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MGP004560

UniProt Annotations

Entry Information
Gene Namelysine (K)-specific demethylase 2A
Protein EntryKDM2A_HUMAN
UniProt IDQ9Y2K7
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=5; Name=1; IsoId=Q9Y2K7-1; Sequence=Displayed; Name=2; IsoId=Q9Y2K7-2; Sequence=VSP_017468; Note=No experimental confirmation available.; Name=4; IsoId=Q9Y2K7-4; Sequence=VSP_046938; Name=5; IsoId=Q9Y2K7-5; Sequence=VSP_046939, VSP_046940; Name=3; IsoId=Q9Y2K7-3; Sequence=VSP_017469, VSP_017470;
Catalytic ActivityProtein N(6)-methyl-L-lysine + 2-oxoglutarate + O(2) = protein L-lysine + succinate + formaldehyde + CO(2). {ECO:0000269|PubMed:16362057}.
Catalytic ActivityProtein N(6),N(6)-dimethyl-L-lysine + 2- oxoglutarate + O(2) = protein N(6)-methyl-L-lysine + succinate + formaldehyde + CO(2). {ECO:0000269|PubMed:16362057}.
CofactorName=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:16362057}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269|PubMed:16362057};
DomainThe CXXC zinc finger preferentially recognizes nonmethylated CpG DNA, and binding is blocked when the CpG DNA is methylated.
DomainThe JmjC domain mediates demethylation activity and is required for satellite silencing.
FunctionHistone demethylase that specifically demethylates 'Lys- 36' of histone H3, thereby playing a central role in histone code. Preferentially demethylates dimethylated H3 'Lys-36' residue while it has weak or no activity for mono- and tri-methylated H3 'Lys- 36'. May also recognize and bind to some phosphorylated proteins and promote their ubiquitination and degradation. Required to maintain the heterochromatic state. Associates with centromeres and represses transcription of small non-coding RNAs that are encoded by the clusters of satellite repeats at the centromere. Required to sustain centromeric integrity and genomic stability, particularly during mitosis. {ECO:0000269|PubMed:16362057, ECO:0000269|PubMed:19001877}.
Sequence CautionSequence=AAD56012.1; Type=Erroneous initiation; Evidence={ECO:0000305}; Sequence=BAA76848.2; Type=Erroneous initiation; Evidence={ECO:0000305}; Sequence=BAB15795.1; Type=Frameshift; Positions=410; Evidence={ECO:0000305}; Sequence=BAJ05817.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
SimilarityBelongs to the JHDM1 histone demethylase family. {ECO:0000305}.
SimilarityContains 1 CXXC-type zinc finger. {ECO:0000255|PROSITE-ProRule:PRU00509}.
SimilarityContains 1 F-box domain. {ECO:0000305}.
SimilarityContains 1 JmjC domain. {ECO:0000255|PROSITE- ProRule:PRU00538}.
SimilarityContains 1 PHD-type zinc finger. {ECO:0000255|PROSITE- ProRule:PRU00146}.
SimilarityContains 6 LRR (leucine-rich) repeats. {ECO:0000305}.
Subcellular LocationNucleus, nucleoplasm {ECO:0000269|PubMed:19001877, ECO:0000269|PubMed:20417597}. Note=Punctate expression throughout the nucleoplasm and enriched in the perinucleolar region. Specifically nucleates at CpG islands where it's presence results in chromatin depleted in H3K36me2.
SubunitPart of a SCF (SKP1-cullin-F-box) protein ligase complex (By similarity). Interacts with CBX5/HP1A; the interaction promotes CBX5 localization to chromatin. {ECO:0000250, ECO:0000269|PubMed:19001877}.
Tissue SpecificityWidely expressed, with highest levels in brain, testis and ovary, followed by lung. {ECO:0000269|PubMed:10231032}.
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