KI67_HUMAN
ID KI67_HUMAN Reviewed; 3256 AA.
AC P46013; Q5VWH2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 216.
DE RecName: Full=Proliferation marker protein Ki-67 {ECO:0000305};
DE AltName: Full=Antigen identified by monoclonal antibody Ki-67 {ECO:0000303|PubMed:8227122};
DE Short=Antigen KI-67 {ECO:0000305};
DE Short=Antigen Ki67 {ECO:0000305};
GN Name=MKI67 {ECO:0000312|HGNC:HGNC:7107};
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] (ISOFORMS SHORT AND LONG), AND VARIANTS VAL-872;
RP TRP-1470; LEU-1622; ALA-1849 AND ASP-3097.
RX PubMed=8227122; DOI=10.1083/jcb.123.3.513;
RA Schlueter C., Duchrow M., Wohlenberg C., Becker M.H.G., Key G., Flad H.-D.,
RA Gerdes J.;
RT "The cell proliferation-associated antigen of antibody Ki-67: a very large,
RT ubiquitous nuclear protein with numerous repeated elements, representing a
RT new kind of cell cycle-maintaining proteins.";
RL J. Cell Biol. 123:513-522(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.
RA Gerdes J.;
RT "Sequence of the human Ki-67 protein gene 5' and promoter region.";
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP BIOTECHNOLOGY.
RX PubMed=6339421; DOI=10.1002/ijc.2910310104;
RA Gerdes J., Schwab U., Lemke H., Stein H.;
RT "Production of a mouse monoclonal antibody reactive with a human nuclear
RT antigen associated with cell proliferation.";
RL Int. J. Cancer 31:13-20(1983).
RN [5]
RP DEVELOPMENTAL STAGE.
RX PubMed=6206131;
RA Gerdes J., Lemke H., Baisch H., Wacker H.H., Schwab U., Stein H.;
RT "Cell cycle analysis of a cell proliferation-associated human nuclear
RT antigen defined by the monoclonal antibody Ki-67.";
RL J. Immunol. 133:1710-1715(1984).
RN [6]
RP DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX PubMed=2674163; DOI=10.1242/jcs.92.1.123;
RA Verheijen R., Kuijpers H.J., Schlingemann R.O., Boehmer A.L., van Driel R.,
RA Brakenhoff G.J., Ramaekers F.C.;
RT "Ki-67 detects a nuclear matrix-associated proliferation-related antigen.
RT I. Intracellular localization during interphase.";
RL J. Cell Sci. 92:123-130(1989).
RN [7]
RP DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX PubMed=8799815; DOI=10.1242/jcs.109.6.1253;
RA Kill I.R.;
RT "Localisation of the Ki-67 antigen within the nucleolus. Evidence for a
RT fibrillarin-deficient region of the dense fibrillar component.";
RL J. Cell Sci. 109:1253-1263(1996).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=9510506; DOI=10.1023/a:1009210206855;
RA Bridger J.M., Kill I.R., Lichter P.;
RT "Association of pKi-67 with satellite DNA of the human genome in early G1
RT cells.";
RL Chromosome Res. 6:13-24(1998).
RN [9]
RP PHOSPHORYLATION.
RX PubMed=10502411; DOI=10.1006/excr.1999.4600;
RA MacCallum D.E., Hall P.A.;
RT "Biochemical characterization of pKi67 with the identification of a
RT mitotic-specific form associated with hyperphosphorylation and altered DNA
RT binding.";
RL Exp. Cell Res. 252:186-198(1999).
RN [10]
RP INTERACTION WITH KIF15.
RX PubMed=10878014; DOI=10.1074/jbc.m003879200;
RA Sueishi M., Takagi M., Yoneda Y.;
RT "The forkhead-associated domain of Ki-67 antigen interacts with the novel
RT kinesin-like protein Hklp2.";
RL J. Biol. Chem. 275:28888-28892(2000).
RN [11]
RP PHOSPHORYLATION.
RX PubMed=10653604;
RX DOI=10.1002/(sici)1097-4652(200003)182:3<371::aid-jcp8>3.0.co;2-j;
RA Endl E., Gerdes J.;
RT "Posttranslational modifications of the KI-67 protein coincide with two
RT major checkpoints during mitosis.";
RL J. Cell. Physiol. 182:371-380(2000).
RN [12]
RP FUNCTION, DNA-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=10878551;
RX DOI=10.1002/1096-9896(2000)9999:9999<::aid-path628>3.0.co;2-j;
RA MacCallum D.E., Hall P.A.;
RT "The biochemical characterization of the DNA binding activity of pKi67.";
RL J. Pathol. 191:286-298(2000).
RN [13]
RP INTERACTION WITH NIFK.
