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Lysine-specific histone demethylase 1A (EC 1.-.-.-) (BRAF35-HDAC complex protein BHC110) (Flavin-containing amine oxidase domain-containing protein 2)

 KDM1A_HUMAN             Reviewed;         852 AA.
O60341; A8MWP9; Q5TH94; Q5TH95; Q86VT7; Q8IXK4; Q8NDP6; Q8TAZ3;
Q96AW4;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
16-AUG-2004, sequence version 2.
27-SEP-2017, entry version 181.
RecName: Full=Lysine-specific histone demethylase 1A;
EC=1.-.-.-;
AltName: Full=BRAF35-HDAC complex protein BHC110;
AltName: Full=Flavin-containing amine oxidase domain-containing protein 2;
Name=KDM1A; Synonyms=AOF2, KDM1, KIAA0601, LSD1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=9628581; DOI=10.1093/dnares/5.1.31;
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
Ohara O.;
"Prediction of the coding sequences of unidentified human genes. IX.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 5:31-39(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, Skin, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 245-852 (ISOFORM 1).
TISSUE=Brain;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
PARTIAL PROTEIN SEQUENCE, INTERACTION WITH A HISTONE
DEACETYLASE-CONTAINING COMPLEX, AND FUNCTION.
PubMed=12032298; DOI=10.1073/pnas.112008599;
Hakimi M.-A., Bochar D.A., Chenoweth J., Lane W.S., Mandel G.,
Shiekhattar R.;
"A core-BRAF35 complex containing histone deacetylase mediates
repression of neuronal-specific genes.";
Proc. Natl. Acad. Sci. U.S.A. 99:7420-7425(2002).
[6]
INTERACTION WITH THE HDAC1 COMPLEX, IDENTIFICATION BY MASS
SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=11102443; DOI=10.1074/jbc.M007372200;
Humphrey G.W., Wang Y., Russanova V.R., Hirai T., Qin J., Nakatani Y.,
Howard B.H.;
"Stable histone deacetylase complexes distinguished by the presence of
SANT domain proteins CoREST/kiaa0071 and Mta-L1.";
J. Biol. Chem. 276:6817-6824(2001).
[7]
INTERACTION WITH A HISTONE DEACETYLASE-CONTAINING COMPLEX, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=12493763; DOI=10.1074/jbc.M208992200;
Hakimi M.-A., Dong Y., Lane W.S., Speicher D.W., Shiekhattar R.;
"A candidate X-linked mental retardation gene is a component of a new
family of histone deacetylase-containing complexes.";
J. Biol. Chem. 278:7234-7239(2003).
[8]
ENZYME ACTIVITY, FUNCTION, AND COFACTOR.
PubMed=15620353; DOI=10.1016/j.cell.2004.12.012;
Shi Y.-J., Lan F., Matson C., Mulligan P., Whetstine J.R., Cole P.A.,
Casero R.A., Shi Y.;
"Histone demethylation mediated by the nuclear amine oxidase homolog
LSD1.";
Cell 119:941-953(2004).
[9]
ENZYME ACTIVITY, AND COFACTOR.
PubMed=15811342; DOI=10.1016/j.febslet.2005.03.015;
Forneris F., Binda C., Vanoni M.A., Mattevi A., Battaglioli E.;
"Histone demethylation catalysed by LSD1 is a flavin-dependent
oxidative process.";
FEBS Lett. 579:2203-2207(2005).
[10]
INTERACTION WITH RCOR1 AND PHF21A.
PubMed=16140033; DOI=10.1016/j.molcel.2005.08.027;
Shi Y.-J., Matson C., Lan F., Iwase S., Baba T., Shi Y.;
"Regulation of LSD1 histone demethylase activity by its associated
factors.";
Mol. Cell 19:857-864(2005).
[11]
INTERACTION WITH RCOR1, AND MUTAGENESIS OF LYS-661.
PubMed=16079794; DOI=10.1038/nature04021;
Lee M.G., Wynder C., Cooch N., Shiekhattar R.;
"An essential role for CoREST in nucleosomal histone 3 lysine 4
demethylation.";
Nature 437:432-435(2005).
[12]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION
WITH ANDR.
PubMed=16079795; DOI=10.1038/nature04020;
Metzger E., Wissmann M., Yin N., Mueller J.M., Schneider R.,
Peters A.H.F.M., Guenther T., Buettner R., Schuele R.;
"LSD1 demethylates repressive histone marks to promote androgen-
receptor-dependent transcription.";
Nature 437:436-439(2005).
[13]
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=16223729; DOI=10.1074/jbc.M509549200;
Forneris F., Binda C., Vanoni M.A., Battaglioli E., Mattevi A.;
"Human histone demethylase LSD1 reads the histone code.";
J. Biol. Chem. 280:41360-41365(2005).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[15]
FUNCTION.
PubMed=17805299; DOI=10.1038/nature06092;
Huang J., Sengupta R., Espejo A.B., Lee M.G., Dorsey J.A., Richter M.,
Opravil S., Shiekhattar R., Bedford M.T., Jenuwein T., Berger S.L.;
"p53 is regulated by the lysine demethylase LSD1.";
Nature 449:105-108(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-59; THR-104; SER-126;
SER-131; SER-166 AND SER-849, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-104; SER-131 AND
SER-137, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[22]
INTERACTION WITH ASXL1.
