ID PLK1_HUMAN Reviewed; 603 AA. AC P53350; Q15153; Q99746; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 27-MAR-2024, entry version 246. DE RecName: Full=Serine/threonine-protein kinase PLK1; DE EC=2.7.11.21 {ECO:0000269|PubMed:11202906, ECO:0000269|PubMed:12207013, ECO:0000269|PubMed:21880710, ECO:0000269|PubMed:37440612, ECO:0000269|PubMed:37674080}; DE AltName: Full=Polo-like kinase 1; DE Short=PLK-1; DE AltName: Full=Serine/threonine-protein kinase 13; DE Short=STPK13; GN Name=PLK1; Synonyms=PLK; 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]. RC TISSUE=Placenta; RX PubMed=8018557; RA Hamanaka R., Maloid S., Smith M.R., O'Connell C.D., Longo D.L., RA Ferris D.K.; RT "Cloning and characterization of human and murine homologues of the RT Drosophila polo serine-threonine kinase."; RL Cell Growth Differ. 5:249-257(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=7902533; DOI=10.1128/mcb.13.12.7793-7801.1993; RA Lake R.J., Jelinek W.R.; RT "Cell cycle- and terminal differentiation-associated regulation of the RT mouse mRNA encoding a conserved mitotic protein kinase."; RL Mol. Cell. Biol. 13:7793-7801(1993). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=7962193; DOI=10.1242/jcs.107.6.1509; RA Golsteyn R.M., Schultz S.J., Bartek J., Ziemiecki A., Ried T., Nigg E.A.; RT "Cell cycle analysis and chromosomal localization of human Plk1, a putative RT homologue of the mitotic kinases Drosophila polo and Saccharomyces RT cerevisiae Cdc5."; RL J. Cell Sci. 107:1509-1517(1994). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Lung; RX PubMed=8127874; DOI=10.1073/pnas.91.5.1736; RA Holtrich U., Wolf G., Braeuninger A., Karn T., Boehme B., RA Ruebsamen-Waigmann H., Strebhardt K.; RT "Induction and down-regulation of PLK, a human serine/threonine kinase RT expressed in proliferating cells and tumors."; RL Proc. Natl. Acad. Sci. U.S.A. 91:1736-1740(1994). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Colon, and Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-136. RX PubMed=7478607; RA Brauninger A., Strebhardt K., Rubsamen-Waigmann H.; RT "Identification and functional characterization of the human and murine RT polo-like kinase (Plk) promoter."; RL Oncogene 11:1793-1800(1995). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-136. RX PubMed=9083047; DOI=10.1074/jbc.272.14.9166; RA Uchiumi T., Longo D.L., Ferris D.K.; RT "Cell cycle regulation of the human polo-like kinase (PLK) promoter."; RL J. Biol. Chem. 272:9166-9174(1997). RN [8] RP FUNCTION IN CENTROSOME MATURATION, AND SUBCELLULAR LOCATION. RX PubMed=8991084; DOI=10.1083/jcb.135.6.1701; RA Lane H.A., Nigg E.A.; RT "Antibody microinjection reveals an essential role for human polo-like RT kinase 1 (Plk1) in the functional maturation of mitotic centrosomes."; RL J. Cell Biol. 135:1701-1713(1996). RN [9] RP FUNCTION IN PHOSPHORYLATION OF CDC25C. RX PubMed=11202906; DOI=10.1016/s0898-6568(00)00080-2; RA Roshak A.K., Capper E.A., Imburgia C., Fornwald J., Scott G., RA Marshall L.A.; RT "The human polo-like kinase, PLK, regulates cdc2/cyclin B through RT phosphorylation and activation of the cdc25C phosphatase."; RL Cell. Signal. 12:405-411(2000). RN [10] RP FUNCTION, PHOSPHORYLATION AT SER-137 AND THR-210, AND MUTAGENESIS OF RP LYS-82; SER-137 AND THR-210. RX PubMed=12207013; DOI=10.1074/jbc.m202172200; RA Jang Y.-J., Ma S., Terada Y., Erikson R.L.; RT "Phosphorylation of threonine 210 and the role of serine 137 in the RT regulation of mammalian polo-like kinase."; RL J. Biol. Chem. 277:44115-44120(2002). RN [11] RP FUNCTION IN PHOSPHORYLATION OF CCNB1, SUBCELLULAR LOCATION, AND MUTAGENESIS RP OF LYS-82 AND THR-210. RX PubMed=12447691; DOI=10.1038/sj.onc.1206011; RA Yuan J., Eckerdt F., Bereiter-Hahn J., Kurunci-Csacsko E., Kaufmann M., RA Strebhardt K.; RT "Cooperative phosphorylation including the activity of polo-like kinase 1 RT regulates the subcellular localization of cyclin B1."; RL Oncogene 21:8282-8292(2002). RN [12] RP PHOSPHORYLATION AT SER-335. RX PubMed=12442251; RX DOI=10.1002/1615-9861(200211)2:11<1516::aid-prot1516>3.0.co;2-y; RA Wind M., Kelm O., Nigg E.A., Lehmann W.D.; RT "Identification of phosphorylation sites in the polo-like kinases Plx1 and RT Plk1 by a novel strategy based on element and electrospray high resolution RT mass spectrometry."; RL Proteomics 2:1516-1523(2002). RN [13] RP FUNCTION IN PHOSPHORYLATION OF NINL. RX PubMed=12852856; DOI=10.1016/s1534-5807(03)00193-x; RA Casenghi M., Meraldi P., Weinhart U., Duncan P.I., Korner R., Nigg E.A.; RT "Polo-like kinase 1 regulates Nlp, a centrosome protein involved in RT microtubule nucleation."; RL Dev. Cell 5:113-125(2003). RN [14] RP PHOSPHORYLATION BY STK10. RX PubMed=12639966; DOI=10.1074/jbc.m212556200; RA Walter S.A., Cutler R.E. Jr., Martinez R., Gishizky M., Hill R.J.; RT "Stk10, a new member of the polo-like kinase kinase family highly expressed RT in hematopoietic tissue."; RL J. Biol. Chem. 278:18221-18228(2003). RN [15] RP FUNCTION IN PHOSPHORYLATION OF PKMYT1. RX PubMed=12738781; DOI=10.1074/jbc.c300126200; RA Nakajima H., Toyoshima-Morimoto F., Taniguchi E., Nishida E.; RT "Identification of a consensus motif for Plk (Polo-like kinase) RT phosphorylation reveals Myt1 as a Plk1 substrate."; RL J. Biol. Chem. 278:25277-25280(2003). RN [16] RP FUNCTION IN PHOSPHORYLATION OF KIF20A, DOMAIN POLO BOX, AND SUBCELLULAR RP LOCATION. RX PubMed=12939256; DOI=10.1083/jcb.200306009; RA Neef R., Preisinger C., Sutcliffe J., Kopajtich R., Nigg E.A., Mayer T.U., RA Barr F.A.; RT "Phosphorylation of mitotic kinesin-like protein 2 by polo-like kinase 1 is RT required for cytokinesis."; RL J. Cell Biol. 162:863-875(2003). RN [17] RP FUNCTION IN PHOSPHORYLATION OF CCNB1, AND SUBCELLULAR LOCATION. RX PubMed=12524548; DOI=10.1038/ncb918; RA Jackman M., Lindon C., Nigg E.A., Pines J.; RT "Active cyclin B1-Cdk1 first appears on centrosomes in prophase."; RL Nat. Cell Biol. 5:143-148(2003). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE RP ANALYSIS]. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [19] RP FUNCTION, PROTEASOMAL DEGRADATION, DOMAIN D-BOX MOTIF, AND MUTAGENESIS OF RP ARG-337 AND LEU-340. RX PubMed=14734534; DOI=10.1083/jcb.200309035; RA Lindon C., Pines J.; RT "Ordered proteolysis in anaphase inactivates Plk1 to contribute to proper RT mitotic exit in human cells."; RL J. Cell Biol. 164:233-241(2004). RN [20] RP FUNCTION IN PHOSPHORYLATION OF FBXO5. RX PubMed=15469984; DOI=10.1091/mbc.e04-07-0598; RA Hansen D.V., Loktev A.V., Ban K.H., Jackson P.K.; RT "Plk1 regulates activation of the anaphase promoting complex by RT phosphorylating and triggering SCFbetaTrCP-dependent destruction of the APC RT inhibitor Emi1."; RL Mol. Biol. Cell 15:5623-5634(2004). RN [21] RP FUNCTION IN PHOSPHORYLATION OF WEE1. RX PubMed=15070733; DOI=10.1073/pnas.0307700101; RA Watanabe N., Arai H., Nishihara Y., Taniguchi M., Watanabe N., Hunter T., RA Osada H.; RT "M-phase kinases induce phospho-dependent ubiquitination of somatic Wee1 by RT SCFbeta-TrCP."; RL Proc. Natl. Acad. Sci. U.S.A. 101:4419-4424(2004). RN [22] RP FUNCTION IN PHOSPHORYLATION OF FBXO5. RX PubMed=15148369; DOI=10.1073/pnas.0402442101; RA Moshe Y., Boulaire J., Pagano M., Hershko A.; RT "Role of Polo-like kinase in the degradation of early mitotic inhibitor 1, RT a regulator of the anaphase promoting complex/cyclosome."; RL Proc. Natl. Acad. Sci. U.S.A. 101:7937-7942(2004). RN [23] RP FUNCTION IN PHOSPHORYLATION OF CEP55. RX PubMed=16198290; DOI=10.1016/j.devcel.2005.09.003; RA Fabbro M., Zhou B.-B., Takahashi M., Sarcevic B., Lal P., Graham M.E., RA Gabrielli B.G., Robinson P.J., Nigg E.A., Ono Y., Khanna K.K.; RT "Cdk1/Erk2- and Plk1-dependent phosphorylation of a centrosome protein, RT Cep55, is required for its recruitment to midbody and cytokinesis."; RL Dev. Cell 9:477-488(2005). RN [24] RP FUNCTION IN PHOSPHORYLATION OF HSF1. RX PubMed=15661742; DOI=10.1074/jbc.m411908200; RA Kim S.A., Yoon J.H., Lee S.H., Ahn S.G.; RT "Polo-like kinase 1 phosphorylates heat shock transcription factor 1 and RT mediates its nuclear translocation during heat stress."; RL J. Biol. Chem. 280:12653-12657(2005). RN [25] RP INTERACTION WITH CEP170. RX PubMed=15616186; DOI=10.1091/mbc.e04-10-0939; RA Guarguaglini G., Duncan P.I., Stierhof Y.D., Holmstroem T., Duensing S., RA Nigg E.A.; RT "The forkhead-associated domain protein Cep170 interacts with Polo-like RT kinase 1 and serves as a marker for mature centrioles."; RL Mol. Biol. Cell 16:1095-1107(2005). RN [26] RP INTERACTION WITH EVI5. RX PubMed=16439210; DOI=10.1016/j.cell.2005.10.038; RA Eldridge A.G., Loktev A.V., Hansen D.V., Verschuren E.W., Reimann J.D.R., RA Jackson P.K.; RT "The evi5 oncogene regulates cyclin accumulation by stabilizing the RT anaphase-promoting complex inhibitor emi1."; RL Cell 124:367-380(2006). RN [27] RP SUBCELLULAR LOCATION, INTERACTION WITH BUB1, AND MUTAGENESIS OF HIS-538 AND RP LYS-540. RX PubMed=16760428; DOI=10.1091/mbc.e06-03-0240; RA Qi W., Tang Z., Yu H.; RT "Phosphorylation- and polo-box-dependent binding of Plk1 to Bub1 is RT required for the kinetochore localization of Plk1."; RL Mol. Biol. Cell 17:3705-3716(2006). RN [28] RP FUNCTION IN PHOSPHORYLATION OF KIZ. RX PubMed=16980960; DOI=10.1038/ncb1474; RA Oshimori N., Ohsugi M., Yamamoto T.; RT "The Plk1 target Kizuna stabilizes mitotic centrosomes to ensure spindle RT bipolarity."; RL Nat. Cell Biol. 8:1095-1101(2006). RN [29] RP FUNCTION IN PHOSPHORYLATION OF ECT2. RX PubMed=16247472; DOI=10.1038/sj.onc.1209124; RA Niiya F., Tatsumoto T., Lee K.S., Miki T.; RT "Phosphorylation of the cytokinesis regulator ECT2 at G2/M phase stimulates RT association of the mitotic kinase Plk1 and accumulation of GTP-bound RT RhoA."; RL Oncogene 25:827-837(2006). RN [30] RP FUNCTION IN PHOSPHORYLATION OF CENPU. RX PubMed=17081991; DOI=10.1016/j.molcel.2006.10.016; RA Kang Y.H., Park J.