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Lysine-specific demethylase 2A (EC 1.14.11.27) (CXXC-type zinc finger protein 8) (F-box and leucine-rich repeat protein 11) (F-box protein FBL7) (F-box protein Lilina) (F-box/LRR-repeat protein 11) (JmjC domain-containing histone demethylation protein 1A) ([Histone-H3]-lysine-36 demethylase 1A)

 KDM2A_HUMAN             Reviewed;        1162 AA.
Q9Y2K7; D4QA03; E9PIL6; I3VM55; Q49A21; Q4G0M3; Q69YY8; Q9BVH5;
Q9H7H5; Q9UK66;
07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
07-NOV-2003, sequence version 3.
18-JUL-2018, entry version 169.
RecName: Full=Lysine-specific demethylase 2A;
EC=1.14.11.27 {ECO:0000269|PubMed:16362057};
AltName: Full=CXXC-type zinc finger protein 8;
AltName: Full=F-box and leucine-rich repeat protein 11;
AltName: Full=F-box protein FBL7;
AltName: Full=F-box protein Lilina;
AltName: Full=F-box/LRR-repeat protein 11;
AltName: Full=JmjC domain-containing histone demethylation protein 1A;
AltName: Full=[Histone-H3]-lysine-36 demethylase 1A;
Name=KDM2A; Synonyms=CXXC8, FBL7, FBXL11, JHDM1A, KIAA1004;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=10945468; DOI=10.1006/geno.2000.6211;
Ilyin G.P., Rialland M., Pigeon C., Guguen-Guillouzo C.;
"cDNA cloning and expression analysis of new members of the mammalian
F-box protein family.";
Genomics 67:40-47(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
Tsuneoka M., Tanaka Y., Okamoto K., Teye K.;
Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
Iuchi S., Green H.;
Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND TISSUE
SPECIFICITY.
TISSUE=Brain;
PubMed=10231032; DOI=10.1093/dnares/6.1.63;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 6:63-70(1999).
[5]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Spleen;
PubMed=11214971; DOI=10.1093/dnares/7.6.357;
Hattori A., Okumura K., Nagase T., Kikuno R., Hirosawa M., Ohara O.;
"Characterization of long cDNA clones from human adult spleen.";
DNA Res. 7:357-366(2000).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
TISSUE=Eye, Testis, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 667-1162.
Pagano M.;
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1134-1162.
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[12]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY,
COFACTOR, DOMAIN, AND MUTAGENESIS OF HIS-212.
PubMed=16362057; DOI=10.1038/nature04433;
Tsukada Y., Fang J., Erdjument-Bromage H., Warren M.E., Borchers C.H.,
Tempst P., Zhang Y.;
"Histone demethylation by a family of JmjC domain-containing
proteins.";
Nature 439:811-816(2006).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-632, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[14]
FUNCTION, INTERACTION WITH CBX5, SUBCELLULAR LOCATION, AND MUTAGENESIS
OF CYS-571; CYS-574 AND CYS-577.
PubMed=19001877; DOI=10.4161/cc.7.22.7062;
Frescas D., Guardavaccaro D., Kuchay S.M., Kato H., Poleshko A.,
Basrur V., Elenitoba-Johnson K.S., Katz R.A., Pagano M.;
"KDM2A represses transcription of centromeric satellite repeats and
maintains the heterochromatic state.";
Cell Cycle 7:3539-3547(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-550; SER-558; THR-713
AND SER-731, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-692, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=T-cell;
PubMed=19367720; DOI=10.1021/pr800500r;
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
"Phosphorylation analysis of primary human T lymphocytes using
sequential IMAC and titanium oxide enrichment.";
J. Proteome Res. 7:5167-5176(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390; THR-550; SER-558;
THR-713; SER-731 AND SER-832, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; THR-550; SER-692 AND
SER-869, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[19]
SUBCELLULAR LOCATION, AND DOMAIN CXXC ZINC-FINGER.
PubMed=20417597; DOI=10.1016/j.molcel.2010.04.009;
Blackledge N.P., Zhou J.C., Tolstorukov M.Y., Farcas A.M., Park P.J.,
Klose R.J.;
"CpG islands recruit a histone H3 lysine 36 demethylase.";
Mol. Cell 38:179-190(2010).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-394; THR-550;
SER-558; SER-869 AND SER-883, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; THR-550; SER-558;
SER-692; SER-825; SER-832 AND SER-869, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[24]
FUNCTION, AND MUTAGENESIS OF 212-HIS--ASP-214.
