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Proliferation marker protein Ki-67 (Antigen identified by monoclonal antibody Ki-67) (Antigen KI-67) (Antigen Ki67)

 KI67_HUMAN              Reviewed;        3256 AA.
P46013; Q5VWH2;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
28-NOV-2006, sequence version 2.
27-SEP-2017, entry version 179.
RecName: Full=Proliferation marker protein Ki-67 {ECO:0000305};
AltName: Full=Antigen identified by monoclonal antibody Ki-67 {ECO:0000303|PubMed:8227122};
Short=Antigen KI-67 {ECO:0000305};
Short=Antigen Ki67 {ECO:0000305};
Name=MKI67 {ECO:0000312|HGNC:HGNC:7107};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SHORT AND LONG), AND VARIANTS
VAL-872; TRP-1470; LEU-1622; ALA-1849 AND ASP-3097.
PubMed=8227122; DOI=10.1083/jcb.123.3.513;
Schlueter C., Duchrow M., Wohlenberg C., Becker M.H.G., Key G.,
Flad H.-D., Gerdes J.;
"The cell proliferation-associated antigen of antibody Ki-67: a very
large, ubiquitous nuclear protein with numerous repeated elements,
representing a new kind of cell cycle-maintaining proteins.";
J. Cell Biol. 123:513-522(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.
Gerdes J.;
"Sequence of the human Ki-67 protein gene 5' and promoter region.";
Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
[4]
BIOTECHNOLOGY.
PubMed=6339421; DOI=10.1002/ijc.2910310104;
Gerdes J., Schwab U., Lemke H., Stein H.;
"Production of a mouse monoclonal antibody reactive with a human
nuclear antigen associated with cell proliferation.";
Int. J. Cancer 31:13-20(1983).
[5]
DEVELOPMENTAL STAGE.
PubMed=6206131;
Gerdes J., Lemke H., Baisch H., Wacker H.H., Schwab U., Stein H.;
"Cell cycle analysis of a cell proliferation-associated human nuclear
antigen defined by the monoclonal antibody Ki-67.";
J. Immunol. 133:1710-1715(1984).
[6]
DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
PubMed=2674163;
Verheijen R., Kuijpers H.J., Schlingemann R.O., Boehmer A.L.,
van Driel R., Brakenhoff G.J., Ramaekers F.C.;
"Ki-67 detects a nuclear matrix-associated proliferation-related
antigen. I. Intracellular localization during interphase.";
J. Cell Sci. 92:123-130(1989).
[7]
DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
PubMed=8799815;
Kill I.R.;
"Localisation of the Ki-67 antigen within the nucleolus. Evidence for
a fibrillarin-deficient region of the dense fibrillar component.";
J. Cell Sci. 109:1253-1263(1996).
[8]
SUBCELLULAR LOCATION.
PubMed=9510506; DOI=10.1023/A:1009210206855;
Bridger J.M., Kill I.R., Lichter P.;
"Association of pKi-67 with satellite DNA of the human genome in early
G1 cells.";
Chromosome Res. 6:13-24(1998).
[9]
PHOSPHORYLATION.
PubMed=10502411; DOI=10.1006/excr.1999.4600;
MacCallum D.E., Hall P.A.;
"Biochemical characterization of pKi67 with the identification of a
mitotic-specific form associated with hyperphosphorylation and altered
DNA binding.";
Exp. Cell Res. 252:186-198(1999).
[10]
INTERACTION WITH KIF15.
PubMed=10878014; DOI=10.1074/jbc.M003879200;
Sueishi M., Takagi M., Yoneda Y.;
"The forkhead-associated domain of Ki-67 antigen interacts with the
novel kinesin-like protein Hklp2.";
J. Biol. Chem. 275:28888-28892(2000).
[11]
PHOSPHORYLATION.
PubMed=10653604;
DOI=10.1002/(SICI)1097-4652(200003)182:3<371::AID-JCP8>3.0.CO;2-J;
Endl E., Gerdes J.;
"Posttranslational modifications of the KI-67 protein coincide with
two major checkpoints during mitosis.";
J. Cell. Physiol. 182:371-380(2000).
[12]
FUNCTION, DNA-BINDING, AND SUBCELLULAR LOCATION.
PubMed=10878551;
DOI=10.1002/1096-9896(2000)9999:9999<::AID-PATH628>3.0.CO;2-J;
MacCallum D.E., Hall P.A.;
"The biochemical characterization of the DNA binding activity of
pKi67.";
J. Pathol. 191:286-298(2000).
[13]
INTERACTION WITH NIFK.
