KDM1A_HUMAN
ID KDM1A_HUMAN Reviewed; 852 AA.
AC O60341; A8MWP9; Q5TH94; Q5TH95; Q86VT7; Q8IXK4; Q8NDP6; Q8TAZ3; Q96AW4;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 217.
DE RecName: Full=Lysine-specific histone demethylase 1A {ECO:0000305};
DE EC=1.14.99.66 {ECO:0000269|PubMed:15620353, ECO:0000269|PubMed:15811342};
DE AltName: Full=BRAF35-HDAC complex protein BHC110;
DE AltName: Full=Flavin-containing amine oxidase domain-containing protein 2;
DE AltName: Full=[histone H3]-dimethyl-L-lysine(4) FAD-dependent demethylase 1A;
GN Name=KDM1A {ECO:0000312|HGNC:HGNC:29079};
GN Synonyms=AOF2, KDM1, KIAA0601, LSD1;
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] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, Skin, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 245-852 (ISOFORM 1).
RC TISSUE=Brain;
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 [5]
RP PARTIAL PROTEIN SEQUENCE, INTERACTION WITH A HISTONE DEACETYLASE-CONTAINING
RP COMPLEX, AND FUNCTION.
RX PubMed=12032298; DOI=10.1073/pnas.112008599;
RA Hakimi M.-A., Bochar D.A., Chenoweth J., Lane W.S., Mandel G.,
RA Shiekhattar R.;
RT "A core-BRAF35 complex containing histone deacetylase mediates repression
RT of neuronal-specific genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:7420-7425(2002).
RN [6]
RP INTERACTION WITH THE HDAC1 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY,
RP AND SUBCELLULAR LOCATION.
RX PubMed=11102443; DOI=10.1074/jbc.m007372200;
RA Humphrey G.W., Wang Y., Russanova V.R., Hirai T., Qin J., Nakatani Y.,
RA Howard B.H.;
RT "Stable histone deacetylase complexes distinguished by the presence of SANT
RT domain proteins CoREST/kiaa0071 and Mta-L1.";
RL J. Biol. Chem. 276:6817-6824(2001).
RN [7]
RP INTERACTION WITH A HISTONE DEACETYLASE-CONTAINING COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12493763; DOI=10.1074/jbc.m208992200;
RA Hakimi M.-A., Dong Y., Lane W.S., Speicher D.W., Shiekhattar R.;
RT "A candidate X-linked mental retardation gene is a component of a new
RT family of histone deacetylase-containing complexes.";
RL J. Biol. Chem. 278:7234-7239(2003).
RN [8]
RP CATALYTIC ACTIVITY, FUNCTION, AND COFACTOR.
RX PubMed=15620353; DOI=10.1016/j.cell.2004.12.012;
RA Shi Y.-J., Lan F., Matson C., Mulligan P., Whetstine J.R., Cole P.A.,
RA Casero R.A., Shi Y.;
RT "Histone demethylation mediated by the nuclear amine oxidase homolog
RT LSD1.";
RL Cell 119:941-953(2004).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=15811342; DOI=10.1016/j.febslet.2005.03.015;
RA Forneris F., Binda C., Vanoni M.A., Mattevi A., Battaglioli E.;
RT "Histone demethylation catalysed by LSD1 is a flavin-dependent oxidative
RT process.";
RL FEBS Lett. 579:2203-2207(2005).
RN [10]
RP FUNCTION, AND INTERACTION WITH RCOR1 AND PHF21A.
RX PubMed=16140033; DOI=10.1016/j.molcel.2005.08.027;
RA Shi Y.-J., Matson C., Lan F., Iwase S., Baba T., Shi Y.;
RT "Regulation of LSD1 histone demethylase activity by its associated
RT factors.";
RL Mol. Cell 19:857-864(2005).
RN [11]
RP FUNCTION, INTERACTION WITH RCOR1, AND MUTAGENESIS OF LYS-661.
RX PubMed=16079794; DOI=10.1038/nature04021;
RA Lee M.G., Wynder C., Cooch N., Shiekhattar R.;
RT "An essential role for CoREST in nucleosomal histone 3 lysine 4
RT demethylation.";
RL Nature 437:432-435(2005).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH
RP AR.
RX PubMed=16079795; DOI=10.1038/nature04020;
RA Metzger E., Wissmann M., Yin N., Mueller J.M., Schneider R.,
RA Peters A.H.F.M., Guenther T., Buettner R., Schuele R.;
RT "LSD1 demethylates repressive histone marks to promote androgen-receptor-
RT dependent transcription.";
RL Nature 437:436-439(2005).
RN [13]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16223729; DOI=10.1074/jbc.m509549200;
RA Forneris F., Binda C., Vanoni M.A., Battaglioli E., Mattevi A.;
RT "Human histone demethylase LSD1 reads the histone code.";
RL J. Biol. Chem. 280:41360-41365(2005).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [15]
RP FUNCTION.
RX PubMed=17805299; DOI=10.1038/nature06092;
RA Huang J., Sengupta R., Espejo A.B., Lee M.G., Dorsey J.A., Richter M.,
RA Opravil S., Shiekhattar R., Bedford M.T., Jenuwein T., Berger S.L.;
RT "p53 is regulated by the lysine demethylase LSD1.";
RL Nature 449:105-108(2007).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-59; THR-104; SER-126;
RP SER-131; SER-166 AND SER-849, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-104; SER-131 AND SER-137, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [22]
RP FUNCTION, INTERACTION WITH SNAI1 AND RCOR1, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=20389281; DOI=10.1038/emboj.2010.63;
RA Lin Y., Wu Y., Li J., Dong C., Ye X., Chi Y.I., Evers B.M., Zhou B.P.;
RT "The SNAG domain of Snail1 functions as a molecular hook for recruiting
RT lysine-specific demethylase 1.";
RL EMBO J. 29:1803-1816(2010).
RN [23]
RP RETRACTED PAPER.
RX PubMed=19880879; DOI=10.1074/jbc.m109.065862;
RA Lee S.W., Cho Y.S., Na J.M., Park U.H., Kang M., Kim E.J., Um S.J.;
RT "ASXL1 represses retinoic acid receptor-mediated transcription through
RT associating with HP1 and LSD1.";
RL J. Biol. Chem. 285:18-29(2010).
RN [24]
RP RETRACTION NOTICE OF PUBMED:19880879 NOTICE FOR PUBMED:19880879.
RX PubMed=25750265; DOI=10.1074/jbc.a109.065862;
RA Lee S.W., Cho Y.S., Na J.M., Park U.H., Kang M., Kim E.J., Um S.J.;
RT "Retraction: 'ASXL1 represses retinoic acid receptor-mediated transcription
RT through associating with HP1 and LSD1'.";
RL J. Biol. Chem. 290:6008-6008(2015).
RN [25]
RP FUNCTION.
RX PubMed=20228790; DOI=10.1038/nature08839;
RA Metzger E., Imhof A., Patel D., Kahl P., Hoffmeyer K., Friedrichs N.,
RA Muller J.M., Greschik H., Kirfel J., Ji S., Kunowska N.,
RA Beisenherz-Huss C., Gunther T., Buettner R., Schule R.;
RT "Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation at
RT histone H3K4.";
RL Nature 464:792-796(2010).
RN [26]
RP FUNCTION, AND INTERACTION WITH SNAI.
RX PubMed=20562920; DOI=10.1038/onc.2010.234;
RA Lin T., Ponn A., Hu X., Law B.K., Lu J.;
RT "Requirement of the histone demethylase LSD1 in Snai1-mediated
RT transcriptional repression during epithelial-mesenchymal transition.";
RL Oncogene 29:4896-4904(2010).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131; SER-137; SER-166 AND
RP SER-849, AND IDENTIFICATION BY 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 [28]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131; SER-137 AND SER-166, AND
RP IDENTIFICATION BY 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 [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131; SER-137; SER-166 AND
RP SER-611, AND 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 [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126; SER-131; TYR-135 AND
RP SER-137, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [32]
RP INTERACTION WITH JADE2, INDUCTION, UBIQUITINATION, AND MUTAGENESIS OF
RP LYS-503.
RX PubMed=25018020; DOI=10.1016/j.molcel.2014.06.006;
RA Han X., Gui B., Xiong C., Zhao L., Liang J., Sun L., Yang X., Yu W., Si W.,
RA Yan R., Yi X., Zhang D., Li W., Li L., Yang J., Wang Y., Sun Y.E.,
RA Zhang D., Meng A., Shang Y.;
RT "Destabilizing LSD1 by Jade-2 promotes neurogenesis: an antibraking system
RT in neural development.";
RL Mol. Cell 55:482-494(2014).
