Conclusion
Assessment
Binding Mode
Motif Status
Notes
Comments
Known motif
1 Monomer or homomultimer
High-throughput in vitro
Description
Description:
lysine demethylase 2B [Source:HGNC Symbol;Acc:HGNC:13610]
Entrez Summary
#!usr/local/bin/perl
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microRNAs (miRNAs) are short (20-24 nt) non-coding RNAs that are
involved in post-transcriptional regulation of gene expression in
multicellular organisms by affecting both the stability and translation of
mRNAs. miRNAs are transcribed by RNA polymerase II as part of capped and
polyadenylated primary transcripts (pri-miRNAs) that can be either
protein-coding or non-coding. The primary transcript is cleaved by the Drosha
ribonuclease III enzyme to produce an approximately 70-nt stem-loop precursor
miRNA (pre-miRNA), which is further cleaved by the cytoplasmic Dicer
ribonuclease to generate the mature miRNA and antisense miRNA star (miRNA*)
products. The mature miRNA is incorporated into a RNA-induced silencing
complex (RISC), which recognizes target mRNAs through imperfect base pairing
with the miRNA and most commonly results in translational inhibition or
destabilization of the target mRNA. The RefSeq represents the predicted
microRNA stem-loop. [provided by RefSeq, Sep 2009]
Ensembl ID:
ENSG00000089094
External Link:
CisBP
Interpro
IPR001810 ; IPR001965 ; IPR002857 ; IPR003347 ; IPR006553 ; IPR011011 ; IPR019787 ; ;
Protein Domain:
ENSP00000366271
Protein Domain:
ENSP00000445196
Protein Domain:
ENSP00000474307
Protein Domain:
ENSP00000366269
Protein Domain:
ENSP00000437821
Domain:
Protein: ENSP00000366271DBD: CxxCOther: Cupin_8, F-box, F-box-like, JmjC, PHD, PHD_4Protein: ENSP00000445196DBD: CxxCOther: Cupin_8, JmjC, PHD_4Protein: ENSP00000474307DBD: CxxCOther: Protein: ENSP00000366269DBD: CxxCOther: Cupin_8, F-box, F-box-like, JmjC, PHD, PHD_4Protein: ENSP00000437821DBD: CxxCOther: F-box, F-box-like, LRR_6, LRR_8, PHD, 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?
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
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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": 1051, "scoreName": "E-value", "accession": "PF00646.31", "start": 1050, "score": 4e-12, "identifier": "F-box domain", "type": "DBD", "aliEnd": 1106}}, {"startStyle": "jagged", "end": 1108, "endStyle": "straight", "aliStart": 1068, "text": "F-box-like", "colour": "#9999ff", "aliEnd": 1107, "start": 1067, "href": "http://pfam.xfam.org/family/PF12937.5", "type": "pfama", "display": "true", "metadata": {"end": 1108, "description": "This is an F-box-like family.", "database": "PfamA", "aliStart": 1068, "scoreName": "E-value", "accession": "PF12937.5", "start": 1067, "score": 3.4000000000000003e-09, "identifier": "F-box-like", "type": "DBD", "aliEnd": 1107}}, {"startStyle": "jagged", "end": 335, "endStyle": "straight", "aliStart": 142, "text": "Cupin_8", "colour": "#9999ff", "aliEnd": 318, "start": 21, "href": "http://pfam.xfam.org/family/PF13621.4", "type": "pfama", "display": "true", "metadata": {"end": 335, "description": "This cupin like domain shares similarity to the JmjC domain.", "database": "PfamA", "aliStart": 142, "scoreName": "E-value", "accession": "PF13621.4", "start": 21, "score": 3.3e-07, "identifier": "Cupin-like domain", "type": "DBD", "aliEnd": 318}}, {"startStyle": "straight", "end": 329, "endStyle": "straight", "aliStart": 229, "text": "JmjC", "colour": "#9999ff", "aliEnd": 322, "start": 229, "href": "http://pfam.xfam.org/family/PF02373.20", "type": "pfama", "display": "true", "metadata": {"end": 329, "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": 229, "scoreName": "E-value", "accession": "PF02373.20", "start": 229, "score": 2.4e-06, "identifier": "JmjC domain, hydroxylase", "type": "DBD", "aliEnd": 322}}, {"startStyle": "straight", "end": 725, "endStyle": "straight", "aliStart": 662, "text": "PHD", "colour": "#9999ff", "aliEnd": 724, "start": 661, "href": "http://pfam.xfam.org/family/PF00628.27", "type": "pfama", "display": "true", "metadata": {"end": 725, "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]. 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{"regions": [{"startStyle": "curved", "end": 651, "endStyle": "curved", "aliStart": 607, "text": "zfCXXC", "colour": "#009900", "aliEnd": 651, "start": 605, "href": "http://pfam.xfam.org/family/PF02008.18", "type": "pfama", "display": "true", "metadata": {"end": 651, "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": 607, "scoreName": "E-value", "accession": "PF02008.18", "start": 605, "score": 7.9e-15, "identifier": "CXXC zinc finger domain", "type": "DBD", "aliEnd": 651}}, {"startStyle": "straight", "end": 705, "endStyle": "jagged", "aliStart": 656, "text": "PHD_4", "colour": "#9999ff", "aliEnd": 702, "start": 656, "href": "http://pfam.xfam.org/family/PF16866.3", "type": "pfama", "display": "true", "metadata": {"end": 705, "description": NaN, "database": "PfamA", "aliStart": 656, "scoreName": "E-value", "accession": "PF16866.3", "start": 656, "score": 1.9e-15, "identifier": "PHD-finger", "type": "DBD", "aliEnd": 702}}, {"startStyle": "jagged", "end": 338, "endStyle": "straight", "aliStart": 142, "text": "Cupin_8", "colour": "#9999ff", "aliEnd": 318, "start": 23, "href": "http://pfam.xfam.org/family/PF13621.4", "type": "pfama", "display": "true", "metadata": {"end": 338, "description": "This cupin like domain shares similarity to the JmjC domain.", "database": "PfamA", "aliStart": 142, "scoreName": "E-value", "accession": "PF13621.4", "start": 23, "score": 9.6e-08, "identifier": "Cupin-like domain", "type": "DBD", "aliEnd": 318}}, {"startStyle": "straight", "end": 329, "endStyle": "straight", "aliStart": 229, "text": "JmjC", "colour": "#9999ff", "aliEnd": 322, "start": 229, "href": "http://pfam.xfam.org/family/PF02373.20", "type": "pfama", "display": "true", "metadata": {"end": 329, "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": 229, "scoreName": "E-value", "accession": "PF02373.20", "start": 229, "score": 8.2e-07, "identifier": "JmjC domain, hydroxylase", "type": "DBD", "aliEnd": 322}}], "length": 707}
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{"regions": [{"startStyle": "jagged", "end": 19, "endStyle": "curved", "aliStart": 1, "text": "zfCXXC", "colour": "#009900", "aliEnd": 19, "start": 1, "href": "http://pfam.xfam.org/family/PF02008.18", "type": "pfama", "display": "true", "metadata": {"end": 19, "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]. 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