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 27-MAR-2024, entry version 177. 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}; GN 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, RC Pancreas, 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 (By similarity). Demethylates methylated 'Lys- CC 44' and methylated 'Lys-119' of SOX2 (By similarity). Required for CC gastrulation during embryogenesis. Component of a RCOR/GFI/KDM1A/HDAC CC complex that suppresses, via histone deacetylase (HDAC) recruitment, a CC number of genes implicated in multilineage blood cell development. CC Effector of SNAI1-mediated transcription repression of E-cadherin/CDH1, CC CDN7 and KRT8. Required for the maintenance of the silenced state of CC the SNAI1 target genes E-cadherin/CDH1 and CDN7. CC {ECO:0000250|UniProtKB:O60341, ECO:0000269|PubMed:17707228, CC 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). Interacts with CC RBPJ (By similarity). Interacts with L3MBTL3 (By similarity). Interacts CC with ZMYND8 (By similarity). {ECO:0000250|UniProtKB:O60341, CC ECO:0000269|PubMed:17707228, ECO:0000269|PubMed:24227653, CC ECO:0000269|PubMed:25018020, ECO:0000269|PubMed:26206133, CC 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. Deubiquitinated by USP38; preventing it from degradation CC by the 26S proteasome (By similarity). {ECO:0000250|UniProtKB:O60341, CC 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}; 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; 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; 218. DR CORUM; Q6ZQ88; -. DR DIP; DIP-38599N; -. DR IntAct; Q6ZQ88; 23. DR MINT; Q6ZQ88; -. DR STRING; 10090.ENSMUSP00000101473; -. DR ChEMBL; CHEMBL4295874; -. DR iPTMnet; Q6ZQ88; -. DR PhosphoSitePlus; Q6ZQ88; -. DR EPD; Q6ZQ88; -. DR jPOST; Q6ZQ88; -. DR MaxQB; Q6ZQ88; -. DR PaxDb; 10090-ENSMUSP00000111977; -. DR PeptideAtlas; Q6ZQ88; -. DR ProteomicsDB; 264984; -. DR Pumba; Q6ZQ88; -. DR Antibodypedia; 3136; 843 antibodies from 47 providers. DR DNASU; 99982; -. DR Ensembl; ENSMUST00000116273.9; ENSMUSP00000111977.3; ENSMUSG00000036940.16. DR GeneID; 99982; -. DR KEGG; mmu:99982; -. DR UCSC; uc008vig.2; mouse. DR AGR; MGI:1196256; -. 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; 5402444at2759; -. 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-9018519; Estrogen-dependent gene expression. DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production. DR BioGRID-ORCS; 99982; 19 hits in 129 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 298 other cell types or tissues. DR ExpressionAtlas; Q6ZQ88; baseline and differential. 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:0140682; F:FAD-dependent H3K4me/H3K4me3 demethylase activity; IDA:MGI. 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:0032453; F:histone H3K4 demethylase activity; IMP:MGI. DR GO; GO:0032454; F:histone H3K9 demethylase activity; ISS:UniProtKB. DR GO; GO:0140684; F:histone H3K9me2/H3K9me3 demethylase activity; IMP:BHF-UCL. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. 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:0003713; F:transcription coactivator activity; IMP:BHF-UCL. DR GO; GO:0003714; F:transcription corepressor activity; IDA:GO_Central. 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:0140861; P:DNA repair-dependent chromatin remodeling; IDA:MGI. DR GO; GO:0030851; P:granulocyte differentiation; IMP:UniProtKB. DR GO; GO:0046098; P:guanine metabolic process; ISO:MGI. 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:0045892; P:negative regulation of DNA-templated transcription; ISS: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:0000122; P:negative regulation of transcription by RNA polymerase II; IDA: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:0045793; P:positive regulation of cell size; ISO:MGI. DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab. DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IMP:UniProtKB. 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:0010976; P:positive regulation of neuron projection development; ISO:MGI. DR GO; GO:0031398; P:positive regulation of protein ubiquitination; 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:BHF-UCL. DR GO; GO:0036211; P:protein modification process; ISO:MGI. DR GO; GO:0090308; P:regulation of DNA methylation-dependent heterochromatin formation; 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; 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 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; Q6ZQ88; MM. 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 //