PubMed=11342549; DOI=10.1074/jbc.M102227200;
Takagi M., Sueishi M., Saiwaki T., Kametaka A., Yoneda Y.;
"A novel nucleolar protein, NIFK, interacts with the forkhead
associated domain of Ki-67 antigen in mitosis.";
J. Biol. Chem. 276:25386-25391(2001).
[14]
SUBCELLULAR LOCATION.
PubMed=15896774; DOI=10.1016/j.yexcr.2005.04.010;
Saiwaki T., Kotera I., Sasaki M., Takagi M., Yoneda Y.;
"In vivo dynamics and kinetics of pKi-67: transition from a mobile to
an immobile form at the onset of anaphase.";
Exp. Cell Res. 308:123-134(2005).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2406 AND SER-2708, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-328; SER-357; SER-579;
SER-584; SER-1131; THR-1327; THR-1569; THR-1801; THR-1923 AND
THR-2406, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1233; THR-1355; SER-1679
AND THR-1764, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa
cells and high confident phosphopeptide identification by cross-
validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357; SER-579; SER-584
AND SER-1861, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308; SER-357; SER-579;
SER-648 AND SER-1679, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-264; SER-308;
THR-328; THR-347; SER-357; THR-401; SER-579; SER-584; SER-648;
THR-761; SER-859; THR-1017; SER-1071; THR-1091; SER-1098; THR-1111;
SER-1131; THR-1139; SER-1142; SER-1207; SER-1253; SER-1256; THR-1261;
THR-1298; THR-1315; THR-1327; SER-1329; THR-1335; THR-1355; SER-1376;
THR-1383; THR-1503; SER-1506; THR-1540; TYR-1552; THR-1557; THR-1569;
SER-1571; SER-1679; SER-1689; THR-1719; SER-1721; SER-1740; THR-1747;
THR-1784; THR-1801; THR-1841; SER-1861; SER-1864; THR-1869; THR-1923;
THR-2065; SER-2072; THR-2085; SER-2105; THR-2113; THR-2203; SER-2223;
THR-2231; SER-2239; THR-2285; THR-2325; THR-2328; THR-2333; SER-2344;
THR-2352; THR-2389; SER-2395; THR-2406; SER-2528; SER-2588; SER-2708;
SER-2827; SER-2828 AND SER-3041, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[22]
IDENTIFICATION IN A COMPLEX WITH ASCL2; EMSY; HCFC1; HSPA8; CCAR2;
MATR3; RBBP5; TUBB2A; WDR5 AND ZNF335.
PubMed=19131338; DOI=10.1074/jbc.M805872200;
Garapaty S., Xu C.F., Trojer P., Mahajan M.A., Neubert T.A.,
Samuels H.H.;
"Identification and characterization of a novel nuclear protein
complex involved in nuclear hormone receptor-mediated gene
regulation.";
J. Biol. Chem. 284:7542-7552(2009).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-648; SER-1131; THR-1335;
THR-1557; THR-1764; SER-1937; THR-2406 AND SER-2420, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[25]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1639 AND LYS-2005, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308; SER-357; SER-579;
SER-584; SER-648; THR-1091; SER-1098; SER-1131; THR-1167; THR-1193;
SER-1207; THR-1233; THR-1315; THR-1327; SER-1329; THR-1335; THR-1355;
THR-1557; THR-1569; SER-1571; SER-1679; THR-1747; THR-1801; SER-1815;
SER-1861; THR-1897; THR-1923; SER-1937; THR-1963; SER-1983; THR-2065;
SER-2072; THR-2085; SER-2105; SER-2135; SER-2223; THR-2231; THR-2233;
SER-2239; THR-2268; THR-2285; THR-2325; SER-2344; THR-2389; SER-2395;
THR-2406; SER-2420; THR-2446; SER-2528; SER-2588; SER-2708 AND
SER-3128, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[27]
REVIEW ON BIOTECHNOLOGY.
PubMed=21960707; DOI=10.1093/jnci/djr393;
International Ki-67 in Breast Cancer Working Group;
Dowsett M., Nielsen T.O., A'Hern R., Bartlett J., Coombes R.C.,
Cuzick J., Ellis M., Henry N.L., Hugh J.C., Lively T., McShane L.,
Paik S., Penault-Llorca F., Prudkin L., Regan M., Salter J.,
Sotiriou C., Smith I.E., Viale G., Zujewski J.A., Hayes D.F.;
"Assessment of Ki67 in breast cancer: recommendations from the
International Ki67 in Breast Cancer working group.";
J. Natl. Cancer Inst. 103:1656-1664(2011).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308; SER-352; SER-357;
SER-1098; SER-1131; SER-1496; SER-1861; SER-1983; SER-2072; SER-2105;
SER-2344; SER-2528; SER-2588 AND SER-2708, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[29]
INTERACTION WITH ZNF335.
