CDCA2_HUMAN
ID CDCA2_HUMAN Reviewed; 1023 AA.
AC Q69YH5; Q3SX74; Q4G0W0; Q5RKN0; Q69YI4; Q6P464; Q8N7C1;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Cell division cycle-associated protein 2;
DE AltName: Full=Recruits PP1 onto mitotic chromatin at anaphase protein;
DE Short=Repo-Man;
GN Name=CDCA2;
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 [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ILE-717.
RC TISSUE=Endometrial tumor, and Melanoma;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 112-1023 (ISOFORM 1), AND VARIANTS ILE-717 AND
RP SER-884.
RC TISSUE=Chondrosarcoma, Skin, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 559-1023 (ISOFORM 1), AND VARIANT ILE-717.
RX PubMed=12188893; DOI=10.2174/1568009013334241;
RA Walker M.G.;
RT "Drug target discovery by gene expression analysis: cell cycle genes.";
RL Curr. Cancer Drug Targets 1:73-83(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 561-1023 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400, 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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, INTERACTION WITH PPP1CC, AND MUTAGENESIS OF 393-VAL--PHE-395.
RX PubMed=16492807; DOI=10.1083/jcb.200508154;
RA Trinkle-Mulcahy L., Andersen J., Lam Y.W., Moorhead G., Mann M.,
RA Lamond A.I.;
RT "Repo-Man recruits PP1 gamma to chromatin and is essential for cell
RT viability.";
RL J. Cell Biol. 172:679-692(2006).
RN [8]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=16998479; DOI=10.1038/ncb1475;
RA Vagnarelli P., Hudson D.F., Ribeiro S.A., Trinkle-Mulcahy L., Spence J.M.,
RA Lai F., Farr C.J., Lamond A.I., Earnshaw W.C.;
RT "Condensin and Repo-Man-PP1 co-operate in the regulation of chromosome
RT architecture during mitosis.";
RL Nat. Cell Biol. 8:1133-1142(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-126; SER-131;
RP SER-291; SER-309; THR-312; SER-400; SER-407; THR-412; SER-591 AND SER-756,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400 AND THR-412, AND
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-400; SER-437 AND
RP SER-591, VARIANT [LARGE SCALE ANALYSIS] ILE-717, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-936 AND SER-977, VARIANT
RP [LARGE SCALE ANALYSIS] ILE-717, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-120; SER-210;
RP SER-400; SER-614; SER-710; SER-936; SER-977 AND SER-1000, VARIANT [LARGE
RP SCALE ANALYSIS] ILE-717, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP 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 [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-762, 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).
CC -!- FUNCTION: Regulator of chromosome structure during mitosis required for
CC condensin-depleted chromosomes to retain their compact architecture
CC through anaphase. Acts by mediating the recruitment of phopsphatase
CC PP1-gamma subunit (PPP1CC) to chromatin at anaphase and into the
CC following interphase. At anaphase onset, its association with chromatin
CC targets a pool of PPP1CC to dephosphorylate substrates.
CC {ECO:0000269|PubMed:16492807, ECO:0000269|PubMed:16998479}.
CC -!- SUBUNIT: Interacts with PPP1CC. {ECO:0000269|PubMed:16492807}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16492807}.
CC Note=Excluded from the nucleolus. Present in nucleoplasm throughout the
CC G1, S and G2 stages of the cell cycle. During M phase, it becomes
CC diffuse throughout the cell as the nuclear membrane breaks down, and
CC faintly accumulates later on metaphase chromatin. As the cell
CC progresses to anaphase, it accumulates on chromatin.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q69YH5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q69YH5-2; Sequence=VSP_025598, VSP_025599;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:16492807}.
CC -!- PTM: Phosphorylated by CDK1. May regulate its subcellular location.
CC {ECO:0000269|PubMed:16998479}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH36214.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC05374.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAH10577.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
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DR EMBL; AL833396; CAH10585.1; -; mRNA.
DR EMBL; AL833627; CAH10577.1; ALT_SEQ; mRNA.
DR EMBL; AC103779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC036214; AAH36214.1; ALT_INIT; mRNA.