PubMed=19880879; DOI=10.1074/jbc.M109.065862;
Lee S.W., Cho Y.S., Na J.M., Park U.H., Kang M., Kim E.J., Um S.J.;
"ASXL1 represses retinoic acid receptor-mediated transcription through
associating with HP1 and LSD1.";
J. Biol. Chem. 285:18-29(2010).
[23]
FUNCTION.
PubMed=20228790; DOI=10.1038/nature08839;
Metzger E., Imhof A., Patel D., Kahl P., Hoffmeyer K., Friedrichs N.,
Muller J.M., Greschik H., Kirfel J., Ji S., Kunowska N.,
Beisenherz-Huss C., Gunther T., Buettner R., Schule R.;
"Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation
at histone H3K4.";
Nature 464:792-796(2010).
[24]
FUNCTION, AND INTERACTION WITH SNAI.
PubMed=20562920; DOI=10.1038/onc.2010.234;
Lin T., Ponn A., Hu X., Law B.K., Lu J.;
"Requirement of the histone demethylase LSD1 in Snai1-mediated
transcriptional repression during epithelial-mesenchymal transition.";
Oncogene 29:4896-4904(2010).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131; SER-137; SER-166
AND SER-849, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131; SER-137 AND
SER-166, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131; SER-137; SER-166
AND SER-611, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126; SER-131; TYR-135
AND SER-137, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[30]
INTERACTION WITH JADE2, INDUCTION, UBIQUITINATION, AND MUTAGENESIS OF
LYS-503.
PubMed=25018020; DOI=10.1016/j.molcel.2014.06.006;
Han X., Gui B., Xiong C., Zhao L., Liang J., Sun L., Yang X., Yu W.,
Si W., Yan R., Yi X., Zhang D., Li W., Li L., Yang J., Wang Y.,
Sun Y.E., Zhang D., Meng A., Shang Y.;
"Destabilizing LSD1 by Jade-2 promotes neurogenesis: an antibraking
system in neural development.";
Mol. Cell 55:482-494(2014).
[31]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-442 AND LYS-469, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[32]
X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS) OF 171-836 IN COMPLEX WITH FAD
AND RCOR1.
PubMed=16885027; DOI=10.1016/j.molcel.2006.07.012;
Yang M., Gocke C.B., Luo X., Borek D., Tomchick D.R., Machius M.,
Otwinowski Z., Yu H.;
"Structural basis for CoREST-dependent demethylation of nucleosomes by
the human LSD1 histone demethylase.";
Mol. Cell 23:377-387(2006).
[33]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 172-835 IN COMPLEX WITH FAD,
AND MUTAGENESIS OF ASN-535; HIS-564 AND TYR-761.
PubMed=16956976; DOI=10.1073/pnas.0606381103;
Chen Y., Yang Y., Wang F., Wan K., Yamane K., Zhang Y., Lei M.;
"Crystal structure of human histone lysine-specific demethylase 1
(LSD1).";
Proc. Natl. Acad. Sci. U.S.A. 103:13956-13961(2006).
[34]
STRUCTURE BY NMR OF 166-285, AND DOMAIN.
PubMed=16531230; DOI=10.1016/j.str.2005.12.004;
Tochio N., Umehara T., Koshiba S., Inoue M., Yabuki T., Aoki M.,
Seki E., Watanabe S., Tomo Y., Hanada M., Ikari M., Sato M.,
Terada T., Nagase T., Ohara O., Shirouzu M., Tanaka A., Kigawa T.,
Yokoyama S.;
"Solution structure of the SWIRM domain of human histone demethylase
LSD1.";
Structure 14:457-468(2006).
[35]
VARIANT CPRF GLY-556.
PubMed=23020937; DOI=10.1016/S0140-6736(12)61480-9;
Rauch A., Wieczorek D., Graf E., Wieland T., Endele S.,
Schwarzmayr T., Albrecht B., Bartholdi D., Beygo J., Di Donato N.,
Dufke A., Cremer K., Hempel M., Horn D., Hoyer J., Joset P.,
Roepke A., Moog U., Riess A., Thiel C.T., Tzschach A., Wiesener A.,
Wohlleber E., Zweier C., Ekici A.B., Zink A.M., Rump A., Meisinger C.,
Grallert H., Sticht H., Schenck A., Engels H., Rappold G.,
Schroeck E., Wieacker P., Riess O., Meitinger T., Reis A., Strom T.M.;
"Range of genetic mutations associated with severe non-syndromic
sporadic intellectual disability: an exome sequencing study.";
Lancet 380:1674-1682(2012).
[36]
VARIANT CPRF HIS-761.
PubMed=24838796; DOI=10.1002/ajmg.a.36450;
Tunovic S., Barkovich J., Sherr E.H., Slavotinek A.M.;
"De novo ANKRD11 and KDM1A gene mutations in a male with features of
KBG syndrome and Kabuki syndrome.";
Am. J. Med. Genet. A 164A:1744-1749(2014).
[37]
VARIANTS CPRF LYS-379; GLY-556 AND HIS-761.
PubMed=26656649; DOI=10.1038/gim.2015.161;
Chong J.X., Yu J.H., Lorentzen P., Park K.M., Jamal S.M., Tabor H.K.,
Rauch A., Saenz M.S., Boltshauser E., Patterson K.E., Nickerson D.A.,
Bamshad M.J.;
"Gene discovery for Mendelian conditions via social networking: de
novo variants in KDM1A cause developmental delay and distinctive
facial features.";
Genet. Med. 18:788-795(2016).