-E., Yu L.-R., Soung N.-K., Yun S.-M., Bang J.K., RA Seong Y.-S., Yu H., Garfield S., Veenstra T.D., Lee K.S.; RT "Self-regulated Plk1 recruitment to kinetochores by the Plk1-PBIP1 RT interaction is critical for proper chromosome segregation."; RL Mol. Cell 24:409-422(2006). RN [31] RP INVOLVEMENT IN CANCER. RX PubMed=16645325; DOI=10.1159/000093003; RA Kanaji S., Saito H., Tsujitani S., Matsumoto S., Tatebe S., Kondo A., RA Ozaki M., Ito H., Ikeguchi M.; RT "Expression of polo-like kinase 1 (PLK1) protein predicts the survival of RT patients with gastric carcinoma."; RL Oncology 70:126-133(2006). RN [32] RP INVOLVEMENT IN CANCER. RX PubMed=17981789; DOI=10.1158/0008-5472.can-07-1887; RA Salvatore G., Nappi T.C., Salerno P., Jiang Y., Garbi C., Ugolini C., RA Miccoli P., Basolo F., Castellone M.D., Cirafici A.M., Melillo R.M., RA Fusco A., Bittner M.L., Santoro M.; RT "A cell proliferation and chromosomal instability signature in anaplastic RT thyroid carcinoma."; RL Cancer Res. 67:10148-10158(2007). RN [33] RP FUNCTION. RX PubMed=17218258; DOI=10.1016/j.cell.2006.11.041; RA Baumann C., Koerner R., Hofmann K., Nigg E.A.; RT "PICH, a centromere-associated SNF2 family ATPase, is regulated by Plk1 and RT required for the spindle checkpoint."; RL Cell 128:101-114(2007). RN [34] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=17617734; DOI=10.4161/cc.6.13.4442; RA Pouwels J., Kukkonen A.M., Lan W., Daum J.R., Gorbsky G.J., Stukenberg T., RA Kallio M.J.; RT "Shugoshin 1 plays a central role in kinetochore assembly and is required RT for kinetochore targeting of Plk1."; RL Cell Cycle 6:1579-1585(2007). RN [35] RP INTERACTION WITH TTDN1. RX PubMed=17310276; DOI=10.1007/s00018-007-6501-8; RA Zhang Y., Tian Y., Chen Q., Chen D., Zhai Z., Shu H.-B.; RT "TTDN1 is a Plk1-interacting protein involved in maintenance of cell cycle RT integrity."; RL Cell. Mol. Life Sci. 64:632-640(2007). RN [36] RP FUNCTION IN PHOSPHORYLATION OF BUB1B. RX PubMed=17376779; DOI=10.1074/jbc.m611053200; RA Matsumura S., Toyoshima F., Nishida E.; RT "Polo-like kinase 1 facilitates chromosome alignment during prometaphase RT through BubR1."; RL J. Biol. Chem. 282:15217-15227(2007). RN [37] RP INVOLVEMENT IN CANCER. RX PubMed=17943598; DOI=10.1080/10428190701615918; RA Liu L., Zhang M., Zou P.; RT "Expression of PLK1 and survivin in diffuse large B-cell lymphoma."; RL Leuk. Lymphoma 48:2179-2183(2007). RN [38] RP FUNCTION IN PHOSPHORYLATION OF PRC1, AND DOMAIN POLO BOX. RX PubMed=17351640; DOI=10.1038/ncb1557; RA Neef R., Gruneberg U., Kopajtich R., Li X., Nigg E.A., Sillje H., RA Barr F.A.; RT "Choice of Plk1 docking partners during mitosis and cytokinesis is RT controlled by the activation state of Cdk1."; RL Nat. Cell Biol. 9:436-444(2007). RN [39] RP INTERACTION WITH CYLD, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=17495026; DOI=10.1073/pnas.0703268104; RA Stegmeier F., Sowa M.E., Nalepa G., Gygi S.P., Harper J.W., Elledge S.J.; RT "The tumor suppressor CYLD regulates entry into mitosis."; RL Proc. Natl. Acad. Sci. U.S.A. 104:8869-8874(2007). RN [40] RP FUNCTION IN PHOSPHORYLATION OF HSF1, AND SUBCELLULAR LOCATION. RX PubMed=18794143; DOI=10.1158/0008-5472.can-08-0129; RA Lee Y.J., Kim E.H., Lee J.S., Jeoung D., Bae S., Kwon S.H., Lee Y.S.; RT "HSF1 as a mitotic regulator: phosphorylation of HSF1 by Plk1 is essential RT for mitotic progression."; RL Cancer Res. 68:7550-7560(2008). RN [41] RP FUNCTION, UBIQUITINATION BY THE APC/C COMPLEX, INTERACTION WITH FZR1, AND RP MUTAGENESIS OF ARG-337 AND LEU-340. RX PubMed=18662541; DOI=10.1016/j.cell.2008.05.043; RA Bassermann F., Frescas D., Guardavaccaro D., Busino L., Peschiaroli A., RA Pagano M.; RT "The Cdc14B-Cdh1-Plk1 axis controls the G2 DNA-damage-response RT checkpoint."; RL Cell 134:256-267(2008). RN [42] RP INTERACTION WITH BIRC6/BRUCE. RX PubMed=18329369; DOI=10.1016/j.cell.2008.01.012; RA Pohl C., Jentsch S.; RT "Final stages of cytokinesis and midbody ring formation are controlled by RT BRUCE."; RL Cell 132:832-845(2008). RN [43] RP FUNCTION IN PHOSPHORYLATION OF TP73. RX PubMed=18418051; DOI=10.4161/cc.7.9.5777; RA Soond S.M., Barry S.P., Melino G., Knight R.A., Latchman D.S., RA Stephanou A.; RT "p73-mediated transcriptional activity is negatively regulated by polo-like RT kinase 1."; RL Cell Cycle 7:1214-1223(2008). RN [44] RP FUNCTION. RX PubMed=18521620; DOI=10.1007/s00412-008-0165-5; RA Chan E.H., Santamaria A., Sillje H.H., Nigg E.A.; RT "Plk1 regulates mitotic Aurora A function through betaTrCP-dependent RT degradation of hBora."; RL Chromosoma 117:457-469(2008). RN [45] RP FUNCTION IN PHOSPHORYLATION OF SGO1. RX PubMed=18331714; DOI=10.1016/j.devcel.2007.12.007; RA Wang X., Yang Y., Duan Q., Jiang N., Huang Y., Darzynkiewicz Z., Dai W.; RT "sSgo1, a major splice variant of Sgo1, functions in centriole cohesion RT where it is regulated by Plk1."; RL Dev. Cell 14:331-341(2008). RN [46] RP FUNCTION IN PHOSPHORYLATION OF PPP1R12A, PHOSPHORYLATION AT THR-210, RP DEPHOSPHORYLATION BY PPP1C, SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP HIS-538 AND LYS-540. RX PubMed=18477460; DOI=10.1016/j.devcel.2008.02.013; RA Yamashiro S., Yamakita Y., Totsukawa G., Goto H., Kaibuchi K., Ito M., RA Hartshorne D.J., Matsumura F.; RT "Myosin phosphatase-targeting subunit 1 regulates mitosis by antagonizing RT polo-like kinase 1."; RL Dev. Cell 14:787-797(2008). RN [47] RP FUNCTION IN PHOSPHORYLATION OF TP73, AND MUTAGENESIS OF LYS-82. RX PubMed=18174154; DOI=10.1074/jbc.m710608200; RA Koida N., Ozaki T., Yamamoto H., Ono S., Koda T., Ando K., Okoshi R., RA Kamijo T., Omura K., Nakagawara A.; RT "Inhibitory role of Plk1 in the regulation of p73-dependent apoptosis RT through physical interaction and phosphorylation."; RL J. Biol. Chem. 283:8555-8563(2008). RN [48] RP INTERACTION WITH FAM29A. RX PubMed=19029337; DOI=10.1083/jcb.200807046; RA Zhu H., Coppinger J.A., Jang C.-Y., Yates J.R. III, Fang G.; RT "FAM29A promotes microtubule amplification via recruitment of the NEDD1- RT gamma-tubulin complex to the mitotic spindle."; RL J. Cell Biol. 183:835-848(2008). RN [49] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-6; SER-103; THR-210; THR-214; RP SER-375; SER-450 AND THR-498, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE 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 [50] RP FUNCTION IN PHOSPHORYLATION OF FOXM1, AND MUTAGENESIS OF LYS-82 AND RP THR-210. RX PubMed=19160488; DOI=10.1038/ncb1767; RA Fu Z., Malureanu L., Huang J., Wang W., Li H., van Deursen J.M., RA Tindall D.J., Chen J.; RT "Plk1-dependent phosphorylation of FoxM1 regulates a transcriptional RT programme required for mitotic progression."; RL Nat. Cell Biol. 10:1076-1082(2008). RN [51] RP FUNCTION, ACTIVITY REGULATION, PHOSPHORYLATION AT THR-210 BY AURKA, RP SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-82; SER-137; ASP-176 AND THR-210, RP AND ACTIVE SITE. RX PubMed=18615013; DOI=10.1038/nature07185; RA Macurek L., Lindqvist A., Lim D., Lampson M.A., Klompmaker R., Freire R., RA Clouin C., Taylor S.S., Yaffe M.B., Medema R.H.; RT "Polo-like kinase-1 is activated by aurora A to promote checkpoint RT recovery."; RL Nature 455:119-123(2008). RN [52] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-210 AND THR-214, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [53] RP INTERACTION WITH SLX4. RX PubMed=19596235; DOI=10.1016/j.cell.2009.06.030; RA Svendsen J.M., Smogorzewska A., Sowa M.E., O'Connell B.C., Gygi S.P., RA Elledge S.J., Harper J.W.; RT "Mammalian BTBD12/SLX4 assembles a Holliday junction resolvase and is RT required for DNA repair."; RL Cell 138:63-77(2009). RN [54] RP FUNCTION IN PHOSPHORYLATION OF TOPORS. RX PubMed=19473992; DOI=10.1074/jbc.c109.001560; RA Yang X., Li H., Zhou Z., Wang W.H., Deng A., Andrisani O., Liu X.; RT "Plk1-mediated phosphorylation of Topors regulates p53 stability."; RL J. Biol. Chem. 284:18588-18592(2009). RN [55] RP FUNCTION AS NEDD1 KINASE. RX PubMed=19509060; DOI=10.1242/jcs.042747; RA Zhang X., Chen Q., Feng J., Hou J., Yang F., Liu J., Jiang Q., Zhang C.; RT "Sequential phosphorylation of Nedd1 by Cdk1 and Plk1 is required for RT targeting of the gammaTuRC to the centrosome."; RL J. Cell Sci. 122:2240-2251(2009). RN [56] RP FUNCTION, INTERACTION WITH KIF2A, AND SUBCELLULAR LOCATION. RX PubMed=19351716; DOI=10.1242/jcs.044321; RA Jang C.Y., Coppinger J.A., Seki A., Yates J.R. III, Fang G.; RT "Plk1 and Aurora A regulate the depolymerase activity and the cellular RT localization of Kif2a."; RL J. Cell Sci. 122:1334-1341(2009). RN [57] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-210 AND THR-214, AND RP IDENTIFICATION BY 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 [58] RP FUNCTION IN PHOSPHORYLATION OF RACGAP1, AND SUBCELLULAR LOCATION. RX PubMed=19468300; DOI=10.1371/journal.pbio.1000110; RA Wolfe B.A., Takaki T., Petronczki M., Glotzer M.; RT "Polo-like kinase 1 directs assembly of the HsCyk-4 RhoGAP/Ect2 RhoGEF RT complex to initiate cleavage furrow formation."; RL PLoS Biol. 7:E1000110-E1000110(2009). RN [59] RP FUNCTION IN PHOSPHORYLATION OF RACGAP1, SUBCELLULAR LOCATION, AND RP MUTAGENESIS OF CYS-67; LEU-130; HIS-538 AND LYS-540. RX PubMed=19468302; DOI=10.1371/journal.pbio.1000111; RA Burkard M.E., Maciejowski J., Rodriguez-Bravo V., Repka M., Lowery D.M., RA Clauser K.R., Zhang C., Shokat K.M., Carr S.A., Yaffe M.B., RA Jallepalli P.V.; RT "Plk1 self-organization and priming phosphorylation of HsCYK-4 at the RT spindle midzone regulate the onset of division in human cells."; RL PLoS Biol. 7:E1000111-E1000111(2009). RN [60] RP REVIEW ON FUNCTION, AND REVIEW ON ACTIVITY REGULATION. RX PubMed=20671765; DOI=10.1038/nrd3184; RA Strebhardt K.; RT "Multifaceted polo-like kinases: drug targets and antitargets for cancer RT therapy."; RL Nat. Rev. Drug Discov. 