PubMed=28262558; DOI=10.1016/j.chembiol.2017.02.006;
Tumber A., Nuzzi A., Hookway E.S., Hatch S.B., Velupillai S.,
Johansson C., Kawamura A., Savitsky P., Yapp C., Szykowska A., Wu N.,
Bountra C., Strain-Damerell C., Burgess-Brown N.A., Ruda G.F.,
Fedorov O., Munro S., England K.S., Nowak R.P., Schofield C.J.,
La Thangue N.B., Pawlyn C., Davies F., Morgan G., Athanasou N.,
Muller S., Oppermann U., Brennan P.E.;
"Potent and Selective KDM5 Inhibitor Stops Cellular Demethylation of
H3K4me3 at Transcription Start Sites and Proliferation of MM1S Myeloma
Cells.";
Cell Chem. Biol. 24:371-380(2017).
[25]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-505, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Histone 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, ECO:0000269|PubMed:28262558}.
-!- CATALYTIC ACTIVITY: Protein N(6),N(6)-dimethyl-L-lysine + 2 2-
oxoglutarate + 2 O(2) = protein L-lysine + 2 succinate + 2
formaldehyde + 2 CO(2). {ECO:0000269|PubMed:16362057}.
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Evidence={ECO:0000269|PubMed:16362057};
Note=Binds 1 Fe(2+) ion per subunit.
{ECO:0000269|PubMed:16362057};
-!- SUBUNIT: Part 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}.
-!- INTERACTION:
Q04206:RELA; NbExp=2; IntAct=EBI-765758, EBI-73886;
P63208:SKP1; NbExp=2; IntAct=EBI-765758, EBI-307486;
-!- SUBCELLULAR LOCATION: Nucleus, 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.
-!- ALTERNATIVE PRODUCTS:
Event=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;
-!- TISSUE SPECIFICITY: Widely expressed, with highest levels in
brain, testis and ovary, followed by lung.
{ECO:0000269|PubMed:10231032}.
-!- DOMAIN: The JmjC domain mediates demethylation activity and is
required for satellite silencing.
-!- DOMAIN: The CXXC zinc finger preferentially recognizes
nonmethylated CpG DNA, and binding is blocked when the CpG DNA is
methylated.
-!- SIMILARITY: Belongs to the JHDM1 histone demethylase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD56012.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAA76848.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; 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};
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EMBL; AB023221; BAA76848.2; ALT_INIT; mRNA.
EMBL; AB490246; BAJ05817.1; ALT_INIT; mRNA.
EMBL; JQ710743; AFK81542.1; -; mRNA.
EMBL; JQ710744; AFK81543.1; -; mRNA.
EMBL; AK024505; BAB15795.1; ALT_FRAME; mRNA.
EMBL; AP000729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP001885; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC001203; AAH01203.1; -; mRNA.
EMBL; BC047371; AAH47371.1; -; mRNA.
EMBL; BC047486; AAH47486.1; -; mRNA.
EMBL; BC064360; AAH64360.1; -; mRNA.
EMBL; AF179221; AAD56012.1; ALT_INIT; mRNA.
EMBL; AL117517; CAH10721.1; -; mRNA.
CCDS; CCDS44657.1; -. [Q9Y2K7-1]
CCDS; CCDS58148.1; -. [Q9Y2K7-5]
RefSeq; NP_001243334.1; NM_001256405.1. [Q9Y2K7-5]
RefSeq; NP_036440.1; NM_012308.2. [Q9Y2K7-1]
RefSeq; XP_011543163.1; XM_011544861.1. [Q9Y2K7-2]
UniGene; Hs.124147; -.
PDB; 2YU1; X-ray; 2.70 A; A=1-517.
PDB; 2YU2; X-ray; 2.70 A; A=1-517.
PDB; 4BBQ; X-ray; 2.24 A; A/B=567-681.
PDBsum; 2YU1; -.
PDBsum; 2YU2; -.
PDBsum; 4BBQ; -.
ProteinModelPortal; Q9Y2K7; -.
SMR; Q9Y2K7; -.
BioGrid; 116639; 38.
DIP; DIP-34596N; -.
IntAct; Q9Y2K7; 21.
MINT; Q9Y2K7; -.
STRING; 9606.ENSP00000432786; -.
BindingDB; Q9Y2K7; -.
ChEMBL; CHEMBL1938210; -.
GuidetoPHARMACOLOGY; 2671; -.
CarbonylDB; Q9Y2K7; -.
iPTMnet; Q9Y2K7; -.
PhosphoSitePlus; Q9Y2K7; -.
BioMuta; KDM2A; -.
DMDM; 38257795; -.
EPD; Q9Y2K7; -.