RX PubMed=11342549; DOI=10.1074/jbc.m102227200;
RA Takagi M., Sueishi M., Saiwaki T., Kametaka A., Yoneda Y.;
RT "A novel nucleolar protein, NIFK, interacts with the forkhead associated
RT domain of Ki-67 antigen in mitosis.";
RL J. Biol. Chem. 276:25386-25391(2001).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=15896774; DOI=10.1016/j.yexcr.2005.04.010;
RA Saiwaki T., Kotera I., Sasaki M., Takagi M., Yoneda Y.;
RT "In vivo dynamics and kinetics of pKi-67: transition from a mobile to an
RT immobile form at the onset of anaphase.";
RL Exp. Cell Res. 308:123-134(2005).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2406 AND SER-2708, AND
RP IDENTIFICATION BY 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-328; SER-357; SER-579;
RP SER-584; SER-1131; THR-1327; THR-1569; THR-1801; THR-1923 AND THR-2406, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1233; THR-1355; SER-1679 AND
RP THR-1764, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357; SER-579; SER-584 AND
RP SER-1861, 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308; SER-357; SER-579;
RP SER-648 AND SER-1679, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-264; SER-308;
RP THR-328; THR-347; SER-357; THR-401; SER-579; SER-584; SER-648; THR-761;
RP SER-859; THR-1017; SER-1071; THR-1091; SER-1098; THR-1111; SER-1131;
RP THR-1139; SER-1142; SER-1207; SER-1253; SER-1256; THR-1261; THR-1298;
RP THR-1315; THR-1327; SER-1329; THR-1335; THR-1355; SER-1376; THR-1383;
RP THR-1503; SER-1506; THR-1540; TYR-1552; THR-1557; THR-1569; SER-1571;
RP SER-1679; SER-1689; THR-1719; SER-1721; SER-1740; THR-1747; THR-1784;
RP THR-1801; THR-1841; SER-1861; SER-1864; THR-1869; THR-1923; THR-2065;
RP SER-2072; THR-2085; SER-2105; THR-2113; THR-2203; SER-2223; THR-2231;
RP SER-2239; THR-2285; THR-2325; THR-2328; THR-2333; SER-2344; THR-2352;
RP THR-2389; SER-2395; THR-2406; SER-2528; SER-2588; SER-2708; SER-2827;
RP SER-2828 AND SER-3041, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [22]
RP IDENTIFICATION IN A COMPLEX WITH ZNF335; HCFC1; CCAR2; EMSY; MKI67; RBBP5;
RP ASH2L AND WDR5.
RX PubMed=19131338; DOI=10.1074/jbc.m805872200;
RA Garapaty S., Xu C.F., Trojer P., Mahajan M.A., Neubert T.A., Samuels H.H.;
RT "Identification and characterization of a novel nuclear protein complex
RT involved in nuclear hormone receptor-mediated gene regulation.";
RL J. Biol. Chem. 284:7542-7552(2009).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-648; SER-1131; THR-1335;
RP THR-1557; THR-1764; SER-1937; THR-2406 AND SER-2420, AND IDENTIFICATION BY
RP 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 [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1639 AND LYS-2005, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308; SER-357; SER-579;
RP SER-584; SER-648; THR-1091; SER-1098; SER-1131; THR-1167; THR-1193;
RP SER-1207; THR-1233; THR-1315; THR-1327; SER-1329; THR-1335; THR-1355;
RP THR-1557; THR-1569; SER-1571; SER-1679; THR-1747; THR-1801; SER-1815;
RP SER-1861; THR-1897; THR-1923; SER-1937; THR-1963; SER-1983; THR-2065;
RP SER-2072; THR-2085; SER-2105; SER-2135; SER-2223; THR-2231; THR-2233;
RP SER-2239; THR-2268; THR-2285; THR-2325; SER-2344; THR-2389; SER-2395;
RP THR-2406; SER-2420; THR-2446; SER-2528; SER-2588; SER-2708 AND SER-3128,
RP AND IDENTIFICATION BY MASS 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 [27]
RP REVIEW ON BIOTECHNOLOGY.
RX PubMed=21960707; DOI=10.1093/jnci/djr393;
RG International Ki-67 in Breast Cancer Working Group;
RA Dowsett M., Nielsen T.O., A'Hern R., Bartlett J., Coombes R.C., Cuzick J.,
RA Ellis M., Henry N.L., Hugh J.C., Lively T., McShane L., Paik S.,
RA Penault-Llorca F., Prudkin L., Regan M., Salter J., Sotiriou C.,
RA Smith I.E., Viale G., Zujewski J.A., Hayes D.F.;
RT "Assessment of Ki67 in breast cancer: recommendations from the
RT International Ki67 in Breast Cancer working group.";
RL J. Natl. Cancer Inst. 103:1656-1664(2011).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308; SER-352; SER-357;
RP SER-1098; SER-1131; SER-1496; SER-1861; SER-1983; SER-2072; SER-2105;
RP SER-2344; SER-2528; SER-2588 AND SER-2708, AND IDENTIFICATION BY MASS
RP 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 [29]
RP INTERACTION WITH ZNF335.
RX PubMed=23178126; DOI=10.1016/j.cell.2012.10.043;
RA Yang Y.J., Baltus A.E., Mathew R.S., Murphy E.A., Evrony G.D.,
RA Gonzalez D.M., Wang E.P., Marshall-Walker C.A., Barry B.J., Murn J.,
RA Tatarakis A., Mahajan M.A., Samuels H.H., Shi Y., Golden J.A., Mahajnah M.,
RA Shenhav R., Walsh C.A.;
RT "Microcephaly gene links trithorax and REST/NRSF to control neural stem
RT cell proliferation and differentiation.";
RL Cell 151:1097-1112(2012).
RN [30]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=22002106; DOI=10.1074/mcp.m111.013680;
RA Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.;
RT "Systematic analysis of protein pools, isoforms, and modifications
RT affecting turnover and subcellular localization.";
RL Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012).