9:643-660(2010). RN [61] RP FUNCTION IN PHOSPHORYLATION OF DCTN1, AND INTERACTION WITH DCTN1. RX PubMed=20679239; DOI=10.1073/pnas.1006615107; RA Li H., Liu X.S., Yang X., Song B., Wang Y., Liu X.; RT "Polo-like kinase 1 phosphorylation of p150Glued facilitates nuclear RT envelope breakdown during prophase."; RL Proc. Natl. Acad. Sci. U.S.A. 107:14633-14638(2010). RN [62] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-210, AND IDENTIFICATION BY RP 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 [63] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [64] RP FUNCTION IN PHOSPHORYLATION OF RIOK2, AND MUTAGENESIS OF LYS-82. RX PubMed=21880710; DOI=10.1074/jbc.m111.250175; RA Liu T., Deng M., Li J., Tong X., Wei Q., Ye X.; RT "Phosphorylation of right open reading frame 2 (Rio2) protein kinase by RT polo-like kinase 1 regulates mitotic progression."; RL J. Biol. Chem. 286:36352-36360(2011). RN [65] RP IDENTIFICATION IN A COMPLEX WITH KNSTRN; SPAG5; DYNLL1 AND SGO2. RX PubMed=21402792; DOI=10.1083/jcb.201008023; RA Dunsch A.K., Linnane E., Barr F.A., Gruneberg U.; RT "The astrin-kinastrin/SKAP complex localizes to microtubule plus ends and RT facilitates chromosome alignment."; RL J. Cell Biol. 192:959-968(2011). RN [66] RP INTERACTION WITH FRY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-194. RX PubMed=22753416; DOI=10.1074/jbc.m112.378968; RA Ikeda M., Chiba S., Ohashi K., Mizuno K.; RT "Furry protein promotes Aurora A-mediated polo-like kinase 1 activation."; RL J. Biol. Chem. 287:27670-27681(2012). RN [67] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=22325354; DOI=10.1016/j.molcel.2011.12.028; RA Yata K., Lloyd J., Maslen S., Bleuyard J.Y., Skehel M., Smerdon S.J., RA Esashi F.; RT "Plk1 and CK2 act in concert to regulate Rad51 during DNA double strand RT break repair."; RL Mol. Cell 45:371-383(2012). RN [68] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [69] RP INTERACTION WITH KLHL22. RX PubMed=24067371; DOI=10.4161/cc.25369; RA Metzger T., Kleiss C., Sumara I.; RT "CUL3 and protein kinases: insights from PLK1/KLHL22 interaction."; RL Cell Cycle 12:2291-2296(2013). RN [70] RP INTERACTION WITH CEP20, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-82; RP TRP-414; VAL-415 AND LEU-427. RX PubMed=24018379; DOI=10.1038/cr.2013.127; RA Shen M., Cai Y., Yang Y., Yan X., Liu X., Zhou T.; RT "Centrosomal protein FOR20 is essential for S-phase progression by RT recruiting Plk1 to centrosomes."; RL Cell Res. 23:1284-1295(2013). RN [71] RP INTERACTION WITH DCTN6, AND SUBCELLULAR LOCATION. RX PubMed=23455152; DOI=10.1038/emboj.2013.30; RA Yeh T.Y., Kowalska A.K., Scipioni B.R., Cheong F.K., Zheng M., RA Derewenda U., Derewenda Z.S., Schroer T.A.; RT "Dynactin helps target Polo-like kinase 1 to kinetochores via its left- RT handed beta-helical p27 subunit."; RL EMBO J. 32:1023-1035(2013). RN [72] RP FUNCTION IN PHOSPHORYLATION OF MISP. RX PubMed=23509069; DOI=10.1083/jcb.201207050; RA Zhu M., Settele F., Kotak S., Sanchez-Pulido L., Ehret L., Ponting C.P., RA Goenczy P., Hoffmann I.; RT "MISP is a novel Plk1 substrate required for proper spindle orientation and RT mitotic progression."; RL J. Cell Biol. 200:773-787(2013). RN [73] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-210, AND IDENTIFICATION BY RP 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 [74] RP FUNCTION, INTERACTION WITH KLHL22, SUBCELLULAR LOCATION, UBIQUITINATION AT RP LYS-9 AND LYS-492, AND MUTAGENESIS OF LYS-492. RX PubMed=23455478; DOI=10.1038/ncb2695; RA Beck J., Maerki S., Posch M., Metzger T., Persaud A., Scheel H., RA Hofmann K., Rotin D., Pedrioli P., Swedlow J.R., Peter M., Sumara I.; RT "Ubiquitylation-dependent localization of PLK1 in mitosis."; RL Nat. Cell Biol. 15:430-439(2013). RN [75] RP FUNCTION IN PHOSPHORYLATION OF HNRNPU. RX PubMed=25986610; DOI=10.1128/mcb.01312-14; RA Douglas P., Ye R., Morrice N., Britton S., Trinkle-Mulcahy L., RA Lees-Miller S.P.; RT "Phosphorylation of SAF-A/hnRNP-U serine 59 by polo-like kinase 1 is RT required for mitosis."; RL Mol. Cell. Biol. 35:2699-2713(2015). RN [76] RP FUNCTION, AND INTERACTION WITH CEP68. RX PubMed=25503564; DOI=10.1038/ncb3076; RA Pagan J.K., Marzio A., Jones M.J., Saraf A., Jallepalli P.V., Florens L., RA Washburn M.P., Pagano M.; RT "Degradation of Cep68 and PCNT cleavage mediate Cep215 removal from the PCM RT to allow centriole separation, disengagement and licensing."; RL Nat. Cell Biol. 17:31-43(2015). RN [77] RP FUNCTION. RX PubMed=26811421; DOI=10.1083/jcb.201507042; RA Moudry P., Watanabe K., Wolanin K.M., Bartkova J., Wassing I.E., RA Watanabe S., Strauss R., Troelsgaard Pedersen R., Oestergaard V.H., RA Lisby M., Andujar-Sanchez M., Maya-Mendoza A., Esashi F., Lukas J., RA Bartek J.; RT "TOPBP1 regulates RAD51 phosphorylation and chromatin loading and RT determines PARP inhibitor sensitivity."; RL J. Cell Biol. 212:281-288(2016). RN [78] RP FUNCTION. RX PubMed=27979967; DOI=10.1074/jbc.m116.765438; RA Zhang B., Wang G., Xu X., Yang S., Zhuang T., Wang G., Ren H., Cheng S.Y., RA Jiang Q., Zhang C.; RT "DAZ-interacting Protein 1 (Dzip1) Phosphorylation by Polo-like Kinase 1 RT (Plk1) Regulates the Centriolar Satellite Localization of the BBSome RT Protein during the Cell Cycle."; RL J. Biol. Chem. 292:1351-1360(2017). RN [79] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-338, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [80] RP INTERACTION WITH NEDD9. RX PubMed=29191835; DOI=10.1074/jbc.m117.802587; RA Lee K.H., Hwang J.A., Kim S.O., Kim J.H., Shin S.C., Kim E.E., Lee K.S., RA Rhee K., Jeon B.H., Bang J.K., Cha-Molstad H., Soung N.K., Jang J.H., RA Ko S.K., Lee H.G., Ahn J.S., Kwon Y.T., Kim B.Y.; RT "Phosphorylation of human enhancer filamentation 1 (HEF1) stimulates RT interaction with Polo-like kinase 1 leading to HEF1 localization to focal RT adhesions."; RL J. Biol. Chem. 293:847-862(2018). RN [81] RP SUBCELLULAR LOCATION. RX PubMed=30715179; DOI=10.1093/brain/awz004; RA Perez Y., Bar-Yaacov R., Kadir R., Wormser O., Shelef I., Birk O.S., RA Flusser H., Birnbaum R.Y.; RT "Mutations in the microtubule-associated protein MAP11 (C7orf43) cause RT microcephaly in humans and zebrafish."; RL Brain 142:574-585(2019). RN [82] RP INTERACTION WITH FIRRM. RX PubMed=34260926; DOI=10.1016/j.celrep.2021.109343; RA Xu L., Ali M., Duan W., Yuan X., Garba F., Mullen M., Sun B., Poser I., RA Duan H., Lu J., Tian R., Ge Y., Chu L., Pan W., Wang D., Hyman A., RA Green H., Li L., Dou Z., Liu D., Liu X., Yao X.; RT "Feedback control of PLK1 by Apolo1 ensures accurate chromosome RT segregation."; RL Cell Rep. 36:109343-109343(2021). RN [83] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=37674080; DOI=10.1038/s41586-023-06506-6; RA Gelot C., Kovacs M.T., Miron S., Mylne E., Haan A., Boeffard-Dosierre L., RA Ghouil R., Popova T., Dingli F., Loew D., Guirouilh-Barbat J., Del Nery E., RA Zinn-Justin S., Ceccaldi R.; RT "Poltheta is phosphorylated by PLK1 to repair double-strand breaks in RT mitosis."; RL Nature 621:415-422(2023). RN [84] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=37440612; DOI=10.1126/science.adh3694; RA Brambati A., Sacco O., Porcella S., Heyza J., Kareh M., Schmidt J.C., RA Sfeir A.; RT "RHINO directs MMEJ to repair DNA breaks in mitosis."; RL Science 381:653-660(2023). RN [85] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 367-603 IN COMPLEX WITH RP PHOSPHORYLATED PEPTIDE, FUNCTION, SUBCELLULAR LOCATION, DOMAIN POLO BOX, RP INTERACTION WITH CDC25C, AND MUTAGENESIS OF HIS-538 AND LYS-540. RX PubMed=14532005; DOI=10.1016/s0092-8674(03)00725-6; RA Elia A.E., Rellos P., Haire L.F., Chao J.W., Ivins F.J., Hoepker K., RA Mohammad D., Cantley L.C., Smerdon S.J., Yaffe M.B.; RT "The molecular basis for phosphodependent substrate targeting and RT regulation of Plks by the Polo-box domain."; RL Cell 115:83-95(2003). RN [86] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 367-603 IN COMPLEX WITH RP PHOSPHORYLATED PEPTIDE. RX PubMed=14592974; DOI=10.1093/emboj/cdg558; RA Cheng K.Y., Lowe E.D., Sinclair J., Nigg E.A., Johnson L.N.; RT "The crystal structure of the human polo-like kinase-1 polo box domain and RT its phospho-peptide complex."; RL EMBO J. 22:5757-5768(2003). RN [87] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 13-345 OF MUTANT VAL-210 IN RP COMPLEXES WITH ATP ANALOGS, AND MUTAGENESIS OF THR-210. RX PubMed=17461553; DOI=10.1021/bi602474j; RA Kothe M., Kohls D., Low S., Coli R., Cheng A.C., Jacques S.L., RA Johnson T.L., Lewis C., Loh C., Nonomiya J., Sheils A.L., Verdries K.A., RA Wynn T.A., Kuhn C., Ding Y.H.; RT "Structure of the catalytic domain of human polo-like kinase 1."; RL Biochemistry 46:5960-5971(2007). RN [88] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 37-330 IN COMPLEX WITH SYNTHETIC RP INHIBITOR BI 2536. RX PubMed=18005335; DOI=10.1111/j.1747-0285.2007.00594.x; RA Kothe M., Kohls D., Low S., Coli R., Rennie G.R., Feru F., Kuhn C., RA Ding Y.H.; RT "Selectivity-determining residues in Plk1."; RL Chem. Biol. Drug Des. 70:540-546(2007). RN [89] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 365-603 IN COMPLEX WITH CDC25C, RP SUBCELLULAR LOCATION, INTERACTION WITH CDC25C, ACTIVITY REGULATION, AND RP