-!- FUNCTION: Histone demethylase that demethylates both 'Lys-4'
(H3K4me) and 'Lys-9' (H3K9me) of histone H3, thereby acting as a
coactivator or a corepressor, depending on the context. Acts by
oxidizing the substrate by FAD to generate the corresponding imine
that is subsequently hydrolyzed. Acts as a corepressor by
mediating demethylation of H3K4me, a specific tag for epigenetic
transcriptional activation. Demethylates both mono- (H3K4me1) and
di-methylated (H3K4me2) H3K4me. May play a role in the repression
of neuronal genes. Alone, it is unable to demethylate H3K4me on
nucleosomes and requires the presence of RCOR1/CoREST to achieve
such activity. Also acts as a coactivator of androgen receptor
(ANDR)-dependent transcription, by being recruited to ANDR target
genes and mediating demethylation of H3K9me, a specific tag for
epigenetic transcriptional repression. The presence of PRKCB in
ANDR-containing complexes, which mediates phosphorylation of 'Thr-
6' of histone H3 (H3T6ph), a specific tag that prevents
demethylation H3K4me, prevents H3K4me demethylase activity of
KDM1A. Demethylates di-methylated 'Lys-370' of p53/TP53 which
prevents interaction of p53/TP53 with TP53BP1 and represses
p53/TP53-mediated transcriptional activation. Demethylates and
stabilizes the DNA methylase DNMT1. Required for gastrulation
during embryogenesis. Component of a RCOR/GFI/KDM1A/HDAC complex
that suppresses, via histone deacetylase (HDAC) recruitment, a
number of genes implicated in multilineage blood cell development.
Effector of SNAI1-mediated transcription repression of E-
cadherin/CDH1, CDN7 and KRT8. Required for the maintenance of the
silenced state of the SNAI1 target genes E-cadherin/CDH1 and CDN7.
{ECO:0000269|PubMed:12032298, ECO:0000269|PubMed:15620353,
ECO:0000269|PubMed:16079795, ECO:0000269|PubMed:17805299,
ECO:0000269|PubMed:20228790, ECO:0000269|PubMed:20562920}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000269|PubMed:15620353,
ECO:0000269|PubMed:15811342};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=3.0 uM for H3 monomethyl-K4 {ECO:0000269|PubMed:16223729};
KM=4.2 uM for H3 dimethyl-K4 {ECO:0000269|PubMed:16223729};
KM=3.9 uM for H3 monomethyl-K4-monomethyl-K9
{ECO:0000269|PubMed:16223729};
KM=17.5 uM for monomethyl-K4-acetyl-K9
{ECO:0000269|PubMed:16223729};
-!- SUBUNIT: Component of a RCOR/GFI/KDM1A/HDAC complex
(PubMed:12032298, PubMed:11102443). Interacts directly with GFI1
and GFI1B. Interacts with INSM1 (By similarity). Component of a
BHC histone deacetylase complex that contains HDAC1, HDAC2,
HMG20B, KDM1A, RCOR1 and PHF21A. The BHC complex may also contain
ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I (PubMed:12493763,
PubMed:16140033, PubMed:16885027). In the complex, RCOR1/CoREST
strongly enhances the demethylase activity and protects it from
the proteasome while PHF21A/BHC80 inhibits the demethylase
activity (PubMed:16079794, PubMed:16956976). Interacts with the
androgen receptor (AR) (PubMed:16079795). Interacts with ASXL1
(PubMed:19880879). Interacts with SNAI1 (via SNAG domain)
(PubMed:20562920). Interacts (via AOD/Tower domain) with JADE2
(via C-terminus) (PubMed:25018020). Interacts with ESRRB; co-
occupes the core set of ESRRB targets (By similarity).
{ECO:0000250|UniProtKB:Q6ZQ88, ECO:0000269|PubMed:11102443,
ECO:0000269|PubMed:12032298, ECO:0000269|PubMed:12493763,
ECO:0000269|PubMed:16079794, ECO:0000269|PubMed:16079795,
ECO:0000269|PubMed:16140033, ECO:0000269|PubMed:16885027,
ECO:0000269|PubMed:16956976, ECO:0000269|PubMed:19880879,
ECO:0000269|PubMed:20562920, ECO:0000269|PubMed:25018020}.