RN [33]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-442 AND LYS-469, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [34]
RP INTERACTION WITH SAMD1, AND SUBCELLULAR LOCATION.
RX PubMed=33980486; DOI=10.1126/sciadv.abf2229;
RA Stielow B., Zhou Y., Cao Y., Simon C., Pogoda H.M., Jiang J., Ren Y.,
RA Phanor S.K., Rohner I., Nist A., Stiewe T., Hammerschmidt M., Shi Y.,
RA Bulyk M.L., Wang Z., Liefke R.;
RT "The SAM domain-containing protein 1 (SAMD1) acts as a repressive chromatin
RT regulator at unmethylated CpG islands.";
RL Sci. Adv. 7:0-0(2021).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS) OF 171-836 IN COMPLEX WITH FAD AND
RP RCOR1.
RX PubMed=16885027; DOI=10.1016/j.molcel.2006.07.012;
RA Yang M., Gocke C.B., Luo X., Borek D., Tomchick D.R., Machius M.,
RA Otwinowski Z., Yu H.;
RT "Structural basis for CoREST-dependent demethylation of nucleosomes by the
RT human LSD1 histone demethylase.";
RL Mol. Cell 23:377-387(2006).
RN [36]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 172-835 IN COMPLEX WITH FAD,
RP FUNCTION, COFACTOR, AND MUTAGENESIS OF ASN-535; HIS-564 AND TYR-761.
RX PubMed=16956976; DOI=10.1073/pnas.0606381103;
RA Chen Y., Yang Y., Wang F., Wan K., Yamane K., Zhang Y., Lei M.;
RT "Crystal structure of human histone lysine-specific demethylase 1 (LSD1).";
RL Proc. Natl. Acad. Sci. U.S.A. 103:13956-13961(2006).
RN [37]
RP STRUCTURE BY NMR OF 166-285, AND DOMAIN.
RX PubMed=16531230; DOI=10.1016/j.str.2005.12.004;
RA Tochio N., Umehara T., Koshiba S., Inoue M., Yabuki T., Aoki M., Seki E.,
RA Watanabe S., Tomo Y., Hanada M., Ikari M., Sato M., Terada T., Nagase T.,
RA Ohara O., Shirouzu M., Tanaka A., Kigawa T., Yokoyama S.;
RT "Solution structure of the SWIRM domain of human histone demethylase
RT LSD1.";
RL Structure 14:457-468(2006).
RN [38] {ECO:0007744|PDB:2Y48}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 123-852 IN COMPLEX WITH FAD;
RP SNAI1 PEPTIDE AND RCOR1, FUNCTION, ACTIVITY REGULATION, COFACTOR, AND
RP SUBUNIT.
RX PubMed=21300290; DOI=10.1016/j.str.2011.01.001;
RA Baron R., Binda C., Tortorici M., McCammon J.A., Mattevi A.;
RT "Molecular mimicry and ligand recognition in binding and catalysis by the
RT histone demethylase LSD1-CoREST complex.";
RL Structure 19:212-220(2011).
RN [39] {ECO:0007744|PDB:3ZMS, ECO:0007744|PDB:3ZMT, ECO:0007744|PDB:3ZMU, ECO:0007744|PDB:3ZMV, ECO:0007744|PDB:3ZMZ, ECO:0007744|PDB:3ZN0, ECO:0007744|PDB:3ZN1}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEXES WITH FAD; RCOR1; INSM1
RP PEPTIDE AND SNAI1 PEPTIDE, FUNCTION, ACTIVITY REGULATION, COFACTOR, AND
RP SUBUNIT.
RX PubMed=23721412; DOI=10.1021/cb4001926;
RA Tortorici M., Borrello M.T., Tardugno M., Chiarelli L.R., Pilotto S.,
RA Ciossani G., Vellore N.A., Bailey S.G., Cowan J., O'Connell M., Crabb S.J.,
RA Packham G., Mai A., Baron R., Ganesan A., Mattevi A.;
RT "Protein recognition by short peptide reversible inhibitors of the
RT chromatin-modifying LSD1/CoREST lysine demethylase.";
RL ACS Chem. Biol. 8:1677-1682(2013).
RN [40]
RP VARIANT CPRF GLY-556.
RX PubMed=23020937; DOI=10.1016/s0140-6736(12)61480-9;
RA Rauch A., Wieczorek D., Graf E., Wieland T., Endele S., Schwarzmayr T.,
RA Albrecht B., Bartholdi D., Beygo J., Di Donato N., Dufke A., Cremer K.,
RA Hempel M., Horn D., Hoyer J., Joset P., Roepke A., Moog U., Riess A.,
RA Thiel C.T., Tzschach A., Wiesener A., Wohlleber E., Zweier C., Ekici A.B.,
RA Zink A.M., Rump A., Meisinger C., Grallert H., Sticht H., Schenck A.,
RA Engels H., Rappold G., Schroeck E., Wieacker P., Riess O., Meitinger T.,
RA Reis A., Strom T.M.;
RT "Range of genetic mutations associated with severe non-syndromic sporadic
RT intellectual disability: an exome sequencing study.";
RL Lancet 380:1674-1682(2012).
RN [41]
RP VARIANT CPRF HIS-761.
RX PubMed=24838796; DOI=10.1002/ajmg.a.36450;
RA Tunovic S., Barkovich J., Sherr E.H., Slavotinek A.M.;
RT "De novo ANKRD11 and KDM1A gene mutations in a male with features of KBG
RT syndrome and Kabuki syndrome.";
RL Am. J. Med. Genet. A 164A:1744-1749(2014).
RN [42]
RP VARIANTS CPRF LYS-379; GLY-556 AND HIS-761.
RX PubMed=26656649; DOI=10.1038/gim.2015.161;
RA Chong J.X., Yu J.H., Lorentzen P., Park K.M., Jamal S.M., Tabor H.K.,
RA Rauch A., Saenz M.S., Boltshauser E., Patterson K.E., Nickerson D.A.,
RA Bamshad M.J.;
RT "Gene discovery for Mendelian conditions via social networking: de novo
RT variants in KDM1A cause developmental delay and distinctive facial
RT features.";
RL Genet. Med. 18:788-795(2016).
CC -!- FUNCTION: Histone demethylase that can demethylate both 'Lys-4'
CC (H3K4me) and 'Lys-9' (H3K9me) of histone H3, thereby acting as a
CC coactivator or a corepressor, depending on the context
CC (PubMed:15620353, PubMed:15811342, PubMed:16140033, PubMed:16079794,
CC PubMed:16079795, PubMed:16223729). Acts by oxidizing the substrate by
CC FAD to generate the corresponding imine that is subsequently hydrolyzed
CC (PubMed:15620353, PubMed:15811342, PubMed:16079794, PubMed:21300290).
CC Acts as a corepressor by mediating demethylation of H3K4me, a specific
CC tag for epigenetic transcriptional activation. Demethylates both
CC mono- (H3K4me1) and di-methylated (H3K4me2) H3K4me (PubMed:15620353,
CC PubMed:20389281, PubMed:21300290, PubMed:23721412). May play a role in
CC the repression of neuronal genes. Alone, it is unable to demethylate
CC H3K4me on nucleosomes and requires the presence of RCOR1/CoREST to
CC achieve such activity (PubMed:16140033, PubMed:16079794,
CC PubMed:16885027, PubMed:21300290, PubMed:23721412). Also acts as a
CC coactivator of androgen receptor (AR)-dependent transcription, by being
CC recruited to AR target genes and mediating demethylation of H3K9me, a
CC specific tag for epigenetic transcriptional repression. The presence of
CC PRKCB in AR-containing complexes, which mediates phosphorylation of
CC 'Thr-6' of histone H3 (H3T6ph), a specific tag that prevents
CC demethylation H3K4me, prevents H3K4me demethylase activity of KDM1A
CC (PubMed:16079795). Demethylates di-methylated 'Lys-370' of p53/TP53
CC which prevents interaction of p53/TP53 with TP53BP1 and represses
CC p53/TP53-mediated transcriptional activation. Demethylates and
CC stabilizes the DNA methylase DNMT1. Required for gastrulation during
CC embryogenesis. Component of a RCOR/GFI/KDM1A/HDAC complex that
CC suppresses, via histone deacetylase (HDAC) recruitment, a number of
CC genes implicated in multilineage blood cell development. Effector of
CC SNAI1-mediated transcription repression of E-cadherin/CDH1, CDN7 and
CC KRT8. Required for the maintenance of the silenced state of the SNAI1
CC target genes E-cadherin/CDH1 and CDN7 (PubMed:20389281).