MUTAGENESIS OF TRP-414. RX PubMed=17307877; DOI=10.1073/pnas.0609131104; RA Garcia-Alvarez B., de Carcer G., Ibanez S., Bragado-Nilsson E., Montoya G.; RT "Molecular and structural basis of polo-like kinase 1 substrate RT recognition: Implications in centrosomal localization."; RL Proc. Natl. Acad. Sci. U.S.A. 104:3107-3112(2007). RN [90] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 33-345 IN COMPLEX WITH A DARPIN. RX PubMed=18391401; DOI=10.1107/s0907444907068217; RA Bandeiras T.M., Hillig R.C., Matias P.M., Eberspaecher U., Fanghanel J., RA Thomaz M., Miranda S., Crusius K., Putter V., Amstutz P., RA Gulotti-Georgieva M., Binz H.K., Holz C., Schmitz A.A., Lang C., Donner P., RA Egner U., Carrondo M.A., Muller-Tiemann B.; RT "Structure of wild-type Plk-1 kinase domain in complex with a selective RT DARPin."; RL Acta Crystallogr. D 64:339-353(2008). RN [91] RP X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 371-603 IN COMPLEX WITH RP PHOSPHOPEPTIDE, FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RP PHOSPHORYLATED CENPU. RX PubMed=19597481; DOI=10.1038/nsmb.1628; RA Yun S.M., Moulaei T., Lim D., Bang J.K., Park J.E., Shenoy S.R., Liu F., RA Kang Y.H., Liao C., Soung N.K., Lee S., Yoon D.Y., Lim Y., Lee D.H., RA Otaka A., Appella E., McMahon J.B., Nicklaus M.C., Burke T.R. Jr., RA Yaffe M.B., Wlodawer A., Lee K.S.; RT "Structural and functional analyses of minimal phosphopeptides targeting RT the polo-box domain of polo-like kinase 1."; RL Nat. Struct. Mol. Biol. 16:876-882(2009). RN [92] RP VARIANTS [LARGE SCALE ANALYSIS] LEU-12; PHE-261; VAL-332; HIS-463 AND RP HIS-518. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., RA Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). CC -!- FUNCTION: Serine/threonine-protein kinase that performs several CC important functions throughout M phase of the cell cycle, including the CC regulation of centrosome maturation and spindle assembly, the removal CC of cohesins from chromosome arms, the inactivation of anaphase- CC promoting complex/cyclosome (APC/C) inhibitors, and the regulation of CC mitotic exit and cytokinesis (PubMed:8991084, PubMed:11202906, CC PubMed:12207013, PubMed:12447691, PubMed:12524548, PubMed:12738781, CC PubMed:12852856, PubMed:12939256, PubMed:14532005, PubMed:14734534, CC PubMed:15070733, PubMed:15148369, PubMed:15469984, PubMed:16198290, CC PubMed:16247472, PubMed:16980960, PubMed:17081991, PubMed:17351640, CC PubMed:17376779, PubMed:17617734, PubMed:18174154, PubMed:18331714, CC PubMed:18418051, PubMed:18477460, PubMed:18521620, PubMed:18615013, CC PubMed:19160488, PubMed:19351716, PubMed:19468300, PubMed:19468302, CC PubMed:19473992, PubMed:19509060, PubMed:19597481, PubMed:23455478, CC PubMed:23509069). Polo-like kinase proteins act by binding and CC phosphorylating proteins that are already phosphorylated on a specific CC motif recognized by the POLO box domains (PubMed:8991084, CC PubMed:11202906, PubMed:12207013, PubMed:12447691, PubMed:12524548, CC PubMed:12738781, PubMed:12852856, PubMed:12939256, PubMed:14532005, CC PubMed:14734534, PubMed:15070733, PubMed:15148369, PubMed:15469984, CC PubMed:16198290, PubMed:16247472, PubMed:16980960, PubMed:17081991, CC PubMed:17351640, PubMed:17376779, PubMed:17617734, PubMed:18174154, CC PubMed:18331714, PubMed:18418051, PubMed:18477460, PubMed:18521620, CC PubMed:18615013, PubMed:19160488, PubMed:19351716, PubMed:19468300, CC PubMed:19468302, PubMed:19473992, PubMed:19509060, PubMed:19597481, CC PubMed:23455478, PubMed:23509069). Phosphorylates BORA, BUB1B/BUBR1, CC CCNB1, CDC25C, CEP55, ECT2, ERCC6L, FBXO5/EMI1, FOXM1, KIF20A/MKLP2, CC CENPU, NEDD1, NINL, NPM1, NUDC, PKMYT1/MYT1, KIZ, PPP1R12A/MYPT1, POLQ, CC PRC1, RACGAP1/CYK4, RAD51, RHNO1, SGO1, STAG2/SA2, TEX14, TOPORS, CC p73/TP73, TPT1, WEE1 and HNRNPU (PubMed:8991084, PubMed:11202906, CC PubMed:12207013, PubMed:12447691, PubMed:12524548, PubMed:12738781, CC PubMed:12852856, PubMed:12939256, PubMed:14532005, PubMed:14734534, CC PubMed:15070733, PubMed:15148369, PubMed:15469984, PubMed:16198290, CC PubMed:16247472, PubMed:16980960, PubMed:17081991, PubMed:17218258, CC PubMed:17351640, PubMed:17376779, PubMed:17617734, PubMed:18174154, CC PubMed:18331714, PubMed:18418051, PubMed:18477460, PubMed:18521620, CC PubMed:18615013, PubMed:19160488, PubMed:19351716, PubMed:19468300, CC PubMed:19468302, PubMed:19473992, PubMed:19509060, PubMed:22325354, CC PubMed:19597481, PubMed:23455478, PubMed:23509069, PubMed:25986610, CC PubMed:26811421, PubMed:37674080, PubMed:37440612). Plays a key role in CC centrosome functions and the assembly of bipolar spindles by CC phosphorylating KIZ, NEDD1 and NINL (PubMed:16980960, PubMed:19509060). CC NEDD1 phosphorylation promotes subsequent targeting of the gamma- CC tubulin ring complex (gTuRC) to the centrosome, an important step for CC spindle formation (PubMed:19509060). Phosphorylation of NINL component CC of the centrosome leads to NINL dissociation from other centrosomal CC proteins (PubMed:12852856). Involved in mitosis exit and cytokinesis by CC phosphorylating CEP55, ECT2, KIF20A/MKLP2, CENPU, PRC1 and RACGAP1 CC (PubMed:12939256, PubMed:16247472, PubMed:17351640, PubMed:19468300, CC PubMed:19468302). Recruited at the central spindle by phosphorylating CC and docking PRC1 and KIF20A/MKLP2; creates its own docking sites on CC PRC1 and KIF20A/MKLP2 by mediating phosphorylation of sites CC subsequently recognized by the POLO box domains (PubMed:12939256, CC PubMed:17351640). Phosphorylates RACGAP1, thereby creating a docking CC site for the Rho GTP exchange factor ECT2 that is essential for the CC cleavage furrow formation (PubMed:19468300, PubMed:19468302). Promotes CC the central spindle recruitment of ECT2 (PubMed:16247472). Plays a CC central role in G2/M transition of mitotic cell cycle by CC phosphorylating CCNB1, CDC25C, FOXM1, CENPU, PKMYT1/MYT1, CC PPP1R12A/MYPT1 and WEE1 (PubMed:11202906, PubMed:12447691, CC PubMed:12524548, PubMed:19160488). Part of a regulatory circuit that CC promotes the activation of CDK1 by phosphorylating the positive CC regulator CDC25C and inhibiting the negative regulators WEE1 and CC PKMYT1/MYT1 (PubMed:11202906). Also acts by mediating phosphorylation CC of cyclin-B1 (CCNB1) on centrosomes in prophase (PubMed:12447691, CC PubMed:12524548). Phosphorylates FOXM1, a key mitotic transcription CC regulator, leading to enhance FOXM1 transcriptional activity CC (PubMed:19160488). Involved in kinetochore functions and sister CC chromatid cohesion by phosphorylating BUB1B/BUBR1, FBXO5/EMI1 and CC STAG2/SA2 (PubMed:15469984, PubMed:15148369, PubMed:17376779, CC PubMed:18331714). PLK1 is high on non-attached kinetochores suggesting CC a role of PLK1 in kinetochore attachment or in spindle assembly CC checkpoint (SAC) regulation (PubMed:17617734). Required for kinetochore CC localization of BUB1B (PubMed:17376779). Regulates the dissociation of CC cohesin from chromosomes by phosphorylating cohesin subunits such as CC STAG2/SA2 (By similarity). Phosphorylates SGO1: required for spindle CC pole localization of isoform 3 of SGO1 and plays a role in regulating CC its centriole cohesion function (PubMed:18331714). Mediates CC phosphorylation of FBXO5/EMI1, a negative regulator of the APC/C CC complex during prophase, leading to FBXO5/EMI1 ubiquitination and CC degradation by the proteasome (PubMed:15469984, PubMed:15148369). Acts CC as a negative regulator of p53 family members: phosphorylates TOPORS, CC leading to inhibit the sumoylation of p53/TP53 and simultaneously CC enhance the ubiquitination and subsequent degradation of p53/TP53 CC (PubMed:19473992). Phosphorylates the transactivation domain of the CC transcription factor p73/TP73, leading to inhibit p73/TP73-mediated CC transcriptional activation and pro-apoptotic functions. Phosphorylates CC BORA, and thereby promotes the degradation of BORA (PubMed:18521620). CC Contributes to the regulation of AURKA function (PubMed:18662541, CC PubMed:18615013). Also required for recovery after DNA damage CC checkpoint and entry into mitosis (PubMed:18662541, PubMed:18615013). CC Phosphorylates MISP, leading to stabilization of cortical and astral CC microtubule attachments required for proper spindle positioning CC (PubMed:23509069). Together with MEIKIN, acts as a regulator of CC kinetochore function during meiosis I: required both for mono- CC orientation of kinetochores on sister chromosomes and protection of CC centromeric cohesin from separase-mediated cleavage (By similarity). CC Phosphorylates CEP68 and is required for its degradation CC (PubMed:25503564). Regulates nuclear envelope breakdown during prophase CC by phosphorylating DCTN1 resulting in its localization in the nuclear CC envelope (PubMed:20679239). Phosphorylates the heat shock transcription CC factor HSF1, promoting HSF1 nuclear translocation upon heat shock CC (PubMed:15661742). Phosphorylates HSF1 also in the early mitotic CC period; this phosphorylation regulates HSF1 localization to the spindle CC pole, the recruitment of the SCF(BTRC) ubiquitin ligase complex CC induicing HSF1 degradation, and hence mitotic progression CC (PubMed:18794143). Regulates mitotic progression by phosphorylating CC RIOK2 (PubMed:21880710). Through the phosphorylation of DZIP1 regulates CC the localization during mitosis of the BBSome, a ciliary protein CC complex involved in cilium biogenesis (PubMed:27979967). Regulates DNA CC repair during mitosis by mediating phosphorylation of POLQ and RHNO1, CC thereby promoting POLQ recruitment to DNA damage sites CC (PubMed:37674080, PubMed:37440612). {ECO:0000250|UniProtKB:P70032, CC