PubMed=23178126; DOI=10.1016/j.cell.2012.10.043;
Yang Y.J., Baltus A.E., Mathew R.S., Murphy E.A., Evrony G.D.,
Gonzalez D.M., Wang E.P., Marshall-Walker C.A., Barry B.J., Murn J.,
Tatarakis A., Mahajan M.A., Samuels H.H., Shi Y., Golden J.A.,
Mahajnah M., Shenhav R., Walsh C.A.;
"Microcephaly gene links trithorax and REST/NRSF to control neural
stem cell proliferation and differentiation.";
Cell 151:1097-1112(2012).
[30]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=22002106; DOI=10.1074/mcp.M111.013680;
Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.;
"Systematic analysis of protein pools, isoforms, and modifications
affecting turnover and subcellular localization.";
Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-128; SER-308;
THR-328; THR-347; SER-357; SER-411; SER-538; THR-543; SER-579;
SER-584; SER-648; THR-761; SER-859; SER-1071; THR-1091; SER-1098;
THR-1111; SER-1131; THR-1176; SER-1207; THR-1233; THR-1327; SER-1329;
THR-1335; THR-1355; THR-1503; THR-1557; THR-1569; SER-1571; THR-1764;
THR-1784; THR-1801; SER-1815; THR-1841; SER-1861; THR-1923; SER-1937;
THR-1963; THR-2065; SER-2072; THR-2085; SER-2105; SER-2135; SER-2223;
THR-2231; THR-2325; SER-2344; THR-2389; THR-2406; SER-2420; THR-2426;
THR-2446; SER-2466; SER-2505; SER-2528; SER-2588; SER-2638 AND
SER-3041, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[32]
FUNCTION, AND INTERACTION WITH PPP1CC.
PubMed=24867636; DOI=10.7554/eLife.01641;
Booth D.G., Takagi M., Sanchez-Pulido L., Petfalski E., Vargiu G.,
Samejima K., Imamoto N., Ponting C.P., Tollervey D., Earnshaw W.C.,
Vagnarelli P.;
"Ki-67 is a PP1-interacting protein that organises the mitotic
chromosome periphery.";
Elife 3:E01641-E01641(2014).
[33]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1035; LYS-1643; LYS-2613;
LYS-2734 AND LYS-2852, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[34]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1093; LYS-2009; LYS-2067;
LYS-2492; LYS-2613; LYS-2734 AND LYS-2852, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[35]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1035; LYS-1643; LYS-2009 AND
LYS-2734, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[36]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1035 AND LYS-1643, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[37]
REVIEW ON BIOTECHNOLOGY.
PubMed=26680267; DOI=10.1136/jclinpath-2015-203340;
Richards-Taylor S., Ewings S.M., Jaynes E., Tilley C., Ellis S.G.,
Armstrong T., Pearce N., Cave J.;
"The assessment of Ki-67 as a prognostic marker in neuroendocrine
tumours: a systematic review and meta-analysis.";
J. Clin. Pathol. 69:612-618(2016).
[38]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=27362226; DOI=10.1038/nature18610;
Cuylen S., Blaukopf C., Politi A.Z., Mueller-Reichert T., Neumann B.,
Poser I., Ellenberg J., Hyman A.A., Gerlich D.W.;
"Ki-67 acts as a biological surfactant to disperse mitotic
chromosomes.";
Nature 535:308-312(2016).
[39]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-245; LYS-1022; LYS-1035;
LYS-1093; LYS-1185; LYS-1188; LYS-1337; LYS-1643; LYS-1703; LYS-2009;
LYS-2067; LYS-2613; LYS-2734; LYS-2852 AND LYS-2967, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[40]
STRUCTURE BY NMR OF 1-120 IN COMPLEX WITH NIFK.
PubMed=14659764; DOI=10.1016/j.jmb.2003.10.032;
Li H., Byeon I.-J., Ju Y., Tsai M.-D.;
"Structure of human Ki67 FHA domain and its binding to a
phosphoprotein fragment from hNIFK reveal unique recognition sites and
new views to the structural basis of FHA domain functions.";
J. Mol. Biol. 335:371-381(2004).
[41]
STRUCTURE BY NMR OF 1-120 IN COMPLEX WITH NIFK.
