KDM3A_HUMAN
ID KDM3A_HUMAN Reviewed; 1321 AA.
AC Q9Y4C1; D6W5M3; Q53S72; Q68D47; Q68UT9; Q6N050; Q8IY08;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 4.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Lysine-specific demethylase 3A;
DE EC=1.14.11.65 {ECO:0000269|PubMed:16603237};
DE AltName: Full=JmjC domain-containing histone demethylation protein 2A;
DE AltName: Full=Jumonji domain-containing protein 1A;
DE AltName: Full=[histone H3]-dimethyl-L-lysine(9) demethylase 3A {ECO:0000305};
GN Name=KDM3A; Synonyms=JHDM2A, JMJD1, JMJD1A, KIAA0742, TSGA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-212.
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS VAL-212 AND PRO-447.
RC TISSUE=Fetal kidney, Salivary gland, and Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-212.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, DOMAIN, AND MUTAGENESIS OF HIS-1120.
RX PubMed=16603237; DOI=10.1016/j.cell.2006.03.027;
RA Yamane K., Toumazou C., Tsukada Y.I., Erdjument-Bromage H., Tempst P.,
RA Wong J., Zhang Y.;
RT "JHDM2A, a JmjC-containing H3K9 demethylase, facilitates transcription
RT activation by androgen receptor.";
RL Cell 125:483-495(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-895, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325; SER-445 AND SER-766, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP FUNCTION, AND MUTAGENESIS OF HIS-1120.
RX PubMed=28262558; DOI=10.1016/j.chembiol.2017.02.006;
RA Tumber A., Nuzzi A., Hookway E.S., Hatch S.B., Velupillai S., Johansson C.,
RA Kawamura A., Savitsky P., Yapp C., Szykowska A., Wu N., Bountra C.,
RA Strain-Damerell C., Burgess-Brown N.A., Ruda G.F., Fedorov O., Munro S.,
RA England K.S., Nowak R.P., Schofield C.J., La Thangue N.B., Pawlyn C.,
RA Davies F., Morgan G., Athanasou N., Muller S., Oppermann U., Brennan P.E.;
RT "Potent and Selective KDM5 Inhibitor Stops Cellular Demethylation of
RT H3K4me3 at Transcription Start Sites and Proliferation of MM1S Myeloma
RT Cells.";
RL Cell Chem. Biol. 24:371-380(2017).
RN [12]
RP VARIANT [LARGE SCALE ANALYSIS] HIS-187.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-9' of
CC histone H3, thereby playing a central role in histone code.
CC Preferentially demethylates mono- and dimethylated H3 'Lys-9' residue,
CC with a preference for dimethylated residue, while it has weak or no
CC activity on trimethylated H3 'Lys-9'. Demethylation of Lys residue
CC generates formaldehyde and succinate. Involved in hormone-dependent
CC transcriptional activation, by participating in recruitment to
CC androgen-receptor target genes, resulting in H3 'Lys-9' demethylation
CC and transcriptional activation. Involved in spermatogenesis by
CC regulating expression of target genes such as PRM1 and TNP1 which are
CC required for packaging and condensation of sperm chromatin. Involved in
CC obesity resistance through regulation of metabolic genes such as PPARA
CC and UCP1. {ECO:0000269|PubMed:16603237, ECO:0000269|PubMed:28262558}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3]
CC + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(9)-[histone H3] + 2
CC succinate; Xref=Rhea:RHEA:60188, Rhea:RHEA-COMP:15541, Rhea:RHEA-
CC COMP:15546, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:61976; EC=1.14.11.65;
CC Evidence={ECO:0000269|PubMed:16603237};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:16603237};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269|PubMed:16603237};
CC -!- INTERACTION:
CC Q9Y4C1; O75582: RPS6KA5; NbExp=3; IntAct=EBI-2515339, EBI-73869;
CC Q9Y4C1; O75582-1: RPS6KA5; NbExp=3; IntAct=EBI-2515339, EBI-16135973;
CC Q9Y4C1; P42224-1: STAT1; NbExp=8; IntAct=EBI-2515339, EBI-15711971;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Nuclear in round spermatids. When spermatids start to elongate,
CC localizes to the cytoplasm where it forms distinct foci which disappear
CC in mature spermatozoa (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The JmjC domain and the C6-type zinc-finger are required for
CC the demethylation activity. {ECO:0000269|PubMed:16603237}.
