ID KDM2A_HUMAN Reviewed; 1162 AA. AC Q9Y2K7; D4QA03; E9PIL6; I3VM55; Q49A21; Q4G0M3; Q69YY8; Q9BVH5; Q9H7H5; AC Q9UK66; DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 07-NOV-2003, sequence version 3. DT 27-MAR-2024, entry version 205. DE RecName: Full=Lysine-specific demethylase 2A; DE EC=1.14.11.27 {ECO:0000269|PubMed:16362057}; DE AltName: Full=CXXC-type zinc finger protein 8; DE AltName: Full=F-box and leucine-rich repeat protein 11; DE AltName: Full=F-box protein FBL7; DE AltName: Full=F-box protein Lilina; DE AltName: Full=F-box/LRR-repeat protein 11; DE AltName: Full=JmjC domain-containing histone demethylation protein 1A; DE AltName: Full=[Histone-H3]-lysine-36 demethylase 1A; GN Name=KDM2A; GN Synonyms=CXXC8, FBL11 {ECO:0000303|PubMed:30033217}, FBL7, FBXL11, GN JHDM1A, KIAA1004; 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 [MRNA] (ISOFORM 1). RX PubMed=10945468; DOI=10.1006/geno.2000.6211; RA Ilyin G.P., Rialland M., Pigeon C., Guguen-Guillouzo C.; RT "cDNA cloning and expression analysis of new members of the mammalian F-box RT protein family."; RL Genomics 67:40-47(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5). RA Tsuneoka M., Tanaka Y., Okamoto K., Teye K.; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4). RA Iuchi S., Green H.; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RC TISSUE=Brain; RX PubMed=10231032; DOI=10.1093/dnares/6.1.63; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XIII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 6:63-70(1999). RN [5] RP SEQUENCE REVISION. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Spleen; RX PubMed=11214971; DOI=10.1093/dnares/7.6.357; RA Hattori A., Okumura K., Nagase T., Kikuno R., Hirosawa M., Ohara O.; RT "Characterization of long cDNA clones from human adult spleen."; RL DNA Res. 7:357-366(2000). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). RC TISSUE=Eye, Testis, and Uterus; 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 [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 667-1162. RA Pagano M.; RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1134-1162. RC TISSUE=Testis; 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, 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 [12] RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, RP COFACTOR, DOMAIN JMJC, AND MUTAGENESIS OF HIS-212. RX PubMed=16362057; DOI=10.1038/nature04433; RA Tsukada Y., Fang J., Erdjument-Bromage H., Warren M.E., Borchers C.H., RA Tempst P., Zhang Y.; RT "Histone demethylation by a family of JmjC domain-containing proteins."; RL Nature 439:811-816(2006). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-632, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [14] RP FUNCTION, INTERACTION WITH CBX5, SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP CYS-571; CYS-574 AND CYS-577. RX PubMed=19001877; DOI=10.4161/cc.7.22.7062; RA Frescas D., Guardavaccaro D., Kuchay S.M., Kato H., Poleshko A., Basrur V., RA Elenitoba-Johnson K.S., Katz R.A., Pagano M.; RT "KDM2A represses transcription of centromeric satellite repeats and RT maintains the heterochromatic state."; RL Cell Cycle 7:3539-3547(2008). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-550; SER-558; THR-713 AND RP SER-731, AND IDENTIFICATION BY 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 [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-692, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=T-cell; RX PubMed=19367720; DOI=10.1021/pr800500r; RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; RT "Phosphorylation analysis of primary human T lymphocytes using sequential RT IMAC and titanium oxide enrichment."; RL J. Proteome Res. 7:5167-5176(2008). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390; THR-550; SER-558; RP THR-713; SER-731 AND SER-832, 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; THR-550; SER-692 AND RP SER-869, AND 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 [19] RP SUBCELLULAR LOCATION, AND DOMAIN CXXC ZINC-FINGER. RX PubMed=20417597; DOI=10.1016/j.molcel.2010.04.009; RA Blackledge N.P., Zhou J.C., Tolstorukov M.Y., Farcas A.M., Park P.J., RA Klose R.J.; RT "CpG islands recruit a histone H3 lysine 36 demethylase."; RL Mol. Cell 38:179-190(2010). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-394; THR-550; RP SER-558; SER-869 AND SER-883, AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, AND IDENTIFICATION BY RP 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 [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; THR-550; SER-558; RP SER-692; SER-825; SER-832 AND SER-869, AND IDENTIFICATION BY MASS RP 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 [23] RP 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 [24] RP FUNCTION, MUTAGENESIS OF HIS-212; CYS-574; CYS-577; CYS-620 AND CYS-623, RP AND DOMAIN CXXC-TYPE ZINC-FINGER. RX PubMed=26037310; DOI=10.1177/0748730415587407; RA Reischl S., Kramer A.; RT "Fbxl11 Is a novel negative element of the mammalian circadian clock."; RL J. Biol. Rhythms 30:291-301(2015). RN [25] RP FUNCTION, AND MUTAGENESIS OF 212-HIS--ASP-214. RX PubMed=28262558; DOI=10.1016/j.chembiol.2017.02.006; RA Tumber A., Nuzzi A., Hookway E.S., Hatch S.B., Velupillai S., Johansson C., RA Kawamura A., Savitsky P., Yapp C., Szykowska A., Wu N., Bountra C., RA Strain-Damerell C., Burgess-Brown N.A., Ruda G.F., Fedorov O., Munro S., RA England K.S., Nowak R.P., Schofield C.J., La Thangue N.B., Pawlyn C., RA Davies F., Morgan G., Athanasou N., Muller S., Oppermann U., Brennan P.E.; RT "Potent and Selective KDM5 Inhibitor Stops Cellular Demethylation of RT H3K4me3 at Transcription Start Sites and Proliferation of MM1S Myeloma RT Cells."; RL Cell Chem. Biol. 24:371-380(2017). RN [26] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-505, AND IDENTIFICATION BY MASS RP 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 [27] {ECO:0007744|PDB:2YU1, ECO:0007744|PDB:2YU2} RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 1-517 IN COMPLEX WITH IRON. RA Han Z., Liu P., Gu L., Zhang Y., Li H., Chen S., Chai J.; RT "Structural basis for histone demethylation by JHDM1."; RL Submitted (APR-2007) to the PDB data bank. RN [28] {ECO:0007744|PDB:4BBQ} RP X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS) OF 567-681 IN COMPLEX WITH ZINC, AND RP ZINC-BINDING. RA Allerston C.K., Watson A.A., Edlich C., Li B., Chen Y., Ball L., Krojer T., RA Arrowsmith C.H., Edwards A., Bountra C., von Delft F., Laue E.D., RA Gileadi O.; RT "Crystal Structure of the Cxxc and Phd Domain of Human Lysine-Specific RT Demethylase 2A (Kdm2A)(Fbxl11)."; RL Submitted (SEP-2012) to the PDB data bank. RN [29] {ECO:0007744|PDB:6BYH, ECO:0007744|PDB:6C16} RP X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 888-932 IN COMPLEX WITH SKP1 AND RP UBB, INTERACTION OF SKP1-KDM2A COMPLEX WITH UBB, AND MUTAGENESIS OF RP TRP-892. RX PubMed=30033217; DOI=10.1016/j.str.2018.06.004; RA Gorelik M., Manczyk N., Pavlenco A., Kurinov I., Sidhu S.S., Sicheri F.; RT "A Structure-Based Strategy for Engineering Selective Ubiquitin Variant RT Inhibitors of Skp1-Cul1-F-Box Ubiquitin Ligases."; RL Structure 26:1226-1236.E3(2018). CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-36' CC of histone H3, thereby playing a central role in histone code. CC Preferentially demethylates dimethylated H3 'Lys-36' residue