PubMed=16244663; DOI=10.1038/nsmb1008;
Byeon I.-J., Li H., Song H., Gronenborn A.M., Tsai M.-D.;
"Sequential phosphorylation and multisite interactions characterize
specific target recognition by the FHA domain of Ki67.";
Nat. Struct. Mol. Biol. 12:987-993(2005).
-!- FUNCTION: Required to maintain individual mitotic chromosomes
dispersed in the cytoplasm following nuclear envelope disassembly
(PubMed:27362226). Associates with the surface of the mitotic
chromosome, the perichromosomal layer, and covers a substantial
fraction of the chromosome surface (PubMed:27362226). Prevents
chromosomes from collapsing into a single chromatin mass by
forming a steric and electrostatic charge barrier: the protein has
a high net electrical charge and acts as a surfactant, dispersing
chromosomes and enabling independent chromosome motility
(PubMed:27362226). Binds DNA, with a preference for supercoiled
DNA and AT-rich DNA (PubMed:10878551). Does not contribute to the
internal structure of mitotic chromosomes (By similarity). May
play a role in chromatin organization (PubMed:24867636). It is
however unclear whether it plays a direct role in chromatin
organization or whether it is an indirect consequence of its
function in maintaining mitotic chromosomes dispersed (Probable).
{ECO:0000250|UniProtKB:E9PVX6, ECO:0000269|PubMed:10878551,
ECO:0000269|PubMed:24867636, ECO:0000269|PubMed:27362226}.
-!- SUBUNIT: Interacts with KIF15 (PubMed:10878014). Interacts (via
the FHA domain) with NIFK (PubMed:11342549, PubMed:14659764,
PubMed:16244663). Interacts with PPP1CC (PubMed:24867636). Part of
a complex composed at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2,
MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may
have a histone H3-specific methyltransferase activity
(PubMed:19131338, PubMed:23178126). {ECO:0000269|PubMed:10878014,
ECO:0000269|PubMed:11342549, ECO:0000269|PubMed:14659764,
ECO:0000269|PubMed:16244663, ECO:0000269|PubMed:19131338,
ECO:0000269|PubMed:23178126, ECO:0000269|PubMed:24867636}.
-!- INTERACTION:
Q9NS87:KIF15; NbExp=4; IntAct=EBI-876367, EBI-712159;
-!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:15896774,
ECO:0000269|PubMed:22002106, ECO:0000269|PubMed:27362226,
ECO:0000269|PubMed:9510506}. Nucleus {ECO:0000269|PubMed:10878551,
ECO:0000269|PubMed:22002106}. Nucleus, nucleolus
{ECO:0000269|PubMed:10878551, ECO:0000269|PubMed:22002106,
ECO:0000269|PubMed:2674163, ECO:0000269|PubMed:8799815}.
Note=Associates with the surface of the mitotic chromosome, the
perichromosomal layer, and covers a substantial fraction of the
mitotic chromosome surface (PubMed:27362226). Associates with
satellite DNA in G1 phase (PubMed:9510506). Binds tightly to
chromatin in interphase, chromatin-binding decreases in mitosis
when it associates with the surface of the condensed chromosomes
(PubMed:15896774, PubMed:22002106). Predominantly localized in the
G1 phase in the perinucleolar region, in the later phases it is
also detected throughout the nuclear interior, being predominantly
localized in the nuclear matrix (PubMed:22002106).
{ECO:0000269|PubMed:15896774, ECO:0000269|PubMed:22002106,
ECO:0000269|PubMed:27362226}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=P46013-1; Sequence=Displayed;
Name=Short;
IsoId=P46013-2; Sequence=VSP_004298;
-!- DEVELOPMENTAL STAGE: Expression occurs preferentially during late
G1, S, G2 and M phases of the cell cycle, while in cells in G0
phase the antigen cannot be detected (at protein level)
(PubMed:6206131). Present at highest level in G2 phase and during
mitosis (at protein level). In interphase, forms fiber-like
structures in fibrillarin-deficient regions surrounding nucleoli
(PubMed:2674163, PubMed:8799815). {ECO:0000269|PubMed:2674163,
ECO:0000269|PubMed:6206131, ECO:0000269|PubMed:8799815}.
