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Serine/threonine-protein kinase PLK1 (EC 2.7.11.21) (Polo-like kinase 1) (PLK-1) (Serine/threonine-protein kinase 13) (STPK13)

 PLK1_HUMAN              Reviewed;         603 AA.
P53350; Q15153; Q99746;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
23-MAY-2018, entry version 208.
RecName: Full=Serine/threonine-protein kinase PLK1;
EC=2.7.11.21 {ECO:0000269|PubMed:11202906, ECO:0000269|PubMed:12207013, ECO:0000269|PubMed:21880710};
AltName: Full=Polo-like kinase 1;
Short=PLK-1;
AltName: Full=Serine/threonine-protein kinase 13;
Short=STPK13;
Name=PLK1; Synonyms=PLK;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=8018557;
Hamanaka R., Maloid S., Smith M.R., O'Connell C.D., Longo D.L.,
Ferris D.K.;
"Cloning and characterization of human and murine homologues of the
Drosophila polo serine-threonine kinase.";
Cell Growth Differ. 5:249-257(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7902533; DOI=10.1128/MCB.13.12.7793;
Lake R.J., Jelinek W.R.;
"Cell cycle- and terminal differentiation-associated regulation of the
mouse mRNA encoding a conserved mitotic protein kinase.";
Mol. Cell. Biol. 13:7793-7801(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7962193;
Golsteyn R.M., Schultz S.J., Bartek J., Ziemiecki A., Ried T.,
Nigg E.A.;
"Cell cycle analysis and chromosomal localization of human Plk1, a
putative homologue of the mitotic kinases Drosophila polo and
Saccharomyces cerevisiae Cdc5.";
J. Cell Sci. 107:1509-1517(1994).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lung;
PubMed=8127874; DOI=10.1073/pnas.91.5.1736;
Holtrich U., Wolf G., Braeuninger A., Karn T., Boehme B.,
Ruebsamen-Waigmann H., Strebhardt K.;
"Induction and down-regulation of PLK, a human serine/threonine kinase
expressed in proliferating cells and tumors.";
Proc. Natl. Acad. Sci. U.S.A. 91:1736-1740(1994).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon, and Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-136.
PubMed=7478607;
Brauninger A., Strebhardt K., Rubsamen-Waigmann H.;
"Identification and functional characterization of the human and
murine polo-like kinase (Plk) promoter.";
Oncogene 11:1793-1800(1995).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-136.
PubMed=9083047; DOI=10.1074/jbc.272.14.9166;
Uchiumi T., Longo D.L., Ferris D.K.;
"Cell cycle regulation of the human polo-like kinase (PLK) promoter.";
J. Biol. Chem. 272:9166-9174(1997).
[8]
FUNCTION IN CENTROSOME MATURATION, AND SUBCELLULAR LOCATION.
PubMed=8991084; DOI=10.1083/jcb.135.6.1701;
Lane H.A., Nigg E.A.;
"Antibody microinjection reveals an essential role for human polo-like
kinase 1 (Plk1) in the functional maturation of mitotic centrosomes.";
J. Cell Biol. 135:1701-1713(1996).
[9]
FUNCTION IN PHOSPHORYLATION OF CDC25C.
PubMed=11202906; DOI=10.1016/S0898-6568(00)00080-2;
Roshak A.K., Capper E.A., Imburgia C., Fornwald J., Scott G.,
Marshall L.A.;
"The human polo-like kinase, PLK, regulates cdc2/cyclin B through
phosphorylation and activation of the cdc25C phosphatase.";
Cell. Signal. 12:405-411(2000).
[10]
FUNCTION, PHOSPHORYLATION AT SER-137 AND THR-210, AND MUTAGENESIS OF
LYS-82; SER-137 AND THR-210.
PubMed=12207013; DOI=10.1074/jbc.M202172200;
Jang Y.-J., Ma S., Terada Y., Erikson R.L.;
"Phosphorylation of threonine 210 and the role of serine 137 in the
regulation of mammalian polo-like kinase.";
J. Biol. Chem. 277:44115-44120(2002).
[11]
FUNCTION IN PHOSPHORYLATION OF CCNB1, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF LYS-82 AND THR-210.
PubMed=12447691; DOI=10.1038/sj.onc.1206011;
Yuan J., Eckerdt F., Bereiter-Hahn J., Kurunci-Csacsko E.,
Kaufmann M., Strebhardt K.;
"Cooperative phosphorylation including the activity of polo-like
kinase 1 regulates the subcellular localization of cyclin B1.";
Oncogene 21:8282-8292(2002).
[12]
PHOSPHORYLATION AT SER-335.