CC {ECO:0000269|PubMed:12032298, ECO:0000269|PubMed:15620353,
CC ECO:0000269|PubMed:15811342, ECO:0000269|PubMed:16079794,
CC ECO:0000269|PubMed:16079795, ECO:0000269|PubMed:16140033,
CC ECO:0000269|PubMed:16223729, ECO:0000269|PubMed:16885027,
CC ECO:0000269|PubMed:16956976, ECO:0000269|PubMed:17805299,
CC ECO:0000269|PubMed:20228790, ECO:0000269|PubMed:20389281,
CC ECO:0000269|PubMed:20562920, ECO:0000269|PubMed:21300290,
CC ECO:0000269|PubMed:23721412}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 A + 2 H2O + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] = 2
CC AH2 + 2 formaldehyde + L-lysyl(4)-[histone H3]; Xref=Rhea:RHEA:60244,
CC Rhea:RHEA-COMP:15540, Rhea:RHEA-COMP:15547, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16842, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:61976; EC=1.14.99.66;
CC Evidence={ECO:0000269|PubMed:15620353, ECO:0000269|PubMed:15811342};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:15620353, ECO:0000269|PubMed:15811342,
CC ECO:0000269|PubMed:16956976, ECO:0000269|PubMed:21300290,
CC ECO:0000269|PubMed:23721412};
CC -!- ACTIVITY REGULATION: The N-terminal sequences of INSM1 and SNAI1
CC compete with histone H3 for the same binding site and thereby inhibit
CC histone demethylation (in vitro). {ECO:0000269|PubMed:21300290,
CC ECO:0000269|PubMed:23721412}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.0 uM for H3 monomethyl-K4 {ECO:0000269|PubMed:16223729};
CC KM=4.2 uM for H3 dimethyl-K4 {ECO:0000269|PubMed:16223729};
CC KM=3.9 uM for H3 monomethyl-K4-monomethyl-K9
CC {ECO:0000269|PubMed:16223729};
CC KM=17.5 uM for monomethyl-K4-acetyl-K9 {ECO:0000269|PubMed:16223729};
CC -!- SUBUNIT: Component of a histone demethylase complex with RCOR1
CC (PubMed:20389281, PubMed:23721412, PubMed:16885027, PubMed:21300290).
CC Component of a RCOR/GFI/KDM1A/HDAC complex (PubMed:12032298,
CC PubMed:11102443). Interacts directly with GFI1 and GFI1B. Interacts
CC with INSM1 (via N-terminus) (PubMed:23721412). Component of a BHC
CC histone deacetylase complex that contains HDAC1, HDAC2, HMG20B, KDM1A,
CC RCOR1 and PHF21A. The BHC complex may also contain ZMYM2, ZNF217,
CC ZMYM3, GSE1 and GTF2I (PubMed:12493763, PubMed:16140033,
CC PubMed:16885027). In the complex, RCOR1/CoREST strongly enhances the
CC demethylase activity and protects it from the proteasome while
CC PHF21A/BHC80 inhibits the demethylase activity (PubMed:16079794,
CC PubMed:16956976). Interacts with the androgen receptor (AR)
CC (PubMed:16079795). Interacts with SNAI1 (via SNAG domain)
CC (PubMed:20389281, PubMed:20562920, PubMed:21300290, PubMed:23721412).
CC Interacts (via AOD/Tower domain) with JADE2 (via C-terminus)
CC (PubMed:25018020). Interacts with ESRRB; co-occupes the core set of
CC ESRRB targets (By similarity). Interacts with SAMD1 (via WH domain);
CC the interaction modulates KDM1A function (PubMed:33980486).
CC {ECO:0000250|UniProtKB:Q6ZQ88, ECO:0000269|PubMed:11102443,
CC ECO:0000269|PubMed:12032298, ECO:0000269|PubMed:12493763,
CC ECO:0000269|PubMed:16079794, ECO:0000269|PubMed:16079795,
CC ECO:0000269|PubMed:16140033, ECO:0000269|PubMed:16885027,
CC ECO:0000269|PubMed:16956976, ECO:0000269|PubMed:20389281,
CC ECO:0000269|PubMed:20562920, ECO:0000269|PubMed:21300290,
CC ECO:0000269|PubMed:23721412, ECO:0000269|PubMed:25018020,
CC ECO:0000269|PubMed:33980486}.
CC -!- INTERACTION:
CC O60341; Q9BYF1: ACE2; NbExp=19; IntAct=EBI-710124, EBI-7730807;
CC O60341; Q99996: AKAP9; NbExp=2; IntAct=EBI-710124, EBI-1048311;
CC O60341; Q86SG2: ANKRD23; NbExp=3; IntAct=EBI-710124, EBI-5661893;
CC O60341; Q13490: BIRC2; NbExp=3; IntAct=EBI-710124, EBI-514538;
CC O60341; Q6P047: C8orf74; NbExp=2; IntAct=EBI-710124, EBI-8466055;
CC O60341; Q8TC20-4: CAGE1; NbExp=3; IntAct=EBI-710124, EBI-11522698;
CC O60341; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-710124, EBI-3866279;
CC O60341; Q49A88-3: CCDC14; NbExp=3; IntAct=EBI-710124, EBI-12105646;
CC O60341; Q99459: CDC5L; NbExp=3; IntAct=EBI-710124, EBI-374880;
CC O60341; Q9BXL8: CDCA4; NbExp=2; IntAct=EBI-710124, EBI-1773949;
CC O60341; Q86XR8-3: CEP57; NbExp=3; IntAct=EBI-710124, EBI-11752486;
CC O60341; Q8NHQ1: CEP70; NbExp=2; IntAct=EBI-710124, EBI-739624;
CC O60341; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-710124, EBI-742887;
CC O60341; Q12873: CHD3; NbExp=4; IntAct=EBI-710124, EBI-523590;
CC O60341; P38432: COIL; NbExp=3; IntAct=EBI-710124, EBI-945751;
CC O60341; Q96EY1: DNAJA3; NbExp=2; IntAct=EBI-710124, EBI-356767;
CC O60341; P26378-2: ELAVL4; NbExp=3; IntAct=EBI-710124, EBI-21603100;
CC O60341; Q9UPT5-1: EXOC7; NbExp=3; IntAct=EBI-710124, EBI-6251402;
CC O60341; Q3B820: FAM161A; NbExp=3; IntAct=EBI-710124, EBI-719941;
CC O60341; Q9H8W3: FAM204A; NbExp=3; IntAct=EBI-710124, EBI-8465160;
CC O60341; Q8IZU1: FAM9A; NbExp=2; IntAct=EBI-710124, EBI-8468186;
CC O60341; Q9BQS8: FYCO1; NbExp=2; IntAct=EBI-710124, EBI-2869338;
CC O60341; O95995: GAS8; NbExp=3; IntAct=EBI-710124, EBI-1052570;
CC O60341; Q96CN9: GCC1; NbExp=3; IntAct=EBI-710124, EBI-746252;
CC O60341; Q08379: GOLGA2; NbExp=3; IntAct=EBI-710124, EBI-618309;
CC O60341; Q9NYA3: GOLGA6A; NbExp=3; IntAct=EBI-710124, EBI-11163335;
CC O60341; Q8NEC7: GSTCD; NbExp=2; IntAct=EBI-710124, EBI-8469616;
CC O60341; Q9BX10: GTPBP2; NbExp=2; IntAct=EBI-710124, EBI-6115579;
CC O60341; Q16695: H3-4; NbExp=2; IntAct=EBI-710124, EBI-358900;
CC O60341; Q96CS2: HAUS1; NbExp=2; IntAct=EBI-710124, EBI-2514791;
CC O60341; O15379: HDAC3; NbExp=4; IntAct=EBI-710124, EBI-607682;
CC O60341; Q9UBX0: HESX1; NbExp=2; IntAct=EBI-710124, EBI-8470369;
CC O60341; Q9NSC5: HOMER3; NbExp=3; IntAct=EBI-710124, EBI-748420;
CC O60341; Q16891: IMMT; NbExp=2; IntAct=EBI-710124, EBI-473801;
CC O60341; O75564-2: JRK; NbExp=3; IntAct=EBI-710124, EBI-17181882;
CC O60341; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-710124, EBI-14069005;
CC O60341; Q8TBB5: KLHDC4; NbExp=2; IntAct=EBI-710124, EBI-8472352;
CC O60341; P19012: KRT15; NbExp=3; IntAct=EBI-710124, EBI-739566;
CC O60341; Q15323: KRT31; NbExp=3; IntAct=EBI-710124, EBI-948001;
