Conclusion
Assessment
Binding Mode
Motif Status
Notes
Comments
Likely to be sequence specific TF
1 Monomer or homomultimer
No motif
Has a CXXC zinc finger that recognizes CGs (PMID: 22083960)
Description
Description:
lysine demethylase 2A [Source:HGNC Symbol;Acc:HGNC:13606]
Entrez Summary
TBA
Ensembl ID:
ENSG00000173120
External Link:
T074512_1.02
Interpro
IPR001810 ; IPR001965 ; IPR002857 ; IPR003347 ; IPR006553 ; IPR011011 ; IPR019786 ; IPR019787 ;
Protein Domain:
Protein: ENSP00000309302DBD: CxxCOther: Cupin_8, F-box, F-box-like, JmjC, LRR_6, PHD_4Protein: ENSP00000381640DBD: CxxCOther: Cupin_8, JmjC, PHD_4Protein: ENSP00000432786DBD: CxxCOther: Cupin_8, F-box, F-box-like, JmjC, LRR_6, PHD_4Protein: ENSP00000435776DBD: CxxCOther: F-box, F-box-like, LRR_6, PHD_4
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
5a, one of the source datasets predicts is as a TF
TF has conditional DNA-binding requirements
Chromatin_Modifier_etc
DNA-Binding
Published Motif Data
Structure
Experimental History
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Structural comparisons show that the mono-CXXC is homologous to the structural-zinc binding domain of medium chain dehydrogenases [4].", "database": "PfamA", "aliStart": 548, "scoreName": "E-value", "accession": "PF02008.18", "start": 546, "score": 5.7e-13, "identifier": "CXXC zinc finger domain", "type": "DBD", "aliEnd": 592}}, {"startStyle": "straight", "end": 659, "endStyle": "straight", "aliStart": 597, "text": "PHD_4", "colour": "#9999ff", "aliEnd": 659, "start": 597, "href": "http://pfam.xfam.org/family/PF16866.3", "type": "pfama", "display": "true", "metadata": {"end": 659, "description": NaN, "database": "PfamA", "aliStart": 597, "scoreName": "E-value", "accession": "PF16866.3", "start": 597, "score": 2.2e-21, "identifier": "PHD-finger", "type": "DBD", "aliEnd": 659}}, {"startStyle": "jagged", "end": 918, "endStyle": "straight", "aliStart": 879, "text": "F-box", "colour": "#9999ff", "aliEnd": 917, "start": 872, "href": "http://pfam.xfam.org/family/PF00646.31", "type": "pfama", "display": "true", "metadata": {"end": 918, "description": "This domain is approximately 50 amino acids long, and is usually found in the N-terminal half of a variety of proteins. Two motifs that are commonly found associated with the F-box domain are the leucine rich repeats (LRRs; Pfam:PF00560 and Pfam:PF07723) and the WD repeat (Pfam:PF00400). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression [3].", "database": "PfamA", "aliStart": 879, "scoreName": "E-value", "accession": "PF00646.31", "start": 872, "score": 3e-09, "identifier": "F-box domain", "type": "DBD", "aliEnd": 917}}, {"startStyle": "jagged", "end": 919, "endStyle": "straight", "aliStart": 879, "text": "F-box-like", "colour": "#9999ff", "aliEnd": 918, "start": 878, "href": "http://pfam.xfam.org/family/PF12937.5", "type": "pfama", "display": "true", "metadata": {"end": 919, "description": "This is an F-box-like family.", "database": "PfamA", "aliStart": 879, "scoreName": "E-value", "accession": "PF12937.5", "start": 878, "score": 1.5e-08, "identifier": "F-box-like", "type": "DBD", "aliEnd": 918}}, {"startStyle": "straight", "end": 282, "endStyle": "straight", "aliStart": 182, "text": "JmjC", "colour": "#9999ff", "aliEnd": 282, "start": 182, "href": "http://pfam.xfam.org/family/PF02373.20", "type": "pfama", "display": "true", "metadata": {"end": 282, "description": "The JmjC domain belongs to the Cupin superfamily [3]. JmjC-domain proteins may be protein hydroxylases that catalyse a novel histone modification [4]. This is confirmed to be a hydroxylase: the human JmjC protein named Tyw5p unexpectedly acts in the biosynthesis