while it CC has weak or no activity for mono- and tri-methylated H3 'Lys-36'. May CC also recognize and bind to some phosphorylated proteins and promote CC their ubiquitination and degradation. Required to maintain the CC heterochromatic state. Associates with centromeres and represses CC transcription of small non-coding RNAs that are encoded by the clusters CC of satellite repeats at the centromere. Required to sustain centromeric CC integrity and genomic stability, particularly during mitosis. Regulates CC circadian gene expression by repressing the transcriptional activator CC activity of CLOCK-BMAL1 heterodimer and RORA in a catalytically- CC independent manner (PubMed:26037310). {ECO:0000269|PubMed:16362057, CC ECO:0000269|PubMed:19001877, ECO:0000269|PubMed:26037310, CC ECO:0000269|PubMed:28262558}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3] CC + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(36)-[histone H3] + 2 CC succinate; Xref=Rhea:RHEA:42032, Rhea:RHEA-COMP:9785, Rhea:RHEA- CC COMP:9787, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, CC ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031, CC ChEBI:CHEBI:61976; EC=1.14.11.27; CC Evidence={ECO:0000269|PubMed:16362057}; CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Evidence={ECO:0000269|PubMed:16362057}; CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269|PubMed:16362057}; CC -!- SUBUNIT: Interacts with CBX5/HP1A; the interaction promotes CBX5 CC localization to chromatin (PubMed:19001877). The SKP1-KDM2A complex CC interacts with UBB (PubMed:30033217). Part of a SCF (SKP1-cullin-F-box) CC protein ligase complex (PubMed:30033217). {ECO:0000269|PubMed:19001877, CC ECO:0000269|PubMed:30033217}. CC -!- INTERACTION: CC Q9Y2K7; Q04206: RELA; NbExp=2; IntAct=EBI-765758, EBI-73886; CC Q9Y2K7; P63208: SKP1; NbExp=3; IntAct=EBI-765758, EBI-307486; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm CC {ECO:0000269|PubMed:19001877, ECO:0000269|PubMed:20417597}. Chromosome CC {ECO:0000269|PubMed:19001877, ECO:0000269|PubMed:20417597}. CC Note=Punctate expression throughout the nucleoplasm and enriched in the CC perinucleolar region (PubMed:19001877, PubMed:20417597). Specifically CC nucleates at CpG islands where it's presence results in chromatin CC depleted in H3K36me2 (PubMed:19001877, PubMed:20417597). CC {ECO:0000269|PubMed:19001877, ECO:0000269|PubMed:20417597}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=Q9Y2K7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9Y2K7-2; Sequence=VSP_017468; CC Name=4; CC IsoId=Q9Y2K7-4; Sequence=VSP_046938; CC Name=5; CC IsoId=Q9Y2K7-5; Sequence=VSP_046939, VSP_046940; CC Name=3; CC IsoId=Q9Y2K7-3; Sequence=VSP_017469, VSP_017470; CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in brain, CC testis and ovary, followed by lung. {ECO:0000269|PubMed:10231032}. CC -!- DOMAIN: The JmjC domain mediates demethylation activity and is required CC for satellite silencing. {ECO:0000269|PubMed:16362057}. CC -!- DOMAIN: The CXXC zinc finger preferentially recognizes nonmethylated CC CpG DNA, and binding is blocked when the CpG DNA is methylated CC (PubMed:20417597). It is essential for its ability to repress the CC transcriptional activator activity of CLOCK-BMAL1 heterodimer CC (PubMed:26037310). {ECO:0000269|PubMed:20417597, CC ECO:0000269|PubMed:26037310}. CC -!- DOMAIN: The F-box domain mediates interaction with UBB. CC {ECO:0000269|PubMed:30033217}. CC -!- PTM: Mono-ADP-ribosylated at Arg-1020 in response to DNA damage, CC leading to displacement from chromatin, resulting in increased CC dimethylation of histone H3 at 'Lys-36'. CC {ECO:0000250|UniProtKB:P59997}. CC -!