CC O60341; Q14525: KRT33B; NbExp=4; IntAct=EBI-710124, EBI-1049638;
CC O60341; Q92764: KRT35; NbExp=3; IntAct=EBI-710124, EBI-1058674;
CC O60341; Q6A163: KRT39; NbExp=3; IntAct=EBI-710124, EBI-11958242;
CC O60341; Q6A162: KRT40; NbExp=3; IntAct=EBI-710124, EBI-10171697;
CC O60341; Q96JB6: LOXL4; NbExp=2; IntAct=EBI-710124, EBI-749562;
CC O60341; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-710124, EBI-1216080;
CC O60341; O95983: MBD3; NbExp=4; IntAct=EBI-710124, EBI-1783068;
CC O60341; P01106: MYC; NbExp=4; IntAct=EBI-710124, EBI-447544;
CC O60341; Q3BBV0: NBPF1; NbExp=5; IntAct=EBI-710124, EBI-2804530;
CC O60341; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-710124, EBI-10172876;
CC O60341; P35240: NF2; NbExp=4; IntAct=EBI-710124, EBI-1014472;
CC O60341; Q16236: NFE2L2; NbExp=5; IntAct=EBI-710124, EBI-2007911;
CC O60341; P46531: NOTCH1; NbExp=8; IntAct=EBI-710124, EBI-636374;
CC O60341; Q13133: NR1H3; NbExp=2; IntAct=EBI-710124, EBI-781356;
CC O60341; Q96F24: NRBF2; NbExp=3; IntAct=EBI-710124, EBI-2362014;
CC O60341; A5D8V7: ODAD3; NbExp=2; IntAct=EBI-710124, EBI-8466445;
CC O60341; Q8IZS5: OFCC1; NbExp=2; IntAct=EBI-710124, EBI-8477661;
CC O60341; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-710124, EBI-10302990;
CC O60341; Q8IZL8: PELP1; NbExp=6; IntAct=EBI-710124, EBI-716449;
CC O60341; Q99471: PFDN5; NbExp=3; IntAct=EBI-710124, EBI-357275;
CC O60341; Q5T6S3: PHF19; NbExp=2; IntAct=EBI-710124, EBI-2339674;
CC O60341; Q03181: PPARD; NbExp=2; IntAct=EBI-710124, EBI-6426768;
CC O60341; P62191: PSMC1; NbExp=2; IntAct=EBI-710124, EBI-357598;
CC O60341; Q9NS23: RASSF1; NbExp=2; IntAct=EBI-710124, EBI-367363;
CC O60341; P50749: RASSF2; NbExp=2; IntAct=EBI-710124, EBI-960081;
CC O60341; Q86WH2: RASSF3; NbExp=3; IntAct=EBI-710124, EBI-2845202;
CC O60341; Q06330: RBPJ; NbExp=4; IntAct=EBI-710124, EBI-632552;
CC O60341; Q9UKL0: RCOR1; NbExp=7; IntAct=EBI-710124, EBI-926563;
CC O60341; Q8IZ40: RCOR2; NbExp=3; IntAct=EBI-710124, EBI-723853;
CC O60341; Q9P2K3-2: RCOR3; NbExp=6; IntAct=EBI-710124, EBI-1504830;
CC O60341; Q96P16-3: RPRD1A; NbExp=3; IntAct=EBI-710124, EBI-12840198;
CC O60341; Q8N6K7: SAMD3; NbExp=2; IntAct=EBI-710124, EBI-748741;
CC O60341; Q9UGK8: SERGEF; NbExp=2; IntAct=EBI-710124, EBI-465368;
CC O60341; Q13435: SF3B2; NbExp=2; IntAct=EBI-710124, EBI-749111;
CC O60341; O15198: SMAD9; NbExp=2; IntAct=EBI-710124, EBI-748763;
CC O60341; O95863: SNAI1; NbExp=32; IntAct=EBI-710124, EBI-1045459;
CC O60341; Q96H20: SNF8; NbExp=2; IntAct=EBI-710124, EBI-747719;
CC O60341; Q8N0Z3: SPICE1; NbExp=4; IntAct=EBI-710124, EBI-2361917;
CC O60341; Q96BD6: SPSB1; NbExp=2; IntAct=EBI-710124, EBI-2659201;
CC O60341; Q8N4C7: STX19; NbExp=2; IntAct=EBI-710124, EBI-8484990;
CC O60341; Q8N6V9: TEX9; NbExp=4; IntAct=EBI-710124, EBI-746341;
CC O60341; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-710124, EBI-1105213;
CC O60341; Q08117-2: TLE5; NbExp=3; IntAct=EBI-710124, EBI-11741437;
CC O60341; Q2M3C6: TMEM266; NbExp=3; IntAct=EBI-710124, EBI-12163061;
CC O60341; P45379-11: TNNT2; NbExp=3; IntAct=EBI-710124, EBI-17559309;
CC O60341; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-710124, EBI-11952721;
CC O60341; Q9BUZ4: TRAF4; NbExp=4; IntAct=EBI-710124, EBI-3650647;
CC O60341; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-710124, EBI-9090990;
CC O60341; Q8TF42: UBASH3B; NbExp=3; IntAct=EBI-710124, EBI-1380492;
CC O60341; Q9H9H4: VPS37B; NbExp=3; IntAct=EBI-710124, EBI-4400866;
CC O60341; Q9Y3C0: WASHC3; NbExp=3; IntAct=EBI-710124, EBI-712969;
CC O60341; O96006: ZBED1; NbExp=4; IntAct=EBI-710124, EBI-740037;
CC O60341; O15060: ZBTB39; NbExp=3; IntAct=EBI-710124, EBI-9995672;
CC O60341; Q92618: ZNF516; NbExp=6; IntAct=EBI-710124, EBI-2799490;
CC O60341-1; O14646: CHD1; NbExp=8; IntAct=EBI-15599570, EBI-1560858;
CC O60341-1; Q96KQ7: EHMT2; NbExp=2; IntAct=EBI-15599570, EBI-744366;
CC O60341-1; Q96KQ7-1: EHMT2; NbExp=3; IntAct=EBI-15599570, EBI-15737402;
CC O60341-1; P05771-1: PRKCB; NbExp=2; IntAct=EBI-15599570, EBI-5774492;
CC O60341-1; Q9UKL0: RCOR1; NbExp=6; IntAct=EBI-15599570, EBI-926563;
CC O60341-1; P17542: TAL1; NbExp=5; IntAct=EBI-15599570, EBI-1753878;
CC O60341-1; P04637: TP53; NbExp=6; IntAct=EBI-15599570, EBI-366083;
CC O60341-1; P22091: Tal1; Xeno; NbExp=2; IntAct=EBI-15599570, EBI-8006437;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11102443,
CC ECO:0000269|PubMed:16079795, ECO:0000269|PubMed:20389281,
CC ECO:0000269|PubMed:33980486}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O60341-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60341-2; Sequence=VSP_011198, VSP_011199;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:16079795}.
CC -!- INDUCTION: Down-regulated during neural differentiation in
CC neuroblastoma cancer. {ECO:0000269|PubMed:25018020}.
CC -!- DOMAIN: The SWIRM domain may act as an anchor site for a histone tail.
CC {ECO:0000269|PubMed:16531230}.
CC -!- PTM: Polyubiquitinated by JADE2; which leads to its proteasomal
CC degradation. {ECO:0000269|PubMed:25018020}.
CC -!- DISEASE: Cleft palate, psychomotor retardation, and distinctive facial
CC features (CPRF) [MIM:616728]: A syndrome characterized by cleft palate,
CC developmental delay, psychomotor retardation, and facial dysmorphic
CC features including a prominent forehead, slightly arched eyebrows,
CC elongated palpebral fissures, a wide nasal bridge, thin lips, and
CC widely spaced teeth. Cleft palate is a congenital fissure of the soft
CC and/or hard palate, due to faulty fusion. {ECO:0000269|PubMed:23020937,
CC ECO:0000269|PubMed:24838796, ECO:0000269|PubMed:26656649}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000305}.
CC -!- CAUTION: Was previously reported to interact with ASXL1. However, this
CC publication has been retracted. {ECO:0000305|PubMed:19880879,
CC ECO:0000305|PubMed:25750265}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA25527.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB011173; BAA25527.1; ALT_INIT; mRNA.
