KDM2A_MOUSE
ID KDM2A_MOUSE Reviewed; 1161 AA.
AC P59997; Q3U1M5; Q3UR56; Q3V3Q1; Q69ZT4;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Lysine-specific demethylase 2A;
DE EC=1.14.11.27 {ECO:0000250|UniProtKB:Q9Y2K7};
DE AltName: Full=F-box and leucine-rich repeat protein 11;
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=Fbl11 {ECO:0000250|UniProtKB:Q9Y2K7}, Fbxl11, Jhdm1a, Kiaa1004;
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] (ISOFORMS 2 AND 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 646-1161.
RC STRAIN=C57BL/6J; TISSUE=Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 453-1161.
RC TISSUE=Thymus;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
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. 11:205-218(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-550, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-632, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-444; SER-692;
RP THR-713; SER-718 AND SER-731, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, 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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND ADP-RIBOSYLATION AT ARG-1019.
RX PubMed=32584788; DOI=10.18632/aging.103567;
RA Rezazadeh S., Yang D., Biashad S.A., Firsanov D., Takasugi M., Gilbert M.,
RA Tombline G., Bhanu N.V., Garcia B.A., Seluanov A., Gorbunova V.;
RT "SIRT6 mono-ADP ribosylates KDM2A to locally increase H3K36me2 at DNA
RT damage sites to inhibit transcription and promote repair.";
RL Aging (Albany NY) 12:11165-11184(2020).
CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-36'
CC of histone H3, thereby playing a central role in histone code
CC (PubMed:32584788). Preferentially demethylates dimethylated H3 'Lys-36'
CC residue while it has weak or no activity for mono- and tri-methylated
CC H3 'Lys-36'. May also recognize and bind to some phosphorylated
CC proteins and promote their ubiquitination and degradation. Required to
CC maintain the heterochromatic state. Associates with centromeres and
CC represses transcription of small non-coding RNAs that are encoded by
CC the clusters of satellite repeats at the centromere. Required to
CC sustain centromeric integrity and genomic stability, particularly
CC during mitosis (By similarity). Regulates circadian gene expression by
CC repressing the transcriptional activator activity of CLOCK-ARNTL/BMAL1
CC heterodimer and RORA in a catalytically-independent manner (By
CC similarity). {ECO:0000250|UniProtKB:Q9Y2K7,
CC ECO:0000269|PubMed:32584788}.
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:0000250|UniProtKB:Q9Y2K7};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2K7};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9Y2K7};
CC -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex.
CC Interacts with CBX5/HP1A; the interaction promotes CBX5 localization to
CC chromatin (By similarity). The SKP1-KDM2A complex interacts with UBB
CC (By similarity). {ECO:0000250|UniProtKB:Q9Y2K7}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q9Y2K7}. Chromosome
CC {ECO:0000269|PubMed:32584788}. Note=Punctate expression throughout the
CC nucleoplasm and enriched in the perinucleolar region. Specifically
CC nucleates at CpG islands where it's presence results in chromatin
CC depleted in H3K36me2 (By similarity). {ECO:0000250|UniProtKB:Q9Y2K7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P59997-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P59997-2; Sequence=VSP_017473, VSP_017474;
CC Name=3;
CC IsoId=P59997-3; Sequence=VSP_017471, VSP_017472;
CC -!- DOMAIN: The JmjC domain mediates demethylation activity and is required
CC for satellite silencing. {ECO:0000250|UniProtKB:Q9Y2K7}.
CC -!- DOMAIN: The CXXC zinc finger preferentially recognizes nonmethylated
CC CpG DNA, and binding is blocked when the CpG DNA is methylated (By
CC similarity). It is essential for its ability to repress the
CC transcriptional activator activity of CLOCK-ARNTL/BMAL1 heterodimer (By
CC similarity). {ECO:0000250|UniProtKB:Q9Y2K7}.