ECO:0000250|UniProtKB:Q5F2C3, ECO:0000269|PubMed:11202906, CC ECO:0000269|PubMed:12207013, ECO:0000269|PubMed:12447691, CC ECO:0000269|PubMed:12524548, ECO:0000269|PubMed:12738781, CC ECO:0000269|PubMed:12852856, ECO:0000269|PubMed:12939256, CC ECO:0000269|PubMed:14532005, ECO:0000269|PubMed:14734534, CC ECO:0000269|PubMed:15070733, ECO:0000269|PubMed:15148369, CC ECO:0000269|PubMed:15469984, ECO:0000269|PubMed:15661742, CC ECO:0000269|PubMed:16198290, ECO:0000269|PubMed:16247472, CC ECO:0000269|PubMed:16980960, ECO:0000269|PubMed:17081991, CC ECO:0000269|PubMed:17218258, ECO:0000269|PubMed:17351640, CC ECO:0000269|PubMed:17376779, ECO:0000269|PubMed:17617734, CC ECO:0000269|PubMed:18174154, ECO:0000269|PubMed:18331714, CC ECO:0000269|PubMed:18418051, ECO:0000269|PubMed:18477460, CC ECO:0000269|PubMed:18521620, ECO:0000269|PubMed:18615013, CC ECO:0000269|PubMed:18662541, ECO:0000269|PubMed:18794143, CC ECO:0000269|PubMed:19160488, ECO:0000269|PubMed:19351716, CC ECO:0000269|PubMed:19468300, ECO:0000269|PubMed:19468302, CC ECO:0000269|PubMed:19473992, ECO:0000269|PubMed:19509060, CC ECO:0000269|PubMed:19597481, ECO:0000269|PubMed:20679239, CC ECO:0000269|PubMed:21880710, ECO:0000269|PubMed:22325354, CC ECO:0000269|PubMed:23455478, ECO:0000269|PubMed:23509069, CC ECO:0000269|PubMed:25503564, ECO:0000269|PubMed:25986610, CC ECO:0000269|PubMed:26811421, ECO:0000269|PubMed:27979967, CC ECO:0000269|PubMed:37440612, ECO:0000269|PubMed:37674080, CC ECO:0000269|PubMed:8991084}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.21; CC Evidence={ECO:0000269|PubMed:11202906, ECO:0000269|PubMed:12207013, CC ECO:0000269|PubMed:21880710, ECO:0000269|PubMed:22325354, CC ECO:0000269|PubMed:37440612, ECO:0000269|PubMed:37674080}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.21; Evidence={ECO:0000269|PubMed:11202906, CC ECO:0000269|PubMed:12207013, ECO:0000269|PubMed:21880710, CC ECO:0000269|PubMed:37674080}; CC -!- ACTIVITY REGULATION: Activated by phosphorylation of Thr-210 by AURKA; CC phosphorylation by AURKA is enhanced by BORA (PubMed:18615013, CC PubMed:17307877). Once activated, activity is stimulated by binding CC target proteins (PubMed:18615013, PubMed:17307877). Binding of target CC proteins has no effect on the non-activated kinase (PubMed:18615013, CC PubMed:17307877). Several inhibitors targeting PLKs are currently in CC development and are under investigation in a growing number of clinical CC trials, such as BI 2536, an ATP-competitive PLK1 inhibitor or BI 6727, CC a dihydropteridinone that specifically inhibits the catalytic activity CC of PLK1 (PubMed:18005335). {ECO:0000269|PubMed:17307877, CC ECO:0000269|PubMed:18005335, ECO:0000269|PubMed:18615013}. CC -!- SUBUNIT: Interacts with CEP170 (PubMed:15616186). Interacts with EVI5 CC (PubMed:16439210). Interacts with FAM29A (PubMed:19029337). Interacts CC with SLX4/BTBD12 (PubMed:19596235). Interacts with TTDN1 CC (PubMed:17310276). Interacts (via POLO-box domain) with the CC phosphorylated form of BUB1, CDC25C and CENPU (PubMed:16760428, CC PubMed:14532005, PubMed:17307877, PubMed:19597481). Interacts with CC KIF2A (PubMed:19351716). Interacts with CYLD (PubMed:17495026). Part of CC an astrin (SPAG5)-kinastrin (SKAP) complex containing KNSTRN, SPAG5, CC PLK1, DYNLL1 and SGO2 (PubMed:21402792). Interacts with BIRC6/bruce CC (PubMed:18329369). Interacts with CDK1-phosphorylated FRY; this CC interaction occurs in mitotic cells, but not in interphase cells CC (PubMed:22753416). FRY interaction facilitates AURKA-mediated PLK1 CC phosphorylation (PubMed:22753416). Interacts with CDK1-phosphorylated CC DCTN6 during mitotic prometaphase; the interaction facilitates CC recruitment to kinetochores (PubMed:23455152). Interacts with CEP68; CC the interaction phosphorylates CEP68 (PubMed:25503564). Interacts (via CC POLO-box domain) with DCTN1 (PubMed:20679239). Interacts with CEP20 in CC later G1, S, G2 and M phases of the cell cycle; this interaction CC recruits PLK1 to centrosomes, a step required for S phase progression CC (PubMed:24018379). Interacts with KLHL22 (PubMed:24067371, CC PubMed:23455478). Interacts (via POLO box domains) with NEDD9/HEF1 (via CC C-terminus) (PubMed:29191835). Interacts with FIRRM (via N-terminus CC region); required for maintaining, but not activating, PLK1 kinase CC activity (PubMed:34260926). Interacts with FZR1 (PubMed:18662541). CC {ECO:0000269|PubMed:14532005, ECO:0000269|PubMed:15616186, CC ECO:0000269|PubMed:16439210, ECO:0000269|PubMed:16760428, CC ECO:0000269|PubMed:17307877, ECO:0000269|PubMed:17310276, CC ECO:0000269|PubMed:17495026, ECO:0000269|PubMed:18329369, CC ECO:0000269|PubMed:18662541, ECO:0000269|PubMed:19029337, CC ECO:0000269|PubMed:19351716, ECO:0000269|PubMed:19596235, CC ECO:0000269|PubMed:19597481, ECO:0000269|PubMed:20679239, CC ECO:0000269|PubMed:21402792, ECO:0000269|PubMed:22753416, CC ECO:0000269|PubMed:23455152, ECO:0000269|PubMed:23455478, CC ECO:0000269|PubMed:24018379, ECO:0000269|PubMed:24067371, CC ECO:0000269|PubMed:25503564, ECO:0000269|PubMed:29191835, CC ECO:0000269|PubMed:34260926}. CC -!- INTERACTION: CC P53350; P05067: APP; NbExp=3; IntAct=EBI-476768, EBI-77613; CC P53350; O14965: AURKA; NbExp=4; IntAct=EBI-476768, EBI-448680; CC P53350; Q9Y2T1: AXIN2; NbExp=2; IntAct=EBI-476768, EBI-4400025; CC P53350; Q9NR09: BIRC6; NbExp=4; IntAct=EBI-476768, EBI-1765160; CC P53350; P54132: BLM; NbExp=4; IntAct=EBI-476768, EBI-621372; CC P53350; Q6PGQ7: BORA; NbExp=5; IntAct=EBI-476768, EBI-719836; CC P53350; Q14790: CASP8; NbExp=3; IntAct=EBI-476768, EBI-78060; CC P53350; P30307: CDC25C; NbExp=5; IntAct=EBI-476768, EBI-974439; CC P53350; Q99741: CDC6; NbExp=6; IntAct=EBI-476768, EBI-374862; CC P53350; Q71F23-1: CENPU; NbExp=5; IntAct=EBI-476768, EBI-15793375; CC P53350; Q76N32: CEP68; NbExp=2; IntAct=EBI-476768, EBI-9051024; CC P53350; O96017: CHEK2; NbExp=7; IntAct=EBI-476768, EBI-1180783; CC P53350; O14641: DVL2; NbExp=2; IntAct=EBI-476768, EBI-740850; CC P53350; P23588: EIF4B; NbExp=3; IntAct=EBI-476768, EBI-970310; CC P53350; Q2NKX8: ERCC6L; NbExp=4; IntAct=EBI-476768, EBI-1042535; CC P53350; O60447: EVI5; NbExp=3; IntAct=EBI-476768, EBI-852291; CC P53350; Q13158: FADD; NbExp=9; IntAct=EBI-476768, EBI-494804; CC P53350; Q9NYZ3: GTSE1; NbExp=6; IntAct=EBI-476768, EBI-2511327; CC P53350; P08107: HSPA1B; NbExp=5; IntAct=EBI-476768, EBI-629985; CC P53350; O95251: KAT7; NbExp=6; IntAct=EBI-476768, EBI-473199; CC P53350; P49736: MCM2; NbExp=2; IntAct=EBI-476768, EBI-374819; CC P53350; P33993: MCM7; NbExp=4; IntAct=EBI-476768, EBI-355924; CC P53350; Q00987: MDM2; NbExp=7; IntAct=EBI-476768, EBI-389668; CC P53350; Q8TD19: NEK9; NbExp=5; IntAct=EBI-476768, EBI-1044009; CC P53350; Q5HYW2: NHSL2; NbExp=3; IntAct=EBI-476768, EBI-2859639; CC P53350; O75665: OFD1; NbExp=4; IntAct=EBI-476768, EBI-716327; CC P53350; Q8IXK0: PHC2; NbExp=2; IntAct=EBI-476768, EBI-713786; CC P53350; P53350: PLK1; NbExp=3; IntAct=EBI-476768, EBI-476768; CC P53350; P49768-2: PSEN1; NbExp=3; IntAct=EBI-476768, EBI-11047108; CC P53350; Q9H0H5: RACGAP1; NbExp=4; IntAct=EBI-476768, EBI-717233; CC P53350; Q8IY92: SLX4; NbExp=8; IntAct=EBI-476768, EBI-2370740; CC P53350; Q92844: TANK; NbExp=3; IntAct=EBI-476768, EBI-356349; CC P53350; Q15583: TGIF1; NbExp=3; IntAct=EBI-476768, EBI-714215; CC P53350; P04637: TP53; NbExp=6; IntAct=EBI-476768, EBI-366083; CC P53350; Q12888: TP53BP1; NbExp=6; IntAct=EBI-476768, EBI-396540; CC P53350; P30291: WEE1; NbExp=2; IntAct=EBI-476768, EBI-914695; CC P53350; P62258: YWHAE; NbExp=2; IntAct=EBI-476768, EBI-356498; CC P53350; Q60838: Dvl2; Xeno; NbExp=12; IntAct=EBI-476768, EBI-641940; CC P53350; P23804: Mdm2; Xeno; NbExp=2; IntAct=EBI-476768, EBI-641788; CC P53350; P70399-1: Tp53bp1; Xeno; NbExp=2; IntAct=EBI-476768, EBI-15790796; CC P53350; PRO_0000045602 [Q99IB8]; Xeno; NbExp=4; IntAct=EBI-476768, EBI-6927873; CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore. CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome CC {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:24018379}. Cytoplasm, CC cytoskeleton, spindle {ECO:0000269|PubMed:18794143, CC ECO:0000269|PubMed:30715179}. Midbody {ECO:0000269|PubMed:30715179}. CC Note=localization at the centrosome starts at the G1/S transition CC (PubMed:24018379). During early stages of mitosis, the phosphorylated CC form is detected on centrosomes and kinetochores. Localizes to the CC outer kinetochore. Presence of SGO1 and interaction with the CC phosphorylated form of BUB1 is required for the kinetochore CC localization. Localizes onto the central spindle by phosphorylating and CC docking at midzone proteins KIF20A/MKLP2 and PRC1. Colocalizes with FRY CC to separating centrosomes and spindle poles from prophase to metaphase CC in mitosis, but not in other stages of the cell cycle. Localization to CC the centrosome is required for S phase progression (PubMed:24018379). CC Colocalizes with HSF1 at the spindle poles during prometaphase CC (PubMed:18794143). {ECO:0000269|PubMed:18794143, CC ECO:0000269|PubMed:24018379}. CC -!- TISSUE SPECIFICITY: Placenta and colon. CC -!- DEVELOPMENTAL STAGE: Accumulates to a maximum during the G2 and M CC phases, declines to a nearly undetectable level following mitosis and CC throughout G1 phase, and then begins to accumulate again during S CC phase. CC -!- INDUCTION: By growth-stimulating agents. CC -!