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 27-MAR-2024, entry version 225. 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 CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 621. DR DIP; DIP-28132N; -. DR IntAct; P46013; 510. DR MINT; P46013; -. DR STRING; 9606.ENSP00000357643; -. DR CarbonylDB; P46013; -. DR GlyCosmos; P46013; 1 site, 1 glycan. DR GlyGen; P46013; 25 sites, 1 O-linked glycan (25 sites). DR iPTMnet; P46013; -. DR MetOSite; P46013; -. DR PhosphoSitePlus; P46013; -. DR SwissPalm; P46013; -. DR BioMuta; MKI67; -. DR DMDM; 118572663; -. DR CPTAC; CPTAC-5908; -. DR CPTAC; CPTAC-5909; -. DR CPTAC; CPTAC-5910; -. DR EPD; P46013; -. DR jPOST; P46013; -. DR MassIVE; P46013; -. DR MaxQB; P46013; -. DR PaxDb; 9606-ENSP00000357643; -. DR PeptideAtlas; P46013; -. DR ProteomicsDB; 55705; -. [P46013-1] DR ProteomicsDB; 55706; -. [P46013-2] DR Pumba; P46013; -. DR Antibodypedia; 741; 2754 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 AGR; HGNC:7107; -. DR CTD; 4288; -. DR DisGeNET; 4288; -. DR GeneCards; MKI67; -. DR HGNC; HGNC:7107; MKI67. DR HPA; ENSG00000148773; Group enriched (bone marrow, lymphoid tissue). DR MalaCards; MKI67; -. 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; KNRAQPL; -. DR OrthoDB; 3140593at2759; -. DR PhylomeDB; P46013; -. DR TreeFam; TF336000; -. DR PathwayCommons; P46013; -. DR SignaLink; P46013; -. DR SIGNOR; P46013; -. DR BioGRID-ORCS; 4288; 18 hits in 1174 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 141 other cell types or tissues. 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:HPA. 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: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; cd22673; FHA_Ki67; 1. DR Gene3D; 2.60.200.20; -; 1. DR InterPro; IPR000253; FHA_dom. DR InterPro; IPR012568; KI67R. DR InterPro; IPR029334; PP1-bd. DR InterPro; IPR008984; SMAD_FHA_dom_sf. DR PANTHER; PTHR21603; ANTIGEN KI-67-LIKE PROTEIN; 1. DR PANTHER; PTHR21603:SF17; PROLIFERATION MARKER PROTEIN KI-67; 1. 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; SMAD/FHA domain; 1. DR PROSITE; PS50006; FHA_DOMAIN; 1. DR Genevisible; P46013; HS. 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 //