PaxDb; Q9Y2K7; -.
PeptideAtlas; Q9Y2K7; -.
PRIDE; Q9Y2K7; -.
ProteomicsDB; 85827; -.
ProteomicsDB; 85828; -. [Q9Y2K7-2]
ProteomicsDB; 85829; -. [Q9Y2K7-3]
Ensembl; ENST00000398645; ENSP00000381640; ENSG00000173120. [Q9Y2K7-3]
Ensembl; ENST00000529006; ENSP00000432786; ENSG00000173120. [Q9Y2K7-1]
Ensembl; ENST00000530342; ENSP00000435776; ENSG00000173120. [Q9Y2K7-5]
GeneID; 22992; -.
KEGG; hsa:22992; -.
UCSC; uc001ojw.4; human. [Q9Y2K7-1]
CTD; 22992; -.
DisGeNET; 22992; -.
EuPathDB; HostDB:ENSG00000173120.14; -.
GeneCards; KDM2A; -.
HGNC; HGNC:13606; KDM2A.
HPA; CAB012272; -.
HPA; HPA044251; -.
MIM; 605657; gene.
neXtProt; NX_Q9Y2K7; -.
OpenTargets; ENSG00000173120; -.
PharmGKB; PA164721195; -.
eggNOG; KOG1633; Eukaryota.
eggNOG; KOG1947; Eukaryota.
eggNOG; ENOG410XQXU; LUCA.
GeneTree; ENSGT00550000074396; -.
HOGENOM; HOG000007396; -.
InParanoid; Q9Y2K7; -.
KO; K10276; -.
OMA; CPKCYQG; -.
OrthoDB; EOG091G00M1; -.
PhylomeDB; Q9Y2K7; -.
TreeFam; TF106480; -.
Reactome; R-HSA-3214842; HDMs demethylate histones.
SIGNOR; Q9Y2K7; -.
ChiTaRS; KDM2A; human.
EvolutionaryTrace; Q9Y2K7; -.
GeneWiki; KDM2A; -.
GenomeRNAi; 22992; -.
PRO; PR:Q9Y2K7; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000173120; -.
CleanEx; HS_FBXL11; -.
ExpressionAtlas; Q9Y2K7; baseline and differential.
Genevisible; Q9Y2K7; HS.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0032452; F:histone demethylase activity; TAS:Reactome.
GO; GO:0051864; F:histone demethylase activity (H3-K36 specific); IMP:UniProtKB.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:UniProtKB.
GO; GO:0070544; P:histone H3-K36 demethylation; IMP:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.30.40.10; -; 1.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR001810; F-box_dom.
InterPro; IPR003347; JmjC_dom.
InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR019786; Zinc_finger_PHD-type_CS.
InterPro; IPR002857; Znf_CXXC.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR001965; Znf_PHD.
InterPro; IPR019787; Znf_PHD-finger.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF00646; F-box; 1.
Pfam; PF02373; JmjC; 1.
Pfam; PF16866; PHD_4; 1.
Pfam; PF02008; zf-CXXC; 1.
SMART; SM00558; JmjC; 1.
SMART; SM00367; LRR_CC; 3.
SMART; SM00249; PHD; 1.
SUPFAM; SSF57903; SSF57903; 1.
PROSITE; PS51184; JMJC; 1.
PROSITE; PS51058; ZF_CXXC; 1.
PROSITE; PS01359; ZF_PHD_1; 1.
PROSITE; PS50016; ZF_PHD_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chromatin regulator;
Complete proteome; Dioxygenase; DNA-binding; Iron; Isopeptide bond;
Leucine-rich repeat; Metal-binding; Nucleus; Oxidoreductase;
Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; Ubl conjugation; Ubl conjugation pathway;
Zinc; Zinc-finger.
CHAIN 1 1162 Lysine-specific demethylase 2A.
/FTId=PRO_0000119855.
DOMAIN 148 316 JmjC. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
DOMAIN 889 936 F-box.
REPEAT 961 982 LRR 1.
REPEAT 984 1010 LRR 2.
REPEAT 1048 1073 LRR 3.
REPEAT 1074 1103 LRR 4.
REPEAT 1104 1128 LRR 5.
REPEAT 1129 1156 LRR 6.
ZN_FING 564 610 CXXC-type. {ECO:0000255|PROSITE-
ProRule:PRU00509}.
ZN_FING 617 678 PHD-type. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
METAL 212 212 Iron; catalytic.
{ECO:0000305|PubMed:16362057}.
METAL 214 214 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
METAL 284 284 Iron; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
BINDING 209 209 Substrate. {ECO:0000250}.