DR EMBL; BC063651; AAH63651.1; -; mRNA.
DR EMBL; BC085609; AAH85609.1; -; mRNA.
DR EMBL; BC104451; AAI04452.1; -; mRNA.
DR EMBL; BC104450; AAI04451.1; -; mRNA.
DR EMBL; BG354575; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK098670; BAC05374.1; ALT_INIT; mRNA.
DR CCDS; CCDS6049.1; -. [Q69YH5-1]
DR RefSeq; NP_001304835.1; NM_001317906.1.
DR RefSeq; NP_001304836.1; NM_001317907.1.
DR RefSeq; NP_689775.2; NM_152562.3. [Q69YH5-1]
DR PDB; 5INB; X-ray; 1.30 A; B=383-423.
DR PDB; 5IOH; X-ray; 2.57 A; B/D=383-441.
DR PDB; 5SW9; X-ray; 2.85 A; B=581-601.
DR PDBsum; 5INB; -.
DR PDBsum; 5IOH; -.
DR PDBsum; 5SW9; -.
DR AlphaFoldDB; Q69YH5; -.
DR SMR; Q69YH5; -.
DR BioGRID; 127593; 56.
DR ELM; Q69YH5; -.
DR IntAct; Q69YH5; 30.
DR MINT; Q69YH5; -.
DR STRING; 9606.ENSP00000328228; -.
DR GlyGen; Q69YH5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q69YH5; -.
DR PhosphoSitePlus; Q69YH5; -.
DR BioMuta; CDCA2; -.
DR DMDM; 308153420; -.
DR EPD; Q69YH5; -.
DR jPOST; Q69YH5; -.
DR MassIVE; Q69YH5; -.
DR MaxQB; Q69YH5; -.
DR PaxDb; Q69YH5; -.
DR PeptideAtlas; Q69YH5; -.
DR PRIDE; Q69YH5; -.
DR ProteomicsDB; 66154; -. [Q69YH5-1]
DR ProteomicsDB; 66155; -. [Q69YH5-2]
DR Antibodypedia; 10001; 143 antibodies from 27 providers.
DR DNASU; 157313; -.
DR Ensembl; ENST00000330560.8; ENSP00000328228.3; ENSG00000184661.14. [Q69YH5-1]
DR GeneID; 157313; -.
DR KEGG; hsa:157313; -.
DR MANE-Select; ENST00000330560.8; ENSP00000328228.3; NM_152562.4; NP_689775.2.
DR UCSC; uc003xep.2; human. [Q69YH5-1]
DR CTD; 157313; -.
DR DisGeNET; 157313; -.
DR GeneCards; CDCA2; -.
DR HGNC; HGNC:14623; CDCA2.
DR HPA; ENSG00000184661; Group enriched (bone marrow, lymphoid tissue, testis).
DR MIM; 618785; gene.
DR neXtProt; NX_Q69YH5; -.
DR OpenTargets; ENSG00000184661; -.
DR PharmGKB; PA26275; -.
DR VEuPathDB; HostDB:ENSG00000184661; -.
DR eggNOG; ENOG502S079; Eukaryota.
DR GeneTree; ENSGT00940000154352; -.
DR HOGENOM; CLU_011968_0_0_1; -.
DR InParanoid; Q69YH5; -.
DR OMA; CDCSEDV; -.
DR OrthoDB; 290017at2759; -.
DR PhylomeDB; Q69YH5; -.
DR TreeFam; TF336000; -.
DR PathwayCommons; Q69YH5; -.
DR SignaLink; Q69YH5; -.
DR BioGRID-ORCS; 157313; 34 hits in 1026 CRISPR screens.
DR ChiTaRS; CDCA2; human.
DR GenomeRNAi; 157313; -.
DR Pharos; Q69YH5; Tbio.
DR PRO; PR:Q69YH5; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q69YH5; protein.
DR Bgee; ENSG00000184661; Expressed in secondary oocyte and 125 other tissues.
DR ExpressionAtlas; Q69YH5; baseline and differential.
DR Genevisible; Q69YH5; HS.
DR GO; GO:0005694; C:chromosome; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IEA:Ensembl.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; IMP:MGI.