RN [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-128; SER-308;
RP THR-328; THR-347; SER-357; SER-411; SER-538; THR-543; SER-579; SER-584;
RP SER-648; THR-761; SER-859; SER-1071; THR-1091; SER-1098; THR-1111;
RP SER-1131; THR-1176; SER-1207; THR-1233; THR-1327; SER-1329; THR-1335;
RP THR-1355; THR-1503; THR-1557; THR-1569; SER-1571; THR-1764; THR-1784;
RP THR-1801; SER-1815; THR-1841; SER-1861; THR-1923; SER-1937; THR-1963;
RP THR-2065; SER-2072; THR-2085; SER-2105; SER-2135; SER-2223; THR-2231;
RP THR-2325; SER-2344; THR-2389; THR-2406; SER-2420; THR-2426; THR-2446;
RP SER-2466; SER-2505; SER-2528; SER-2588; SER-2638 AND SER-3041, AND
RP IDENTIFICATION BY MASS 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 [32]
RP FUNCTION, AND INTERACTION WITH PPP1CC.
RX PubMed=24867636; DOI=10.7554/elife.01641;
RA Booth D.G., Takagi M., Sanchez-Pulido L., Petfalski E., Vargiu G.,
RA Samejima K., Imamoto N., Ponting C.P., Tollervey D., Earnshaw W.C.,
RA Vagnarelli P.;
RT "Ki-67 is a PP1-interacting protein that organises the mitotic chromosome
RT periphery.";
RL Elife 3:E01641-E01641(2014).
RN [33]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1035; LYS-1643; LYS-2613;
RP LYS-2734 AND LYS-2852, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [34]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1093; LYS-2009; LYS-2067;
RP LYS-2492; LYS-2613; LYS-2734 AND LYS-2852, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [35]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1035; LYS-1643; LYS-2009 AND
RP LYS-2734, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [36]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1035 AND LYS-1643, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [37]
RP REVIEW ON BIOTECHNOLOGY.
RX PubMed=26680267; DOI=10.1136/jclinpath-2015-203340;
RA Richards-Taylor S., Ewings S.M., Jaynes E., Tilley C., Ellis S.G.,
RA Armstrong T., Pearce N., Cave J.;
RT "The assessment of Ki-67 as a prognostic marker in neuroendocrine tumours:
RT a systematic review and meta-analysis.";
RL J. Clin. Pathol. 69:612-618(2016).
RN [38]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=27362226; DOI=10.1038/nature18610;
RA Cuylen S., Blaukopf C., Politi A.Z., Mueller-Reichert T., Neumann B.,
RA Poser I., Ellenberg J., Hyman A.A., Gerlich D.W.;
RT "Ki-67 acts as a biological surfactant to disperse mitotic chromosomes.";
RL Nature 535:308-312(2016).
RN [39]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-245; LYS-1022; LYS-1035;
RP LYS-1093; LYS-1185; LYS-1188; LYS-1337; LYS-1643; LYS-1703; LYS-2009;
RP LYS-2067; LYS-2613; LYS-2734; LYS-2852 AND LYS-2967, AND IDENTIFICATION BY
RP MASS 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 [40]
RP STRUCTURE BY NMR OF 1-120 IN COMPLEX WITH NIFK.
RX PubMed=14659764; DOI=10.1016/j.jmb.2003.10.032;
RA Li H., Byeon I.-J., Ju Y., Tsai M.-D.;
RT "Structure of human Ki67 FHA domain and its binding to a phosphoprotein
RT fragment from hNIFK reveal unique recognition sites and new views to the
RT structural basis of FHA domain functions.";
RL J. Mol. Biol. 335:371-381(2004).
RN [41]
RP STRUCTURE BY NMR OF 1-120 IN COMPLEX WITH NIFK.
RX PubMed=16244663; DOI=10.1038/nsmb1008;
RA Byeon I.-J., Li H., Song H., Gronenborn A.M., Tsai M.-D.;
RT "Sequential phosphorylation and multisite interactions characterize
RT specific target recognition by the FHA domain of Ki67.";
RL Nat. Struct. Mol. Biol. 12:987-993(2005).
CC -!- FUNCTION: Required to maintain individual mitotic chromosomes dispersed
CC in the cytoplasm following nuclear envelope disassembly
CC (PubMed:27362226). Associates with the surface of the mitotic
CC chromosome, the perichromosomal layer, and covers a substantial
CC fraction of the chromosome surface (PubMed:27362226). Prevents
CC chromosomes from collapsing into a single chromatin mass by forming a
CC steric and electrostatic charge barrier: the protein has a high net
CC electrical charge and acts as a surfactant, dispersing chromosomes and
CC enabling independent chromosome motility (PubMed:27362226). Binds DNA,
CC with a preference for supercoiled DNA and AT-rich DNA
CC (PubMed:10878551). Does not contribute to the internal structure of
CC mitotic chromosomes (By similarity). May play a role in chromatin
CC organization (PubMed:24867636). It is however unclear whether it plays
CC a direct role in chromatin organization or whether it is an indirect
CC consequence of its function in maintaining mitotic chromosomes
CC dispersed (Probable). {ECO:0000250|UniProtKB:E9PVX6,
CC ECO:0000269|PubMed:10878551, ECO:0000269|PubMed:24867636,
CC ECO:0000269|PubMed:27362226}.
CC -!- SUBUNIT: Interacts with KIF15 (PubMed:10878014). Interacts (via the FHA
CC domain) with NIFK (PubMed:11342549, PubMed:14659764, PubMed:16244663).