CC -!- DOMAIN: Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are known to mediate the
CC association with nuclear receptors. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the JHDM2 histone demethylase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34462.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB018285; BAA34462.2; ALT_INIT; mRNA.
DR EMBL; AL832150; CAH18459.3; -; Transcribed_RNA.
DR EMBL; BX640698; CAE45820.1; -; mRNA.
DR EMBL; CR749581; CAH18373.1; -; mRNA.
DR EMBL; AC068288; AAY24210.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99453.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99456.1; -; Genomic_DNA.
DR CCDS; CCDS1990.1; -.
DR RefSeq; NP_001140160.1; NM_001146688.1.
DR RefSeq; NP_060903.2; NM_018433.5.
DR RefSeq; XP_016859982.1; XM_017004493.1.
DR AlphaFoldDB; Q9Y4C1; -.
DR SMR; Q9Y4C1; -.
DR BioGRID; 120927; 47.
DR DIP; DIP-53661N; -.
DR IntAct; Q9Y4C1; 12.
DR MINT; Q9Y4C1; -.
DR STRING; 9606.ENSP00000386660; -.
DR BindingDB; Q9Y4C1; -.
DR ChEMBL; CHEMBL1938209; -.
DR GuidetoPHARMACOLOGY; 2673; -.
DR CarbonylDB; Q9Y4C1; -.
DR GlyGen; Q9Y4C1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y4C1; -.
DR PhosphoSitePlus; Q9Y4C1; -.
DR SwissPalm; Q9Y4C1; -.
DR BioMuta; KDM3A; -.
DR DMDM; 308153659; -.
DR EPD; Q9Y4C1; -.
DR jPOST; Q9Y4C1; -.
DR MassIVE; Q9Y4C1; -.
DR MaxQB; Q9Y4C1; -.
DR PaxDb; Q9Y4C1; -.
DR PeptideAtlas; Q9Y4C1; -.
DR PRIDE; Q9Y4C1; -.
DR ProteomicsDB; 86157; -.
DR Antibodypedia; 32101; 435 antibodies from 35 providers.
DR DNASU; 55818; -.
DR Ensembl; ENST00000312912.10; ENSP00000323659.5; ENSG00000115548.17.
DR Ensembl; ENST00000409064.5; ENSP00000386516.1; ENSG00000115548.17.
DR Ensembl; ENST00000409556.5; ENSP00000386660.1; ENSG00000115548.17.
DR GeneID; 55818; -.
DR KEGG; hsa:55818; -.
DR MANE-Select; ENST00000312912.10; ENSP00000323659.5; NM_018433.6; NP_060903.2.
DR UCSC; uc002sri.5; human.
DR CTD; 55818; -.
DR DisGeNET; 55818; -.
DR GeneCards; KDM3A; -.
DR HGNC; HGNC:20815; KDM3A.
DR HPA; ENSG00000115548; Low tissue specificity.
DR MIM; 611512; gene.
DR neXtProt; NX_Q9Y4C1; -.
DR OpenTargets; ENSG00000115548; -.
DR PharmGKB; PA164721293; -.
DR VEuPathDB; HostDB:ENSG00000115548; -.
DR eggNOG; KOG1356; Eukaryota.
DR GeneTree; ENSGT00940000160135; -.
DR HOGENOM; CLU_002991_0_0_1; -.
DR InParanoid; Q9Y4C1; -.
DR OMA; SPQVTTH; -.
DR OrthoDB; 262871at2759; -.
DR PhylomeDB; Q9Y4C1; -.
DR TreeFam; TF324723; -.
DR BioCyc; MetaCyc:ENSG00000115548-MON; -.