BINDING 229 229 Substrate. {ECO:0000250}.
MOD_RES 28 28 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 390 390 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 394 394 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 550 550 Phosphothreonine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 558 558 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 632 632 Phosphothreonine.
{ECO:0000244|PubMed:17525332}.
MOD_RES 692 692 Phosphoserine.
{ECO:0000244|PubMed:19367720,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 713 713 Phosphothreonine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648}.
MOD_RES 718 718 Phosphoserine.
{ECO:0000250|UniProtKB:P59997}.
MOD_RES 731 731 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648}.
MOD_RES 825 825 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 832 832 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 869 869 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 883 883 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
CROSSLNK 505 505 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 542 Missing (in isoform 4).
{ECO:0000303|Ref.3}.
/FTId=VSP_046938.
VAR_SEQ 1 439 Missing (in isoform 5).
{ECO:0000303|Ref.2}.
/FTId=VSP_046939.
VAR_SEQ 1 306 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_017468.
VAR_SEQ 440 492 DPQCAPRKDRQVHLTHFELEGLRCLVDKLESLPLHKKCVPT
GIEDEDALIADV -> MCSGRFQNIQVNPDFPRGRISNSFR
RTSSTENKTKTLGKLHQEPRQLQSDGKR (in isoform
5). {ECO:0000303|Ref.2}.
/FTId=VSP_046940.
VAR_SEQ 774 782 REKENNPSG -> LRQETLDKN (in isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.3}.
/FTId=VSP_017469.
VAR_SEQ 783 1162 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.3}.
/FTId=VSP_017470.
MUTAGEN 212 214 HVD->AVA: Abolishes lysine-specific
histone demethylase activity.
{ECO:0000269|PubMed:28262558}.
MUTAGEN 212 212 H->A: Abolishes histone demethylase
activity. {ECO:0000269|PubMed:16362057}.
MUTAGEN 571 571 C->A: Abolishes association with
centromeric heterochromatin; when
associated with A-574 and A-577.
{ECO:0000269|PubMed:19001877}.
MUTAGEN 574 574 C->A: Abolishes association with
centromeric heterochromatin; when
associated with A-571 and A-577.
{ECO:0000269|PubMed:19001877}.
MUTAGEN 577 577 C->A: Abolishes association with
centromeric heterochromatin; when
associated with A-571 and A-574.
{ECO:0000269|PubMed:19001877}.
CONFLICT 518 518 K -> I (in Ref. 8; AAH47371).
{ECO:0000305}.
CONFLICT 657 657 D -> G (in Ref. 8; AAH47371).
{ECO:0000305}.
CONFLICT 1128 1128 Missing (in Ref. 8; AAH01203).
{ECO:0000305}.
STRAND 36 38 {ECO:0000244|PDB:2YU2}.
HELIX 40 45 {ECO:0000244|PDB:2YU1}.
HELIX 59 61 {ECO:0000244|PDB:2YU1}.
HELIX 64 70 {ECO:0000244|PDB:2YU1}.
STRAND 76 80 {ECO:0000244|PDB:2YU1}.
TURN 82 85 {ECO:0000244|PDB:2YU2}.
HELIX 95 101 {ECO:0000244|PDB:2YU1}.
HELIX 123 130 {ECO:0000244|PDB:2YU1}.
TURN 134 136 {ECO:0000244|PDB:2YU1}.
STRAND 141 146 {ECO:0000244|PDB:2YU1}.
HELIX 154 156 {ECO:0000244|PDB:2YU1}.
HELIX 161 166 {ECO:0000244|PDB:2YU1}.
HELIX 168 172 {ECO:0000244|PDB:2YU1}.
HELIX 175 177 {ECO:0000244|PDB:2YU1}.
STRAND 199 203 {ECO:0000244|PDB:2YU1}.
STRAND 208 212 {ECO:0000244|PDB:2YU1}.
HELIX 215 217 {ECO:0000244|PDB:2YU1}.
STRAND 219 227 {ECO:0000244|PDB:2YU1}.
STRAND 229 234 {ECO:0000244|PDB:2YU1}.
HELIX 238 249 {ECO:0000244|PDB:2YU1}.
STRAND 254 256 {ECO:0000244|PDB:2YU1}.
HELIX 258 261 {ECO:0000244|PDB:2YU1}.
STRAND 266 270 {ECO:0000244|PDB:2YU1}.
STRAND 275 278 {ECO:0000244|PDB:2YU1}.
STRAND 283 287 {ECO:0000244|PDB:2YU1}.
STRAND 292 299 {ECO:0000244|PDB:2YU1}.