of a hypermodified nucleoside, hydroxy-wybutosine, in tRNA-Phe by catalysing hydroxylation [5].", "database": "PfamA", "aliStart": 182, "scoreName": "E-value", "accession": "PF02373.20", "start": 182, "score": 5.3e-06, "identifier": "JmjC domain, hydroxylase", "type": "DBD", "aliEnd": 282}}, {"startStyle": "jagged", "end": 290, "endStyle": "straight", "aliStart": 99, "text": "Cupin_8", "colour": "#9999ff", "aliEnd": 271, "start": 69, "href": "http://pfam.xfam.org/family/PF13621.4", "type": "pfama", "display": "true", "metadata": {"end": 290, "description": "This cupin like domain shares similarity to the JmjC domain.", "database": "PfamA", "aliStart": 99, "scoreName": "E-value", "accession": "PF13621.4", "start": 69, "score": 0.0025, "identifier": "Cupin-like domain", "type": "DBD", "aliEnd": 271}}, {"startStyle": "jagged", "end": 1098, "endStyle": "jagged", "aliStart": 1078, "text": "LRR_6", "colour": "#9999ff", "aliEnd": 1093, "start": 1077, "href": "http://pfam.xfam.org/family/PF13516.4", "type": "pfama", "display": "true", "metadata": {"end": 1098, "description": NaN, "database": "PfamA", "aliStart": 1078, "scoreName": "E-value", "accession": "PF13516.4", "start": 1077, "score": 0.0061, "identifier": "Leucine Rich repeat", "type": "DBD", "aliEnd": 1093}}], "length": 1146}
{"regions": [{"startStyle": "curved", "end": 609, "endStyle": "curved", "aliStart": 565, "text": "zfCXXC", "colour": "#009900", "aliEnd": 609, "start": 563, "href": "http://pfam.xfam.org/family/PF02008.18", "type": "pfama", "display": "true", "metadata": {"end": 609, "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": 565, "scoreName": "E-value", "accession": "PF02008.18", "start": 563, "score": 3.6000000000000003e-13, "identifier": "CXXC zinc finger domain", "type": "DBD", "aliEnd": 609}}, {"startStyle": "straight", "end": 676, "endStyle": "straight", "aliStart": 614, "text": "PHD_4", "colour": "#9999ff", "aliEnd": 676, "start": 614, "href": "http://pfam.xfam.org/family/PF16866.3", "type": "pfama", "display": "true", "metadata": {"end": 676, "description": NaN, "database": "PfamA", "aliStart": 614, "scoreName": "E-value", "accession": "PF16866.3", "start": 614, "score": 1.4000000000000002e-21, "identifier": "PHD-finger", "type": "DBD", "aliEnd": 676}}, {"startStyle": "straight", "end": 299, "endStyle": "straight", "aliStart": 199, "text": "JmjC", "colour": "#9999ff", "aliEnd": 299, "start": 199, "href": "http://pfam.xfam.org/family/PF02373.20", "type": "pfama", "display": "true", "metadata": {"end": 299, "description": "The JmjC domain belongs to the Cupin superfamily [3]. JmjC-domain proteins may be protein hydroxylases that catalyse a novel histone modification [4]. This is confirmed to be a hydroxylase: the human JmjC protein named Tyw5p unexpectedly acts in the biosynthesis of a hypermodified nucleoside, hydroxy-wybutosine, in tRNA-Phe by catalysing hydroxylation [5].", "database": "PfamA", "aliStart": 199, "scoreName": "E-value", "accession": "PF02373.20", "start": 199, "score": 3.2e-06, "identifier": "JmjC domain, hydroxylase", "type": "DBD", "aliEnd": 299}}, {"startStyle": "jagged", "end": 308, "endStyle": "straight", "aliStart": 115, "text": "Cupin_8", "colour": "#9999ff", "aliEnd": 289, "start": 42, "href": "http://pfam.xfam.org/family/PF13621.4", "type": "pfama", "display": "true", "metadata": {"end": 308, "description": "This cupin like domain shares similarity to the JmjC domain.", "database": "PfamA", "aliStart": 115, "scoreName": "E-value", "accession": "PF13621.4", "start": 42, "score": 0.0013, "identifier": "Cupin-like domain", "type": "DBD", "aliEnd": 289}}], "length": 783}