DR EMBL; AL031428; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC016639; AAH16639.1; -; mRNA.
DR EMBL; BC025362; AAH25362.1; -; mRNA.
DR EMBL; BC040194; AAH40194.3; -; mRNA.
DR EMBL; BC048134; AAH48134.2; -; mRNA.
DR EMBL; AL833812; CAD38675.2; -; mRNA.
DR CCDS; CCDS30627.1; -. [O60341-1]
DR CCDS; CCDS53278.1; -. [O60341-2]
DR RefSeq; NP_001009999.1; NM_001009999.2. [O60341-2]
DR RefSeq; NP_055828.2; NM_015013.3. [O60341-1]
DR PDB; 2COM; NMR; -; A=169-279.
DR PDB; 2DW4; X-ray; 2.30 A; A=172-831.
DR PDB; 2EJR; X-ray; 2.70 A; A=172-833.
DR PDB; 2H94; X-ray; 2.90 A; A=172-835.
DR PDB; 2HKO; X-ray; 2.80 A; A=172-835.
DR PDB; 2IW5; X-ray; 2.57 A; A=171-836.
DR PDB; 2L3D; NMR; -; A=174-273.
DR PDB; 2UXN; X-ray; 2.72 A; A=171-836.
DR PDB; 2UXX; X-ray; 2.74 A; A=171-836.
DR PDB; 2V1D; X-ray; 3.10 A; A=123-852.
DR PDB; 2X0L; X-ray; 3.00 A; A=123-852.
DR PDB; 2XAF; X-ray; 3.25 A; A=1-852.
DR PDB; 2XAG; X-ray; 3.10 A; A=1-852.
DR PDB; 2XAH; X-ray; 3.10 A; A=1-852.
DR PDB; 2XAJ; X-ray; 3.30 A; A=1-852.
DR PDB; 2XAQ; X-ray; 3.20 A; A=1-852.
DR PDB; 2XAS; X-ray; 3.20 A; A=1-852.
DR PDB; 2Y48; X-ray; 3.00 A; A=123-852.
DR PDB; 2Z3Y; X-ray; 2.25 A; A=172-833.
DR PDB; 2Z5U; X-ray; 2.25 A; A=172-833.
DR PDB; 3ABT; X-ray; 3.20 A; A=172-833.
DR PDB; 3ABU; X-ray; 3.10 A; A=172-833.
DR PDB; 3ZMS; X-ray; 2.96 A; A=1-852.
DR PDB; 3ZMT; X-ray; 3.10 A; A=1-852.
DR PDB; 3ZMU; X-ray; 3.20 A; A=1-852.
DR PDB; 3ZMV; X-ray; 3.00 A; A=1-852.
DR PDB; 3ZMZ; X-ray; 3.00 A; A=1-852.
DR PDB; 3ZN0; X-ray; 2.80 A; A=1-852.
DR PDB; 3ZN1; X-ray; 3.10 A; A=1-852.
DR PDB; 4BAY; X-ray; 3.10 A; A=172-852.
DR PDB; 4CZZ; X-ray; 3.00 A; A=1-852.
DR PDB; 4KUM; X-ray; 3.05 A; A=171-836.
DR PDB; 4UV8; X-ray; 2.80 A; A=1-852.
DR PDB; 4UV9; X-ray; 3.00 A; A=1-852.
DR PDB; 4UVA; X-ray; 2.90 A; A=1-852.
DR PDB; 4UVB; X-ray; 2.80 A; A=1-852.
DR PDB; 4UVC; X-ray; 3.10 A; A=1-852.
DR PDB; 4UXN; X-ray; 2.85 A; A=1-852.
DR PDB; 4XBF; X-ray; 2.80 A; A=171-836.
DR PDB; 5AFW; X-ray; 1.60 A; B=108-119.
DR PDB; 5H6Q; X-ray; 2.53 A; A=172-833.
DR PDB; 5H6R; X-ray; 2.60 A; A=172-833.
DR PDB; 5IT3; X-ray; 1.40 A; A/B=183-267.
DR PDB; 5L3B; X-ray; 3.30 A; A=1-852.
DR PDB; 5L3C; X-ray; 3.31 A; A=1-852.
DR PDB; 5L3D; X-ray; 2.60 A; A=1-852.
DR PDB; 5L3E; X-ray; 2.80 A; A=123-852.
DR PDB; 5L3F; X-ray; 3.50 A; A=123-852.
DR PDB; 5L3G; X-ray; 3.10 A; A=123-852.
DR PDB; 5LBQ; X-ray; 3.30 A; A=123-852.
DR PDB; 5LGN; X-ray; 3.20 A; A=172-836.
DR PDB; 5LGT; X-ray; 3.00 A; A=123-852.
DR PDB; 5LGU; X-ray; 3.20 A; A=123-852.
DR PDB; 5LHG; X-ray; 3.34 A; A=1-852.
DR PDB; 5LHH; X-ray; 3.05 A; A=1-852.
DR PDB; 5LHI; X-ray; 3.40 A; A=1-852.
DR PDB; 5X60; X-ray; 2.69 A; A=172-833.
DR PDB; 5YJB; X-ray; 2.96 A; A=172-833.
DR PDB; 6E1F; X-ray; 1.16 A; A/B/C/D=183-267.
DR PDB; 6K3E; X-ray; 2.87 A; A=172-833.
DR PDB; 6KGK; X-ray; 2.70 A; A=172-833.
DR PDB; 6KGL; X-ray; 2.70 A; A=172-833.
DR PDB; 6KGM; X-ray; 2.62 A; A=172-833.
DR PDB; 6KGN; X-ray; 2.62 A; A=172-833.
DR PDB; 6KGO; X-ray; 2.25 A; A=172-833.
DR PDB; 6KGP; X-ray; 2.25 A; A=172-833.
DR PDB; 6KGQ; X-ray; 2.32 A; A=172-833.
DR PDB; 6KGR; X-ray; 2.32 A; A=172-833.
DR PDB; 6NQM; X-ray; 2.90 A; A=173-830.
DR PDB; 6NQU; X-ray; 2.70 A; A=173-830.
DR PDB; 6NR5; X-ray; 2.90 A; A=173-830.
DR PDB; 6S35; X-ray; 3.10 A; A=172-833.
DR PDB; 6TE1; X-ray; 3.11 A; A=1-852.
DR PDB; 6TUY; X-ray; 2.60 A; A=1-852.
DR PDB; 6VYP; X-ray; 4.99 A; K/M/k/m=171-852.
DR PDB; 6W4K; X-ray; 2.93 A; A=174-832.
DR PDB; 6WC6; X-ray; 3.10 A; A=171-836, C=137-151.
DR PDB; 7CDC; X-ray; 2.64 A; A=172-833.
DR PDB; 7CDD; X-ray; 2.76 A; A=172-833.
DR PDB; 7CDE; X-ray; 2.68 A; A=172-833.
DR PDB; 7CDF; X-ray; 2.68 A; A=172-833.
DR PDB; 7CDG; X-ray; 2.80 A; A=172-833.
DR PDB; 7E0G; X-ray; 2.25 A; A=172-833.
DR PDB; 7JJL; X-ray; 2.60 A; B=104-129.
DR PDB; 7JJM; X-ray; 2.06 A; A=104-129.
DR PDB; 7JK7; X-ray; 1.96 A; A=104-129.
DR PDBsum; 2COM; -.
DR PDBsum; 2DW4; -.
DR PDBsum; 2EJR; -.
DR PDBsum; 2H94; -.
DR PDBsum; 2HKO; -.
DR PDBsum; 2IW5; -.
DR PDBsum; 2L3D; -.
DR PDBsum; 2UXN; -.
DR PDBsum; 2UXX; -.
DR PDBsum; 2V1D; -.
DR PDBsum; 2X0L; -.
DR PDBsum; 2XAF; -.
DR PDBsum; 2XAG; -.
DR PDBsum; 2XAH; -.
DR PDBsum; 2XAJ; -.
DR PDBsum; 2XAQ; -.
DR PDBsum; 2XAS; -.
DR PDBsum; 2Y48; -.
DR PDBsum; 2Z3Y; -.
DR PDBsum; 2Z5U; -.
DR PDBsum; 3ABT; -.
DR PDBsum; 3ABU; -.
DR PDBsum; 3ZMS; -.
DR PDBsum; 3ZMT; -.
DR PDBsum; 3ZMU; -.
DR PDBsum; 3ZMV; -.
DR PDBsum; 3ZMZ; -.