STRAND 302 304 {ECO:0000244|PDB:2YU1}.
HELIX 305 317 {ECO:0000244|PDB:2YU1}.
HELIX 329 345 {ECO:0000244|PDB:2YU1}.
HELIX 352 362 {ECO:0000244|PDB:2YU1}.
HELIX 455 469 {ECO:0000244|PDB:2YU1}.
HELIX 473 475 {ECO:0000244|PDB:2YU1}.
STRAND 480 483 {ECO:0000244|PDB:2YU1}.
HELIX 485 498 {ECO:0000244|PDB:2YU1}.
STRAND 499 501 {ECO:0000244|PDB:2YU1}.
HELIX 504 507 {ECO:0000244|PDB:2YU1}.
HELIX 575 578 {ECO:0000244|PDB:4BBQ}.
HELIX 586 590 {ECO:0000244|PDB:4BBQ}.
HELIX 592 594 {ECO:0000244|PDB:4BBQ}.
HELIX 605 607 {ECO:0000244|PDB:4BBQ}.
TURN 621 623 {ECO:0000244|PDB:4BBQ}.
HELIX 629 632 {ECO:0000244|PDB:4BBQ}.
HELIX 635 637 {ECO:0000244|PDB:4BBQ}.
STRAND 640 642 {ECO:0000244|PDB:4BBQ}.
TURN 643 645 {ECO:0000244|PDB:4BBQ}.
HELIX 651 653 {ECO:0000244|PDB:4BBQ}.
STRAND 664 671 {ECO:0000244|PDB:4BBQ}.
TURN 673 675 {ECO:0000244|PDB:4BBQ}.
SEQUENCE 1162 AA; 132793 MW; 88620A363A5C5842 CRC64;
MEPEEERIRY SQRLRGTMRR RYEDDGISDD EIEGKRTFDL EEKLHTNKYN ANFVTFMEGK
DFNVEYIQRG GLRDPLIFKN SDGLGIKMPD PDFTVNDVKM CVGSRRMVDV MDVNTQKGIE
MTMAQWTRYY ETPEEEREKL YNVISLEFSH TRLENMVQRP STVDFIDWVD NMWPRHLKES
QTESTNAILE MQYPKVQKYC LMSVRGCYTD FHVDFGGTSV WYHIHQGGKV FWLIPPTAHN
LELYENWLLS GKQGDIFLGD RVSDCQRIEL KQGYTFVIPS GWIHAVYTPT DTLVFGGNFL
HSFNIPMQLK IYNIEDRTRV PNKFRYPFYY EMCWYVLERY VYCITNRSHL TKEFQKESLS
MDLELNGLES GNGDEEAVDR EPRRLSSRRS VLTSPVANGV NLDYDGLGKT CRSLPSLKKT
LAGDSSSDCS RGSHNGQVWD PQCAPRKDRQ VHLTHFELEG LRCLVDKLES LPLHKKCVPT
GIEDEDALIA DVKILLEELA NSDPKLALTG VPIVQWPKRD KLKFPTRPKV RVPTIPITKP
HTMKPAPRLT PVRPAAASPI VSGARRRRVR CRKCKACVQG ECGVCHYCRD MKKFGGPGRM
KQSCVLRQCL APRLPHSVTC SLCGEVDQNE ETQDFEKKLM ECCICNEIVH PGCLQMDGEG
LLNEELPNCW ECPKCYQEDS SEKAQKRKME ESDEEAVQAK VLRPLRSCDE PLTPPPHSPT
SMLQLIHDPV SPRGMVTRSS PGAGPSDHHS ASRDERFKRR QLLRLQATER TMVREKENNP
SGKKELSEVE KAKIRGSYLT VTLQRPTKEL HGTSIVPKLQ AITASSANLR HSPRVLVQHC
PARTPQRGDE EGLGGEEEEE EEEEEEDDSA EEGGAARLNG RGSWAQDGDE SWMQREVWMS
VFRYLSRREL CECMRVCKTW YKWCCDKRLW TKIDLSRCKA IVPQALSGII KRQPVSLDLS
WTNISKKQLT WLVNRLPGLK DLLLAGCSWS AVSALSTSSC PLLRTLDLRW AVGIKDPQIR
DLLTPPADKP GQDNRSKLRN MTDFRLAGLD ITDATLRLII RHMPLLSRLD LSHCSHLTDQ
SSNLLTAVGS STRYSLTELN MAGCNKLTDQ TLIYLRRIAN VTLIDLRGCK QITRKACEHF
ISDLSINSLY CLSDEKLIQK IS


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