KDM1A_MOUSE
ID KDM1A_MOUSE Reviewed; 853 AA.
AC Q6ZQ88; A3KG94; Q6PB53; Q8VEA1;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Lysine-specific histone demethylase 1A {ECO:0000305};
DE EC=1.14.99.66 {ECO:0000250|UniProtKB:O60341};
DE AltName: Full=BRAF35-HDAC complex protein BHC110;
DE AltName: Full=Flavin-containing amine oxidase domain-containing protein 2;
GN Name=Kdm1a {ECO:0000312|MGI:MGI:1196256}; Synonyms=Aof2, Kiaa0601, Lsd1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Mammary gland;
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 TISSUE SPECIFICITY.
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY AS A COMPONENT OF A GFI-RCOR-KDM1A-HDAC
RP COMPLEX, INTERACTION WITH GFI1 AND GFI1B, AND FUNCTION.
RX PubMed=17707228; DOI=10.1016/j.molcel.2007.06.039;
RA Saleque S., Kim J., Rooke H.M., Orkin S.H.;
RT "Epigenetic regulation of hematopoietic differentiation by Gfi-1 and Gfi-1b
RT is mediated by the cofactors CoREST and LSD1.";
RL Mol. Cell 27:562-572(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=19098913; DOI=10.1038/ng.268;
RA Wang J., Hevi S., Kurash J.K., Lei H., Gay F., Bajko J., Su H., Sun W.,
RA Chang H., Xu G., Gaudet F., Li E., Chen T.;
RT "The lysine demethylase LSD1 (KDM1) is required for maintenance of global
RT DNA methylation.";
RL Nat. Genet. 41:125-129(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-138, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP INTERACTION WITH INSM1.
RX PubMed=24227653; DOI=10.1242/dev.097642;
RA Welcker J.E., Hernandez-Miranda L.R., Paul F.E., Jia S., Ivanov A.,
RA Selbach M., Birchmeier C.;
RT "Insm1 controls development of pituitary endocrine cells and requires a
RT SNAG domain for function and for recruitment of histone-modifying
RT factors.";
RL Development 140:4947-4958(2013).
RN [10]
RP INTERACTION WITH JADE2, INDUCTION, UBIQUITINATION, AND DISRUPTION
RP PHENOTYPE.
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 [11]
RP INTERACTION WITH ESRRB.
RX PubMed=26206133; DOI=10.1038/ncomms8776;
RA Latos P.A., Goncalves A., Oxley D., Mohammed H., Turro E., Hemberger M.;
RT "Fgf and Esrrb integrate epigenetic and transcriptional networks that
RT regulate self-renewal of trophoblast stem cells.";
RL Nat. Commun. 6:7776-7776(2015).
RN [12]
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).
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. Acts by
CC oxidizing the substrate by FAD to generate the corresponding imine that
CC is subsequently hydrolyzed. Acts as a corepressor by mediating
CC demethylation of H3K4me, a specific tag for epigenetic transcriptional
CC activation. Demethylates both mono- (H3K4me1) and di-methylated
CC (H3K4me2) H3K4me. May play a role in the repression of neuronal genes.
CC Alone, it is unable to demethylate H3K4me on nucleosomes and requires
CC the presence of RCOR1/CoREST to achieve such activity. Also acts as a
CC coactivator of androgen receptor (ANDR)-dependent transcription, by
CC being recruited to ANDR target genes and mediating demethylation of
CC H3K9me, a specific tag for epigenetic transcriptional repression. The
CC presence of PRKCB in ANDR-containing complexes, which mediates
CC phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag that
CC prevents demethylation H3K4me, prevents H3K4me demethylase activity of
CC KDM1A. Demethylates di-methylated 'Lys-370' of p53/TP53 which prevents
CC interaction of p53/TP53 with TP53BP1 and represses p53/TP53-mediated
CC transcriptional activation (By similarity). Demethylates and stabilizes
CC the DNA methylase DNMT1. Required for gastrulation during
CC embryogenesis. Component of a RCOR/GFI/KDM1A/HDAC complex that
CC suppresses, via histone deacetylase (HDAC) recruitment, a number of
CC genes implicated in multilineage blood cell development. Effector of
CC SNAI1-mediated transcription repression of E-cadherin/CDH1, CDN7 and
CC KRT8. Required for the maintenance of the silenced state of the SNAI1
CC target genes E-cadherin/CDH1 and CDN7. {ECO:0000250|UniProtKB:O60341,
CC ECO:0000269|PubMed:17707228, ECO:0000269|PubMed:19098913}.
