": 250}