- DOMAIN: The POLO box domains act as phosphopeptide-binding module that CC recognizes and binds serine-[phosphothreonine/phosphoserine]- CC (proline/X) motifs. PLK1 recognizes and binds docking proteins that are CC already phosphorylated on these motifs, and then phosphorylates them. CC PLK1 can also create its own docking sites by mediating phosphorylation CC of serine-[phosphothreonine/phosphoserine]-(proline/X) motifs CC subsequently recognized by the POLO box domains. CC {ECO:0000269|PubMed:12939256, ECO:0000269|PubMed:14532005, CC ECO:0000269|PubMed:14734534, ECO:0000269|PubMed:17351640}. CC -!- PTM: Catalytic activity is enhanced by phosphorylation of Thr-210. CC Phosphorylation at Thr-210 is first detected on centrosomes in the G2 CC phase of the cell cycle, peaks in prometaphase and gradually disappears CC from centrosomes during anaphase. Dephosphorylation at Thr-210 at CC centrosomes is probably mediated by protein phosphatase 1C (PP1C), via CC interaction with PPP1R12A/MYPT1. Autophosphorylation and CC phosphorylation of Ser-137 may not be significant for the activation of CC PLK1 during mitosis, but may enhance catalytic activity during recovery CC after DNA damage checkpoint. Phosphorylated in vitro by STK10. CC {ECO:0000269|PubMed:12207013, ECO:0000269|PubMed:12442251, CC ECO:0000269|PubMed:12639966, ECO:0000269|PubMed:18477460, CC ECO:0000269|PubMed:18615013}. CC -!- PTM: Ubiquitinated by the anaphase promoting complex/cyclosome (APC/C) CC in anaphase and following DNA damage, leading to its degradation by the CC proteasome. Ubiquitination is mediated via its interaction with CC FZR1/CDH1. Ubiquitination and subsequent degradation prevents entry CC into mitosis and is essential to maintain an efficient G2 DNA damage CC checkpoint. Monoubiquitination at Lys-492 by the BCR(KLHL22) ubiquitin CC ligase complex does not lead to degradation: it promotes PLK1 CC dissociation from phosphoreceptor proteins and subsequent removal from CC kinetochores, allowing silencing of the spindle assembly checkpoint CC (SAC) and chromosome segregation. {ECO:0000269|PubMed:18662541, CC ECO:0000269|PubMed:23455478}. CC -!- DISEASE: Note=Defects in PLK1 are associated with some cancers, such as CC gastric, thyroid or B-cell lymphomas. Expression is cancer increased in CC tumor tissues with a poor prognosis, suggesting a role in malignant CC transformations and carcinogenesis. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. CDC5/Polo subfamily. {ECO:0000255|PROSITE- CC ProRule:PRU00159}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/41747/PLK1"; 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; U01038; AAA56634.1; -; mRNA. DR EMBL; L19559; AAA36659.1; -; mRNA. DR EMBL; X73458; CAA51837.1; -; mRNA. DR EMBL; X75932; CAA53536.1; -; mRNA. DR EMBL; BC002369; AAH02369.1; -; mRNA. DR EMBL; BC003002; AAH03002.1; -; mRNA. DR EMBL; BC014846; AAH14846.1; -; mRNA. DR EMBL; X90725; CAA62260.1; -; Genomic_DNA. DR EMBL; U78073; AAB36946.1; -; Genomic_DNA. DR CCDS; CCDS10616.1; -. DR PIR; S34130; S34130. DR RefSeq; NP_005021.2; NM_005030.5. DR PDB; 1Q4K; X-ray; 2.30 A; A/B/C=345-603. DR PDB; 1Q4O; X-ray; 2.20 A; A/B=367-603. DR PDB; 1UMW; X-ray; 1.90 A; A/B=367-603. DR PDB; 2OGQ; X-ray; 1.95 A; A=365-603. DR PDB; 2OJX; X-ray; 2.85 A; A=365-603. DR PDB; 2OU7; X-ray; 2.40 A; A=13-345. DR PDB; 2OWB; X-ray; 2.10 A; A=13-345. DR PDB; 2RKU; X-ray; 1.95 A; A=37-330. DR PDB; 2V5Q; X-ray; 2.30 A; A/B=33-345. DR PDB; 2YAC; X-ray; 2.20 A; A=36-345. DR PDB; 3BZI; X-ray; 2.10 A; A=365-603. DR PDB; 3C5L; X-ray; 2.33 A; A=373-593. DR PDB; 3FC2; X-ray; 2.45 A; A=13-345. DR PDB; 3FVH; X-ray; 1.58 A; A=371-603. DR PDB; 3HIH; X-ray; 1.70 A; A/B=371-593. DR PDB; 3HIK; X-ray; 1.77 A; A=367-603. DR PDB; 3KB7; X-ray; 2.50 A; A=36-345. DR PDB; 3P2W; X-ray; 1.66 A; A=371-594. DR PDB; 3P2Z; X-ray; 1.79 A; A=371-594. DR PDB; 3P34; X-ray; 1.40 A; A=371-594. DR PDB; 3P35; X-ray; 2.09 A; A/B/C=371-594. DR PDB; 3P36; X-ray; 1.59 A; A=371-594. DR PDB; 3P37; X-ray; 2.38 A; A/B/C=371-594. DR PDB; 3Q1I; X-ray; 1.40 A; A=371-594. DR PDB; 3RQ7; X-ray; 1.55 A; A=371-603. DR PDB; 3THB; X-ray; 2.50 A; A=13-345. DR PDB; 4A4L; X-ray; 2.35 A; A=36-345. DR PDB; 4A4O; X-ray; 2.70 A; A=36-345. DR PDB; 4DFW; X-ray; 1.55 A; A=367-603. DR PDB; 4E67; X-ray; 2.10 A; A=371-594. DR PDB; 4E9C; X-ray; 1.70 A; A=371-594. DR PDB; 4E9D; X-ray; 2.75 A; A=371-594. DR PDB; 4H5X; X-ray; 1.95 A; A/B=367-603. DR PDB; 4H71; X-ray; 1.93 A; A/B=367-603. DR PDB; 4HAB; X-ray; 2.65 A; A/B/C=371-593. DR PDB; 4HCO; X-ray; 2.75 A; A/B=367-603. DR PDB; 4HY2; X-ray; 2.00 A; A=371-595. DR PDB; 4J52; X-ray; 2.30 A; A=38-330. DR PDB; 4J53; X-ray; 2.50 A; A=38-330. DR PDB; 4LKL; X-ray; 1.58 A; A=372-593. DR PDB; 4LKM; X-ray; 2.00 A; A/C=371-601. DR PDB; 4O56; X-ray; 1.80 A; A=367-603. DR PDB; 4O6W; X-ray; 1.45 A; A=371-603. DR PDB; 4O9W; X-ray; 1.69 A; A=373-594. DR PDB; 4RCP; X-ray; 1.60 A; A=372-599. DR PDB; 4WHH; X-ray; 1.90 A; A=371-603. DR PDB; 4WHK; X-ray; 1.80 A; A=371-603. DR PDB; 4WHL; X-ray; 2.71 A; A=371-603. DR PDB; 4X9R; X-ray; 1.40 A; A=371-603. DR PDB; 4X9V; X-ray; 1.43 A; A=371-603. DR PDB; 4X9W; X-ray; 1.80 A; A=371-603. DR PDB; 5J19; X-ray; 2.00 A; A/B=367-594. DR PDB; 5NEI; X-ray; 2.68 A; A=371-603. DR PDB; 5NFU; X-ray; 1.81 A; A=371-602. DR PDB; 5NJE; X-ray; 1.98 A; A=371-603. DR PDB; 5NMM; X-ray; 2.02 A; A=371-603. DR PDB; 5NN1; X-ray; 1.78 A; A=371-603. DR PDB; 5NN2; X-ray; 1.81 A; A=371-594. DR PDB; 5TA6; X-ray; 2.50 A; A=13-345. DR PDB; 5TA8; X-ray; 2.60 A; A=13-345. DR PDB; 6AX4; X-ray; 1.45 A; A=371-603. DR PDB; 6GY2; X-ray; 3.11 A; A/B=365-603. DR PDB; 7MSO; X-ray; 1.85 A; A/B=371-603. DR PDB; 7MX1; X-ray; 1.64 A; A/B=371-603. DR PDB; 8BJT; X-ray; 2.19 A; A=37-330. DR PDB; 8CRC; X-ray; 1.65 A; A=371-594. DR PDB; 8JOQ; X-ray; 1.80 A; A=371-594. DR PDB; 8JOY; X-ray; 2.61 A; A=371-594. DR PDBsum; 1Q4K; -. DR PDBsum; 1Q4O; -. DR PDBsum; 1UMW; -. DR PDBsum; 2OGQ; -. DR PDBsum; 2OJX; -. DR PDBsum; 2OU7; -. DR PDBsum; 2OWB; -. DR PDBsum; 2RKU; -. DR PDBsum; 2V5Q; -. DR PDBsum; 2YAC; -. DR PDBsum; 3BZI; -. DR PDBsum; 3C5L; -. DR PDBsum; 3FC2; -. DR PDBsum; 3FVH; -. DR PDBsum; 3HIH; -. DR PDBsum; 3HIK; -. DR PDBsum; 3KB7; -. DR PDBsum; 3P2W; -. DR PDBsum; 3P2Z; -. DR PDBsum; 3P34; -. DR PDBsum; 3P35; -. DR PDBsum; 3P36; -. DR PDBsum; 3P37; -. DR PDBsum; 3Q1I; -. DR PDBsum; 3RQ7; -. DR PDBsum; 3THB; -. DR PDBsum; 4A4L; -. DR PDBsum; 4A4O; -. DR PDBsum; 4DFW; -. DR PDBsum; 4E67; -. DR PDBsum; 4E9C; -. DR PDBsum; 4E9D; -. DR PDBsum; 4H5X; -. DR PDBsum; 4H71; -. DR PDBsum; 4HAB; -. DR PDBsum; 4HCO; -. DR PDBsum; 4HY2; -. DR PDBsum; 4J52; -. DR PDBsum; 4J53; -. DR PDBsum; 4LKL; -. DR PDBsum; 4LKM; -. DR PDBsum; 4O56; -. DR PDBsum; 4O6W; -. DR PDBsum; 4O9W; -. DR PDBsum; 4RCP; -. DR PDBsum; 4WHH; -. DR PDBsum; 4WHK; -. DR PDBsum; 4WHL; -. DR PDBsum; 4X9R; -. DR PDBsum; 4X9V; -. DR PDBsum; 4X9W; -. DR PDBsum; 5J19; -. DR PDBsum; 5NEI; -. DR PDBsum; 5NFU; -. DR PDBsum; 5NJE; -. DR PDBsum; 5NMM; -. DR PDBsum; 5NN1; -. DR PDBsum; 5NN2; -. DR PDBsum; 5TA6; -. DR PDBsum; 5TA8; -. DR PDBsum; 6AX4; -. DR PDBsum; 6GY2; -. DR PDBsum; 7MSO; -. DR PDBsum; 7MX1; -. DR PDBsum; 8BJT; -. DR PDBsum; 8CRC; -. DR PDBsum; 8JOQ; -. DR PDBsum; 8JOY; -. DR AlphaFoldDB; P53350; -. DR SMR; P53350; -. DR BioGRID; 111362; 505. DR CORUM; P53350; -. DR DIP; DIP-29696N; -. DR ELM; P53350; -. DR IntAct; P53350; 271. DR MINT; P53350; -. DR STRING; 9606.ENSP00000300093; -. DR BindingDB; P53350; -. DR ChEMBL; CHEMBL3024; -. DR DrugBank; DB07789; 1-[5-Methyl-2-(trifluoromethyl)furan-3-yl]-3-[5-[2-[[6-(1H-1,2,4-triazol-5-ylamino)pyrimidin-4-yl]amino]ethyl]-1,3-thiazol-2-yl]urea. DR DrugBank; DB06963; 3-[3-(3-methyl-6-{[(1S)-1-phenylethyl]amino}-1H-pyrazolo[4,3-c]pyridin-1-yl)phenyl]propanamide. DR DrugBank; DB06897; 3-[3-chloro-5-(5-{[(1S)-1-phenylethyl]amino}isoxazolo[5,4-c]pyridin-3-yl)phenyl]propan-1-ol. DR DrugBank; DB07186; 4-(4-METHYLPIPERAZIN-1-YL)-N-[5-(2-THIENYLACETYL)-1,5-DIHYDROPYRROLO[3,4-C]PYRAZOL-3-YL]BENZAMIDE. DR DrugBank; DB12010; Fostamatinib. DR DrugBank; DB12062; Volasertib. DR DrugBank; DB08059; Wortmannin. DR DrugCentral; P53350; -. DR GuidetoPHARMACOLOGY; 2168; -. DR MoonDB; P53350; Curated. DR GlyGen; P53350; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P53350; -. DR PhosphoSitePlus; P53350; -. DR SwissPalm; P53350; -. DR BioMuta; PLK1; -. DR DMDM; 1709658; -. DR CPTAC; CPTAC-1264; -. DR CPTAC; CPTAC-1326; -. DR CPTAC; CPTAC-1327; -. DR CPTAC; CPTAC-2908; -. DR CPTAC; CPTAC-2909; -. DR EPD; P53350; -. DR jPOST; P53350; -. DR MassIVE; P53350; -. DR MaxQB; P53350; -. DR PaxDb; 9606-ENSP00000300093; -. DR PeptideAtlas; P53350; -. DR ProteomicsDB; 56569; -. DR Pumba; P53350; -. DR Antibodypedia; 12634; 1380 antibodies from 48 providers. DR DNASU; 5347; -. DR Ensembl; ENST00000300093.9; ENSP00000300093.4; ENSG00000166851.15. DR GeneID; 5347; -. DR KEGG; hsa:5347; -. DR MANE-Select; ENST00000300093.9; ENSP00000300093.4; NM_005030.6; NP_005021.2. DR UCSC; uc002dlz.2; human. DR AGR; HGNC:9077; -. DR CTD; 5347; -. DR DisGeNET; 5347; -. DR GeneCards; PLK1; -. DR HGNC; HGNC:9077; PLK1. DR HPA; ENSG00000166851; Tissue enhanced (bone marrow, lymphoid tissue, testis). DR MIM; 602098; gene. DR neXtProt; NX_P53350; -. DR OpenTargets; ENSG00000166851; -. DR PharmGKB; PA33410; -. DR VEuPathDB; HostDB:ENSG00000166851; -. DR eggNOG; KOG0575; Eukaryota. DR GeneTree; ENSGT00940000157752; -. DR HOGENOM; CLU_000288_46_1_1; -. DR InParanoid; P53350; -. DR OMA; IQIHKSM; -. DR OrthoDB; 5471704at2759; -. DR PhylomeDB; P53350; -. DR TreeFam; TF101089; -. DR BRENDA; 2.7.11.21; 2681. DR PathwayCommons; P53350; -. DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal. DR Reactome; R-HSA-156711; Polo-like kinase mediated events. DR Reactome; R-HSA-162658; Golgi Cisternae Pericentriolar Stack Reorganization. DR Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1. DR Reactome; R-HSA-176412; Phosphorylation of the APC/C. DR Reactome; R-HSA-176417; Phosphorylation