PubMed=12442251;
DOI=10.1002/1615-9861(200211)2:11<1516::AID-PROT1516>3.0.CO;2-Y;
Wind M., Kelm O., Nigg E.A., Lehmann W.D.;
"Identification of phosphorylation sites in the polo-like kinases Plx1
and Plk1 by a novel strategy based on element and electrospray high
resolution mass spectrometry.";
Proteomics 2:1516-1523(2002).
[13]
FUNCTION IN PHOSPHORYLATION OF NINL.
PubMed=12852856; DOI=10.1016/S1534-5807(03)00193-X;
Casenghi M., Meraldi P., Weinhart U., Duncan P.I., Korner R.,
Nigg E.A.;
"Polo-like kinase 1 regulates Nlp, a centrosome protein involved in
microtubule nucleation.";
Dev. Cell 5:113-125(2003).
[14]
PHOSPHORYLATION BY STK10.
PubMed=12639966; DOI=10.1074/jbc.M212556200;
Walter S.A., Cutler R.E. Jr., Martinez R., Gishizky M., Hill R.J.;
"Stk10, a new member of the polo-like kinase kinase family highly
expressed in hematopoietic tissue.";
J. Biol. Chem. 278:18221-18228(2003).
[15]
FUNCTION IN PHOSPHORYLATION OF PKMYT1.
PubMed=12738781; DOI=10.1074/jbc.C300126200;
Nakajima H., Toyoshima-Morimoto F., Taniguchi E., Nishida E.;
"Identification of a consensus motif for Plk (Polo-like kinase)
phosphorylation reveals Myt1 as a Plk1 substrate.";
J. Biol. Chem. 278:25277-25280(2003).
[16]
FUNCTION IN PHOSPHORYLATION OF KIF20A, DOMAIN POLO BOX, SUBCELLULAR
LOCATION, AND INTERACTION WITH KIF20A.
PubMed=12939256; DOI=10.1083/jcb.200306009;
Neef R., Preisinger C., Sutcliffe J., Kopajtich R., Nigg E.A.,
Mayer T.U., Barr F.A.;
"Phosphorylation of mitotic kinesin-like protein 2 by polo-like kinase
1 is required for cytokinesis.";
J. Cell Biol. 162:863-875(2003).
[17]
FUNCTION IN PHOSPHORYLATION OF CCNB1, AND SUBCELLULAR LOCATION.
PubMed=12524548; DOI=10.1038/ncb918;
Jackman M., Lindon C., Nigg E.A., Pines J.;
"Active cyclin B1-Cdk1 first appears on centrosomes in prophase.";
Nat. Cell Biol. 5:143-148(2003).
[18]
FUNCTION, PROTEASOMAL DEGRADATION, DOMAIN D-BOX MOTIF, AND MUTAGENESIS
OF ARG-337 AND LEU-340.
PubMed=14734534; DOI=10.1083/jcb.200309035;
Lindon C., Pines J.;
"Ordered proteolysis in anaphase inactivates Plk1 to contribute to
proper mitotic exit in human cells.";
J. Cell Biol. 164:233-241(2004).
[19]
FUNCTION IN PHOSPHORYLATION OF FBXO5.
PubMed=15469984; DOI=10.1091/mbc.E04-07-0598;
Hansen D.V., Loktev A.V., Ban K.H., Jackson P.K.;
"Plk1 regulates activation of the anaphase promoting complex by
phosphorylating and triggering SCFbetaTrCP-dependent destruction of
the APC inhibitor Emi1.";
Mol. Biol. Cell 15:5623-5634(2004).
[20]
FUNCTION IN PHOSPHORYLATION OF WEE1.
PubMed=15070733; DOI=10.1073/pnas.0307700101;
Watanabe N., Arai H., Nishihara Y., Taniguchi M., Watanabe N.,
Hunter T., Osada H.;
"M-phase kinases induce phospho-dependent ubiquitination of somatic
Wee1 by SCFbeta-TrCP.";
Proc. Natl. Acad. Sci. U.S.A. 101:4419-4424(2004).
[21]
FUNCTION IN PHOSPHORYLATION OF FBXO5.
PubMed=15148369; DOI=10.1073/pnas.0402442101;
Moshe Y., Boulaire J., Pagano M., Hershko A.;
"Role of Polo-like kinase in the degradation of early mitotic
inhibitor 1, a regulator of the anaphase promoting
complex/cyclosome.";
Proc. Natl. Acad. Sci. U.S.A. 101:7937-7942(2004).
[22]
FUNCTION IN PHOSPHORYLATION OF CEP55.
PubMed=16198290; DOI=10.1016/j.devcel.2005.09.003;
Fabbro M., Zhou B.-B., Takahashi M., Sarcevic B., Lal P., Graham M.E.,
Gabrielli B.G., Robinson P.J., Nigg E.A., Ono Y., Khanna K.K.;
"Cdk1/Erk2- and Plk1-dependent phosphorylation of a centrosome
protein, Cep55, is required for its recruitment to midbody and
cytokinesis.";
Dev. Cell 9:477-488(2005).