CC -!- DOMAIN: The F-box domain mediates interaction with UBB.
CC {ECO:0000250|UniProtKB:Q9Y2K7}.
CC -!- PTM: Mono-ADP-ribosylated at Arg-1019 in response to DNA damage,
CC leading to displacement from chromatin, resulting in increased
CC dimethylation of histone H3 at 'Lys-36'. {ECO:0000269|PubMed:32584788}.
CC -!- SIMILARITY: Belongs to the JHDM1 histone demethylase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BC076576; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK037157; BAE20506.1; -; mRNA.
DR EMBL; AK141779; BAE24832.1; -; mRNA.
DR EMBL; AK155866; BAE33470.1; -; mRNA.
DR EMBL; BC057051; AAH57051.1; -; mRNA.
DR EMBL; BC076576; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK173084; BAD32362.1; -; mRNA.
DR CCDS; CCDS37886.1; -. [P59997-1]
DR RefSeq; NP_001001984.2; NM_001001984.2.
DR PDB; 4QWN; X-ray; 2.10 A; A/C=36-364, B/D=450-517.
DR PDB; 4QX7; X-ray; 2.34 A; A/C=36-364, B/D=450-517.
DR PDB; 4QX8; X-ray; 1.65 A; A/C=36-364, B/D=450-517.
DR PDB; 4QXB; X-ray; 1.60 A; A/C=36-364, B/D=450-517.
DR PDB; 4QXC; X-ray; 1.75 A; A/C=36-364, B/D=450-517.
DR PDB; 4QXH; X-ray; 2.20 A; A/C=36-364, B/D=450-517.
DR PDB; 4TN7; X-ray; 2.20 A; A/C=36-364, B/D=450-517.
DR PDBsum; 4QWN; -.
DR PDBsum; 4QX7; -.
DR PDBsum; 4QX8; -.
DR PDBsum; 4QXB; -.
DR PDBsum; 4QXC; -.
DR PDBsum; 4QXH; -.
DR PDBsum; 4TN7; -.
DR AlphaFoldDB; P59997; -.
DR SMR; P59997; -.
DR BioGRID; 230438; 3.
DR DIP; DIP-46352N; -.
DR IntAct; P59997; 1.
DR STRING; 10090.ENSMUSP00000047683; -.
DR iPTMnet; P59997; -.
DR PhosphoSitePlus; P59997; -.
DR EPD; P59997; -.
DR jPOST; P59997; -.
DR MaxQB; P59997; -.
DR PaxDb; P59997; -.
DR PeptideAtlas; P59997; -.
DR PRIDE; P59997; -.
DR ProteomicsDB; 269285; -. [P59997-1]
DR ProteomicsDB; 269286; -. [P59997-2]
DR ProteomicsDB; 269287; -. [P59997-3]
DR DNASU; 225876; -.
DR GeneID; 225876; -.
DR KEGG; mmu:225876; -.
DR CTD; 22992; -.
DR MGI; MGI:1354736; Kdm2a.
DR eggNOG; KOG1633; Eukaryota.
DR eggNOG; KOG1947; Eukaryota.
DR InParanoid; P59997; -.
DR OrthoDB; 324938at2759; -.
DR PhylomeDB; P59997; -.
DR Reactome; R-MMU-3214842; HDMs demethylate histones.
DR BioGRID-ORCS; 225876; 8 hits in 116 CRISPR screens.
DR ChiTaRS; Kdm2a; mouse.
DR PRO; PR:P59997; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P59997; protein.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0045322; F:unmethylated CpG binding; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; ISO:MGI.
DR GO; GO:0001947; P:heart looping; IMP:MGI.
DR GO; GO:0070544; P:histone H3-K36 demethylation; IMP:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
DR GO; GO:0010944; P:negative regulation of transcription by competitive promoter binding; ISS:UniProtKB.
DR GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR GO; GO:0060563; P:neuroepithelial cell differentiation; IMP:MGI.
