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 27-MAR-2024, entry version 226. 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. 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 INTERACTION WITH ZMYND8, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=25593309; DOI=10.1101/gad.252189.114; RA Gong F., Chiu L.Y., Cox B., Aymard F., Clouaire T., Leung J.W., RA Cammarata M., Perez M., Agarwal P., Brodbelt J.S., Legube G., Miller K.M.; RT "Screen identifies bromodomain protein ZMYND8 in chromatin recognition of RT transcription-associated DNA damage that promotes homologous RT recombination."; RL Genes Dev. 29:197-211(2015). RN [34] RP INTERACTION WITH RBPJ AND L3MBTL3. RX PubMed=29030483; DOI=10.15252/embj.201796525; RA Xu T., Park S.S., Giaimo B.D., Hall D., Ferrante F., Ho D.M., Hori K., RA Anhezini L., Ertl I., Bartkuhn M., Zhang H., Milon E., Ha K., Conlon K.P., RA Kuick R., Govindarajoo B., Zhang Y., Sun Y., Dou Y., Basrur V., RA Elenitoba-Johnson K.S., Nesvizhskii A.I., Ceron J., Lee C.Y., Borggrefe T., RA Kovall R.A., Rual J.F.; RT "RBPJ/CBF1 interacts with L3MBTL3/MBT1 to promote repression of Notch RT signaling via histone demethylase KDM1A/LSD1."; RL EMBO J. 36:3232-3249(2017). RN [35] 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 [36] RP DEUBIQUITINATION BY USP38. RX PubMed=30497519; DOI=10.1186/s40659-018-0201-8; RA Liu W., Zhang Q., Fang Y., Wang Y.; RT "The deubiquitinase USP38 affects cellular functions through interacting RT with LSD1."; RL Biol. Res. 51:53-53(2018). RN [37] RP FUNCTION. RX PubMed=29358331; DOI=10.1074/jbc.ra117.000342; RA Zhang C., Hoang N., Leng F., Saxena L., Lee L., Alejo S., Qi D., Khal A., RA Sun H., Lu F., Zhang H.; RT "LSD1 demethylase and the methyl-binding protein PHF20L1 prevent SET7 RT methyltransferase-dependent proteolysis of the stem-cell protein SOX2."; RL J. Biol. Chem. 293:3663-3674(2018). RN [38] RP FUNCTION. RX PubMed=29691401; DOI=10.1038/s41467-018-04019-9; RA Leng F., Yu J., Zhang C., Alejo S., Hoang N., Sun H., Lu F., Zhang H.; RT "Methylated DNMT1 and E2F1 are targeted for proteolysis by L3MBTL3 and RT CRL4-DCAF5 ubiquitin ligase."; RL Nat. Commun. 9:1641-1641(2018). RN [39] 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 [40] 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 [41] 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 [42] 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 [43] {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 [44] {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 [45] 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 [46] 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 [47] 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 (PubMed:29691401). Demethylates CC methylated 'Lys-42' and methylated 'Lys-117' of SOX2 (PubMed:29358331). CC Required for gastrulation during embryogenesis. Component of a CC RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase CC (HDAC) recruitment, a number of genes implicated in multilineage blood CC cell development. Effector of SNAI1-mediated transcription repression CC of E-cadherin/CDH1, CDN7 and KRT8. Required for the maintenance of the CC silenced state of the SNAI1 target genes E-cadherin/CDH1 and CDN7 CC (PubMed:20389281). {ECO:0000269|PubMed:12032298, CC ECO:0000269|PubMed:15620353, ECO:0000269|PubMed:15811342, CC ECO:0000269|PubMed:16079794, ECO:0000269|PubMed:16079795, CC ECO:0000269|PubMed:16140033, ECO:0000269|PubMed:16223729, CC ECO:0000269|PubMed:16885027, ECO:0000269|PubMed:16956976, CC ECO:0000269|PubMed:17805299, ECO:0000269|PubMed:20228790, CC ECO:0000269|PubMed:20389281, ECO:0000269|PubMed:20562920, CC ECO:0000269|PubMed:21300290, ECO:0000269|PubMed:23721412, CC ECO:0000269|PubMed:29358331, ECO:0000269|PubMed:29691401}. 