CC Interacts with PPP1CC (PubMed:24867636). Component of a complex at
CC least composed of ZNF335, HCFC1, CCAR2, EMSY, MKI67, RBBP5, ASH2L and
CC WDR5; the complex is formed as a result of interactions between
CC components of a nuclear receptor-mediated transcription complex and a
CC histone methylation complex (PubMed:19131338). Interacts with ZNF335
CC (PubMed:19131338, PubMed:23178126). {ECO:0000269|PubMed:10878014,
CC ECO:0000269|PubMed:11342549, ECO:0000269|PubMed:14659764,
CC ECO:0000269|PubMed:16244663, ECO:0000269|PubMed:19131338,
CC ECO:0000269|PubMed:23178126, ECO:0000269|PubMed:24867636}.
CC -!- INTERACTION:
CC P46013; Q9NS87: KIF15; NbExp=3; IntAct=EBI-876367, EBI-712159;
CC P46013; Q9BYG3: NIFK; NbExp=3; IntAct=EBI-876367, EBI-2561019;
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:15896774,
CC ECO:0000269|PubMed:22002106, ECO:0000269|PubMed:27362226,
CC ECO:0000269|PubMed:9510506}. Nucleus {ECO:0000269|PubMed:10878551,
CC ECO:0000269|PubMed:22002106}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:10878551, ECO:0000269|PubMed:22002106,
CC ECO:0000269|PubMed:2674163, ECO:0000269|PubMed:8799815}.
CC Note=Associates with the surface of the mitotic chromosome, the
CC perichromosomal layer, and covers a substantial fraction of the mitotic
CC chromosome surface (PubMed:27362226). Associates with satellite DNA in
CC G1 phase (PubMed:9510506). Binds tightly to chromatin in interphase,
CC chromatin-binding decreases in mitosis when it associates with the
CC surface of the condensed chromosomes (PubMed:15896774,
CC PubMed:22002106). Predominantly localized in the G1 phase in the
CC perinucleolar region, in the later phases it is also detected
CC throughout the nuclear interior, being predominantly localized in the
CC nuclear matrix (PubMed:22002106). {ECO:0000269|PubMed:15896774,
CC ECO:0000269|PubMed:22002106, ECO:0000269|PubMed:27362226}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P46013-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P46013-2; Sequence=VSP_004298;
CC -!- DEVELOPMENTAL STAGE: Expression occurs preferentially during late G1,
CC S, G2 and M phases of the cell cycle, while in cells in G0 phase the
CC antigen cannot be detected (at protein level) (PubMed:6206131). Present
CC at highest level in G2 phase and during mitosis (at protein level). In
CC interphase, forms fiber-like structures in fibrillarin-deficient
CC regions surrounding nucleoli (PubMed:2674163, PubMed:8799815).
CC {ECO:0000269|PubMed:2674163, ECO:0000269|PubMed:6206131,
CC ECO:0000269|PubMed:8799815}.
CC -!- PTM: Phosphorylated. Hyperphosphorylated in mitosis (PubMed:10502411,
CC PubMed:10653604). Hyperphosphorylated form does not bind DNA.
CC {ECO:0000269|PubMed:10502411, ECO:0000269|PubMed:10653604}.
CC -!- BIOTECHNOLOGY: Widely used as a marker to assess cell proliferation, as
CC it is detected in the nucleus of proliferating cells only
CC (PubMed:6339421, PubMed:21960707). In cancer research field for
CC example, MKI67 is the most widely used marker for comparing
CC proliferation between tumor samples (PubMed:21960707, PubMed:26680267).
CC {ECO:0000269|PubMed:6339421, ECO:0000303|PubMed:21960707,
CC ECO:0000303|PubMed:26680267}.
CC -!- CAUTION: Was thought to play a key role in cell proliferation, and is
CC commonly used as a marker of cell proliferation (PubMed:6339421,
CC PubMed:21960707). However, its primary function is uncoupled from cell
CC proliferation: it is required to maintain mitotic chromosomes dispersed
CC by forming a steric and electrostatic charge barrier (PubMed:27362226).
CC {ECO:0000269|PubMed:27362226, ECO:0000269|PubMed:6339421,
CC ECO:0000303|PubMed:21960707}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Ki-67 entry;
CC URL="https://en.wikipedia.org/wiki/Ki-67_%28Biology%29";
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=The contours of heredity
CC - Issue 186 of December 2016;
CC URL="https://web.expasy.org/spotlight/back_issues/186/";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
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DR EMBL; X65550; CAA46519.1; -; mRNA.
DR EMBL; X65551; CAA46520.1; -; mRNA.
DR EMBL; AL355529; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL390236; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X94762; CAA64388.1; -; Genomic_DNA.
DR CCDS; CCDS53588.1; -. [P46013-2]
DR CCDS; CCDS7659.1; -. [P46013-1]
DR PIR; A48666; A48666.
DR RefSeq; NP_001139438.1; NM_001145966.1. [P46013-2]
DR RefSeq; NP_002408.3; NM_002417.4. [P46013-1]
DR PDB; 1R21; NMR; -; A=1-120.
DR PDB; 2AFF; NMR; -; A=1-120.
DR PDB; 5J28; X-ray; 2.00 A; C/D=496-536.
DR PDBsum; 1R21; -.
DR PDBsum; 2AFF; -.
DR PDBsum; 5J28; -.
DR BMRB; P46013; -.
DR SMR; P46013; -.
DR BioGRID; 110434; 541.
DR DIP; DIP-28132N; -.
DR IntAct; P46013; 502.
DR MINT; P46013; -.
DR STRING; 9606.ENSP00000357643; -.
DR CarbonylDB; P46013; -.
DR GlyGen; P46013; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P46013; -.
DR MetOSite; P46013; -.
DR PhosphoSitePlus; P46013; -.
DR SwissPalm; P46013; -.
DR BioMuta; MKI67; -.