-!- PTM: Phosphorylated. Hyperphosphorylated in mitosis
(PubMed:10502411, PubMed:10653604). Hyperphosphorylated form does
not bind DNA. {ECO:0000269|PubMed:10502411,
ECO:0000269|PubMed:10653604}.
-!- BIOTECHNOLOGY: Widely used as a marker to assess cell
proliferation, as it is detected in the nucleus of proliferating
cells only (PubMed:6339421, PubMed:21960707). In cancer research
field for example, MKI67 is the most widely used marker for
comparing proliferation between tumor samples (PubMed:21960707,
PubMed:26680267). {ECO:0000269|PubMed:6339421,
ECO:0000303|PubMed:21960707, ECO:0000303|PubMed:26680267}.
-!- CAUTION: Was thought to play a key role in cell proliferation, and
is commonly used as a marker of cell proliferation
(PubMed:6339421, PubMed:21960707). However, its primary function
is uncoupled from cell proliferation: it is required to maintain
mitotic chromosomes dispersed by forming a steric and
electrostatic charge barrier (PubMed:27362226).
{ECO:0000269|PubMed:27362226, ECO:0000269|PubMed:6339421,
ECO:0000303|PubMed:21960707}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Ki-67 entry;
URL="https://en.wikipedia.org/wiki/Ki-67_%28Biology%29";
-!- WEB RESOURCE: Name=Protein Spotlight; Note=The contours of
heredity - Issue 186 of December 2016;
URL="http://web.expasy.org/spotlight/back_issues/186/";
-----------------------------------------------------------------------
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EMBL; X65550; CAA46519.1; -; mRNA.
EMBL; X65551; CAA46520.1; -; mRNA.
EMBL; AL390236; CAH73169.1; -; Genomic_DNA.
EMBL; AL355529; CAH73169.1; JOINED; Genomic_DNA.
EMBL; X94762; CAA64388.1; -; Genomic_DNA.
CCDS; CCDS53588.1; -. [P46013-2]
CCDS; CCDS7659.1; -. [P46013-1]
PIR; A48666; A48666.
RefSeq; NP_001139438.1; NM_001145966.1. [P46013-2]
RefSeq; NP_002408.3; NM_002417.4. [P46013-1]
UniGene; Hs.689823; -.
UniGene; Hs.80976; -.
PDB; 1R21; NMR; -; A=1-120.
PDB; 2AFF; NMR; -; A=1-120.
PDB; 5J28; X-ray; 2.00 A; C/D=496-536.
PDBsum; 1R21; -.
PDBsum; 2AFF; -.
PDBsum; 5J28; -.
ProteinModelPortal; P46013; -.
SMR; P46013; -.
BioGrid; 110434; 53.
DIP; DIP-28132N; -.
IntAct; P46013; 44.
MINT; MINT-137995; -.
STRING; 9606.ENSP00000357643; -.
iPTMnet; P46013; -.
PhosphoSitePlus; P46013; -.
SwissPalm; P46013; -.
BioMuta; MKI67; -.
DMDM; 118572663; -.
EPD; P46013; -.
MaxQB; P46013; -.
PaxDb; P46013; -.
PeptideAtlas; P46013; -.
PRIDE; P46013; -.
Ensembl; ENST00000368653; ENSP00000357642; ENSG00000148773. [P46013-2]
Ensembl; ENST00000368654; ENSP00000357643; ENSG00000148773. [P46013-1]
GeneID; 4288; -.
KEGG; hsa:4288; -.
UCSC; uc001lke.4; human. [P46013-1]
CTD; 4288; -.
DisGeNET; 4288; -.
EuPathDB; HostDB:ENSG00000148773.12; -.
GeneCards; MKI67; -.
HGNC; HGNC:7107; MKI67.
HPA; CAB000058; -.
HPA; CAB068198; -.
HPA; HPA000451; -.
HPA; HPA001164; -.
MIM; 176741; gene.
neXtProt; NX_P46013; -.
OpenTargets; ENSG00000148773; -.
PharmGKB; PA30825; -.
eggNOG; ENOG410JR7C; Eukaryota.
eggNOG; ENOG410ZXYW; LUCA.
GeneTree; ENSGT00530000064425; -.
HOGENOM; HOG000113223; -.
HOVERGEN; HBG006213; -.
InParanoid; P46013; -.
KO; K17582; -.
OMA; QTPKEKA; -.
OrthoDB; EOG091G005S; -.
PhylomeDB; P46013; -.
TreeFam; TF336000; -.
ChiTaRS; MKI67; human.
EvolutionaryTrace; P46013; -.
GeneWiki; Ki-67_(protein); -.