- SIMILARITY: Belongs to the JHDM1 histone demethylase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD56012.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAA76848.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB15795.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BAJ05817.1; Type=Erroneous initiation; Note=Truncated 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; AB023221; BAA76848.2; ALT_INIT; mRNA. DR EMBL; AB490246; BAJ05817.1; ALT_INIT; mRNA. DR EMBL; JQ710743; AFK81542.1; -; mRNA. DR EMBL; JQ710744; AFK81543.1; -; mRNA. DR EMBL; AK024505; BAB15795.1; ALT_FRAME; mRNA. DR EMBL; AP000729; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP001885; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC001203; AAH01203.1; -; mRNA. DR EMBL; BC047371; AAH47371.1; -; mRNA. DR EMBL; BC047486; AAH47486.1; -; mRNA. DR EMBL; BC064360; AAH64360.1; -; mRNA. DR EMBL; AF179221; AAD56012.1; ALT_INIT; mRNA. DR EMBL; AL117517; CAH10721.1; -; mRNA. DR CCDS; CCDS44657.1; -. [Q9Y2K7-1] DR CCDS; CCDS58148.1; -. [Q9Y2K7-5] DR RefSeq; NP_001243334.1; NM_001256405.1. [Q9Y2K7-5] DR RefSeq; NP_036440.1; NM_012308.2. [Q9Y2K7-1] DR RefSeq; XP_011543163.1; XM_011544861.1. [Q9Y2K7-2] DR PDB; 2YU1; X-ray; 2.70 A; A=1-517. DR PDB; 2YU2; X-ray; 2.70 A; A=1-517. DR PDB; 4BBQ; X-ray; 2.24 A; A/B=567-681. DR PDB; 6BYH; X-ray; 2.61 A; E/F/I=888-932. DR PDB; 6C16; X-ray; 3.27 A; C/F=888-932. DR PDB; 7UV9; EM; 3.20 A; K=2-685. DR PDBsum; 2YU1; -. DR PDBsum; 2YU2; -. DR PDBsum; 4BBQ; -. DR PDBsum; 6BYH; -. DR PDBsum; 6C16; -. DR PDBsum; 7UV9; -. DR AlphaFoldDB; Q9Y2K7; -. DR EMDB; EMD-26809; -. DR EMDB; EMD-26810; -. DR SMR; Q9Y2K7; -. DR BioGRID; 116639; 98. DR ComplexPortal; CPX-2538; SCF E3 ubiquitin ligase complex, KDM2A variant. DR DIP; DIP-34596N; -. DR IntAct; Q9Y2K7; 36. DR MINT; Q9Y2K7; -. DR STRING; 9606.ENSP00000432786; -. DR BindingDB; Q9Y2K7; -. DR ChEMBL; CHEMBL1938210; -. DR GuidetoPHARMACOLOGY; 2671; -. DR CarbonylDB; Q9Y2K7; -. DR GlyGen; Q9Y2K7; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9Y2K7; -. DR PhosphoSitePlus; Q9Y2K7; -. DR SwissPalm; Q9Y2K7; -. DR BioMuta; KDM2A; -. DR DMDM; 38257795; -. DR EPD; Q9Y2K7; -. DR jPOST; Q9Y2K7; -. DR MassIVE; Q9Y2K7; -. DR MaxQB; Q9Y2K7; -. DR PaxDb; 9606-ENSP00000432786; -. DR PeptideAtlas; Q9Y2K7; -. DR ProteomicsDB; 12834; -. DR ProteomicsDB; 20849; -. DR ProteomicsDB; 85827; -. [Q9Y2K7-1] DR ProteomicsDB; 85828; -. [Q9Y2K7-2] DR ProteomicsDB; 85829; -. [Q9Y2K7-3] DR Pumba; Q9Y2K7; -. DR ABCD; Q9Y2K7; 1 sequenced antibody. DR Antibodypedia; 3222; 312 antibodies from 34 providers. DR DNASU; 22992; -. DR Ensembl; ENST00000398645.6; ENSP00000381640.2; ENSG00000173120.15. [Q9Y2K7-3] DR Ensembl; ENST00000529006.7; ENSP00000432786.1; ENSG00000173120.15. [Q9Y2K7-1] DR Ensembl; ENST00000530342.2; ENSP00000435776.1; ENSG00000173120.15. [Q9Y2K7-5] DR GeneID; 22992; -. DR KEGG; hsa:22992; -. DR MANE-Select; ENST00000529006.7; ENSP00000432786.1; NM_012308.3; NP_036440.1. DR UCSC; uc001ojw.4; human. [Q9Y2K7-1] DR AGR; HGNC:13606; -. DR CTD; 22992; -. DR DisGeNET; 22992; -. DR GeneCards; KDM2A; -. DR HGNC; HGNC:13606; KDM2A. DR HPA; ENSG00000173120; Low tissue specificity. DR MIM; 605657; gene. DR neXtProt; NX_Q9Y2K7; -. DR OpenTargets; ENSG00000173120; -. DR PharmGKB; PA164721195; -. DR VEuPathDB; HostDB:ENSG00000173120; -. DR eggNOG; KOG1633; Eukaryota. DR eggNOG; KOG1947; Eukaryota. DR GeneTree; ENSGT00940000155484; -. DR HOGENOM; CLU_003540_4_0_1; -. DR InParanoid; Q9Y2K7; -. DR OMA; XQDNRSK; -. DR OrthoDB; 2784357at2759; -. DR PhylomeDB; Q9Y2K7; -. DR TreeFam; TF106480; -. DR BioCyc; MetaCyc:HS10620-MONOMER; -. DR PathwayCommons; Q9Y2K7; -. DR Reactome; R-HSA-3214842; HDMs demethylate