DR GO; GO:0051983; P:regulation of chromosome segregation; IBA:GO_Central.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; IBA:GO_Central.
DR InterPro; IPR033064; CDCA2.
DR InterPro; IPR029334; PP1-bd.
DR PANTHER; PTHR21603:SF16; PTHR21603:SF16; 1.
DR Pfam; PF15276; PP1_bind; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cell division;
KW Isopeptide bond; Mitosis; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..1023
FT /note="Cell division cycle-associated protein 2"
FT /id="PRO_0000287695"
FT DOMAIN 389..449
FT /note="PP1-binding"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 803..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 936..1023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..572
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..720
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..845
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..860
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..966
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..1007
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 312
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 412
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 614
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 710
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 756
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 936
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 977
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1000
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 762
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 68
FT /note="T -> N (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025598"
FT VAR_SEQ 69..1023
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025599"
FT VARIANT 717
FT /note="V -> I (in dbSNP:rs4872318)"
FT /evidence="ECO:0000269|PubMed:12188893,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT /id="VAR_032350"
FT VARIANT 884
FT /note="R -> S (in dbSNP:rs3829009)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_032351"
FT MUTAGEN 393..395
FT /note="VTF->ATA: Abolishes interaction with PPP1CC but not
FT subcellular location."
FT /evidence="ECO:0000269|PubMed:16492807"
FT CONFLICT 662
FT /note="Y -> D (in Ref. 4; BG354575)"
FT /evidence="ECO:0000305"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:5INB"
SQ SEQUENCE 1023 AA; 112676 MW; 2A073D6DD928B1E5 CRC64;
MDANSKDKPP ETKESAMNNA GNASFILGTG KIVTPQKHAE LPPNPCTPDT FKSPLNFSTV
TVEQLGITPE SFVRNSAGKS SSYLKKCRRR SAVGARGSPE TNHLIRFIAR QQNIKNARKS
PLAQDSPSQG SPALYRNVNT LRERISAFQS AFHSIKENEK MTGCLEFSEA GKESEMTDLT
RKEGLSACQQ SGFPAVLSSK RRRISYQRDS DENLTDAEGK VIGLQIFNID TDRACAVETS
VDLSEISSKL GSTQSGFLVE ESLPLSELTE TSNALKVADC VVGKGSSDAV SPDTFTAEVS
SDAVPDVRSP ATPACRRDLP TPKTFVLRSV LKKPSVKMCL ESLQEHCNNL YDDDGTHPSL
ISNLPNCCKE KEAEDEENFE APAFLNMRKR KRVTFGEDLS PEVFDESLPA NTPLRKGGTP
VCKKDFSGLS SLLLEQSPVP EPLPQPDFDD KGENLENIEP LQVSFAVLSS PNKSSISETL
SGTDTFSSSN NHEKISSPKV GRITRTSNRR NQLVSVVEES VCNLLNTEVQ PCKEKKINRR
KSQETKCTKR ALPKKSQVLK SCRKKKGKGK KSVQKSLYGE RDIASKKPLL SPIPELPEVP
EMTPSIPSIR RLGSGYFSSN GKLEEVKTPK NPVKRKDLLR HDPDLHMHQG YDKYDVSEFC
SYIKSSSSLG NATSDEDPNT NIMNINENKN IPKAKNKSES ENEPKAGTDS PVSCASVTEE
RVASDSPKPA LTLQQGQEFS AGGQNAENLC QFFKISPDLN IKCERKDDFL GAAEGKLQCN
RLMPNSQKDC HCLGDVLIEN TKESKSQSED LGRKPMESSS VVSCRDRKDR RRSMCYSDGR
SLHLEKNGNH TPSSSVGSSV EISLENSELF KDLSDAIEQT FQRRNSETKV RRSTRLQKDL
ENEGLVWISL PLPSTSQKAK RRTICTFDSS GFESMSPIKE TVSSRQKPQM APPVSDPENS
QGPAAGSSDE PGKRRKSFCI STLANTKATS QFKGYRRRSS LNGKGESSLT ALERIEHNGE
RKQ