GenomeRNAi; 4288; -.
PRO; PR:P46013; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000148773; -.
CleanEx; HS_MKI67; -.
Genevisible; P46013; HS.
GO; GO:0000775; C:chromosome, centromeric region; IEA:Ensembl.
GO; GO:0000793; C:condensed chromosome; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
GO; GO:0008283; P:cell proliferation; TAS:UniProtKB.
GO; GO:0034605; P:cellular response to heat; IEA:Ensembl.
GO; GO:0006259; P:DNA metabolic process; IEA:Ensembl.
GO; GO:0030212; P:hyaluronan metabolic process; IEA:Ensembl.
GO; GO:0051321; P:meiotic cell cycle; IEA:Ensembl.
GO; GO:1902275; P:regulation of chromatin organization; ISS:UniProtKB.
GO; GO:0051983; P:regulation of chromosome segregation; IDA:UniProtKB.
GO; GO:0007088; P:regulation of mitotic nuclear division; IDA:UniProtKB.
GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
InterPro; IPR000253; FHA_dom.
InterPro; IPR012568; K167R.
InterPro; IPR029334; PP1-bd.
InterPro; IPR008984; SMAD_FHA_domain.
Pfam; PF00498; FHA; 1.
Pfam; PF08065; K167R; 16.
Pfam; PF15276; PP1_bind; 1.
SMART; SM00240; FHA; 1.
SMART; SM01295; K167R; 16.
SUPFAM; SSF49879; SSF49879; 1.
PROSITE; PS50006; FHA_DOMAIN; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; ATP-binding;
Cell cycle; Chromosome; Complete proteome; DNA-binding;
Isopeptide bond; Nucleotide-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Ubl conjugation.
CHAIN 1 3256 Proliferation marker protein Ki-67.
/FTId=PRO_0000084301.
DOMAIN 27 76 FHA. {ECO:0000255|PROSITE-
ProRule:PRU00086}.
DOMAIN 502 549 PP1-binding. {ECO:0000255}.
REPEAT 1001 1112 K167R 1. {ECO:0000255}.
REPEAT 1123 1234 K167R 2. {ECO:0000255}.
REPEAT 1245 1356 K167R 3. {ECO:0000255}.
REPEAT 1367 1477 K167R 4. {ECO:0000255}.
REPEAT 1488 1597 K167R 5. {ECO:0000255}.
REPEAT 1609 1720 K167R 6. {ECO:0000255}.
REPEAT 1731 1842 K167R 7. {ECO:0000255}.
REPEAT 1854 1964 K167R 8. {ECO:0000255}.
REPEAT 1975 2086 K167R 9. {ECO:0000255}.
REPEAT 2097 2204 K167R 10. {ECO:0000255}.
REPEAT 2215 2326 K167R 11. {ECO:0000255}.
REPEAT 2336 2447 K167R 12. {ECO:0000255}.
REPEAT 2458 2569 K167R 13. {ECO:0000255}.
REPEAT 2700 2805 K167R 15. {ECO:0000255}.
REPEAT 2819 2928 K167R 16. {ECO:0000255}.
NP_BIND 3034 3041 ATP. {ECO:0000255}.
REGION 1000 2928 16 X 122 AA approximate repeats.
{ECO:0000305|PubMed:8227122}.
MOD_RES 125 125 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 128 128 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 166 166 Phosphoserine.
{ECO:0000250|UniProtKB:E9PVX6}.
MOD_RES 264 264 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 296 296 Phosphoserine.
{ECO:0000250|UniProtKB:E9PVX6}.
MOD_RES 308 308 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 328 328 Phosphothreonine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 347 347 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 352 352 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 357 357 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 374 374 Phosphoserine.
{ECO:0000250|UniProtKB:E9PVX6}.
MOD_RES 401 401 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 411 411 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 538 538 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 543 543 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 579 579 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 584 584 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 648 648 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 761 761 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 859 859 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1017 1017 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1071 1071 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1091 1091 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1098 1098 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1111 1111 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1131 1131 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1139 1139 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1142 1142 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1167 1167 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1169 1169 Phosphoserine.
{ECO:0000250|UniProtKB:E9PVX6}.
MOD_RES 1176 1176 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1193 1193 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1207 1207 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1233 1233 Phosphothreonine.
{ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1253 1253 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1256 1256 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1261 1261 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1298 1298 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1315 1315 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 1327 1327 Phosphothreonine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1329 1329 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1335 1335 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1355 1355 Phosphothreonine.
{ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1376 1376 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1383 1383 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1386 1386 Phosphoserine.
{ECO:0000250|UniProtKB:E9PVX6}.
MOD_RES 1420 1420 Phosphothreonine.
{ECO:0000250|UniProtKB:E9PVX6}.
MOD_RES 1437 1437 Phosphothreonine.
{ECO:0000250|UniProtKB:E9PVX6}.
MOD_RES 1496 1496 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1503 1503 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1506 1506 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1540 1540 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1552 1552 Phosphotyrosine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1557 1557 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1569 1569 Phosphothreonine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1571 1571 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1617 1617 Phosphoserine.
{ECO:0000250|UniProtKB:E9PVX6}.
MOD_RES 1639 1639 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1679 1679 Phosphoserine.
{ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231}.
MOD_RES 1689 1689 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1719 1719 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1721 1721 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1740 1740 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1747 1747 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 1764 1764 Phosphothreonine.
{ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 1784 1784 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1801 1801 Phosphothreonine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1815 1815 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1841 1841 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1861 1861 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1864 1864 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1869 1869 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1897 1897 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1906 1906 Phosphothreonine.
{ECO:0000250|UniProtKB:E9PVX6}.
MOD_RES 1923 1923 Phosphothreonine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1937 1937 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1963 1963 Phosphothreonine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1983 1983 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 2005 2005 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 2028 2028 Phosphothreonine.
{ECO:0000250|UniProtKB:E9PVX6}.
MOD_RES 2065 2065 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 2072 2072 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 2085 2085 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 2105 2105 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 2113 2113 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 2116 2116 Phosphoserine.
{ECO:0000250|UniProtKB:E9PVX6}.
MOD_RES 2135 2135 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 2146 2146 Phosphothreonine.
{ECO:0000250|UniProtKB:E9PVX6}.
MOD_RES 2163 2163 Phosphothreonine.
{ECO:0000250|UniProtKB:E9PVX6}.
MOD_RES 2203 2203 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 2223 2223 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 2231 2231 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 2233 2233 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 2239 2239 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 2259 2259 Phosphothreonine.
{ECO:0000250|UniProtKB:E9PVX6}.
MOD_RES 2261 2261 Phosphoserine.
{ECO:0000250|UniProtKB:E9PVX6}.
MOD_RES 2268 2268 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 2285 2285 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 2325 2325 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 2328 2328 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 2333 2333 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 2344 2344 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 2352 2352 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 2389 2389 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 2395 2395 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 2406 2406 Phosphothreonine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 2420 2420 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 2426 2426 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2446 2446 Phosphothreonine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 2466 2466 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2505 2505 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2528 2528 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 2588 2588 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 2638 2638 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2708 2708 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 2827 2827 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 2828 2828 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 2838 2838 Phosphoserine.
{ECO:0000250|UniProtKB:E9PVX6}.
MOD_RES 2986 2986 N6-acetyllysine.
{ECO:0000250|UniProtKB:E9PVX6}.
MOD_RES 3041 3041 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 3128 3128 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
CROSSLNK 245 245 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1022 1022 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1035 1035 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 1093 1093 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 1093 1093 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1185 1185 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1188 1188 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1337 1337 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1643 1643 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 1703 1703 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 2009 2009 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 2009 2009 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 2067 2067 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 2067 2067 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 2492 2492 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 2613 2613 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 2613 2613 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 2734 2734 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 2734 2734 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 2852 2852 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 2852 2852 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 2967 2967 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 136 495 Missing (in isoform Short).
{ECO:0000303|PubMed:8227122}.
/FTId=VSP_004298.
VARIANT 104 104 N -> S (in dbSNP:rs2071498).
/FTId=VAR_029055.
VARIANT 238 238 W -> R (in dbSNP:rs7095325).
/FTId=VAR_029056.
VARIANT 497 497 E -> D (in dbSNP:rs11016076).
/FTId=VAR_029057.
VARIANT 574 574 Q -> P (in dbSNP:rs4471342).
/FTId=VAR_029058.
VARIANT 631 631 I -> L (in dbSNP:rs997983).
/FTId=VAR_024161.
VARIANT 832 832 R -> W (in dbSNP:rs34916904).
/FTId=VAR_033995.
VARIANT 854 854 L -> V (in dbSNP:rs2240).
/FTId=VAR_024162.
VARIANT 872 872 A -> V (in dbSNP:rs2853344).
{ECO:0000269|PubMed:8227122}.
/FTId=VAR_029059.