DR DMDM; 118572663; -.
DR EPD; P46013; -.
DR jPOST; P46013; -.
DR MassIVE; P46013; -.
DR MaxQB; P46013; -.
DR PaxDb; P46013; -.
DR PeptideAtlas; P46013; -.
DR PRIDE; P46013; -.
DR ProteomicsDB; 55705; -. [P46013-1]
DR ProteomicsDB; 55706; -. [P46013-2]
DR Antibodypedia; 741; 2260 antibodies from 60 providers.
DR CPTC; P46013; 4 antibodies.
DR DNASU; 4288; -.
DR Ensembl; ENST00000368653.7; ENSP00000357642.3; ENSG00000148773.14. [P46013-2]
DR Ensembl; ENST00000368654.8; ENSP00000357643.3; ENSG00000148773.14. [P46013-1]
DR GeneID; 4288; -.
DR KEGG; hsa:4288; -.
DR MANE-Select; ENST00000368654.8; ENSP00000357643.3; NM_002417.5; NP_002408.3.
DR UCSC; uc001lke.4; human. [P46013-1]
DR CTD; 4288; -.
DR DisGeNET; 4288; -.
DR GeneCards; MKI67; -.
DR HGNC; HGNC:7107; MKI67.
DR HPA; ENSG00000148773; Group enriched (bone marrow, lymphoid tissue).
DR MIM; 176741; gene.
DR neXtProt; NX_P46013; -.
DR OpenTargets; ENSG00000148773; -.
DR PharmGKB; PA30825; -.
DR VEuPathDB; HostDB:ENSG00000148773; -.
DR eggNOG; ENOG502QRVV; Eukaryota.
DR GeneTree; ENSGT00940000154352; -.
DR HOGENOM; CLU_000534_0_0_1; -.
DR InParanoid; P46013; -.
DR OMA; GNSTGHK; -.
DR OrthoDB; 290017at2759; -.
DR PhylomeDB; P46013; -.
DR TreeFam; TF336000; -.
DR PathwayCommons; P46013; -.
DR SignaLink; P46013; -.
DR SIGNOR; P46013; -.
DR BioGRID-ORCS; 4288; 18 hits in 1094 CRISPR screens.
DR ChiTaRS; MKI67; human.
DR EvolutionaryTrace; P46013; -.
DR GeneWiki; Ki-67_(protein); -.
DR GenomeRNAi; 4288; -.
DR Pharos; P46013; Tbio.
DR PRO; PR:P46013; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P46013; protein.
DR Bgee; ENSG00000148773; Expressed in ventricular zone and 140 other tissues.
DR Genevisible; P46013; HS.
DR GO; GO:0005694; C:chromosome; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0008283; P:cell population proliferation; TAS:ProtInc.
DR GO; GO:1902275; P:regulation of chromatin organization; ISS:UniProtKB.
DR GO; GO:0051983; P:regulation of chromosome segregation; IDA:UniProtKB.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; IDA:UniProtKB.
DR CDD; cd00060; FHA; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR012568; KI67R.
DR InterPro; IPR029334; PP1-bd.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF08065; KI67R; 16.
DR Pfam; PF15276; PP1_bind; 1.
DR SMART; SM00240; FHA; 1.
DR SMART; SM01295; K167R; 16.
DR SUPFAM; SSF49879; SSF49879; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Cell cycle;
KW Chromosome; DNA-binding; Isopeptide bond; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..3256
FT /note="Proliferation marker protein Ki-67"
FT /id="PRO_0000084301"
FT DOMAIN 27..76
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT DOMAIN 502..549
FT /note="PP1-binding"
FT /evidence="ECO:0000255"
FT REPEAT 1001..1112
FT /note="K167R 1"
FT /evidence="ECO:0000255"
FT REPEAT 1123..1234
FT /note="K167R 2"
FT /evidence="ECO:0000255"
FT REPEAT 1245..1356
FT /note="K167R 3"
FT /evidence="ECO:0000255"
FT REPEAT 1367..1477
FT /note="K167R 4"
FT /evidence="ECO:0000255"
FT REPEAT 1488..1597
FT /note="K167R 5"
FT /evidence="ECO:0000255"
FT REPEAT 1609..1720
FT /note="K167R 6"
FT /evidence="ECO:0000255"
FT REPEAT 1731..1842
FT /note="K167R 7"
FT /evidence="ECO:0000255"
FT REPEAT 1854..1964
FT /note="K167R 8"
FT /evidence="ECO:0000255"
FT REPEAT 1975..2086
FT /note="K167R 9"
FT /evidence="ECO:0000255"
FT REPEAT 2097..2204
FT /note="K167R 10"
FT /evidence="ECO:0000255"
FT REPEAT 2215..2326
FT /note="K167R 11"
FT /evidence="ECO:0000255"
FT REPEAT 2336..2447
FT /note="K167R 12"
FT /evidence="ECO:0000255"
FT REPEAT 2458..2569
FT /note="K167R 13"
FT /evidence="ECO:0000255"
FT REPEAT 2580..2688
FT /note="K167R 14"
FT /evidence="ECO:0000255"
FT REPEAT 2700..2805
FT /note="K167R 15"
FT /evidence="ECO:0000255"
FT REPEAT 2819..2928
FT /note="K167R 16"
FT /evidence="ECO:0000255"
FT REGION 101..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 853..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1000..2928
FT /note="16 X 122 AA approximate repeats"
FT /evidence="ECO:0000305|PubMed:8227122"
FT REGION 1045..1073
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1109..1151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1246..1276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1323..1518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1597..1675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1689..1708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1717..1765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1771..1790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1801..1824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1839..1886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1961..2002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2017..2192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2205..2400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2445..2480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2497..2521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2570..3256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1070
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1249..1266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1331..1345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1373..1390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1391..1405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1406..1420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1421..1436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1452..1466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1719..1755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1801..1817
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1984..2000