histones. DR SignaLink; Q9Y2K7; -. DR SIGNOR; Q9Y2K7; -. DR BioGRID-ORCS; 22992; 425 hits in 1217 CRISPR screens. DR ChiTaRS; KDM2A; human. DR EvolutionaryTrace; Q9Y2K7; -. DR GeneWiki; KDM2A; -. DR GenomeRNAi; 22992; -. DR Pharos; Q9Y2K7; Tchem. DR PRO; PR:Q9Y2K7; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q9Y2K7; Protein. DR Bgee; ENSG00000173120; Expressed in amniotic fluid and 209 other cell types or tissues. DR ExpressionAtlas; Q9Y2K7; baseline and differential. DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0032452; F:histone demethylase activity; IBA:GO_Central. DR GO; GO:0051864; F:histone H3K36 demethylase activity; IMP:UniProtKB. DR GO; GO:0140680; F:histone H3K36me/H3K36me2 demethylase activity; IEA:UniProtKB-EC. DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central. DR GO; GO:0045322; F:unmethylated CpG binding; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB. DR GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB. DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:UniProtKB. DR GO; GO:0010944; P:negative regulation of transcription by competitive promoter binding; IMP:UniProtKB. DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR CDD; cd21784; CTD_KDM2A; 1. DR CDD; cd22181; F-box_FBXL11; 1. DR CDD; cd15643; PHD_KDM2A; 1. DR Gene3D; 1.20.58.1360; -; 1. DR Gene3D; 2.60.120.650; Cupin; 1. DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR001810; F-box_dom. DR InterPro; IPR041070; JHD. DR InterPro; IPR003347; JmjC_dom. DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp. DR InterPro; IPR032675; LRR_dom_sf. DR InterPro; IPR019786; Zinc_finger_PHD-type_CS. DR InterPro; IPR002857; Znf_CXXC. DR InterPro; IPR011011; Znf_FYVE_PHD. DR InterPro; IPR001965; Znf_PHD. DR InterPro; IPR019787; Znf_PHD-finger. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR PANTHER; PTHR23123:SF3; LYSINE-SPECIFIC DEMETHYLASE 2A; 1. DR PANTHER; PTHR23123; PHD/F-BOX CONTAINING PROTEIN; 1. DR Pfam; PF12937; F-box-like; 1. DR Pfam; PF17811; JHD; 1. DR Pfam; PF16866; PHD_4; 1. DR Pfam; PF02008; zf-CXXC; 1. DR SMART; SM00558; JmjC; 1. DR SMART; SM00367; LRR_CC; 3. DR SMART; SM00249; PHD; 1. DR SUPFAM; SSF51197; Clavaminate synthase-like; 1. DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1. DR SUPFAM; SSF52047; RNI-like; 1. DR PROSITE; PS51184; JMJC; 1. DR PROSITE; PS51058; ZF_CXXC; 1. DR PROSITE; PS01359; ZF_PHD_1; 1. DR PROSITE; PS50016; ZF_PHD_2; 1. DR Genevisible; Q9Y2K7; HS. PE 1: Evidence at protein level; KW 3D-structure; ADP-ribosylation; Alternative splicing; Biological rhythms; KW Chromatin regulator; Chromosome; Dioxygenase; DNA-binding; Iron; KW Isopeptide bond; Leucine-rich repeat; Metal-binding; Nucleus; KW Oxidoreductase; Phosphoprotein; Reference proteome; Repeat; Repressor; KW Transcription; Transcription regulation; Ubl conjugation; KW Ubl conjugation pathway; Zinc; Zinc-finger. FT CHAIN 1..1162 FT /note="Lysine-specific demethylase 2A" FT /id="PRO_0000119855" FT DOMAIN 148..316 FT /note="JmjC" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538" FT DOMAIN 889..936 FT /note="F-box" FT REPEAT 961..982 FT /note="LRR 1" FT REPEAT 984..1010 FT /note="LRR 2" FT REPEAT 1048..1073 FT /note="LRR 3" FT REPEAT 1074..1103 FT /note="LRR 4" FT REPEAT 1104..1128 FT /note="LRR 5" FT REPEAT 1129..1156 FT /note="LRR 6" FT ZN_FING 564..610 FT /note="CXXC-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509, FT ECO:0007744|PDB:4BBQ" FT ZN_FING 617..678 FT /note="PHD-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146, FT ECO:0007744|PDB:4BBQ" FT REGION 367..389 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 532..557 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 704..789 