VARIANT 1042 1042 G -> S (in dbSNP:rs2152143).
/FTId=VAR_024163.
VARIANT 1120 1120 T -> S (in dbSNP:rs11016074).
/FTId=VAR_029060.
VARIANT 1247 1247 T -> I (in dbSNP:rs4750685).
/FTId=VAR_021838.
VARIANT 1403 1403 E -> V (in dbSNP:rs3740423).
/FTId=VAR_020047.
VARIANT 1470 1470 L -> W (in dbSNP:rs2853345).
{ECO:0000269|PubMed:8227122}.
/FTId=VAR_029061.
VARIANT 1559 1559 V -> M (in dbSNP:rs7918199).
/FTId=VAR_029062.
VARIANT 1622 1622 P -> L (in dbSNP:rs2782871).
{ECO:0000269|PubMed:8227122}.
/FTId=VAR_029063.
VARIANT 1849 1849 T -> A (in dbSNP:rs2782872).
{ECO:0000269|PubMed:8227122}.
/FTId=VAR_029064.
VARIANT 1876 1876 R -> Q (in dbSNP:rs11591817).
/FTId=VAR_029065.
VARIANT 1951 1951 L -> I (in dbSNP:rs34116632).
/FTId=VAR_033996.
VARIANT 2101 2101 I -> T (in dbSNP:rs11016073).
/FTId=VAR_029066.
VARIANT 2337 2337 T -> N (in dbSNP:rs7083622).
/FTId=VAR_024164.
VARIANT 2363 2363 N -> S (in dbSNP:rs7071768).
/FTId=VAR_029067.
VARIANT 2607 2607 R -> H (in dbSNP:rs34688192).
/FTId=VAR_061671.
VARIANT 2608 2608 P -> L (in dbSNP:rs1063535).
/FTId=VAR_024165.
VARIANT 2649 2649 R -> H (in dbSNP:rs12777740).
/FTId=VAR_029068.
VARIANT 2720 2720 T -> P (in dbSNP:rs1050767).
/FTId=VAR_024166.
VARIANT 2760 2760 D -> G (in dbSNP:rs10082391).
/FTId=VAR_029069.
VARIANT 2786 2786 R -> Q (in dbSNP:rs10764749).
/FTId=VAR_029070.
VARIANT 2793 2793 S -> N (in dbSNP:rs10082533).
/FTId=VAR_029071.
VARIANT 2845 2845 R -> H (in dbSNP:rs11016072).
/FTId=VAR_029072.
VARIANT 2868 2868 T -> S (in dbSNP:rs2071496).
/FTId=VAR_024167.
VARIANT 2904 2904 Q -> R (in dbSNP:rs11016071).
/FTId=VAR_029073.
VARIANT 3097 3097 N -> D (in dbSNP:rs2798669).
{ECO:0000269|PubMed:8227122}.
/FTId=VAR_029074.
VARIANT 3102 3102 E -> G (in dbSNP:rs34750407).
/FTId=VAR_033997.
VARIANT 3150 3150 T -> S (in dbSNP:rs11106).
/FTId=VAR_014858.
VARIANT 3217 3217 K -> E (in dbSNP:rs8473).
/FTId=VAR_014859.
CONFLICT 619 626 RKSGNLPS -> ERVATCLQ (in Ref. 1;
CAA46519/CAA46520). {ECO:0000305}.
CONFLICT 2205 2205 I -> V (in Ref. 1; CAA46519/CAA46520).
{ECO:0000305}.
CONFLICT 2892 2893 KL -> NV (in Ref. 1; CAA46519/CAA46520).
{ECO:0000305}.
CONFLICT 3246 3246 R -> T (in Ref. 1; CAA46519/CAA46520).
{ECO:0000305}.
STRAND 5 12 {ECO:0000244|PDB:1R21}.
STRAND 15 21 {ECO:0000244|PDB:1R21}.
STRAND 24 32 {ECO:0000244|PDB:1R21}.
STRAND 35 38 {ECO:0000244|PDB:1R21}.
STRAND 49 53 {ECO:0000244|PDB:1R21}.
STRAND 58 60 {ECO:0000244|PDB:1R21}.
STRAND 65 67 {ECO:0000244|PDB:1R21}.
STRAND 80 82 {ECO:0000244|PDB:2AFF}.
STRAND 86 89 {ECO:0000244|PDB:1R21}.
STRAND 94 99 {ECO:0000244|PDB:1R21}.
STRAND 515 517 {ECO:0000244|PDB:5J28}.
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


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