-!- INTERACTION:
Q99996:AKAP9; NbExp=2; IntAct=EBI-710124, EBI-1048311;
Q8IXJ9:ASXL1; NbExp=2; IntAct=EBI-710124, EBI-1646500;
P59598:Asxl1 (xeno); NbExp=2; IntAct=EBI-710124, EBI-5743705;
Q6P047:C8orf74; NbExp=2; IntAct=EBI-710124, EBI-8466055;
A5D8V7:CCDC151; NbExp=2; IntAct=EBI-710124, EBI-8466445;
Q9BXL8:CDCA4; NbExp=2; IntAct=EBI-710124, EBI-1773949;
Q8NHQ1:CEP70; NbExp=2; IntAct=EBI-710124, EBI-739624;
Q12873:CHD3; NbExp=4; IntAct=EBI-710124, EBI-523590;
P38432:COIL; NbExp=4; IntAct=EBI-710124, EBI-945751;
Q96EY1:DNAJA3; NbExp=2; IntAct=EBI-710124, EBI-356767;
Q8IZU1:FAM9A; NbExp=2; IntAct=EBI-710124, EBI-8468186;
Q9BQS8:FYCO1; NbExp=2; IntAct=EBI-710124, EBI-2869338;
Q8NEC7:GSTCD; NbExp=2; IntAct=EBI-710124, EBI-8469616;
Q9BX10:GTPBP2; NbExp=2; IntAct=EBI-710124, EBI-6115579;
Q96CS2:HAUS1; NbExp=2; IntAct=EBI-710124, EBI-2514791;
O15379:HDAC3; NbExp=4; IntAct=EBI-710124, EBI-607682;
Q9UBX0:HESX1; NbExp=2; IntAct=EBI-710124, EBI-8470369;
Q16695:HIST3H3; NbExp=2; IntAct=EBI-710124, EBI-358900;
Q9NP66:HMG20A; NbExp=3; IntAct=EBI-710124, EBI-740641;
Q16891:IMMT; NbExp=2; IntAct=EBI-710124, EBI-473801;
Q8TBB5:KLHDC4; NbExp=2; IntAct=EBI-710124, EBI-8472352;
Q14525:KRT33B; NbExp=3; IntAct=EBI-710124, EBI-1049638;
Q6A163:KRT39; NbExp=4; IntAct=EBI-710124, EBI-11958242;
Q96JB6:LOXL4; NbExp=2; IntAct=EBI-710124, EBI-749562;
O95983:MBD3; NbExp=4; IntAct=EBI-710124, EBI-1783068;
P46531:NOTCH1; NbExp=8; IntAct=EBI-710124, EBI-636374;
Q13133:NR1H3; NbExp=2; IntAct=EBI-710124, EBI-781356;
Q8IZS5:OFCC1; NbExp=2; IntAct=EBI-710124, EBI-8477661;
Q8IZL8:PELP1; NbExp=6; IntAct=EBI-710124, EBI-716449;
Q5T6S3:PHF19; NbExp=2; IntAct=EBI-710124, EBI-2339674;
Q03181:PPARD; NbExp=2; IntAct=EBI-710124, EBI-6426768;
P62191:PSMC1; NbExp=2; IntAct=EBI-710124, EBI-357598;
Q9NS23:RASSF1; NbExp=2; IntAct=EBI-710124, EBI-367363;
P50749:RASSF2; NbExp=2; IntAct=EBI-710124, EBI-960081;
Q06330:RBPJ; NbExp=4; IntAct=EBI-710124, EBI-632552;
Q9UKL0:RCOR1; NbExp=7; IntAct=EBI-710124, EBI-926563;
Q9P2K3-2:RCOR3; NbExp=4; IntAct=EBI-710124, EBI-1504830;
Q8N6K7:SAMD3; NbExp=2; IntAct=EBI-710124, EBI-748741;
Q9UGK8:SERGEF; NbExp=2; IntAct=EBI-710124, EBI-465368;
Q13435:SF3B2; NbExp=2; IntAct=EBI-710124, EBI-749111;
O15198:SMAD9; NbExp=2; IntAct=EBI-710124, EBI-748763;
O95863:SNAI1; NbExp=32; IntAct=EBI-710124, EBI-1045459;
Q96H20:SNF8; NbExp=2; IntAct=EBI-710124, EBI-747719;
Q8N0Z3:SPICE1; NbExp=3; IntAct=EBI-710124, EBI-2361917;
Q96BD6:SPSB1; NbExp=2; IntAct=EBI-710124, EBI-2659201;
Q8N4C7:STX19; NbExp=2; IntAct=EBI-710124, EBI-8484990;
Q8N6V9:TEX9; NbExp=3; IntAct=EBI-710124, EBI-746341;
Q9BUZ4:TRAF4; NbExp=3; IntAct=EBI-710124, EBI-3650647;
Q9Y3C0:WASHC3; NbExp=4; IntAct=EBI-710124, EBI-712969;
O96006:ZBED1; NbExp=3; IntAct=EBI-710124, EBI-740037;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11102443,
ECO:0000269|PubMed:16079795}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O60341-1; Sequence=Displayed;
Name=2;
IsoId=O60341-2; Sequence=VSP_011198, VSP_011199;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:16079795}.
-!- INDUCTION: Down-regulated during neural differentiation in
neuroblastoma cancer. {ECO:0000269|PubMed:25018020}.
-!- DOMAIN: The SWIRM domain may act as an anchor site for a histone
tail. {ECO:0000269|PubMed:16531230}.
-!- PTM: Polyubiquitinated by JADE2; which leads to its proteasomal
degradation. {ECO:0000269|PubMed:25018020}.
-!- DISEASE: Cleft palate, psychomotor retardation, and distinctive
facial features (CPRF) [MIM:616728]: A syndrome characterized by
cleft palate, developmental delay, psychomotor retardation, and
facial dysmorphic features including a prominent forehead,
slightly arched eyebrows, elongated palpebral fissures, a wide
nasal bridge, thin lips, and widely spaced teeth. Cleft palate is
a congenital fissure of the soft and/or hard palate, due to faulty
fusion. {ECO:0000269|PubMed:23020937, ECO:0000269|PubMed:24838796,
ECO:0000269|PubMed:26656649}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA25527.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AB011173; BAA25527.1; ALT_INIT; mRNA.
EMBL; AL031428; CAI19707.2; -; Genomic_DNA.
EMBL; AL031428; CAI19708.2; -; Genomic_DNA.
EMBL; BC016639; AAH16639.1; -; mRNA.
EMBL; BC025362; AAH25362.1; -; mRNA.
EMBL; BC040194; AAH40194.3; -; mRNA.