DR PDBsum; 3ZN0; -.
DR PDBsum; 3ZN1; -.
DR PDBsum; 4BAY; -.
DR PDBsum; 4CZZ; -.
DR PDBsum; 4KUM; -.
DR PDBsum; 4UV8; -.
DR PDBsum; 4UV9; -.
DR PDBsum; 4UVA; -.
DR PDBsum; 4UVB; -.
DR PDBsum; 4UVC; -.
DR PDBsum; 4UXN; -.
DR PDBsum; 4XBF; -.
DR PDBsum; 5AFW; -.
DR PDBsum; 5H6Q; -.
DR PDBsum; 5H6R; -.
DR PDBsum; 5IT3; -.
DR PDBsum; 5L3B; -.
DR PDBsum; 5L3C; -.
DR PDBsum; 5L3D; -.
DR PDBsum; 5L3E; -.
DR PDBsum; 5L3F; -.
DR PDBsum; 5L3G; -.
DR PDBsum; 5LBQ; -.
DR PDBsum; 5LGN; -.
DR PDBsum; 5LGT; -.
DR PDBsum; 5LGU; -.
DR PDBsum; 5LHG; -.
DR PDBsum; 5LHH; -.
DR PDBsum; 5LHI; -.
DR PDBsum; 5X60; -.
DR PDBsum; 5YJB; -.
DR PDBsum; 6E1F; -.
DR PDBsum; 6K3E; -.
DR PDBsum; 6KGK; -.
DR PDBsum; 6KGL; -.
DR PDBsum; 6KGM; -.
DR PDBsum; 6KGN; -.
DR PDBsum; 6KGO; -.
DR PDBsum; 6KGP; -.
DR PDBsum; 6KGQ; -.
DR PDBsum; 6KGR; -.
DR PDBsum; 6NQM; -.
DR PDBsum; 6NQU; -.
DR PDBsum; 6NR5; -.
DR PDBsum; 6S35; -.
DR PDBsum; 6TE1; -.
DR PDBsum; 6TUY; -.
DR PDBsum; 6VYP; -.
DR PDBsum; 6W4K; -.
DR PDBsum; 6WC6; -.
DR PDBsum; 7CDC; -.
DR PDBsum; 7CDD; -.
DR PDBsum; 7CDE; -.
DR PDBsum; 7CDF; -.
DR PDBsum; 7CDG; -.
DR PDBsum; 7E0G; -.
DR PDBsum; 7JJL; -.
DR PDBsum; 7JJM; -.
DR PDBsum; 7JK7; -.
DR AlphaFoldDB; O60341; -.
DR BMRB; O60341; -.
DR SASBDB; O60341; -.
DR SMR; O60341; -.
DR BioGRID; 116667; 526.
DR CORUM; O60341; -.
DR DIP; DIP-34641N; -.
DR IntAct; O60341; 320.
DR MINT; O60341; -.
DR STRING; 9606.ENSP00000383042; -.
DR BindingDB; O60341; -.
DR ChEMBL; CHEMBL6136; -.
DR DrugBank; DB16446; Vafidemstat.
DR DrugCentral; O60341; -.
DR GuidetoPHARMACOLOGY; 2669; -.
DR MoonDB; O60341; Predicted.
DR iPTMnet; O60341; -.
DR MetOSite; O60341; -.
DR PhosphoSitePlus; O60341; -.
DR BioMuta; KDM1A; -.
DR EPD; O60341; -.
DR jPOST; O60341; -.
DR MassIVE; O60341; -.
DR MaxQB; O60341; -.
DR PaxDb; O60341; -.
DR PeptideAtlas; O60341; -.
DR PRIDE; O60341; -.
DR ProteomicsDB; 49364; -. [O60341-1]
DR ProteomicsDB; 49365; -. [O60341-2]
DR Antibodypedia; 3136; 710 antibodies from 47 providers.
DR DNASU; 23028; -.
DR Ensembl; ENST00000356634.7; ENSP00000349049.3; ENSG00000004487.18. [O60341-1]
DR Ensembl; ENST00000400181.9; ENSP00000383042.5; ENSG00000004487.18. [O60341-2]
DR GeneID; 23028; -.
DR KEGG; hsa:23028; -.
DR MANE-Select; ENST00000400181.9; ENSP00000383042.5; NM_001009999.3; NP_001009999.1. [O60341-2]
DR UCSC; uc001bgi.3; human. [O60341-1]
DR CTD; 23028; -.
DR DisGeNET; 23028; -.
DR GeneCards; KDM1A; -.
DR HGNC; HGNC:29079; KDM1A.
DR HPA; ENSG00000004487; Low tissue specificity.
DR MalaCards; KDM1A; -.
DR MIM; 609132; gene.
DR MIM; 616728; phenotype.
DR neXtProt; NX_O60341; -.
DR OpenTargets; ENSG00000004487; -.
DR Orphanet; 477993; Palatal anomalies-widely spaced teeth-facial dysmorphism-developmental delay syndrome.
DR PharmGKB; PA165751392; -.
DR VEuPathDB; HostDB:ENSG00000004487; -.
DR eggNOG; KOG0029; Eukaryota.
DR eggNOG; KOG0685; Eukaryota.
DR GeneTree; ENSGT00940000157193; -.
DR HOGENOM; CLU_004498_5_1_1; -.
DR InParanoid; O60341; -.
DR OMA; SSRGEMF; -.
DR OrthoDB; 1034142at2759; -.
DR PhylomeDB; O60341; -.
DR TreeFam; TF312972; -.
DR BioCyc; MetaCyc:ENSG00000004487-MON; -.
DR BRENDA; 1.14.11.65; 2681.
DR BRENDA; 1.14.11.66; 2681.
DR BRENDA; 1.14.11.67; 2681.
DR BRENDA; 1.14.99.66; 2681.
DR PathwayCommons; O60341; -.
DR Reactome; R-HSA-3214815; HDACs deacetylate histones.
DR Reactome; R-HSA-3214842; HDMs demethylate histones.
DR Reactome; R-HSA-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR Reactome; R-HSA-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR Reactome; R-HSA-9679191; Potential therapeutics for SARS.
DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR SABIO-RK; O60341; -.
DR SignaLink; O60341; -.
DR SIGNOR; O60341; -.
DR BioGRID-ORCS; 23028; 108 hits in 1114 CRISPR screens.
DR ChiTaRS; KDM1A; human.
DR EvolutionaryTrace; O60341; -.
DR GenomeRNAi; 23028; -.
DR Pharos; O60341; Tchem.
DR PRO; PR:O60341; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O60341; protein.
DR Bgee; ENSG00000004487; Expressed in ganglionic eminence and 208 other tissues.
DR ExpressionAtlas; O60341; baseline and differential.
DR Genevisible; O60341; HS.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:BHF-UCL.
DR GO; GO:1990391; C:DNA repair complex; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0005667; C:transcription regulator complex; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0032451; F:demethylase activity; IMP:BHF-UCL.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IDA:BHF-UCL.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR GO; GO:0032452; F:histone demethylase activity; IDA:BHF-UCL.
DR GO; GO:0140682; F:histone H3-di/monomethyl-lysine-4 FAD-dependent demethylase activity; IDA:UniProtKB.
DR GO; GO:0032453; F:histone H3-methyl-lysine-4 demethylase activity; IDA:UniProtKB.
DR GO; GO:0032454; F:histone H3-methyl-lysine-9 demethylase activity; IDA:UniProtKB.
DR GO; GO:0043426; F:MRF binding; IDA:BHF-UCL.
DR GO; GO:0050681; F:nuclear androgen receptor binding; IDA:UniProtKB.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IMP:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0002039; F:p53 binding; IPI:BHF-UCL.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:BHF-UCL.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISS:ARUK-UCL.
DR GO; GO:0061752; F:telomeric repeat-containing RNA binding; IDA:BHF-UCL.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IEA:Ensembl.
DR GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
DR GO; GO:0071480; P:cellular response to gamma radiation; IMP:MGI.
DR GO; GO:0034644; P:cellular response to UV; IDA:MGI.
DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0046098; P:guanine metabolic process; IEA:Ensembl.
DR GO; GO:0034720; P:histone H3-K4 demethylation; IDA:UniProtKB.
DR GO; GO:0033169; P:histone H3-K9 demethylation; IDA:UniProtKB.
DR GO; GO:0055001; P:muscle cell development; ISS:BHF-UCL.
DR GO; GO:0043392; P:negative regulation of DNA binding; IC:BHF-UCL.