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2030..2044
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2084..2098
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2147..2162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2240..2257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2361..2378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2460..2480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2501..2518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2602..2618
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2619..2633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2634..2674
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2685..2699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2752..2767
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2810..2826
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2833..2855
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2871..2913
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2919..2950
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2978..2992
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3053..3083
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3114..3128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3135..3158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3159..3220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3221..3256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 3034..3041
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PVX6"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PVX6"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 328
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 347
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 374
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PVX6"
FT MOD_RES 401
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 538
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 543
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 579
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 584
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 648
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 761
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 859
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1017
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1071
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1091
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1098
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1111
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1131
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1139
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1167
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PVX6"
FT MOD_RES 1176
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1193
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1233
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1253
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1256
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1261
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1298
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1315
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 1327
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1335
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1355
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1376
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1383
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1386
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PVX6"
FT MOD_RES 1420
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:E9PVX6"
FT MOD_RES 1437
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:E9PVX6"
FT MOD_RES 1496
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1503
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1506
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1540
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1552
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1557
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1569
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1571
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1617
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PVX6"
FT MOD_RES 1639
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1679
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 1689
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1719
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1721
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1740
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1747
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 1764
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 1784
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1801
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1815
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1841
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1861
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1864
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1869
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1897
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1906
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:E9PVX6"
FT MOD_RES 1923
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1937
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1963
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1983
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 2005
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 2028
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:E9PVX6"
FT MOD_RES 2065