EMBL; BC048134; AAH48134.2; -; mRNA.
EMBL; AL833812; CAD38675.2; -; mRNA.
CCDS; CCDS30627.1; -. [O60341-1]
CCDS; CCDS53278.1; -. [O60341-2]
RefSeq; NP_001009999.1; NM_001009999.2. [O60341-2]
RefSeq; NP_055828.2; NM_015013.3. [O60341-1]
UniGene; Hs.591518; -.
PDB; 2COM; NMR; -; A=169-279.
PDB; 2DW4; X-ray; 2.30 A; A=172-831.
PDB; 2EJR; X-ray; 2.70 A; A=172-833.
PDB; 2H94; X-ray; 2.90 A; A=172-835.
PDB; 2HKO; X-ray; 2.80 A; A=172-835.
PDB; 2IW5; X-ray; 2.57 A; A=171-836.
PDB; 2L3D; NMR; -; A=174-273.
PDB; 2UXN; X-ray; 2.72 A; A=171-836.
PDB; 2UXX; X-ray; 2.74 A; A=171-836.
PDB; 2V1D; X-ray; 3.10 A; A=123-852.
PDB; 2X0L; X-ray; 3.00 A; A=123-852.
PDB; 2XAF; X-ray; 3.25 A; A=1-852.
PDB; 2XAG; X-ray; 3.10 A; A=1-852.
PDB; 2XAH; X-ray; 3.10 A; A=1-852.
PDB; 2XAJ; X-ray; 3.30 A; A=1-852.
PDB; 2XAQ; X-ray; 3.20 A; A=1-852.
PDB; 2XAS; X-ray; 3.20 A; A=1-852.
PDB; 2Y48; X-ray; 3.00 A; A=123-852.
PDB; 2Z3Y; X-ray; 2.25 A; A=172-833.
PDB; 2Z5U; X-ray; 2.25 A; A=172-833.
PDB; 3ABT; X-ray; 3.20 A; A=172-833.
PDB; 3ABU; X-ray; 3.10 A; A=172-833.
PDB; 3ZMS; X-ray; 2.96 A; A=1-852.
PDB; 3ZMT; X-ray; 3.10 A; A=1-852.
PDB; 3ZMU; X-ray; 3.20 A; A=1-852.
PDB; 3ZMV; X-ray; 3.00 A; A=1-852.
PDB; 3ZMZ; X-ray; 3.00 A; A=1-852.
PDB; 3ZN0; X-ray; 2.80 A; A=1-852.
PDB; 3ZN1; X-ray; 3.10 A; A=1-852.
PDB; 4BAY; X-ray; 3.10 A; A=172-852.
PDB; 4CZZ; X-ray; 3.00 A; A=1-852.
PDB; 4KUM; X-ray; 3.05 A; A=171-836.
PDB; 4UV8; X-ray; 2.80 A; A=1-852.
PDB; 4UV9; X-ray; 3.00 A; A=1-852.
PDB; 4UVA; X-ray; 2.90 A; A=1-852.
PDB; 4UVB; X-ray; 2.80 A; A=1-852.
PDB; 4UVC; X-ray; 3.10 A; A=1-852.
PDB; 4UXN; X-ray; 2.85 A; A=1-852.
PDB; 4XBF; X-ray; 2.80 A; A=171-836.
PDB; 5AFW; X-ray; 1.60 A; B=108-119.
PDB; 5H6Q; X-ray; 2.53 A; A=172-833.
PDB; 5H6R; X-ray; 2.60 A; A=172-833.
PDB; 5IT3; X-ray; 1.40 A; A/B=183-267.
PDB; 5L3B; X-ray; 3.30 A; A=1-852.
PDB; 5L3C; X-ray; 3.31 A; A=1-852.
PDB; 5L3D; X-ray; 2.60 A; A=1-852.
PDB; 5L3E; X-ray; 2.80 A; A=123-852.
PDB; 5L3F; X-ray; 3.50 A; A=123-852.
PDB; 5L3G; X-ray; 3.10 A; A=123-852.
PDB; 5LBQ; X-ray; 3.30 A; A=123-852.
PDB; 5LGN; X-ray; 3.20 A; A=172-836.
PDB; 5LGT; X-ray; 3.00 A; A=123-852.
PDB; 5LGU; X-ray; 3.20 A; A=123-852.
PDB; 5LHG; X-ray; 3.34 A; A=1-852.
PDB; 5LHH; X-ray; 3.05 A; A=1-852.
PDB; 5LHI; X-ray; 3.40 A; A=1-852.
PDB; 5X60; X-ray; 2.69 A; A=172-833.
PDBsum; 2COM; -.
PDBsum; 2DW4; -.
PDBsum; 2EJR; -.
PDBsum; 2H94; -.
PDBsum; 2HKO; -.
PDBsum; 2IW5; -.
PDBsum; 2L3D; -.
PDBsum; 2UXN; -.
PDBsum; 2UXX; -.
PDBsum; 2V1D; -.
PDBsum; 2X0L; -.
PDBsum; 2XAF; -.
PDBsum; 2XAG; -.
PDBsum; 2XAH; -.
PDBsum; 2XAJ; -.
PDBsum; 2XAQ; -.
PDBsum; 2XAS; -.
PDBsum; 2Y48; -.
PDBsum; 2Z3Y; -.
PDBsum; 2Z5U; -.
PDBsum; 3ABT; -.
PDBsum; 3ABU; -.
PDBsum; 3ZMS; -.