DR GO; GO:0030182; P:neuron differentiation; IMP:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR GO; GO:0033184; P:positive regulation of histone ubiquitination; IMP:MGI.
DR GO; GO:0006482; P:protein demethylation; IBA:GO_Central.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS: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; Allosteric enzyme; Alternative splicing;
KW Biological rhythms; Chromatin regulator; Chromosome; Dioxygenase;
KW DNA-binding; Iron; Isopeptide bond; Leucine-rich repeat; Metal-binding;
KW Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1161
FT /note="Lysine-specific demethylase 2A"
FT /id="PRO_0000119856"
FT DOMAIN 148..316
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT DOMAIN 888..935
FT /note="F-box"
FT REPEAT 960..981
FT /note="LRR 1"
FT REPEAT 983..1009
FT /note="LRR 2"
FT REPEAT 1047..1072
FT /note="LRR 3"
FT REPEAT 1073..1102
FT /note="LRR 4"
FT REPEAT 1103..1127
FT /note="LRR 5"
FT REPEAT 1128..1155
FT /note="LRR 6"
FT ZN_FING 564..610
FT /note="CXXC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT ZN_FING 617..678
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 419..445
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 705..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 840..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..440
FT /note="Polar 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..870
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:0000255|PROSITE-ProRule:PRU00538"
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 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 BINDING 571
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
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 BINDING 577
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
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 BINDING 585
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
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 BINDING 604
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
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 BINDING 620
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K7"
FT BINDING 623
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K7"
FT BINDING 642
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K7"
FT BINDING 645
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K7"
FT BINDING 650
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K7"
FT BINDING 653
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K7"
FT BINDING 672
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K7"
FT BINDING 675
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K7"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K7"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K7"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 550
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 558
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K7"
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:21183079"
FT MOD_RES 713
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 718
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 731
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 825
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K7"
FT MOD_RES 868
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K7"
FT MOD_RES 882
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K7"
FT MOD_RES 1019
FT /note="ADP-ribosylarginine"
FT /evidence="ECO:0000269|PubMed:32584788"
FT CROSSLNK 505
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K7"
FT VAR_SEQ 321..338
FT /note="PNKFRYPFYYEMCWYVLE -> SNVTIICVDVSPFKADVR (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017471"
FT VAR_SEQ 339..1161
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017472"
FT VAR_SEQ 494
FT /note="I -> S (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017473"
