KDM2A_HUMAN
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 03-AUG-2022, entry version 196.
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, JHDM1A,
GN 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-ARNTL/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-ARNTL/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};
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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 PDBsum; 2YU1; -.
DR PDBsum; 2YU2; -.
DR PDBsum; 4BBQ; -.
DR PDBsum; 6BYH; -.
DR PDBsum; 6C16; -.
DR AlphaFoldDB; Q9Y2K7; -.
DR SMR; Q9Y2K7; -.
DR BioGRID; 116639; 82.
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 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; Q9Y2K7; -.
DR PeptideAtlas; Q9Y2K7; -.
DR PRIDE; Q9Y2K7; -.
DR ProteomicsDB; 12834; -.
DR ProteomicsDB; 20849; -.
DR ProteomicsDB; 85827; -. [Q9Y2K7-1]
DR ProteomicsDB; 85828; -. [Q9Y2K7-2]
DR ProteomicsDB; 85829; -. [Q9Y2K7-3]
DR ABCD; Q9Y2K7; 1 sequenced antibody.
DR Antibodypedia; 3222; 282 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 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; KQVHLTH; -.
DR PhylomeDB; Q9Y2K7; -.
DR TreeFam; TF106480; -.
DR BioCyc; MetaCyc:HS10620-MON; -.
DR PathwayCommons; Q9Y2K7; -.
DR Reactome; R-HSA-3214842; HDMs demethylate histones.
DR SignaLink; Q9Y2K7; -.
DR SIGNOR; Q9Y2K7; -.
DR BioGRID-ORCS; 22992; 403 hits in 1137 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 207 other tissues.
DR ExpressionAtlas; Q9Y2K7; baseline and differential.
DR Genevisible; Q9Y2K7; HS.
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:0140680; F:histone H3-di/monomethyl-lysine-36 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0051864; F:histone H3-methyl-lysine-36 demethylase activity; IMP:UniProtKB.
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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
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:0070544; P:histone H3-K36 demethylation; IMP:UniProtKB.
DR GO; GO:0010944; P:negative regulation of transcription by competitive promoter binding; IMP:UniProtKB.
DR GO; GO:0006482; P:protein demethylation; IBA:GO_Central.
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 Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.80.10.10; -; 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 Pfam; PF00646; F-box; 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; SSF57903; SSF57903; 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.
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-ARNTL/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-ARNTL/BMAL1 heterodimer; when
FT associated 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-ARNTL/BMAL1 heterodimer; when
FT associated 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-ARNTL/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-ARNTL/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 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 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 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