of Emi1. DR Reactome; R-HSA-2299718; Condensation of Prophase Chromosomes. DR Reactome; R-HSA-2467813; Separation of Sister Chromatids. DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion. DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition. DR Reactome; R-HSA-2980767; Activation of NIMA Kinases NEK9, NEK6, NEK7. DR Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes. DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes. DR Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome. DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes. DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane. DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins. DR Reactome; R-HSA-68877; Mitotic Prometaphase. DR Reactome; R-HSA-68881; Mitotic Metaphase/Anaphase Transition. DR Reactome; R-HSA-68884; Mitotic Telophase/Cytokinesis. DR Reactome; R-HSA-69273; Cyclin A/B1/B2 associated events during G2/M transition. DR Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint. DR Reactome; R-HSA-8854518; AURKA Activation by TPX2. DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation. DR SignaLink; P53350; -. DR SIGNOR; P53350; -. DR BioGRID-ORCS; 5347; 876 hits in 1186 CRISPR screens. DR ChiTaRS; PLK1; human. DR EvolutionaryTrace; P53350; -. DR GeneWiki; PLK1; -. DR GenomeRNAi; 5347; -. DR Pharos; P53350; Tchem. DR PRO; PR:P53350; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; P53350; Protein. DR Bgee; ENSG00000166851; Expressed in ventricular zone and 103 other cell types or tissues. DR ExpressionAtlas; P53350; baseline and differential. DR GO; GO:0034451; C:centriolar satellite; IEA:Ensembl. DR GO; GO:0005814; C:centriole; IEA:Ensembl. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0000785; C:chromatin; IEA:Ensembl. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB. DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:BHF-UCL. DR GO; GO:0030496; C:midbody; IDA:UniProtKB. DR GO; GO:0097431; C:mitotic spindle pole; IEA:Ensembl. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0000940; C:outer kinetochore; IDA:BHF-UCL. DR GO; GO:0005819; C:spindle; IDA:UniProtKB. DR GO; GO:0051233; C:spindle midzone; IDA:UniProtKB. DR GO; GO:0000922; C:spindle pole; IDA:MGI. DR GO; GO:0000795; C:synaptonemal complex; IEA:Ensembl. DR GO; GO:0010997; F:anaphase-promoting complex binding; IPI:UniProtKB. DR GO; GO:0005524; F:ATP binding; IMP:CAFA. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0000287; F:magnesium ion binding; IMP:CAFA. DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB. DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB. DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB. DR GO; GO:0106310; F:protein serine kinase activity; IDA:UniProt. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB. DR GO; GO:0007098; P:centrosome cycle; IMP:UniProtKB. DR GO; GO:0006302; P:double-strand break repair; IDA:UniProtKB. DR GO; GO:0097681; P:double-strand break repair via alternative nonhomologous end joining; IDA:UniProt. DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IDA:UniProtKB. DR GO; GO:0045184; P:establishment of protein localization; IMP:MGI. DR GO; GO:0016321; P:female meiosis chromosome segregation; IEA:Ensembl. DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IDA:UniProtKB. DR GO; GO:0048313; P:Golgi inheritance; TAS:Reactome. DR GO; GO:0045143; P:homologous chromosome segregation; IEA:Ensembl. DR GO; GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; TAS:Reactome. DR GO; GO:0001578; P:microtubule bundle formation; IDA:UniProtKB. DR GO; GO:0000278; P:mitotic cell cycle; IDA:UniProtKB. DR GO; GO:0007076; P:mitotic chromosome condensation; TAS:Reactome. DR GO; GO:0000281; P:mitotic cytokinesis; IDA:UniProtKB. DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IDA:UniProtKB. DR GO; GO:0007077; P:mitotic nuclear membrane disassembly; TAS:Reactome. DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:UniProtKB. DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IMP:UniProtKB. DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central. DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB. DR GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IMP:BHF-UCL. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB. DR GO; GO:0051081; P:nuclear membrane disassembly; IMP:UniProtKB. DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:UniProtKB. DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IMP:BHF-UCL. DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB. DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; TAS:Reactome. DR GO; GO:0045862; P:positive regulation of proteolysis; IDA:UniProtKB. DR GO; GO:1904668; P:positive regulation of ubiquitin protein ligase activity; IDA:UniProtKB. DR GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; IMP:UniProtKB. DR GO; GO:0031648; P:protein destabilization; IDA:UniProtKB. DR GO; GO:0071168; P:protein localization to chromatin; IDA:UniProtKB. DR GO; GO:0090435; P:protein localization to nuclear envelope; IMP:UniProtKB. DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB. DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB. DR GO; GO:1905784; P:regulation of anaphase-promoting complex-dependent catabolic process; TAS:Reactome. DR GO; GO:0051726; P:regulation of cell cycle; TAS:Reactome. DR GO; GO:0032465; P:regulation of cytokinesis; IDA:UniProtKB. DR GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:UniProtKB. DR GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; TAS:Reactome. DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IDA:UniProtKB. DR GO; GO:1901673; P:regulation of mitotic spindle assembly; IDA:CACAO. DR GO; GO:0043393; P:regulation of protein binding; IMP:BHF-UCL. DR GO; GO:1904776; P:regulation of protein localization to cell cortex; IDA:UniProtKB. DR GO; GO:0007062; P:sister chromatid cohesion; TAS:Reactome. DR GO; GO:0070194; P:synaptonemal complex disassembly; IEA:Ensembl. DR CDD; cd13118; POLO_box_1; 1. DR CDD; cd13117; POLO_box_2; 1. DR CDD; cd14187; STKc_PLK1; 1. DR Gene3D; 3.30.1120.30; POLO box domain; 2. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR IDEAL; IID00200; -. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR033702; PLK1_cat. DR InterPro; IPR033701; POLO_box_1. DR InterPro; IPR033695; POLO_box_2. DR InterPro; IPR000959; POLO_box_dom. DR InterPro; IPR036947; POLO_box_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24345; SERINE/THREONINE-PROTEIN KINASE PLK; 1. DR PANTHER; PTHR24345:SF0; SERINE_THREONINE-PROTEIN KINASE PLK1; 1. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF00659; POLO_box; 2. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF82615; Polo-box domain; 2. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS50078; POLO_BOX; 2. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR Genevisible; P53350; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ATP-binding; Cell cycle; Cell division; KW Centromere; Chromosome; Cytoplasm; Cytoskeleton; Isopeptide bond; Kinase; KW Kinetochore; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase; KW Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22814378" FT CHAIN 2..603 FT /note="Serine/threonine-protein kinase PLK1" FT /id="PRO_0000086556" FT DOMAIN 53..305 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT DOMAIN 410..488 FT /note="POLO box 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154" FT DOMAIN 510..592 FT /note="POLO box 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154" FT REGION 1..35 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 194..221 FT /note="Activation loop" FT REGION 338..364 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 493..507 FT /note="Linker" FT REGION 538..540 FT /note="Important for interaction with phosphorylated FT proteins" FT /evidence="ECO:0000250" FT MOTIF 337..340 FT /note="D-box that targets the protein for proteasomal FT degradation in anaphase" FT COMPBIAS 350..364 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 176 FT /note="Proton acceptor" FT /evidence="ECO:0000269|PubMed:18615013" FT BINDING 59..67 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 82 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 131 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 178..181 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 194 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 6 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18691976" FT MOD_RES 103 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976" FT MOD_RES 137 FT /note="Phosphoserine" FT /evidence="ECO:0000305|PubMed:12207013" FT MOD_RES 210 FT /note="Phosphothreonine; by AURKA" FT /evidence="ECO:0000269|PubMed:12207013, FT ECO:0000269|PubMed:18477460, ECO:0000269|PubMed:18615013, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 214 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195" FT MOD_RES 269 FT /note="Phosphoserine; by autocatalysis" FT /evidence="ECO:0000250" FT MOD_RES 335 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:12442251" FT MOD_RES 375 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976" FT MOD_RES 450 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976" FT MOD_RES 498 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18691976" FT CROSSLNK 19 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:18662541" FT CROSSLNK 338 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 492 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:23455478" FT VARIANT 12 FT /note="R -> L (in a lung squamous cell carcinoma sample; FT somatic mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041018" FT VARIANT 261 FT /note="L -> F (in dbSNP:rs35056440)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041019" FT VARIANT 297 FT /note="N -> D (in dbSNP:rs16972799)" FT /id="VAR_051659" FT VARIANT 332 FT /note="L -> V (in dbSNP:rs45489499)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041020" FT VARIANT 463 FT /note="L -> H (in dbSNP:rs45569335)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041021" FT VARIANT 518 FT /note="R -> H (in dbSNP:rs56027600)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041022" FT VARIANT 595 FT /note="S -> L (in dbSNP:rs34001032)" FT /id="VAR_051660" FT VARIANT 599 FT /note="R -> H (in dbSNP:rs34954545)" FT /id="VAR_051661" FT MUTAGEN 67 FT /note="C->V: In analog-sensitive mutant; enlarged catalytic FT pocket to accommodate purine analogs; when associated with FT G-130." FT /evidence="ECO:0000269|PubMed:19468302" FT MUTAGEN 82 FT /note="K->M: Loss of kinase activity. No effect on S-phase FT progression." FT /evidence="ECO:0000269|PubMed:12207013, FT ECO:0000269|PubMed:12447691, ECO:0000269|PubMed:18174154, FT ECO:0000269|PubMed:24018379" FT MUTAGEN 82 FT /note="K->R: Loss of kinase activity. No effect on FT RIOK2-binding." FT /evidence="ECO:0000269|PubMed:18615013, FT ECO:0000269|PubMed:19160488, ECO:0000269|PubMed:21880710" FT MUTAGEN 130 FT /note="L->G: In analog-sensitive mutant; enlarged catalytic FT pocket to accommodate purine analogs; when associated with FT V-67." FT /evidence="ECO:0000269|PubMed:19468302" FT MUTAGEN 137 FT /note="S->A: No change in activity. Increases activity and FT restores recovery after DNA damage checkpoint; when FT associated with D-210." FT /evidence="ECO:0000269|PubMed:12207013, FT ECO:0000269|PubMed:18615013" FT MUTAGEN 137 FT /note="S->D: Increases activity. Results in a block in FT G1/S." FT /evidence="ECO:0000269|PubMed:12207013, FT ECO:0000269|PubMed:18615013" FT MUTAGEN 176 FT /note="D->N: Abolishes kinase activity." FT /evidence="ECO:0000269|PubMed:18615013" FT MUTAGEN 194 FT /note="D->A: Does not interfere with FRY-binding." FT /evidence="ECO:0000269|PubMed:22753416" FT MUTAGEN 210 FT /note="T->A: Abolishes activity. Abolishes checkpoint FT recovery." FT /evidence="ECO:0000269|PubMed:12207013, FT ECO:0000269|PubMed:12447691, ECO:0000269|PubMed:17461553, FT ECO:0000269|PubMed:18615013, ECO:0000269|PubMed:19160488" FT MUTAGEN 210 FT /note="T->D: Increases activity and restores recovery after FT DNA damage checkpoint." FT /evidence="ECO:0000269|PubMed:12207013, FT ECO:0000269|PubMed:12447691, ECO:0000269|PubMed:17461553, FT ECO:0000269|PubMed:18615013, ECO:0000269|PubMed:19160488" FT MUTAGEN 210 FT /note="T->V: Reduced catalytic activity, but no effect on FT affinity for ATP." FT /evidence="ECO:0000269|PubMed:12207013, FT ECO:0000269|PubMed:12447691, ECO:0000269|PubMed:17461553, FT ECO:0000269|PubMed:18615013, ECO:0000269|PubMed:19160488" FT MUTAGEN 337 FT /note="R->A: Interferes with ubiquitination and subsequent FT proteasomal degradation in anaphase; when associated with FT A-340." FT /evidence="ECO:0000269|PubMed:14734534, FT ECO:0000269|PubMed:18662541" FT MUTAGEN 340 FT /note="L->A: Interferes with ubiquitination and subsequent FT proteasomal degradation in anaphase; when associated with FT A-337." FT /evidence="ECO:0000269|PubMed:14734534, FT ECO:0000269|PubMed:18662541" FT MUTAGEN 414 FT /note="W->F: Abolishes interaction with CDC25C and reduces FT centrosomal localization." FT /evidence="ECO:0000269|PubMed:17307877" FT MUTAGEN 414 FT /note="W->F: No effect on centrosomal localization, nor on FT S-phase progression; when asscociated with A-427. Loss of FT centrosomal localization and of S-phase progression; when FT associated with A- 415 and A-427." FT /evidence="ECO:0000269|PubMed:24018379" FT MUTAGEN 415 FT /note="V->A: Loss of centrosomal localization and of FT S-phase progression; when associated with A- 414 and FT A-427." FT /evidence="ECO:0000269|PubMed:24018379" FT MUTAGEN 427 FT /note="L->A: No effect on centrosomal localization, nor on FT S-phase progression; when associated with A-414. Loss of FT centrosomal localization and of S-phase progression; when FT associated with A- 414 and A-415." FT /evidence="ECO:0000269|PubMed:24018379" FT MUTAGEN 492 FT /note="K->R: Severe mitotic defects leading to prometaphase FT delay. Increased localization at kinetochores leading to FT increased levels of phosphorylated BUBR1." FT /evidence="ECO:0000269|PubMed:23455478" FT MUTAGEN 538 FT /note="H->A: In pincer mutant; loss of centrosomal location FT and decreased interaction with phosphorylated CDC25C and FT BUB1; when associated with M-540." FT /evidence="ECO:0000269|PubMed:14532005, FT ECO:0000269|PubMed:16760428, ECO:0000269|PubMed:18477460, FT ECO:0000269|PubMed:19468302" FT MUTAGEN 540 FT /note="K->M: In pincer mutant; loss of centrosomal location FT and decreased interaction with phosphorylated CDC25C and FT BUB1; when associated with A-538." FT /evidence="ECO:0000269|PubMed:14532005, FT ECO:0000269|PubMed:16760428, ECO:0000269|PubMed:18477460, FT ECO:0000269|PubMed:19468302" FT CONFLICT 2 FT /note="S -> T (in Ref. 1; AAA56634)" FT /evidence="ECO:0000305" FT CONFLICT 11 FT /note="A -> P (in Ref. 1; AAA56634)" FT /evidence="ECO:0000305" FT CONFLICT 58 FT /note="F -> L (in Ref. 1; AAA56634)" FT /evidence="ECO:0000305" FT CONFLICT 60 FT /note="G -> S (in Ref. 1; AAA56634)" FT /evidence="ECO:0000305" FT CONFLICT 73 FT /note="A -> V (in Ref. 2; AAA36659 and 7; AAB36946)" FT /evidence="ECO:0000305" FT CONFLICT 123 FT /note="N -> T (in Ref. 6; CAA62260)" FT /evidence="ECO:0000305" FT CONFLICT 141 FT /note="L -> P (in Ref. 4; CAA53536)" FT /evidence="ECO:0000305" FT CONFLICT 227 FT /note="G -> E (in Ref. 4; CAA53536)" FT /evidence="ECO:0000305" FT CONFLICT 301 FT /note="N -> G (in Ref. 2; AAA36659)" FT /evidence="ECO:0000305" FT CONFLICT 495 FT /note="A -> G (in Ref. 2; AAA36659)" FT /evidence="ECO:0000305" FT CONFLICT 501 FT /note="E -> Q (in Ref. 2; AAA36659)" FT /evidence="ECO:0000305" FT STRAND 42..46 FT /evidence="ECO:0007829|PDB:2RKU" FT TURN 47..50 FT /evidence="ECO:0007829|PDB:2RKU" FT STRAND 51..62 FT /evidence="ECO:0007829|PDB:2RKU" FT STRAND 65..72 FT /evidence="ECO:0007829|PDB:2RKU" FT TURN 73..75 FT /evidence="ECO:0007829|PDB:2RKU" FT STRAND 78..85 FT /evidence="ECO:0007829|PDB:2RKU" FT HELIX 86..88 FT /evidence="ECO:0007829|PDB:2RKU" FT HELIX 92..106 FT /evidence="ECO:0007829|PDB:2RKU" FT STRAND 116..121 FT /evidence="ECO:0007829|PDB:2RKU" FT STRAND 123..131 FT /evidence="ECO:0007829|PDB:2RKU" FT HELIX 138..145 FT /evidence="ECO:0007829|PDB:2RKU" FT HELIX 150..169 FT /evidence="ECO:0007829|PDB:2RKU" FT HELIX 179..181 FT /evidence="ECO:0007829|PDB:2RKU" FT STRAND 182..184 FT /evidence="ECO:0007829|PDB:2RKU" FT STRAND 190..192 FT /evidence="ECO:0007829|PDB:2RKU" FT HELIX 220..223 FT /evidence="ECO:0007829|PDB:2RKU" FT STRAND 224..226 FT /evidence="ECO:0007829|PDB:2V5Q" FT HELIX 231..246 FT /evidence="ECO:0007829|PDB:2RKU" FT HELIX 256..264 FT /evidence="ECO:0007829|PDB:2RKU" FT HELIX 276..285 FT /evidence="ECO:0007829|PDB:2RKU" FT HELIX 290..292 FT /evidence="ECO:0007829|PDB:2RKU" FT HELIX 296..301 FT /evidence="ECO:0007829|PDB:2RKU" FT HELIX 303..306 FT /evidence="ECO:0007829|PDB:2RKU" FT HELIX 316..319 FT /evidence="ECO:0007829|PDB:2RKU" FT HELIX 367..370 FT /evidence="ECO:0007829|PDB:5J19" FT HELIX 374..386 FT /evidence="ECO:0007829|PDB:4X9R" FT HELIX 389..391 FT /evidence="ECO:0007829|PDB:4X9R" FT STRAND 392..394 FT /evidence="ECO:0007829|PDB:3P34" FT HELIX 397..400 FT /evidence="ECO:0007829|PDB:4X9R" FT HELIX 403..405 FT /evidence="ECO:0007829|PDB:4X9R" FT STRAND 411..417 FT /evidence="ECO:0007829|PDB:4X9R" FT TURN 418..421 FT /evidence="ECO:0007829|PDB:4X9R" FT STRAND 422..427 FT /evidence="ECO:0007829|PDB:4X9R" FT STRAND 432..436 FT /evidence="ECO:0007829|PDB:4X9R" FT STRAND 441..444 FT /evidence="ECO:0007829|PDB:4X9R" FT STRAND 448..454 FT /evidence="ECO:0007829|PDB:4X9R" FT STRAND 460..464 FT /evidence="ECO:0007829|PDB:4X9R" FT TURN 465..467 FT /evidence="ECO:0007829|PDB:3Q1I" FT HELIX 470..472 FT /evidence="ECO:0007829|PDB:4X9R" FT HELIX 473..488 FT /evidence="ECO:0007829|PDB:4X9R" FT TURN 493..496 FT /evidence="ECO:0007829|PDB:4X9R" FT TURN 503..505 FT /evidence="ECO:0007829|PDB:3P34" FT STRAND 511..516 FT /evidence="ECO:0007829|PDB:4X9R" FT STRAND 518..525 FT /evidence="ECO:0007829|PDB:4X9R" FT TURN 526..528 FT /evidence="ECO:0007829|PDB:4WHL" FT STRAND 530..534 FT /evidence="ECO:0007829|PDB:4X9R" FT TURN 535..537 FT /evidence="ECO:0007829|PDB:4X9R" FT STRAND 540..544 FT /evidence="ECO:0007829|PDB:4X9R" FT TURN 545..548 FT /evidence="ECO:0007829|PDB:4X9R" FT STRAND 549..553 FT /evidence="ECO:0007829|PDB:4X9R" FT STRAND 559..563 FT /evidence="ECO:0007829|PDB:4X9R" FT HELIX 564..570 FT /evidence="ECO:0007829|PDB:4X9R" FT HELIX 574..591 FT /evidence="ECO:0007829|PDB:4X9R" FT STRAND 593..595 FT /evidence="ECO:0007829|PDB:4O56" FT STRAND 598..602 FT /evidence="ECO:0007829|PDB:4O56" SQ SEQUENCE 603 AA; 68255 MW; 178C2F13C10E8206 CRC64; MSAAVTAGKL ARAPADPGKA GVPGVAAPGA PAAAPPAKEI PEVLVDPRSR RRYVRGRFLG KGGFAKCFEI SDADTKEVFA GKIVPKSLLL KPHQREKMSM EISIHRSLAH QHVVGFHGFF EDNDFVFVVL ELCRRRSLLE LHKRRKALTE PEARYYLRQI VLGCQYLHRN RVIHRDLKLG NLFLNEDLEV KIGDFGLATK VEYDGERKKT LCGTPNYIAP EVLSKKGHSF EVDVWSIGCI MYTLLVGKPP FETSCLKETY LRIKKNEYSI PKHINPVAAS LIQKMLQTDP TARPTINELL NDEFFTSGYI PARLPITCLT IPPRFSIAPS SLDPSNRKPL TVLNKGLENP LPERPREKEE PVVRETGEVV DCHLSDMLQQ LHSVNASKPS ERGLVRQEEA EDPACIPIFW VSKWVDYSDK YGLGYQLCDN SVGVLFNDST RLILYNDGDS LQYIERDGTE SYLTVSSHPN SLMKKITLLK YFRNYMSEHL LKAGANITPR EGDELARLPY LRTWFRTRSA IILHLSNGSV QINFFQDHTK LILCPLMAAV TYIDEKRDFR TYRLSLLEEY GCCKELASRL RYARTMVDKL LSSRSASNRL KAS //