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:0000250|UniProtKB:O60341};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:O60341};
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:0000250|UniProtKB:O60341}.
CC -!- SUBUNIT: Component of a histone demethylase complex with RCOR1 (By
CC similarity). Component of a BHC histone deacetylase complex that
CC contains HDAC1, HDAC2, HMG20B, KDM1A, RCOR1 and PHF21A. The BHC complex
CC may also contain ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. In the complex,
CC RCOR1 strongly enhances the demethylase activity and protects it from
CC the proteasome while PHF21A inhibits the demethylase activity.
CC Interacts with the androgen receptor (AR) (By similarity). Component of
CC a RCOR/GFI/KDM1A/HDAC complex. Interacts directly with GFI1 and GFI1B
CC (PubMed:17707228). Interacts with SNAI1 (via SNAG domain) (By
CC similarity). Interacts with INSM1 (PubMed:24227653). Interacts (via
CC AOD/Tower domain) with JADE2 (via C-terminus) (PubMed:25018020).
CC Interacts with ESRRB; co-occupes the core set of ESRRB targets
CC (PubMed:26206133). Interacts with SAMD1 (via WH domain); the
CC interaction modulates KDM1A function (PubMed:33980486).
CC {ECO:0000250|UniProtKB:O60341, ECO:0000269|PubMed:17707228,
CC ECO:0000269|PubMed:24227653, ECO:0000269|PubMed:25018020,
CC ECO:0000269|PubMed:26206133, ECO:0000269|PubMed:33980486}.
CC -!- INTERACTION:
CC Q6ZQ88; P53566: Cebpa; NbExp=4; IntAct=EBI-1216284, EBI-2644207;
CC Q6ZQ88; O09106: Hdac1; NbExp=7; IntAct=EBI-1216284, EBI-301912;
CC Q6ZQ88; P70288: Hdac2; NbExp=4; IntAct=EBI-1216284, EBI-302251;
CC Q6ZQ88; Q8CFE3: Rcor1; NbExp=2; IntAct=EBI-1216284, EBI-2337309;
CC Q6ZQ88; Q9CQJ4: Rnf2; NbExp=3; IntAct=EBI-1216284, EBI-927321;
CC Q6ZQ88; O35615: Zfpm1; NbExp=2; IntAct=EBI-1216284, EBI-4394596;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:33980486}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:16079795}.
CC -!- DEVELOPMENTAL STAGE: Zygotic expression first appears at the morula
CC stage. In blastocysts, expressed in the inner cell mass and
CC trophectodermal cells. In postimplantation embryos, expression becomes
CC ubiquitous. {ECO:0000269|PubMed:19098913}.
CC -!- INDUCTION: Down-regulated during neural differentiation.
CC {ECO:0000269|PubMed:25018020}.
CC -!- DOMAIN: The SWIRM domain may act as an anchor site for a histone tail.
CC {ECO:0000250}.
CC -!- PTM: Polyubiquitinated by JADE2; which leads to its proteasomal
CC degradation. {ECO:0000269|PubMed:25018020}.
CC -!- DISRUPTION PHENOTYPE: Promotes neural differentiation. Accelerated
CC emergence of neural progenitors and mature neurons in differentiating
CC embryonic stem cells. {ECO:0000269|PubMed:25018020}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH59885.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC97980.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK129170; BAC97980.1; ALT_INIT; mRNA.
DR EMBL; AL671173; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019417; AAH19417.1; -; mRNA.
DR EMBL; BC059885; AAH59885.1; ALT_INIT; mRNA.
DR CCDS; CCDS51331.1; -.
DR RefSeq; NP_598633.2; NM_133872.2.
DR AlphaFoldDB; Q6ZQ88; -.
DR BMRB; Q6ZQ88; -.
DR SMR; Q6ZQ88; -.
DR BioGRID; 221360; 77.
DR CORUM; Q6ZQ88; -.
DR DIP; DIP-38599N; -.
DR IntAct; Q6ZQ88; 22.
DR MINT; Q6ZQ88; -.
DR STRING; 10090.ENSMUSP00000111977; -.