DR GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IMP:BHF-UCL.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
DR GO; GO:0051572; P:negative regulation of histone H3-K4 methylation; ISS:ARUK-UCL.
DR GO; GO:0051573; P:negative regulation of histone H3-K9 methylation; ISS:ARUK-UCL.
DR GO; GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:BHF-UCL.
DR GO; GO:0032091; P:negative regulation of protein binding; IMP:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR GO; GO:0042551; P:neuron maturation; IEA:Ensembl.
DR GO; GO:0045793; P:positive regulation of cell size; IEA:Ensembl.
DR GO; GO:0035563; P:positive regulation of chromatin binding; IEA:Ensembl.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
DR GO; GO:0033184; P:positive regulation of histone ubiquitination; IMP:MGI.
DR GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; ISS:ARUK-UCL.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; IMP:BHF-UCL.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; ISS:ARUK-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0006482; P:protein demethylation; IMP:BHF-UCL.
DR GO; GO:0060765; P:regulation of androgen receptor signaling pathway; TAS:Reactome.
DR GO; GO:0090308; P:regulation of DNA methylation-dependent heterochromatin assembly; IDA:UniProtKB.
DR GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; IMP:MGI.
DR GO; GO:0032880; P:regulation of protein localization; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0060992; P:response to fungicide; IEA:Ensembl.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR IDEAL; IID00009; -.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR017366; Hist_Lys-spec_deMease.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR007526; SWIRM.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF01593; Amino_oxidase; 1.
DR Pfam; PF04433; SWIRM; 1.
DR PIRSF; PIRSF038051; Histone_Lys-demethylase; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS50934; SWIRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromatin regulator; Coiled coil;
KW Developmental protein; Direct protein sequencing; Disease variant; FAD;
KW Flavoprotein; Isopeptide bond; Nucleus; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..852
FT /note="Lysine-specific histone demethylase 1A"
FT /id="PRO_0000099881"
FT DOMAIN 174..273
FT /note="SWIRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00247"
FT REGION 1..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..852
FT /note="Demethylase activity"
FT COILED 110..151
FT /evidence="ECO:0000255"
FT COILED 428..514
FT /evidence="ECO:0000255"
FT COMPBIAS 105..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 289
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16885027,
FT ECO:0000269|PubMed:16956976, ECO:0000269|PubMed:21300290,
FT ECO:0000269|PubMed:23721412, ECO:0007744|PDB:2DW4,
FT ECO:0007744|PDB:2H94, ECO:0007744|PDB:2HKO,
FT ECO:0007744|PDB:2IW5, ECO:0007744|PDB:2V1D,
FT ECO:0007744|PDB:2X0L, ECO:0007744|PDB:2XAF,
FT ECO:0007744|PDB:2XAG, ECO:0007744|PDB:2XAH,
FT ECO:0007744|PDB:2XAJ, ECO:0007744|PDB:2XAQ,
FT ECO:0007744|PDB:2XAS, ECO:0007744|PDB:2Y48,
FT ECO:0007744|PDB:3ZMS, ECO:0007744|PDB:3ZMT,
FT ECO:0007744|PDB:3ZMU, ECO:0007744|PDB:3ZMV,
FT ECO:0007744|PDB:3ZMZ, ECO:0007744|PDB:3ZN0,
FT ECO:0007744|PDB:3ZN1"
FT BINDING 308
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16885027,
FT ECO:0000269|PubMed:16956976, ECO:0000269|PubMed:21300290,
FT ECO:0000269|PubMed:23721412, ECO:0007744|PDB:2DW4,
FT ECO:0007744|PDB:2H94, ECO:0007744|PDB:2HKO,
FT ECO:0007744|PDB:2IW5, ECO:0007744|PDB:2V1D,
FT ECO:0007744|PDB:2X0L, ECO:0007744|PDB:2XAF,
FT ECO:0007744|PDB:2XAG, ECO:0007744|PDB:2XAH,
FT ECO:0007744|PDB:2XAJ, ECO:0007744|PDB:2XAQ,
FT ECO:0007744|PDB:2XAS, ECO:0007744|PDB:2Y48,
FT ECO:0007744|PDB:3ZMS, ECO:0007744|PDB:3ZMT,
FT ECO:0007744|PDB:3ZMU, ECO:0007744|PDB:3ZMV,
FT ECO:0007744|PDB:3ZMZ, ECO:0007744|PDB:3ZN0,
FT ECO:0007744|PDB:3ZN1"
FT BINDING 310
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16885027,
FT ECO:0000269|PubMed:16956976, ECO:0000269|PubMed:21300290,
FT ECO:0000269|PubMed:23721412, ECO:0007744|PDB:2DW4,
FT ECO:0007744|PDB:2H94, ECO:0007744|PDB:2HKO,
FT ECO:0007744|PDB:2IW5, ECO:0007744|PDB:2V1D,
FT ECO:0007744|PDB:2X0L, ECO:0007744|PDB:2XAF,
FT ECO:0007744|PDB:2XAG, ECO:0007744|PDB:2XAH,
FT ECO:0007744|PDB:2XAJ, ECO:0007744|PDB:2XAQ,
FT ECO:0007744|PDB:2XAS, ECO:0007744|PDB:2Y48,
FT ECO:0007744|PDB:3ZMS, ECO:0007744|PDB:3ZMT,
FT ECO:0007744|PDB:3ZMU, ECO:0007744|PDB:3ZMV,
FT ECO:0007744|PDB:3ZMZ, ECO:0007744|PDB:3ZN0,
FT ECO:0007744|PDB:3ZN1"
FT BINDING 316
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16885027,
FT ECO:0000269|PubMed:16956976, ECO:0000269|PubMed:21300290,
FT ECO:0000269|PubMed:23721412, ECO:0007744|PDB:2DW4,
FT ECO:0007744|PDB:2H94, ECO:0007744|PDB:2HKO,
FT ECO:0007744|PDB:2IW5, ECO:0007744|PDB:2V1D,
FT ECO:0007744|PDB:2X0L, ECO:0007744|PDB:2XAF,
FT ECO:0007744|PDB:2XAG, ECO:0007744|PDB:2XAH,
FT ECO:0007744|PDB:2XAJ, ECO:0007744|PDB:2XAQ,
FT ECO:0007744|PDB:2XAS, ECO:0007744|PDB:2Y48,
FT ECO:0007744|PDB:3ZMS, ECO:0007744|PDB:3ZMT,
FT ECO:0007744|PDB:3ZMU, ECO:0007744|PDB:3ZMV,
FT ECO:0007744|PDB:3ZMZ, ECO:0007744|PDB:3ZN0,
FT ECO:0007744|PDB:3ZN1"
FT BINDING 332..333
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16885027,
FT ECO:0000269|PubMed:16956976, ECO:0000269|PubMed:21300290,
FT ECO:0000269|PubMed:23721412, ECO:0007744|PDB:2DW4,
FT ECO:0007744|PDB:2H94, ECO:0007744|PDB:2HKO,
FT ECO:0007744|PDB:2IW5, ECO:0007744|PDB:2V1D,
FT ECO:0007744|PDB:2X0L, ECO:0007744|PDB:2XAF,
FT ECO:0007744|PDB:2XAG, ECO:0007744|PDB:2XAH,
FT ECO:0007744|PDB:2XAJ, ECO:0007744|PDB:2XAQ,
FT ECO:0007744|PDB:2XAS, ECO:0007744|PDB:2Y48,
FT ECO:0007744|PDB:3ZMS, ECO:0007744|PDB:3ZMT,
FT ECO:0007744|PDB:3ZMU, ECO:0007744|PDB:3ZMV,
FT ECO:0007744|PDB:3ZMZ, ECO:0007744|PDB:3ZN0,
FT ECO:0007744|PDB:3ZN1"
FT BINDING 801
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16885027,
FT ECO:0000269|PubMed:16956976, ECO:0000269|PubMed:21300290,
FT ECO:0000269|PubMed:23721412, ECO:0007744|PDB:2DW4,
FT ECO:0007744|PDB:2H94, ECO:0007744|PDB:2HKO,
FT ECO:0007744|PDB:2IW5, ECO:0007744|PDB:2V1D,
FT ECO:0007744|PDB:2X0L, ECO:0007744|PDB:2XAF,
FT ECO:0007744|PDB:2XAG, ECO:0007744|PDB:2XAH,
FT ECO:0007744|PDB:2XAJ, ECO:0007744|PDB:2XAQ,
FT ECO:0007744|PDB:2XAS, ECO:0007744|PDB:2Y48,
FT ECO:0007744|PDB:3ZMS, ECO:0007744|PDB:3ZMT,
FT ECO:0007744|PDB:3ZMU, ECO:0007744|PDB:3ZMV,
FT ECO:0007744|PDB:3ZMZ, ECO:0007744|PDB:3ZN0,
FT ECO:0007744|PDB:3ZN1"
FT BINDING 810..811
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16885027,
FT ECO:0000269|PubMed:16956976, ECO:0000269|PubMed:21300290,
FT ECO:0000269|PubMed:23721412, ECO:0007744|PDB:2DW4,
FT ECO:0007744|PDB:2H94, ECO:0007744|PDB:2HKO,
FT ECO:0007744|PDB:2IW5, ECO:0007744|PDB:2V1D,
FT ECO:0007744|PDB:2X0L, ECO:0007744|PDB:2XAF,
FT ECO:0007744|PDB:2XAG, ECO:0007744|PDB:2XAH,
FT ECO:0007744|PDB:2XAJ, ECO:0007744|PDB:2XAQ,
FT ECO:0007744|PDB:2XAS, ECO:0007744|PDB:2Y48,
FT ECO:0007744|PDB:3ZMS, ECO:0007744|PDB:3ZMT,
FT ECO:0007744|PDB:3ZMU, ECO:0007744|PDB:3ZMV,
FT ECO:0007744|PDB:3ZMZ, ECO:0007744|PDB:3ZN0,
FT ECO:0007744|PDB:3ZN1"
FT MOD_RES 59
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 104