DR BRENDA; 1.14.11.65; 2681.
DR PathwayCommons; Q9Y4C1; -.
DR Reactome; R-HSA-3214842; HDMs demethylate histones.
DR Reactome; R-HSA-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR SignaLink; Q9Y4C1; -.
DR SIGNOR; Q9Y4C1; -.
DR BioGRID-ORCS; 55818; 11 hits in 1088 CRISPR screens.
DR ChiTaRS; KDM3A; human.
DR GenomeRNAi; 55818; -.
DR Pharos; Q9Y4C1; Tchem.
DR PRO; PR:Q9Y4C1; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9Y4C1; protein.
DR Bgee; ENSG00000115548; Expressed in secondary oocyte and 205 other tissues.
DR ExpressionAtlas; Q9Y4C1; baseline and differential.
DR Genevisible; Q9Y4C1; HS.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0140683; F:histone H3-di/monomethyl-lysine-9 demethylase activity; IDA:FlyBase.
DR GO; GO:0032454; F:histone H3-methyl-lysine-9 demethylase activity; IMP:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IMP:UniProtKB.
DR GO; GO:0050681; F:nuclear androgen receptor binding; IDA:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0030521; P:androgen receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0046293; P:formaldehyde biosynthetic process; IDA:UniProtKB.
DR GO; GO:0033169; P:histone H3-K9 demethylation; IDA:UniProtKB.
DR GO; GO:0036123; P:histone H3-K9 dimethylation; IEA:Ensembl.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0051573; P:negative regulation of histone H3-K9 methylation; IEA:Ensembl.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:2000736; P:regulation of stem cell differentiation; IEA:Ensembl.
DR GO; GO:2000036; P:regulation of stem cell population maintenance; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007290; P:spermatid nucleus elongation; IEA:Ensembl.
DR InterPro; IPR045109; JHDM2-like.
DR InterPro; IPR003347; JmjC_dom.
DR PANTHER; PTHR12549; PTHR12549; 1.
DR Pfam; PF02373; JmjC; 1.
DR SMART; SM00558; JmjC; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Chromatin regulator; Cytoplasm; Differentiation;
KW Dioxygenase; Iron; Metal-binding; Nucleus; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Spermatogenesis; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1321
FT /note="Lysine-specific demethylase 3A"
FT /id="PRO_0000084285"
FT DOMAIN 1058..1281
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT ZN_FING 662..687
FT /note="C6-type"
FT /evidence="ECO:0000255"
FT REGION 307..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 885..889
FT /note="LXXLL motif"
FT COMPBIAS 310..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1120
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305|PubMed:16603237,
FT ECO:0000305|PubMed:28262558"
FT BINDING 1122
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 1249
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 766
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 895
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VARIANT 187
FT /note="D -> H (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035940"
FT VARIANT 194
FT /note="E -> K (in dbSNP:rs13424350)"
FT /id="VAR_030623"
FT VARIANT 212
FT /note="I -> V (in dbSNP:rs2030259)"
FT /evidence="ECO:0000269|PubMed:17974005,
FT ECO:0000269|PubMed:9872452, ECO:0000269|Ref.4"
FT /id="VAR_026220"
FT VARIANT 447
FT /note="S -> P (in dbSNP:rs34605051)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_055977"
FT VARIANT 710
FT /note="V -> E (in dbSNP:rs11677451)"
FT /id="VAR_030624"
FT MUTAGEN 1120
FT /note="H->A: Abolishes lysine-specific histone demethylase
FT activity."
FT /evidence="ECO:0000269|PubMed:28262558"
FT MUTAGEN 1120
FT /note="H->Y: Abolishes histone demethylase activity."