DR ChEMBL; CHEMBL4295874; -.
DR iPTMnet; Q6ZQ88; -.
DR PhosphoSitePlus; Q6ZQ88; -.
DR EPD; Q6ZQ88; -.
DR jPOST; Q6ZQ88; -.
DR MaxQB; Q6ZQ88; -.
DR PaxDb; Q6ZQ88; -.
DR PeptideAtlas; Q6ZQ88; -.
DR PRIDE; Q6ZQ88; -.
DR ProteomicsDB; 264984; -.
DR Antibodypedia; 3136; 710 antibodies from 47 providers.
DR DNASU; 99982; -.
DR Ensembl; ENSMUST00000116273; ENSMUSP00000111977; ENSMUSG00000036940.
DR GeneID; 99982; -.
DR KEGG; mmu:99982; -.
DR UCSC; uc008vig.2; mouse.
DR CTD; 23028; -.
DR MGI; MGI:1196256; Kdm1a.
DR VEuPathDB; HostDB:ENSMUSG00000036940; -.
DR eggNOG; KOG0029; Eukaryota.
DR eggNOG; KOG0685; Eukaryota.
DR GeneTree; ENSGT00940000157193; -.
DR InParanoid; Q6ZQ88; -.
DR OrthoDB; 1034142at2759; -.
DR PhylomeDB; Q6ZQ88; -.
DR TreeFam; TF312972; -.
DR BRENDA; 1.14.11.65; 3474.
DR BRENDA; 1.14.99.66; 3474.
DR Reactome; R-MMU-3214815; HDACs deacetylate histones.
DR Reactome; R-MMU-3214842; HDMs demethylate histones.
DR Reactome; R-MMU-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR BioGRID-ORCS; 99982; 18 hits in 123 CRISPR screens.
DR ChiTaRS; Kdm1a; mouse.
DR PRO; PR:Q6ZQ88; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q6ZQ88; protein.
DR Bgee; ENSMUSG00000036940; Expressed in urethra and 295 other tissues.
DR ExpressionAtlas; Q6ZQ88; baseline and differential.
DR Genevisible; Q6ZQ88; MM.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:MGI.
DR GO; GO:1990391; C:DNA repair complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0032451; F:demethylase activity; ISO:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; ISS:UniProtKB.
DR GO; GO:0032452; F:histone demethylase activity; ISS:BHF-UCL.
DR GO; GO:0140682; F:histone H3-di/monomethyl-lysine-4 FAD-dependent demethylase activity; IDA:MGI.
DR GO; GO:0032453; F:histone H3-methyl-lysine-4 demethylase activity; ISS:UniProtKB.
DR GO; GO:0032454; F:histone H3-methyl-lysine-9 demethylase activity; ISS:UniProtKB.
DR GO; GO:0106222; F:lncRNA binding; IDA:MGI.
DR GO; GO:0043426; F:MRF binding; IPI:BHF-UCL.
DR GO; GO:0050681; F:nuclear androgen receptor binding; ISS:UniProtKB.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISS:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; ISS:UniProtKB.
DR GO; GO:0002039; F:p53 binding; ISO:MGI.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:BHF-UCL.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0061752; F:telomeric repeat-containing RNA binding; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IMP:MGI.
DR GO; GO:0071480; P:cellular response to gamma radiation; ISO:MGI.
DR GO; GO:0034644; P:cellular response to UV; ISO:MGI.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0030851; P:granulocyte differentiation; IMP:UniProtKB.
DR GO; GO:0034720; P:histone H3-K4 demethylation; IDA:MGI.
DR GO; GO:0033169; P:histone H3-K9 demethylation; IMP:BHF-UCL.
DR GO; GO:0055001; P:muscle cell development; IMP:BHF-UCL.
DR GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; ISO:MGI.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISS:BHF-UCL.
DR GO; GO:0051572; P:negative regulation of histone H3-K4 methylation; IMP:BHF-UCL.
DR GO; GO:0051573; P:negative regulation of histone H3-K9 methylation; IMP:BHF-UCL.
DR GO; GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; ISO:MGI.
DR GO; GO:0050768; P:negative regulation of neurogenesis; IDA:MGI.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:BHF-UCL.
DR GO; GO:1990138; P:neuron projection extension; IMP:MGI.