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 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). Interacts CC with RBPJ (PubMed:29030483). Interacts with L3MBTL3 (PubMed:29030483). CC Interacts with ZMYND8 (PubMed:25593309). {ECO:0000250|UniProtKB:Q6ZQ88, CC ECO:0000269|PubMed:11102443, ECO:0000269|PubMed:12032298, CC ECO:0000269|PubMed:12493763, ECO:0000269|PubMed:16079794, CC ECO:0000269|PubMed:16079795, ECO:0000269|PubMed:16140033, CC ECO:0000269|PubMed:16885027, ECO:0000269|PubMed:16956976, CC ECO:0000269|PubMed:20389281, ECO:0000269|PubMed:20562920, CC ECO:0000269|PubMed:21300290, ECO:0000269|PubMed:23721412, CC ECO:0000269|PubMed:25018020, ECO:0000269|PubMed:25593309, CC ECO:0000269|PubMed:29030483, 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; O60341: KDM1A; NbExp=3; IntAct=EBI-710124, EBI-710124; 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; Q9Y466: NR2E1; NbExp=7; IntAct=EBI-710124, EBI-11792373; 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 (PubMed:25018020). Deubiquitinated by USP38; preventing it CC from degradation by the 26S proteasome (PubMed:30497519). CC {ECO:0000269|PubMed:25018020, ECO:0000269|PubMed:30497519}. 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 PDB; 7VQS; X-ray; 2.94 A; A=172-833. DR PDB; 7VQT; X-ray; 2.91 A; A=172-833. DR PDB; 7VQU; X-ray; 2.94 A; A=172-833. DR PDB; 7W3L; X-ray; 2.51 A; A=172-833. DR PDB; 7XW8; X-ray; 2.28 A; A=172-833. DR PDB; 7ZRY; X-ray; 2.70 A; A=1-852. 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 PDBsum; 7VQS; -. DR PDBsum; 7VQT; -. DR PDBsum; 7VQU; -. DR PDBsum; 7W3L; -. DR PDBsum; 7XW8; -. DR PDBsum; 7ZRY; -. DR AlphaFoldDB; O60341; -. DR BMRB; O60341; -. DR SASBDB; O60341; -. DR SMR; O60341; -. DR BioGRID; 116667; 817. DR CORUM; O60341; -. DR DIP; DIP-34641N; -. DR IntAct; O60341; 323. 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 GlyGen; O60341; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O60341; -. DR MetOSite; O60341; -. DR PhosphoSitePlus; O60341; -. DR SwissPalm; O60341; -. DR BioMuta; KDM1A; -. DR EPD; O60341; -. DR jPOST; O60341; -. DR MassIVE; O60341; -. DR MaxQB; O60341; -. DR PaxDb; 9606-ENSP00000383042; -. DR PeptideAtlas; O60341; -. DR ProteomicsDB; 49364; -. [O60341-1] DR ProteomicsDB; 49365; -. [O60341-2] DR Pumba; O60341; -. DR Antibodypedia; 3136; 843 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 AGR; HGNC:29079; -. 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; 5402444at2759; -. DR PhylomeDB; O60341; -. DR TreeFam; TF312972; -. DR BioCyc; MetaCyc:ENSG00000004487-MONOMER; -. 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; 121 hits in 1204 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 210 other cell types or tissues. DR ExpressionAtlas; O60341; baseline and differential. 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:0140682; F:FAD-dependent H3K4me/H3K4me3 demethylase activity; IDA:UniProtKB. 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:0032453; F:histone H3K4 demethylase activity; IDA:UniProtKB. DR GO; GO:0032454; F:histone H3K9 demethylase activity; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. 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:0003713; F:transcription coactivator activity; IDA:BHF-UCL. 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:0140861; P:DNA repair-dependent chromatin remodeling; IDA:MGI. DR GO; GO:0046098; P:guanine metabolic process; IEA:Ensembl. 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:0045892; P:negative regulation of DNA-templated transcription; IDA:BHF-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:UniProtKB. DR GO; GO:0042551; P:neuron maturation; IEA:Ensembl. DR GO; GO:0045793; P:positive regulation of cell size; IEA:Ensembl. DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab. 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:0031398; P:positive regulation of protein ubiquitination; IMP:MGI. 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 formation; 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; 3.90.660.10; -; 1. DR Gene3D; 1.10.287.80; ATP synthase, gamma subunit, helix hairpin domain; 1. DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. 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 PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1. DR PANTHER; PTHR10742:SF386; LYSINE-SPECIFIC HISTONE DEMETHYLASE 1A; 1. DR Pfam; PF01593; Amino_oxidase; 1. DR Pfam; PF04433; SWIRM; 1. DR PIRSF; PIRSF038051; Histone_Lys-demethylase; 1. DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. DR SUPFAM; SSF46689; Homeodomain-like; 1. DR PROSITE; PS50934; SWIRM; 1. DR Genevisible; O60341; HS. 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:7ZRY" 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:7VQT" 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 //