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 2072
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2085
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 2105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2113
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 2116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PVX6"
FT MOD_RES 2135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2146
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:E9PVX6"
FT MOD_RES 2163
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:E9PVX6"
FT MOD_RES 2203
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 2223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 2231
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 2233
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 2239
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 2259
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:E9PVX6"
FT MOD_RES 2261
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PVX6"
FT MOD_RES 2268
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 2285
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 2325
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 2328
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 2333
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 2344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2352
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 2389
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 2395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 2406
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2420
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 2426
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2446
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2466
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2505
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2528
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2588
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2638
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2708
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 2827
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 2828
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 2838
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PVX6"
FT MOD_RES 2986
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:E9PVX6"
FT MOD_RES 3041
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 3128
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CROSSLNK 245
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1022
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1035
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 1093
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 1093
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1185
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1188
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1337
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1643
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 1703
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 2009
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 2009
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 2067
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 2067
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 2492
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 2613
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 2613
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 2734
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 2734
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 2852
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 2852
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 2967
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 136..495
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:8227122"
FT /id="VSP_004298"
FT VARIANT 104
FT /note="N -> S (in dbSNP:rs2071498)"
FT /id="VAR_029055"
FT VARIANT 238
FT /note="W -> R (in dbSNP:rs7095325)"
FT /id="VAR_029056"
FT VARIANT 497
FT /note="E -> D (in dbSNP:rs11016076)"
FT /id="VAR_029057"
FT VARIANT 574
FT /note="Q -> P (in dbSNP:rs4471342)"
FT /id="VAR_029058"
FT VARIANT 631
FT /note="I -> L (in dbSNP:rs997983)"
FT /id="VAR_024161"
FT VARIANT 832
FT /note="R -> W (in dbSNP:rs34916904)"
FT /id="VAR_033995"
FT VARIANT 854
FT /note="L -> V (in dbSNP:rs2240)"
FT /id="VAR_024162"
FT VARIANT 872
FT /note="A -> V (in dbSNP:rs2853344)"
FT /evidence="ECO:0000269|PubMed:8227122"
FT /id="VAR_029059"
FT VARIANT 1042
FT /note="G -> S (in dbSNP:rs2152143)"
FT /id="VAR_024163"
FT VARIANT 1120
FT /note="T -> S (in dbSNP:rs11016074)"
FT /id="VAR_029060"
FT VARIANT 1247
FT /note="T -> I (in dbSNP:rs4750685)"
FT /id="VAR_021838"
FT VARIANT 1403
FT /note="E -> V (in dbSNP:rs3740423)"
FT /id="VAR_020047"
FT VARIANT 1470
FT /note="L -> W (in dbSNP:rs2853345)"
FT /evidence="ECO:0000269|PubMed:8227122"
FT /id="VAR_029061"
FT VARIANT 1559
FT /note="V -> M (in dbSNP:rs7918199)"
FT /id="VAR_029062"
FT VARIANT 1622
FT /note="P -> L (in dbSNP:rs2782871)"
FT /evidence="ECO:0000269|PubMed:8227122"
FT /id="VAR_029063"
FT VARIANT 1849
FT /note="T -> A (in dbSNP:rs2782872)"
FT /evidence="ECO:0000269|PubMed:8227122"
FT /id="VAR_029064"
FT VARIANT 1876
FT /note="R -> Q (in dbSNP:rs11591817)"
FT /id="VAR_029065"
FT VARIANT 1951
FT /note="L -> I (in dbSNP:rs34116632)"
FT /id="VAR_033996"
FT VARIANT 2101
FT /note="I -> T (in dbSNP:rs11016073)"
FT /id="VAR_029066"
FT VARIANT 2337
FT /note="T -> N (in dbSNP:rs7083622)"
FT /id="VAR_024164"
FT VARIANT 2363
FT /note="N -> S (in dbSNP:rs7071768)"
FT /id="VAR_029067"
FT VARIANT 2607
FT /note="R -> H (in dbSNP:rs34688192)"