DR GO; GO:0021983; P:pituitary gland development; IMP:MGI.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0033184; P:positive regulation of histone ubiquitination; ISO:MGI.
DR GO; GO:0045654; P:positive regulation of megakaryocyte differentiation; IMP:UniProtKB.
DR GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; IMP:BHF-UCL.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; ISO:MGI.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IMP:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0006482; P:protein demethylation; ISO:MGI.
DR GO; GO:0090308; P:regulation of DNA methylation-dependent heterochromatin assembly; ISS:UniProtKB.
DR GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; ISO:MGI.
DR GO; GO:0050767; P:regulation of neurogenesis; IGI:MGI.
DR GO; GO:0010725; P:regulation of primitive erythrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:MGI.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR017366; Hist_Lys-spec_deMease.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR007526; SWIRM.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF01593; Amino_oxidase; 1.
DR Pfam; PF04433; SWIRM; 1.
DR PIRSF; PIRSF038051; Histone_Lys-demethylase; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS50934; SWIRM; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Coiled coil; Developmental protein; FAD; Flavoprotein;
KW Isopeptide bond; Nucleus; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..853
FT /note="Lysine-specific histone demethylase 1A"
FT /id="PRO_0000099882"
FT DOMAIN 175..274
FT /note="SWIRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00247"
FT REGION 1..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..853
FT /note="Demethylase activity"
FT /evidence="ECO:0000250"
FT COILED 111..152
FT /evidence="ECO:0000255"
FT COILED 429..515
FT /evidence="ECO:0000255"
FT COMPBIAS 106..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 290
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O60341"
FT BINDING 309
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O60341"
FT BINDING 311
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O60341"
FT BINDING 317
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O60341"
FT BINDING 333..334
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O60341"
FT BINDING 802
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O60341"
FT BINDING 811..812
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O60341"
FT MOD_RES 60
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60341"
FT MOD_RES 105
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60341"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60341"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 136
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O60341"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 612
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60341"
FT MOD_RES 850
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60341"
FT CROSSLNK 443
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60341"
FT CROSSLNK 470
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60341"
FT CROSSLNK 504
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O60341"
FT CONFLICT 226
FT /note="P -> S (in Ref. 3; AAH59885)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 853 AA; 92851 MW; 43CD401FA0452B2F CRC64;
MLSGKKAAAA AAAAAAAAAA GTEAGSGAAG GAENGSEVAA PPAGLTGPTD MATGAAGERT
PRKKEPPRAS PPGGLAEPPG SAGPQAGPTA GPGSATPMET GIAETPEGRR TSRRKRAKVE
YREMDESLAN LSEDEYYSEE ERNAKAEKEK KLPPPPPQAP PEEENESEPE EPSGVEGAAF
QSRLPHDRMT SQEAACFPDI ISGPQQTQKV FLFIRNRTLQ LWLDNPKIQL TFEATLQQLE
APYNSDTVLV HRVHSYLERH GLINFGIYKR IKPLPIKKTG KVIIIGSGVS GLAAARQLQS
FGMDVTLLEA RDRVGGRVAT FRKGNYVADL GAMVVTGLGG NPMAVVSKQV NMELAKIKQK
CPLYEANGQA VPKEKDEMVE QEFNRLLEAT SYLSHQLDFN VLNNKPVSLG QALEVVIQLQ
EKHVKDEQIE HWKKIVKTQE ELKELLNKMV NLKEKIKELH QQYKEASEVK PPRDITAEFL
VKSKHRDLTA LCKEYDELAE TQGKLEEKLQ ELEANPPSDV YLSSRDRQIL DWHFANLEFA
NATPLSTLSL KHWDQDDDFE FTGSHLTVRN GYSCVPVALA EGLDIKLNTA VRQVRYTASG
CEVIAVNTRS TSQTFIYKCD AVLCTLPLGV LKQQPPAVQF VPPLPEWKTS AVQRMGFGNL
NKVVLCFDRV FWDPSVNLFG HVGSTTASRG ELFLFWNLYK APILLALVAG EAAGIMENIS
DDVIVGRCLA ILKGIFGSSA VPQPKETVVS RWRADPWARG SYSYVAAGSS GNDYDLMAQP
ITPGPSIPGA PQPIPRLFFA GEHTIRNYPA TVHGALLSGL REAGRIADQF LGAMYTLPRQ
ATPGVPAQQS PSM