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 839..887 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 373..387 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 748..789 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 852..871 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 209 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 212 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000305|PubMed:16362057, FT ECO:0007744|PDB:2YU1, ECO:0007744|PDB:2YU2" FT BINDING 214 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538, FT ECO:0000269|Ref.27, ECO:0007744|PDB:2YU1, FT ECO:0007744|PDB:2YU2" FT BINDING 229 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 284 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538, FT ECO:0000269|Ref.27, ECO:0007744|PDB:2YU1, FT ECO:0007744|PDB:2YU2" FT BINDING 571 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509, FT ECO:0000269|Ref.28, ECO:0007744|PDB:4BBQ" FT BINDING 574 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509, FT ECO:0000269|Ref.28, ECO:0007744|PDB:4BBQ" FT BINDING 577 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509, FT ECO:0000269|Ref.28, ECO:0007744|PDB:4BBQ" FT BINDING 582 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509, FT ECO:0000269|Ref.28, ECO:0007744|PDB:4BBQ" FT BINDING 585 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509, FT ECO:0000269|Ref.28, ECO:0007744|PDB:4BBQ" FT BINDING 588 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509, FT ECO:0000269|Ref.28, ECO:0007744|PDB:4BBQ" FT BINDING 604 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509, FT ECO:0000269|Ref.28, ECO:0007744|PDB:4BBQ" FT BINDING 609 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509, FT ECO:0000269|Ref.28, ECO:0007744|PDB:4BBQ" FT BINDING 620 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000269|Ref.28, ECO:0007744|PDB:4BBQ" FT BINDING 623 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000269|Ref.28, ECO:0007744|PDB:4BBQ" FT BINDING 642 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000269|Ref.28, ECO:0007744|PDB:4BBQ" FT BINDING 645 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000269|Ref.28, ECO:0007744|PDB:4BBQ" FT BINDING 650 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000269|Ref.28, ECO:0007744|PDB:4BBQ" FT BINDING 653 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000269|Ref.28, ECO:0007744|PDB:4BBQ" FT BINDING 672 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000269|Ref.28, ECO:0007744|PDB:4BBQ" FT BINDING 675 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000269|Ref.28, ECO:0007744|PDB:4BBQ" FT MOD_RES 28 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 390 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 394 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 550 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18220336, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 558 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18220336, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 632 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17525332" FT MOD_RES 692 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19367720, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163" FT MOD_RES 713 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18220336, FT ECO:0007744|PubMed:18669648" FT MOD_RES 718 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P59997" FT MOD_RES 731 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18220336, FT ECO:0007744|PubMed:18669648" FT MOD_RES 825 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 832 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 869 