PDBsum; 3ZMT; -.
PDBsum; 3ZMU; -.
PDBsum; 3ZMV; -.
PDBsum; 3ZMZ; -.
PDBsum; 3ZN0; -.
PDBsum; 3ZN1; -.
PDBsum; 4BAY; -.
PDBsum; 4CZZ; -.
PDBsum; 4KUM; -.
PDBsum; 4UV8; -.
PDBsum; 4UV9; -.
PDBsum; 4UVA; -.
PDBsum; 4UVB; -.
PDBsum; 4UVC; -.
PDBsum; 4UXN; -.
PDBsum; 4XBF; -.
PDBsum; 5AFW; -.
PDBsum; 5H6Q; -.
PDBsum; 5H6R; -.
PDBsum; 5IT3; -.
PDBsum; 5L3B; -.
PDBsum; 5L3C; -.
PDBsum; 5L3D; -.
PDBsum; 5L3E; -.
PDBsum; 5L3F; -.
PDBsum; 5L3G; -.
PDBsum; 5LBQ; -.
PDBsum; 5LGN; -.
PDBsum; 5LGT; -.
PDBsum; 5LGU; -.
PDBsum; 5LHG; -.
PDBsum; 5LHH; -.
PDBsum; 5LHI; -.
PDBsum; 5X60; -.
ProteinModelPortal; O60341; -.
SMR; O60341; -.
BioGrid; 116667; 315.
CORUM; O60341; -.
DIP; DIP-34641N; -.
IntAct; O60341; 281.
MINT; MINT-1372817; -.
STRING; 9606.ENSP00000383042; -.
BindingDB; O60341; -.
ChEMBL; CHEMBL6136; -.
GuidetoPHARMACOLOGY; 2669; -.
iPTMnet; O60341; -.
PhosphoSitePlus; O60341; -.
BioMuta; KDM1A; -.
EPD; O60341; -.
MaxQB; O60341; -.
PaxDb; O60341; -.
PeptideAtlas; O60341; -.
PRIDE; O60341; -.
Ensembl; ENST00000356634; ENSP00000349049; ENSG00000004487. [O60341-1]
Ensembl; ENST00000400181; ENSP00000383042; ENSG00000004487. [O60341-2]
GeneID; 23028; -.
KEGG; hsa:23028; -.
UCSC; uc001bgi.3; human. [O60341-1]
CTD; 23028; -.
DisGeNET; 23028; -.
EuPathDB; HostDB:ENSG00000004487.15; -.
GeneCards; KDM1A; -.
HGNC; HGNC:29079; KDM1A.
HPA; CAB005884; -.
HPA; HPA053660; -.
MalaCards; KDM1A; -.
MIM; 609132; gene.
MIM; 616728; phenotype.
neXtProt; NX_O60341; -.
OpenTargets; ENSG00000004487; -.
PharmGKB; PA165751392; -.
eggNOG; KOG0029; Eukaryota.
eggNOG; KOG0685; Eukaryota.
eggNOG; ENOG410XSNC; LUCA.
GeneTree; ENSGT00530000062888; -.
InParanoid; O60341; -.
KO; K11450; -.
OMA; TTVRNGY; -.
OrthoDB; EOG091G04NO; -.
PhylomeDB; O60341; -.
TreeFam; TF312972; -.
BRENDA; 1.14.11.B1; 2681.
BRENDA; 1.14.11.B2; 2681.
Reactome; R-HSA-3214815; HDACs deacetylate histones.
Reactome; R-HSA-3214842; HDMs demethylate histones.
Reactome; R-HSA-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
SABIO-RK; O60341; -.
SIGNOR; O60341; -.
ChiTaRS; KDM1A; human.
EvolutionaryTrace; O60341; -.
GenomeRNAi; 23028; -.
PRO; PR:O60341; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000004487; -.
CleanEx; HS_AOF2; -.
ExpressionAtlas; O60341; baseline and differential.
Genevisible; O60341; HS.
GO; GO:1990391; C:DNA repair complex; IDA:MGI.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:MGI.
GO; GO:0005667; C:transcription factor complex; ISS:UniProtKB.
GO; GO:0050681; F:androgen receptor binding; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0032451; F:demethylase activity; IMP:BHF-UCL.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
GO; GO:0004407; F:histone deacetylase activity; TAS:Reactome.
GO; GO:0032452; F:histone demethylase activity; IDA:BHF-UCL.
GO; GO:0034648; F:histone demethylase activity (H3-dimethyl-K4 specific); IDA:UniProtKB.
GO; GO:0032453; F:histone demethylase activity (H3-K4 specific); IDA:UniProtKB.
GO; GO:0032454; F:histone demethylase activity (H3-K9 specific); IDA:UniProtKB.
GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; IMP:UniProtKB.
GO; GO:0043426; F:MRF binding; IDA:BHF-UCL.
GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
GO; GO:0002039; F:p53 binding; IPI:BHF-UCL.
GO; GO:0042162; F:telomeric DNA binding; IMP:BHF-UCL.
GO; GO:0061752; F:telomeric repeat-containing RNA binding; IDA:BHF-UCL.
GO; GO:0008134; F:transcription factor binding; IDA:BHF-UCL.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISS:BHF-UCL.
GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IEA:Ensembl.
GO; GO:0007596; P:blood coagulation; TAS:Reactome.
GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
GO; GO:0071480; P:cellular response to gamma radiation; IMP:MGI.
GO; GO:0034644; P:cellular response to UV; IDA:MGI.
GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
GO; GO:0046098; P:guanine metabolic process; IEA:Ensembl.
GO; GO:0034720; P:histone H3-K4 demethylation; IDA:UniProtKB.
GO; GO:0033169; P:histone H3-K9 demethylation; IDA:UniProtKB.
GO; GO:0055001; P:muscle cell development; ISS:BHF-UCL.
GO; GO:0043392; P:negative regulation of DNA binding; IC:BHF-UCL.
GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IMP:BHF-UCL.
GO; GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:BHF-UCL.
GO; GO:0032091; P:negative regulation of protein binding; IMP:BHF-UCL.
GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IDA:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL.
GO; GO:0042551; P:neuron maturation; IEA:Ensembl.
GO; GO:0045793; P:positive regulation of cell size; IEA:Ensembl.
GO; GO:0035563; P:positive regulation of chromatin binding; IEA:Ensembl.
GO; GO:0033184; P:positive regulation of histone ubiquitination; IMP:MGI.
GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0006482; P:protein demethylation; IMP:BHF-UCL.
GO; GO:1903827; P:regulation of cellular protein localization; IMP:MGI.
GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; IMP:MGI.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0060992; P:response to fungicide; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.10.10.10; -; 1.
Gene3D; 3.50.50.60; -; 1.
InterPro; IPR002937; Amino_oxidase.
InterPro; IPR023753; FAD/NAD-binding_dom.
InterPro; IPR017366; Hist_Lys-spec_deMease.
InterPro; IPR009057; Homeobox-like.
InterPro; IPR007526; SWIRM.
InterPro; IPR011991; WHTH_DNA-bd_dom.
Pfam; PF01593; Amino_oxidase; 1.
Pfam; PF04433; SWIRM; 1.
PIRSF; PIRSF038051; Histone_Lys-demethylase; 1.
SUPFAM; SSF46689; SSF46689; 1.
SUPFAM; SSF51905; SSF51905; 3.
PROSITE; PS50934; SWIRM; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chromatin regulator; Coiled coil;
Complete proteome; Developmental protein; Direct protein sequencing;
Disease mutation; FAD; Flavoprotein; Isopeptide bond; Nucleus;
Oxidoreductase; Phosphoprotein; Reference proteome; Repressor;
Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 852 Lysine-specific histone demethylase 1A.
/FTId=PRO_0000099881.
DOMAIN 174 273 SWIRM. {ECO:0000255|PROSITE-
ProRule:PRU00247}.
NP_BIND 281 309 FAD. {ECO:0000255}.
NP_BIND 332 333 FAD. {ECO:0000269|PubMed:16885027,
ECO:0000269|PubMed:16956976}.
NP_BIND 810 811 FAD. {ECO:0000269|PubMed:16885027,
ECO:0000269|PubMed:16956976}.
REGION 300 852 Demethylase activity.
COILED 110 151 {ECO:0000255}.
COILED 428 514 {ECO:0000255}.
COMPBIAS 7 42 Ala-rich.
COMPBIAS 152 156 Poly-Pro.
BINDING 289 289 FAD. {ECO:0000269|PubMed:16885027,
ECO:0000269|PubMed:16956976}.
BINDING 308 308 FAD. {ECO:0000269|PubMed:16885027,
ECO:0000269|PubMed:16956976}.
BINDING 310 310 FAD. {ECO:0000269|PubMed:16885027,
ECO:0000269|PubMed:16956976}.
BINDING 316 316 FAD. {ECO:0000269|PubMed:16885027,
ECO:0000269|PubMed:16956976}.
BINDING 801 801 FAD. {ECO:0000269|PubMed:16885027,
ECO:0000269|PubMed:16956976}.
MOD_RES 59 59 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 104 104 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 126 126 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
MOD_RES 131 131 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 135 135 Phosphotyrosine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 137 137 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 166 166 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 611 611 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 849 849 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
CROSSLNK 442 442 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 469 469 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 503 503 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000305|PubMed:25018020}.
VAR_SEQ 173 173 G -> GQAGGLQDDSSGGYGDGQASG (in isoform
2). {ECO:0000303|PubMed:15489334}.
/FTId=VSP_011198.
VAR_SEQ 369 369 A -> ADTVK (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_011199.
VARIANT 379 379 E -> K (in CPRF; dbSNP:rs864309715).
{ECO:0000269|PubMed:26656649}.
/FTId=VAR_076366.
VARIANT 556 556 D -> G (in CPRF; dbSNP:rs864309716).
{ECO:0000269|PubMed:23020937,
ECO:0000269|PubMed:26656649}.
/FTId=VAR_076367.
VARIANT 761 761 Y -> H (in CPRF; dbSNP:rs864309714).
{ECO:0000269|PubMed:24838796,
ECO:0000269|PubMed:26656649}.
/FTId=VAR_076368.
MUTAGEN 503 503 K->R: Loss of polyubiquitination.
{ECO:0000269|PubMed:25018020}.
MUTAGEN 535 535 N->A: Strongly reduces demethylase
activity. {ECO:0000269|PubMed:16956976}.
MUTAGEN 564 564 H->A: Strongly reduces demethylase
activity. {ECO:0000269|PubMed:16956976}.
MUTAGEN 661 661 K->A: Abolishes histone demethylase
activity. {ECO:0000269|PubMed:16079794}.
MUTAGEN 761 761 Y->A: Strongly reduces demethylase
activity. {ECO:0000269|PubMed:16956976}.