FT VAR_SEQ 495..1161
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017474"
FT CONFLICT 159
FT /note="W -> R (in Ref. 1; BAE20506 and 2; BC076576)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="I -> M (in Ref. 1; BAE20506 and 2; BC076576)"
FT /evidence="ECO:0000305"
FT CONFLICT 913
FT /note="M -> I (in Ref. 2; AAH57051)"
FT /evidence="ECO:0000305"
FT HELIX 40..45
FT /evidence="ECO:0007829|PDB:4QXB"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:4QXB"
FT HELIX 64..70
FT /evidence="ECO:0007829|PDB:4QXB"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:4QXB"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:4TN7"
FT HELIX 95..102
FT /evidence="ECO:0007829|PDB:4QXB"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:4QXB"
FT TURN 113..116
FT /evidence="ECO:0007829|PDB:4QXB"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:4QXB"
FT HELIX 123..131
FT /evidence="ECO:0007829|PDB:4QXB"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:4QXB"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:4QXB"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:4QXB"
FT HELIX 161..166
FT /evidence="ECO:0007829|PDB:4QXB"
FT HELIX 168..172
FT /evidence="ECO:0007829|PDB:4QXB"
FT HELIX 175..180
FT /evidence="ECO:0007829|PDB:4QXB"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:4QXB"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:4QXB"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:4QXB"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:4QXB"
FT STRAND 219..227
FT /evidence="ECO:0007829|PDB:4QXB"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:4QXB"
FT HELIX 238..250
FT /evidence="ECO:0007829|PDB:4QXB"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:4QXB"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:4QXB"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:4QXB"
FT STRAND 266..270
FT /evidence="ECO:0007829|PDB:4QXB"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:4QXB"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:4QXB"
FT STRAND 292..299
FT /evidence="ECO:0007829|PDB:4QXB"
FT HELIX 305..317
FT /evidence="ECO:0007829|PDB:4QXB"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:4QXB"
FT HELIX 329..345
FT /evidence="ECO:0007829|PDB:4QXB"
FT HELIX 352..362
FT /evidence="ECO:0007829|PDB:4QXB"
FT HELIX 455..469
FT /evidence="ECO:0007829|PDB:4QXB"
FT HELIX 473..476
FT /evidence="ECO:0007829|PDB:4QXB"
FT HELIX 485..499
FT /evidence="ECO:0007829|PDB:4QXB"
FT TURN 504..507
FT /evidence="ECO:0007829|PDB:4QXB"
SQ SEQUENCE 1161 AA; 132680 MW; 210BD9F65BED0AE4 CRC64;
MEPEEERIRY SQRLRGTMRR RYEDDGISDD EIEGKRTFDL EEKLQTNKYN ANFVTFMEGK
DFNVEYIQRG GLRDPLIFKN SDGLGIKMPD PDFTVNDVKM CVGSRRMVDV MDVNTQKGIE
MTMAQWTRYY ETPEEEREKL YNVISLEFSH TRLENMVQWP STVDFIDWVD NMWPRHLKES
QTESTNAILE MQYPKVQKYC LISVRGCYTD FHVDFGGTSV WYHIHQGGKV FWLIPPTAHN
LELYENWLLS GKQGDIFLGD RVSDCQRIEL KQGYTFVIPS GWIHAVYTPT DTLVFGGNFL
HSFNIPMQLK IYSIEDRTRV PNKFRYPFYY EMCWYVLERY VYCITNRSHL TKDFQKESLS
MDMELNELES GNGDEEGVDR EARRMNNKRS VLTSPVANGV NLDYDGLGKA CRSLPSLKKT
LSGDSSSDST RGSHNGQVWD PQCSPKKDRQ VHLTHFELEG LRCLVDKLES LPLHKKCVPT
GIEDEDALIA DVKILLEELA SSDPKLALTG VPIVQWPKRD KLKFPTRPKV RVPTIPITKP
HTMKPAPRLT PVRPAAASPI VSGARRRRVR CRKCKACVQG ECGVCHYCRD MKKFGGPGRM
KQSCVLRQCL APRLPHSVTC SLCGEVDQNE ETQDFEKKLM ECCICNEIVH PGCLQMDGEG
LLNEELPNCW ECPKCYQEDS SDKAQKRKIE ESDEEAVQAK VLRPLRSCEE PLTPPPHSPT
SMLQLIHDPV SPRGMVTRSS PGAGPSDHHS ASRDERFKRR QLLRLQATER TMVREKENNP
SGKKELSEVE KAKIRGSYLT VTLQRPTKEL HGTSIVPKLQ AITASSANLR PNPRVLMQHC
PARNPQHGDE EGLGGEEEEE EEEEEDDSAE EGGAARLNGR GSWAQDGDES WMQREVWMSV
FRYLSRKELC ECMRVCKTWY KWCCDKRLWT KIDLSRCKAI VPQALSGIIK RQPVSLDLSW
TNISKKQLTW LVNRLPGLKD LLLAGCSWSA VSALSTSSCP LLRTLDLRWA VGIKDPQIRD
LLTPPTDKPG QDNRSKLRNM TDFRLAGLDI TDATLRLIIR HMPLLSRLDL SHCSHLTDQS
SNLLTAVGSS TRYSLTELNM AGCNKLTDQT LFFLRRIANV TLIDLRGCKQ ITRKACEHFI
SDLSINSLYC LSDEKLIQKI S