FT /evidence="ECO:0000269|PubMed:16603237"
FT CONFLICT 24
FT /note="D -> G (in Ref. 2; CAH18459/CAH18373)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="V -> A (in Ref. 2; CAE45820)"
FT /evidence="ECO:0000305"
FT CONFLICT 500
FT /note="S -> G (in Ref. 2; CAH18373)"
FT /evidence="ECO:0000305"
FT CONFLICT 698
FT /note="G -> GG (in Ref. 2; CAH18459)"
FT /evidence="ECO:0000305"
FT CONFLICT 729
FT /note="K -> KG (in Ref. 2; CAH18459)"
FT /evidence="ECO:0000305"
FT CONFLICT 767
FT /note="K -> R (in Ref. 2; CAH18459)"
FT /evidence="ECO:0000305"
FT CONFLICT 773
FT /note="T -> TQT (in Ref. 2; CAH18459)"
FT /evidence="ECO:0000305"
FT CONFLICT 980
FT /note="G -> R (in Ref. 2; CAE45820)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1321 AA; 147341 MW; 9689B3279F450C8A CRC64;
MVLTLGESWP VLVGRRFLSL SAADGSDGSH DSWDVERVAE WPWLSGTIRA VSHTDVTKKD
LKVCVEFDGE SWRKRRWIEV YSLLRRAFLV EHNLVLAERK SPEISERIVQ WPAITYKPLL
DKAGLGSITS VRFLGDQQRV FLSKDLLKPI QDVNSLRLSL TDNQIVSKEF QALIVKHLDE
SHLLKGDKNL VGSEVKIYSL DPSTQWFSAT VINGNPASKT LQVNCEEIPA LKIVDPSLIH
VEVVHDNLVT CGNSARIGAV KRKSSENNGT LVSKQAKSCS EASPSMCPVQ SVPTTVFKEI
LLGCTAATPP SKDPRQQSTP QAANSPPNLG AKIPQGCHKQ SLPEEISSCL NTKSEALRTK
PDVCKAGLLS KSSQIGTGDL KILTEPKGSC TQPKTNTDQE NRLESVPQAL TGLPKECLPT
KASSKAELEI ANPPELQKHL EHAPSPSDVS NAPEVKAGVN SDSPNNCSGK KVEPSALACR
SQNLKESSVK VDNESCCSRS NNKIQNAPSR KSVLTDPAKL KKLQQSGEAF VQDDSCVNIV
AQLPKCRECR LDSLRKDKEQ QKDSPVFCRF FHFRRLQFNK HGVLRVEGFL TPNKYDNEAI
GLWLPLTKNV VGIDLDTAKY ILANIGDHFC QMVISEKEAM STIEPHRQVA WKRAVKGVRE
MCDVCDTTIF NLHWVCPRCG FGVCVDCYRM KRKNCQQGAA YKTFSWLKCV KSQIHEPENL
MPTQIIPGKA LYDVGDIVHS VRAKWGIKAN CPCSNRQFKL FSKPASKEDL KQTSLAGEKP
TLGAVLQQNP SVLEPAAVGG EAASKPAGSM KPACPASTSP LNWLADLTSG NVNKENKEKQ
PTMPILKNEI KCLPPLPPLS KSSTVLHTFN STILTPVSNN NSGFLRNLLN SSTGKTENGL
KNTPKILDDI FASLVQNKTT SDLSKRPQGL TIKPSILGFD TPHYWLCDNR LLCLQDPNNK
SNWNVFRECW KQGQPVMVSG VHHKLNSELW KPESFRKEFG EQEVDLVNCR TNEIITGATV
GDFWDGFEDV PNRLKNEKEP MVLKLKDWPP GEDFRDMMPS RFDDLMANIP LPEYTRRDGK
LNLASRLPNY FVRPDLGPKM YNAYGLITPE DRKYGTTNLH LDVSDAANVM VYVGIPKGQC
EQEEEVLKTI QDGDSDELTI KRFIEGKEKP GALWHIYAAK DTEKIREFLK KVSEEQGQEN
PADHDPIHDQ SWYLDRSLRK RLHQEYGVQG WAIVQFLGDV VFIPAGAPHQ VHNLYSCIKV
AEDFVSPEHV KHCFWLTQEF RYLSQTHTNH EDKLQVKNVI YHAVKDAVAM LKASESSFGK
P