CONFLICT 78 78 P -> Q (in Ref. 3; AAH40194).
{ECO:0000305}.
CONFLICT 405 405 P -> H (in Ref. 3; AAH48134).
{ECO:0000305}.
CONFLICT 669 669 V -> A (in Ref. 4; CAD38675).
{ECO:0000305}.
CONFLICT 814 814 A -> V (in Ref. 3; AAH16639).
{ECO:0000305}.
HELIX 173 180 {ECO:0000244|PDB:2Z3Y}.
STRAND 181 183 {ECO:0000244|PDB:2COM}.
STRAND 185 187 {ECO:0000244|PDB:2HKO}.
HELIX 190 195 {ECO:0000244|PDB:5IT3}.
HELIX 197 200 {ECO:0000244|PDB:5IT3}.
HELIX 204 223 {ECO:0000244|PDB:5IT3}.
HELIX 231 236 {ECO:0000244|PDB:5IT3}.
TURN 240 243 {ECO:0000244|PDB:5IT3}.
HELIX 246 258 {ECO:0000244|PDB:5IT3}.
STRAND 261 263 {ECO:0000244|PDB:5IT3}.
STRAND 265 267 {ECO:0000244|PDB:2COM}.
STRAND 280 284 {ECO:0000244|PDB:2Z3Y}.
HELIX 288 299 {ECO:0000244|PDB:2Z3Y}.
STRAND 303 307 {ECO:0000244|PDB:2Z3Y}.
STRAND 309 314 {ECO:0000244|PDB:2Z3Y}.
STRAND 319 322 {ECO:0000244|PDB:2Z3Y}.
STRAND 325 330 {ECO:0000244|PDB:2Z3Y}.
STRAND 333 335 {ECO:0000244|PDB:2H94}.
HELIX 341 349 {ECO:0000244|PDB:2Z3Y}.
STRAND 353 355 {ECO:0000244|PDB:2Z3Y}.
STRAND 362 366 {ECO:0000244|PDB:4BAY}.
STRAND 367 369 {ECO:0000244|PDB:5LHH}.
HELIX 372 393 {ECO:0000244|PDB:2Z3Y}.
TURN 394 396 {ECO:0000244|PDB:2HKO}.
STRAND 400 405 {ECO:0000244|PDB:5L3D}.
HELIX 408 456 {ECO:0000244|PDB:2Z3Y}.
TURN 457 461 {ECO:0000244|PDB:2Z3Y}.
HELIX 476 487 {ECO:0000244|PDB:2Z3Y}.
TURN 488 490 {ECO:0000244|PDB:2Z3Y}.
HELIX 491 497 {ECO:0000244|PDB:2Z3Y}.
HELIX 499 511 {ECO:0000244|PDB:2Z3Y}.
STRAND 518 521 {ECO:0000244|PDB:3ABU}.
HELIX 523 539 {ECO:0000244|PDB:2Z3Y}.
HELIX 544 546 {ECO:0000244|PDB:2Z3Y}.
TURN 549 555 {ECO:0000244|PDB:2Z3Y}.
HELIX 556 558 {ECO:0000244|PDB:2Z3Y}.
STRAND 565 567 {ECO:0000244|PDB:2Z3Y}.
HELIX 573 578 {ECO:0000244|PDB:2Z3Y}.
TURN 579 581 {ECO:0000244|PDB:2Z3Y}.
STRAND 583 585 {ECO:0000244|PDB:2Z3Y}.
STRAND 588 596 {ECO:0000244|PDB:2Z3Y}.
STRAND 599 608 {ECO:0000244|PDB:2Z3Y}.
STRAND 613 623 {ECO:0000244|PDB:2Z3Y}.
HELIX 627 631 {ECO:0000244|PDB:2Z3Y}.
STRAND 636 641 {ECO:0000244|PDB:2Z3Y}.
HELIX 645 653 {ECO:0000244|PDB:2Z3Y}.
STRAND 654 656 {ECO:0000244|PDB:2Z3Y}.
STRAND 660 665 {ECO:0000244|PDB:2Z3Y}.
STRAND 676 680 {ECO:0000244|PDB:2Z3Y}.
STRAND 683 685 {ECO:0000244|PDB:2Z3Y}.
TURN 686 689 {ECO:0000244|PDB:2Z3Y}.
STRAND 690 695 {ECO:0000244|PDB:2Z3Y}.
STRAND 698 707 {ECO:0000244|PDB:2Z3Y}.
HELIX 710 715 {ECO:0000244|PDB:2Z3Y}.
HELIX 720 735 {ECO:0000244|PDB:2Z3Y}.
TURN 737 739 {ECO:0000244|PDB:2DW4}.
STRAND 744 748 {ECO:0000244|PDB:2Z3Y}.
TURN 751 753 {ECO:0000244|PDB:2Z3Y}.
TURN 755 757 {ECO:0000244|PDB:2Z3Y}.
STRAND 758 760 {ECO:0000244|PDB:2Z3Y}.
HELIX 771 777 {ECO:0000244|PDB:2Z3Y}.
STRAND 796 798 {ECO:0000244|PDB:2Z3Y}.
HELIX 801 803 {ECO:0000244|PDB:2Z3Y}.
STRAND 805 807 {ECO:0000244|PDB:2UXX}.
HELIX 811 829 {ECO:0000244|PDB:2Z3Y}.
HELIX 833 835 {ECO:0000244|PDB:5L3D}.
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


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