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 883 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 1020 FT /note="ADP-ribosylarginine" FT /evidence="ECO:0000250|UniProtKB:P59997" FT CROSSLNK 505 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..542 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_046938" FT VAR_SEQ 1..439 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_046939" FT VAR_SEQ 1..306 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_017468" FT VAR_SEQ 440..492 FT /note="DPQCAPRKDRQVHLTHFELEGLRCLVDKLESLPLHKKCVPTGIEDEDALIAD FT V -> MCSGRFQNIQVNPDFPRGRISNSFRRTSSTENKTKTLGKLHQEPRQLQSDGKR FT (in isoform 5)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_046940" FT VAR_SEQ 774..782 FT /note="REKENNPSG -> LRQETLDKN (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3" FT /id="VSP_017469" FT VAR_SEQ 783..1162 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3" FT /id="VSP_017470" FT MUTAGEN 212..214 FT /note="HVD->AVA: Abolishes lysine-specific histone FT demethylase activity." FT /evidence="ECO:0000269|PubMed:28262558" FT MUTAGEN 212 FT /note="H->A: Abolishes histone demethylase activity. No FT loss of its ability to repress the transcriptional FT activator activity of the CLOCK-BMAL1 heterodimer." FT /evidence="ECO:0000269|PubMed:16362057, FT ECO:0000269|PubMed:26037310" FT MUTAGEN 571 FT /note="C->A: Abolishes association with centromeric FT heterochromatin; when associated with A-574 and A-577." FT /evidence="ECO:0000269|PubMed:19001877" FT MUTAGEN 574 FT /note="C->A: Abolishes association with centromeric FT heterochromatin; when associated with A-571 and A-577. Loss FT of its ability to repress the transcriptional activator FT activity of the CLOCK-BMAL1 heterodimer; when associated FT with A-577." FT /evidence="ECO:0000269|PubMed:19001877, FT ECO:0000269|PubMed:26037310" FT MUTAGEN 577 FT /note="C->A: Abolishes association with centromeric FT heterochromatin; when associated with A-571 and A-574. Loss FT of its ability to repress the transcriptional activator FT activity of the CLOCK-BMAL1 heterodimer; when associated FT with A-574." FT /evidence="ECO:0000269|PubMed:19001877, FT ECO:0000269|PubMed:26037310" FT MUTAGEN 620 FT /note="C->A: No loss of its ability to repress the FT transcriptional activator activity of the CLOCK-BMAL1 FT heterodimer; when associated with A-623." FT /evidence="ECO:0000269|PubMed:26037310" FT MUTAGEN 623 FT /note="C->A: No loss of its ability to repress the FT transcriptional activator activity of the CLOCK-BMAL1 FT heterodimer; when associated with A-620." FT /evidence="ECO:0000269|PubMed:26037310" FT MUTAGEN 892 FT /note="W->V: Reduced interaction with UBB." FT /evidence="ECO:0000269|PubMed:30033217" FT CONFLICT 518 FT /note="K -> I (in Ref. 8; AAH47371)" FT /evidence="ECO:0000305" FT CONFLICT 657 FT /note="D -> G (in Ref. 8; AAH47371)" FT /evidence="ECO:0000305" FT CONFLICT 1128 FT /note="Missing (in Ref. 8; AAH01203)" FT /evidence="ECO:0000305" FT STRAND 36..38 FT /evidence="ECO:0007829|PDB:2YU2" FT HELIX 40..45 FT /evidence="ECO:0007829|PDB:2YU1" FT HELIX 59..61 FT /evidence="ECO:0007829|PDB:2YU1" FT HELIX 64..70 FT /evidence="ECO:0007829|PDB:2YU1" FT STRAND 76..80 FT /evidence="ECO:0007829|PDB:2YU1" FT TURN 82..85 FT /evidence="ECO:0007829|PDB:2YU2" FT HELIX 95..101 FT /evidence="ECO:0007829|PDB:2YU1" FT STRAND 107..112 FT /evidence="ECO:0007829|PDB:7UV9" FT TURN 113..116 FT /evidence="ECO:0007829|PDB:7UV9" FT STRAND 117..122 FT /evidence="ECO:0007829|PDB:7UV9" FT HELIX 123..130 FT /evidence="ECO:0007829|PDB:2YU1" FT TURN 134..136 FT /evidence="ECO:0007829|PDB:2YU1" FT STRAND 141..146 FT /evidence="ECO:0007829|PDB:2YU1" FT HELIX 154..156 FT /evidence="ECO:0007829|PDB:2YU1" FT HELIX 161..166 FT /evidence="ECO:0007829|PDB:2YU1" FT HELIX 168..172 FT /evidence="ECO:0007829|PDB:2YU1" FT HELIX 175..177 FT /evidence="ECO:0007829|PDB:2YU1" FT HELIX 188..190 FT /evidence="ECO:0007829|PDB:7UV9" FT STRAND 199..203 FT /evidence="ECO:0007829|PDB:2YU1" FT STRAND 208..212 FT /evidence="ECO:0007829|PDB:2YU1" FT HELIX 215..217 FT /evidence="ECO:0007829|PDB:2YU1" FT STRAND 219..227 FT /evidence="ECO:0007829|PDB:2YU1" FT STRAND 229..234 FT /evidence="ECO:0007829|PDB:2YU1" FT HELIX 238..249 FT /evidence="ECO:0007829|PDB:2YU1" FT STRAND 254..256 FT /evidence="ECO:0007829|PDB:2YU1" FT HELIX 258..261 FT /evidence="ECO:0007829|PDB:2YU1" FT STRAND 266..270 FT /evidence="ECO:0007829|PDB:2YU1" FT STRAND 275..278 FT /evidence="ECO:0007829|PDB:2YU1" FT STRAND 283..287 FT /evidence="ECO:0007829|PDB:2YU1" FT STRAND 292..299 FT /evidence="ECO:0007829|PDB:2YU1" FT STRAND 302..304 FT /evidence="ECO:0007829|PDB:2YU1" FT HELIX 305..317 FT /evidence="ECO:0007829|PDB:2YU1" FT HELIX 322..324 FT /evidence="ECO:0007829|PDB:7UV9" FT HELIX 329..345 FT /evidence="ECO:0007829|PDB:2YU1" FT HELIX 352..362 FT /evidence="ECO:0007829|PDB:2YU1" FT HELIX 455..469 FT /evidence="ECO:0007829|PDB:2YU1" FT HELIX 473..475 FT /evidence="ECO:0007829|PDB:2YU1" FT STRAND 480..483 FT /evidence="ECO:0007829|PDB:2YU1" FT HELIX 485..498 FT /evidence="ECO:0007829|PDB:2YU1" FT STRAND 499..501 FT /evidence="ECO:0007829|PDB:2YU1" FT HELIX 504..507 FT /evidence="ECO:0007829|PDB:2YU1" FT HELIX 575..578 FT /evidence="ECO:0007829|PDB:4BBQ" FT HELIX 586..590 FT /evidence="ECO:0007829|PDB:4BBQ" FT HELIX 592..594 FT /evidence="ECO:0007829|PDB:4BBQ" FT HELIX 605..607 FT /evidence="ECO:0007829|PDB:4BBQ" FT TURN 621..623 FT /evidence="ECO:0007829|PDB:4BBQ" FT HELIX 629..632 FT /evidence="ECO:0007829|PDB:4BBQ" FT HELIX 635..637 FT /evidence="ECO:0007829|PDB:4BBQ" FT STRAND 640..642 FT /evidence="ECO:0007829|PDB:4BBQ" FT TURN 643..645 FT /evidence="ECO:0007829|PDB:4BBQ" FT HELIX 651..653 FT /evidence="ECO:0007829|PDB:4BBQ" FT STRAND 664..671 FT /evidence="ECO:0007829|PDB:4BBQ" FT TURN 673..675 FT /evidence="ECO:0007829|PDB:4BBQ" FT HELIX 892..902 FT /evidence="ECO:0007829|PDB:6BYH" FT HELIX 907..913 FT /evidence="ECO:0007829|PDB:6BYH" FT TURN 914..916 FT /evidence="ECO:0007829|PDB:6BYH" FT HELIX 918..923 FT /evidence="ECO:0007829|PDB:6BYH" SQ SEQUENCE 1162 AA; 132793 MW; 88620A363A5C5842 CRC64; MEPEEERIRY SQRLRGTMRR RYEDDGISDD EIEGKRTFDL EEKLHTNKYN ANFVTFMEGK DFNVEYIQRG GLRDPLIFKN SDGLGIKMPD PDFTVNDVKM CVGSRRMVDV MDVNTQKGIE MTMAQWTRYY ETPEEEREKL YNVISLEFSH TRLENMVQRP STVDFIDWVD NMWPRHLKES QTESTNAILE MQYPKVQKYC LMSVRGCYTD FHVDFGGTSV WYHIHQGGKV FWLIPPTAHN LELYENWLLS GKQGDIFLGD RVSDCQRIEL KQGYTFVIPS GWIHAVYTPT DTLVFGGNFL HSFNIPMQLK IYNIEDRTRV PNKFRYPFYY EMCWYVLERY VYCITNRSHL TKEFQKESLS MDLELNGLES GNGDEEAVDR EPRRLSSRRS VLTSPVANGV NLDYDGLGKT CRSLPSLKKT LAGDSSSDCS RGSHNGQVWD PQCAPRKDRQ VHLTHFELEG LRCLVDKLES LPLHKKCVPT GIEDEDALIA DVKILLEELA NSDPKLALTG VPIVQWPKRD KLKFPTRPKV RVPTIPITKP HTMKPAPRLT PVRPAAASPI VSGARRRRVR CRKCKACVQG ECGVCHYCRD MKKFGGPGRM KQSCVLRQCL APRLPHSVTC SLCGEVDQNE ETQDFEKKLM ECCICNEIVH PGCLQMDGEG LLNEELPNCW ECPKCYQEDS SEKAQKRKME ESDEEAVQAK VLRPLRSCDE PLTPPPHSPT SMLQLIHDPV SPRGMVTRSS PGAGPSDHHS ASRDERFKRR QLLRLQATER TMVREKENNP SGKKELSEVE KAKIRGSYLT VTLQRPTKEL HGTSIVPKLQ AITASSANLR HSPRVLVQHC PARTPQRGDE EGLGGEEEEE EEEEEEDDSA EEGGAARLNG RGSWAQDGDE SWMQREVWMS VFRYLSRREL CECMRVCKTW YKWCCDKRLW TKIDLSRCKA IVPQALSGII KRQPVSLDLS WTNISKKQLT WLVNRLPGLK DLLLAGCSWS AVSALSTSSC PLLRTLDLRW AVGIKDPQIR DLLTPPADKP GQDNRSKLRN MTDFRLAGLD ITDATLRLII RHMPLLSRLD LSHCSHLTDQ SSNLLTAVGS STRYSLTELN MAGCNKLTDQ TLIYLRRIAN VTLIDLRGCK QITRKACEHF ISDLSINSLY CLSDEKLIQK IS //