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 135
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 611
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 849
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT CROSSLNK 442
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 469
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 503
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000305|PubMed:25018020"
FT VAR_SEQ 173
FT /note="G -> GQAGGLQDDSSGGYGDGQASG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011198"
FT VAR_SEQ 369
FT /note="A -> ADTVK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011199"
FT VARIANT 379
FT /note="E -> K (in CPRF; dbSNP:rs864309715)"
FT /evidence="ECO:0000269|PubMed:26656649"
FT /id="VAR_076366"
FT VARIANT 556
FT /note="D -> G (in CPRF; dbSNP:rs864309716)"
FT /evidence="ECO:0000269|PubMed:23020937,
FT ECO:0000269|PubMed:26656649"
FT /id="VAR_076367"
FT VARIANT 761
FT /note="Y -> H (in CPRF; dbSNP:rs864309714)"
FT /evidence="ECO:0000269|PubMed:24838796,
FT ECO:0000269|PubMed:26656649"
FT /id="VAR_076368"
FT MUTAGEN 503
FT /note="K->R: Loss of polyubiquitination."
FT /evidence="ECO:0000269|PubMed:25018020"
FT MUTAGEN 535
FT /note="N->A: Strongly reduces demethylase activity."
FT /evidence="ECO:0000269|PubMed:16956976"
FT MUTAGEN 564
FT /note="H->A: Strongly reduces demethylase activity."
FT /evidence="ECO:0000269|PubMed:16956976"
FT MUTAGEN 661
FT /note="K->A: Abolishes histone demethylase activity."
FT /evidence="ECO:0000269|PubMed:16079794"
FT MUTAGEN 761
FT /note="Y->A: Strongly reduces demethylase activity."
FT /evidence="ECO:0000269|PubMed:16956976"
FT CONFLICT 78
FT /note="P -> Q (in Ref. 3; AAH40194)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="P -> H (in Ref. 3; AAH48134)"
FT /evidence="ECO:0000305"
FT CONFLICT 669
FT /note="V -> A (in Ref. 4; CAD38675)"
FT /evidence="ECO:0000305"
FT CONFLICT 814
FT /note="A -> V (in Ref. 3; AAH16639)"
FT /evidence="ECO:0000305"
FT HELIX 138..150
FT /evidence="ECO:0007829|PDB:6WC6"
FT HELIX 173..180
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:2COM"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:2HKO"
FT HELIX 190..195
FT /evidence="ECO:0007829|PDB:6E1F"
FT HELIX 197..200
FT /evidence="ECO:0007829|PDB:6E1F"
FT HELIX 204..223
FT /evidence="ECO:0007829|PDB:6E1F"
FT HELIX 231..236
FT /evidence="ECO:0007829|PDB:6E1F"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:6E1F"
FT HELIX 246..258
FT /evidence="ECO:0007829|PDB:6E1F"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:5IT3"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:2COM"
FT STRAND 280..284
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT HELIX 288..299
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT STRAND 303..307
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT STRAND 309..314
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT STRAND 325..330
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:6NQU"
FT HELIX 341..349
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:6KGM"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:5LHH"
FT HELIX 372..393
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT TURN 394..396
FT /evidence="ECO:0007829|PDB:2HKO"
FT STRAND 400..405
FT /evidence="ECO:0007829|PDB:5H6Q"
FT HELIX 408..456
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT TURN 457..461
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT HELIX 476..487
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT TURN 488..490
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT HELIX 491..497
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT HELIX 499..511
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT STRAND 518..521
FT /evidence="ECO:0007829|PDB:3ABU"
FT HELIX 523..539
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT HELIX 544..546
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT TURN 549..555
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT HELIX 556..558
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT STRAND 565..567
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT HELIX 573..578
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT TURN 579..581
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT STRAND 583..585
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT STRAND 588..596
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT STRAND 599..608
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT STRAND 613..623
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT HELIX 627..631
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT STRAND 636..641
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT HELIX 645..653
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT STRAND 654..656
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT STRAND 660..665
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT STRAND 676..680
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT STRAND 683..685
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT TURN 686..689
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT STRAND 690..695
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT STRAND 698..707
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT HELIX 710..715
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT HELIX 720..735
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT HELIX 737..739
FT /evidence="ECO:0007829|PDB:6KGO"
FT STRAND 744..748
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT TURN 751..753
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT TURN 755..757
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT STRAND 758..760
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT STRAND 765..767
FT /evidence="ECO:0007829|PDB:6NQM"
FT HELIX 771..777
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT STRAND 785..788
FT /evidence="ECO:0007829|PDB:6S35"
FT STRAND 796..798
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT HELIX 801..803
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT STRAND 805..807
FT /evidence="ECO:0007829|PDB:5H6R"
FT HELIX 811..829
FT /evidence="ECO:0007829|PDB:2Z3Y"
FT HELIX 833..835
FT /evidence="ECO:0007829|PDB:5L3D"
SQ SEQUENCE 852 AA; 92903 MW; A61CEDE51E4E0C1D CRC64;
MLSGKKAAAA AAAAAAAATG TEAGPGTAGG SENGSEVAAQ PAGLSGPAEV GPGAVGERTP
RKKEPPRASP PGGLAEPPGS AGPQAGPTVV PGSATPMETG IAETPEGRRT SRRKRAKVEY
REMDESLANL SEDEYYSEEE RNAKAEKEKK LPPPPPQAPP EEENESEPEE PSGVEGAAFQ
SRLPHDRMTS QEAACFPDII SGPQQTQKVF LFIRNRTLQL WLDNPKIQLT FEATLQQLEA
PYNSDTVLVH RVHSYLERHG LINFGIYKRI KPLPTKKTGK VIIIGSGVSG LAAARQLQSF
GMDVTLLEAR DRVGGRVATF RKGNYVADLG AMVVTGLGGN PMAVVSKQVN MELAKIKQKC
PLYEANGQAV PKEKDEMVEQ EFNRLLEATS YLSHQLDFNV LNNKPVSLGQ ALEVVIQLQE
KHVKDEQIEH WKKIVKTQEE LKELLNKMVN LKEKIKELHQ QYKEASEVKP PRDITAEFLV
KSKHRDLTAL CKEYDELAET QGKLEEKLQE LEANPPSDVY LSSRDRQILD WHFANLEFAN
ATPLSTLSLK HWDQDDDFEF TGSHLTVRNG YSCVPVALAE GLDIKLNTAV RQVRYTASGC
EVIAVNTRST SQTFIYKCDA VLCTLPLGVL KQQPPAVQFV PPLPEWKTSA VQRMGFGNLN
KVVLCFDRVF WDPSVNLFGH VGSTTASRGE LFLFWNLYKA PILLALVAGE AAGIMENISD
DVIVGRCLAI LKGIFGSSAV PQPKETVVSR WRADPWARGS YSYVAAGSSG NDYDLMAQPI
TPGPSIPGAP QPIPRLFFAG EHTIRNYPAT VHGALLSGLR EAGRIADQFL GAMYTLPRQA
TPGVPAQQSP SM