FT /id="VAR_061671"
FT VARIANT 2608
FT /note="P -> L (in dbSNP:rs1063535)"
FT /id="VAR_024165"
FT VARIANT 2649
FT /note="R -> H (in dbSNP:rs12777740)"
FT /id="VAR_029068"
FT VARIANT 2720
FT /note="T -> P (in dbSNP:rs1050767)"
FT /id="VAR_024166"
FT VARIANT 2760
FT /note="D -> G (in dbSNP:rs10082391)"
FT /id="VAR_029069"
FT VARIANT 2786
FT /note="R -> Q (in dbSNP:rs10764749)"
FT /id="VAR_029070"
FT VARIANT 2793
FT /note="S -> N (in dbSNP:rs10082533)"
FT /id="VAR_029071"
FT VARIANT 2845
FT /note="R -> H (in dbSNP:rs11016072)"
FT /id="VAR_029072"
FT VARIANT 2868
FT /note="T -> S (in dbSNP:rs2071496)"
FT /id="VAR_024167"
FT VARIANT 2904
FT /note="Q -> R (in dbSNP:rs11016071)"
FT /id="VAR_029073"
FT VARIANT 3097
FT /note="N -> D (in dbSNP:rs2798669)"
FT /evidence="ECO:0000269|PubMed:8227122"
FT /id="VAR_029074"
FT VARIANT 3102
FT /note="E -> G (in dbSNP:rs34750407)"
FT /id="VAR_033997"
FT VARIANT 3150
FT /note="T -> S (in dbSNP:rs11106)"
FT /id="VAR_014858"
FT VARIANT 3217
FT /note="K -> E (in dbSNP:rs8473)"
FT /id="VAR_014859"
FT CONFLICT 619..626
FT /note="RKSGNLPS -> ERVATCLQ (in Ref. 1; CAA46519/CAA46520)"
FT /evidence="ECO:0000305"
FT CONFLICT 2205
FT /note="I -> V (in Ref. 1; CAA46519/CAA46520)"
FT /evidence="ECO:0000305"
FT CONFLICT 2892..2893
FT /note="KL -> NV (in Ref. 1; CAA46519/CAA46520)"
FT /evidence="ECO:0000305"
FT CONFLICT 3246
FT /note="R -> T (in Ref. 1; CAA46519/CAA46520)"
FT /evidence="ECO:0000305"
FT STRAND 5..12
FT /evidence="ECO:0007829|PDB:1R21"
FT STRAND 15..21
FT /evidence="ECO:0007829|PDB:1R21"
FT STRAND 24..32
FT /evidence="ECO:0007829|PDB:1R21"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:1R21"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:1R21"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:1R21"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:1R21"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:2AFF"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:1R21"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:1R21"
FT STRAND 515..517
FT /evidence="ECO:0007829|PDB:5J28"
SQ SEQUENCE 3256 AA; 358694 MW; 1332BC6C799AD64D CRC64;
MWPTRRLVTI KRSGVDGPHF PLSLSTCLFG RGIECDIRIQ LPVVSKQHCK IEIHEQEAIL
HNFSSTNPTQ VNGSVIDEPV RLKHGDVITI IDRSFRYENE SLQNGRKSTE FPRKIREQEP
ARRVSRSSFS SDPDEKAQDS KAYSKITEGK VSGNPQVHIK NVKEDSTADD SKDSVAQGTT
NVHSSEHAGR NGRNAADPIS GDFKEISSVK LVSRYGELKS VPTTQCLDNS KKNESPFWKL
YESVKKELDV KSQKENVLQY CRKSGLQTDY ATEKESADGL QGETQLLVSR KSRPKSGGSG
HAVAEPASPE QELDQNKGKG RDVESVQTPS KAVGASFPLY EPAKMKTPVQ YSQQQNSPQK
HKNKDLYTTG RRESVNLGKS EGFKAGDKTL TPRKLSTRNR TPAKVEDAAD SATKPENLSS
KTRGSIPTDV EVLPTETEIH NEPFLTLWLT QVERKIQKDS LSKPEKLGTT AGQMCSGLPG
LSSVDINNFG DSINESEGIP LKRRRVSFGG HLRPELFDEN LPPNTPLKRG EAPTKRKSLV
MHTPPVLKKI IKEQPQPSGK QESGSEIHVE VKAQSLVISP PAPSPRKTPV ASDQRRRSCK
TAPASSSKSQ TEVPKRGGRK SGNLPSKRVS ISRSQHDILQ MICSKRRSGA SEANLIVAKS
WADVVKLGAK QTQTKVIKHG PQRSMNKRQR RPATPKKPVG EVHSQFSTGH ANSPCTIIIG
KAHTEKVHVP ARPYRVLNNF ISNQKMDFKE DLSGIAEMFK TPVKEQPQLT STCHIAISNS
ENLLGKQFQG TDSGEEPLLP TSESFGGNVF FSAQNAAKQP SDKCSASPPL RRQCIRENGN
VAKTPRNTYK MTSLETKTSD TETEPSKTVS TANRSGRSTE FRNIQKLPVE SKSEETNTEI
VECILKRGQK ATLLQQRREG EMKEIERPFE TYKENIELKE NDEKMKAMKR SRTWGQKCAP
MSDLTDLKSL PDTELMKDTA RGQNLLQTQD HAKAPKSEKG KITKMPCQSL QPEPINTPTH
TKQQLKASLG KVGVKEELLA VGKFTRTSGE TTHTHREPAG DGKSIRTFKE SPKQILDPAA
RVTGMKKWPR TPKEEAQSLE DLAGFKELFQ TPGPSEESMT DEKTTKIACK SPPPESVDTP
TSTKQWPKRS LRKADVEEEF LALRKLTPSA GKAMLTPKPA GGDEKDIKAF MGTPVQKLDL
AGTLPGSKRQ LQTPKEKAQA LEDLAGFKEL FQTPGHTEEL VAAGKTTKIP CDSPQSDPVD
TPTSTKQRPK RSIRKADVEG ELLACRNLMP SAGKAMHTPK PSVGEEKDII IFVGTPVQKL
DLTENLTGSK RRPQTPKEEA QALEDLTGFK ELFQTPGHTE EAVAAGKTTK MPCESSPPES
ADTPTSTRRQ PKTPLEKRDV QKELSALKKL TQTSGETTHT DKVPGGEDKS INAFRETAKQ
KLDPAASVTG SKRHPKTKEK AQPLEDLAGL KELFQTPVCT DKPTTHEKTT KIACRSQPDP
VDTPTSSKPQ SKRSLRKVDV EEEFFALRKR TPSAGKAMHT PKPAVSGEKN IYAFMGTPVQ
KLDLTENLTG SKRRLQTPKE KAQALEDLAG FKELFQTRGH TEESMTNDKT AKVACKSSQP
DPDKNPASSK RRLKTSLGKV GVKEELLAVG KLTQTSGETT HTHTEPTGDG KSMKAFMESP
KQILDSAASL TGSKRQLRTP KGKSEVPEDL AGFIELFQTP SHTKESMTNE KTTKVSYRAS
QPDLVDTPTS SKPQPKRSLR KADTEEEFLA FRKQTPSAGK AMHTPKPAVG EEKDINTFLG
TPVQKLDQPG NLPGSNRRLQ TRKEKAQALE ELTGFRELFQ TPCTDNPTTD EKTTKKILCK
SPQSDPADTP TNTKQRPKRS LKKADVEEEF LAFRKLTPSA GKAMHTPKAA VGEEKDINTF
VGTPVEKLDL LGNLPGSKRR PQTPKEKAKA LEDLAGFKEL FQTPGHTEES MTDDKITEVS
CKSPQPDPVK TPTSSKQRLK ISLGKVGVKE EVLPVGKLTQ TSGKTTQTHR ETAGDGKSIK
AFKESAKQML DPANYGTGME RWPRTPKEEA QSLEDLAGFK ELFQTPDHTE ESTTDDKTTK
IACKSPPPES MDTPTSTRRR PKTPLGKRDI VEELSALKQL TQTTHTDKVP GDEDKGINVF
RETAKQKLDP AASVTGSKRQ PRTPKGKAQP LEDLAGLKEL FQTPICTDKP TTHEKTTKIA
CRSPQPDPVG TPTIFKPQSK RSLRKADVEE ESLALRKRTP SVGKAMDTPK PAGGDEKDMK
AFMGTPVQKL DLPGNLPGSK RWPQTPKEKA QALEDLAGFK ELFQTPGTDK PTTDEKTTKI
ACKSPQPDPV DTPASTKQRP KRNLRKADVE EEFLALRKRT PSAGKAMDTP KPAVSDEKNI
NTFVETPVQK LDLLGNLPGS KRQPQTPKEK AEALEDLVGF KELFQTPGHT EESMTDDKIT
EVSCKSPQPE SFKTSRSSKQ RLKIPLVKVD MKEEPLAVSK LTRTSGETTQ THTEPTGDSK
SIKAFKESPK QILDPAASVT GSRRQLRTRK EKARALEDLV DFKELFSAPG HTEESMTIDK
NTKIPCKSPP PELTDTATST KRCPKTRPRK EVKEELSAVE RLTQTSGQST HTHKEPASGD
EGIKVLKQRA KKKPNPVEEE PSRRRPRAPK EKAQPLEDLA GFTELSETSG HTQESLTAGK
ATKIPCESPP LEVVDTTAST KRHLRTRVQK VQVKEEPSAV KFTQTSGETT DADKEPAGED
KGIKALKESA KQTPAPAASV TGSRRRPRAP RESAQAIEDL AGFKDPAAGH TEESMTDDKT
TKIPCKSSPE LEDTATSSKR RPRTRAQKVE VKEELLAVGK LTQTSGETTH TDKEPVGEGK
GTKAFKQPAK RKLDAEDVIG SRRQPRAPKE KAQPLEDLAS FQELSQTPGH TEELANGAAD
SFTSAPKQTP DSGKPLKISR RVLRAPKVEP VGDVVSTRDP VKSQSKSNTS LPPLPFKRGG
GKDGSVTGTK RLRCMPAPEE IVEELPASKK QRVAPRARGK SSEPVVIMKR SLRTSAKRIE
PAEELNSNDM KTNKEEHKLQ DSVPENKGIS LRSRRQNKTE AEQQITEVFV LAERIEINRN
EKKPMKTSPE MDIQNPDDGA RKPIPRDKVT ENKRCLRSAR QNESSQPKVA EESGGQKSAK
VLMQNQKGKG EAGNSDSMCL RSRKTKSQPA ASTLESKSVQ RVTRSVKRCA ENPKKAEDNV
CVKKIRTRSH RDSEDI