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JmjC-domain proteins may be protein hydroxylases that catalyse a novel histone modification [4]. 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{"regions": [{"startStyle": "curved", "end": 170, "endStyle": "curved", "aliStart": 126, "text": "zfCXXC", "colour": "#009900", "aliEnd": 170, "start": 124, "href": "http://pfam.xfam.org/family/PF02008.18", "type": "pfama", "display": "true", "metadata": {"end": 170, "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": 126, "scoreName": "E-value", "accession": "PF02008.18", "start": 124, "score": 3.3e-13, "identifier": "CXXC zinc finger domain", "type": "DBD", "aliEnd": 170}}, {"startStyle": "straight", "end": 237, "endStyle": "straight", "aliStart": 175, "text": "PHD_4", "colour": "#9999ff", "aliEnd": 237, "start": 175, "href": "http://pfam.xfam.org/family/PF16866.3", "type": "pfama", "display": "true", "metadata": {"end": 237, "description": NaN, "database": "PfamA", "aliStart": 175, "scoreName": "E-value", "accession": "PF16866.3", "start": 175, "score": 1.2e-21, "identifier": "PHD-finger", "type": "DBD", "aliEnd": 237}}, {"startStyle": "jagged", "end": 496, "endStyle": "straight", "aliStart": 457, "text": "F-box", "colour": "#9999ff", "aliEnd": 495, "start": 450, "href": "http://pfam.xfam.org/family/PF00646.31", "type": "pfama", "display": "true", "metadata": {"end": 496, "description": "This domain is approximately 50 amino acids long, and is usually found in the N-terminal half of a variety of proteins. Two motifs that are commonly found associated with the F-box domain are the leucine rich repeats (LRRs; Pfam:PF00560 and Pfam:PF07723) and the WD repeat (Pfam:PF00400). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression [3].", "database": "PfamA", "aliStart": 457, "scoreName": "E-value", "accession": "PF00646.31", "start": 450, "score": 1.8e-09, "identifier": "F-box domain", "type": "DBD", "aliEnd": 495}}, {"startStyle": "jagged", "end": 638, "endStyle": "jagged", "aliStart": 614, "text": "F-box", "colour": "#9999ff", "aliEnd": 636, "start": 610, "href": "http://pfam.xfam.org/family/PF00646.31", "type": "pfama", "display": "true", "metadata": {"end": 638, "description": "This domain is approximately 50 amino acids long, and is usually found in the N-terminal half of a variety of proteins. Two motifs that are commonly found associated with the F-box domain are the leucine rich repeats (LRRs; Pfam:PF00560 and Pfam:PF07723) and the WD repeat (Pfam:PF00400). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression [3].", "database": "PfamA", "aliStart": 614, "scoreName": "E-value", "accession": "PF00646.31", "start": 610, "score": 1.8e-09, "identifier": "F-box domain", "type": "DBD", "aliEnd": 636}}, {"startStyle": "jagged", "end": 497, "endStyle": "straight", "aliStart": 457, "text": "F-box-like", "colour": "#9999ff", "aliEnd": 496, "start": 456, "href": "http://pfam.xfam.org/family/PF12937.5", "type": "pfama", "display": "true", "metadata": {"end": 497, "description": "This is an F-box-like family.", "database": "PfamA", "aliStart": 457, "scoreName": "E-value", "accession": "PF12937.5", "start": 456, "score": 7.8e-09, "identifier": "F-box-like", "type": "DBD", "aliEnd": 496}}, {"startStyle": "jagged", "end": 676, "endStyle": "jagged", "aliStart": 656, "text": "LRR_6", "colour": "#9999ff", "aliEnd": 671, "start": 655, "href": "http://pfam.xfam.org/family/PF13516.4", "type": "pfama", "display": "true", "metadata": {"end": 676, "description": NaN, "database": "PfamA", "aliStart": 656, "scoreName": "E-value", "accession": "PF13516.4", "start": 655, "score": 0.00044, "identifier": "Leucine Rich repeat", "type": "DBD", "aliEnd": 671}}], "length": 724}