[23]
FUNCTION IN PHOSPHORYLATION OF HSF1, AND INTERACTION WITH HSF1.
PubMed=15661742; DOI=10.1074/jbc.M411908200;
Kim S.A., Yoon J.H., Lee S.H., Ahn S.G.;
"Polo-like kinase 1 phosphorylates heat shock transcription factor 1
and mediates its nuclear translocation during heat stress.";
J. Biol. Chem. 280:12653-12657(2005).
[24]
INTERACTION WITH CEP170.
PubMed=15616186; DOI=10.1091/mbc.E04-10-0939;
Guarguaglini G., Duncan P.I., Stierhof Y.D., Holmstroem T.,
Duensing S., Nigg E.A.;
"The forkhead-associated domain protein Cep170 interacts with Polo-
like kinase 1 and serves as a marker for mature centrioles.";
Mol. Biol. Cell 16:1095-1107(2005).
[25]
INTERACTION WITH EVI5.
PubMed=16439210; DOI=10.1016/j.cell.2005.10.038;
Eldridge A.G., Loktev A.V., Hansen D.V., Verschuren E.W.,
Reimann J.D.R., Jackson P.K.;
"The evi5 oncogene regulates cyclin accumulation by stabilizing the
anaphase-promoting complex inhibitor emi1.";
Cell 124:367-380(2006).
[26]
SUBCELLULAR LOCATION, INTERACTION WITH BUB1 AND BUB1B, AND MUTAGENESIS
OF HIS-538 AND LYS-540.
PubMed=16760428; DOI=10.1091/mbc.E06-03-0240;
Qi W., Tang Z., Yu H.;
"Phosphorylation- and polo-box-dependent binding of Plk1 to Bub1 is
required for the kinetochore localization of Plk1.";
Mol. Biol. Cell 17:3705-3716(2006).
[27]
FUNCTION IN PHOSPHORYLATION OF KIZ.
PubMed=16980960; DOI=10.1038/ncb1474;
Oshimori N., Ohsugi M., Yamamoto T.;
"The Plk1 target Kizuna stabilizes mitotic centrosomes to ensure
spindle bipolarity.";
Nat. Cell Biol. 8:1095-1101(2006).
[28]
FUNCTION IN PHOSPHORYLATION OF ECT2, AND INTERACTION WITH ECT2.
PubMed=16247472; DOI=10.1038/sj.onc.1209124;
Niiya F., Tatsumoto T., Lee K.S., Miki T.;
"Phosphorylation of the cytokinesis regulator ECT2 at G2/M phase
stimulates association of the mitotic kinase Plk1 and accumulation of
GTP-bound RhoA.";
Oncogene 25:827-837(2006).
[29]
FUNCTION IN PHOSPHORYLATION OF CENPU.
PubMed=17081991; DOI=10.1016/j.molcel.2006.10.016;
Kang Y.H., Park J.-E., Yu L.-R., Soung N.-K., Yun S.-M., Bang J.K.,
Seong Y.-S., Yu H., Garfield S., Veenstra T.D., Lee K.S.;
"Self-regulated Plk1 recruitment to kinetochores by the Plk1-PBIP1
interaction is critical for proper chromosome segregation.";
Mol. Cell 24:409-422(2006).
[30]
INVOLVEMENT IN CANCER.
PubMed=16645325; DOI=10.1159/000093003;
Kanaji S., Saito H., Tsujitani S., Matsumoto S., Tatebe S., Kondo A.,
Ozaki M., Ito H., Ikeguchi M.;
"Expression of polo-like kinase 1 (PLK1) protein predicts the survival
of patients with gastric carcinoma.";
Oncology 70:126-133(2006).
[31]
INVOLVEMENT IN CANCER.
PubMed=17981789; DOI=10.1158/0008-5472.CAN-07-1887;
Salvatore G., Nappi T.C., Salerno P., Jiang Y., Garbi C., Ugolini C.,
Miccoli P., Basolo F., Castellone M.D., Cirafici A.M., Melillo R.M.,
Fusco A., Bittner M.L., Santoro M.;
"A cell proliferation and chromosomal instability signature in
anaplastic thyroid carcinoma.";
Cancer Res. 67:10148-10158(2007).
[32]
INTERACTION WITH ERCC6L.
PubMed=17218258; DOI=10.1016/j.cell.2006.11.041;
Baumann C., Koerner R., Hofmann K., Nigg E.A.;
"PICH, a centromere-associated SNF2 family ATPase, is regulated by
Plk1 and required for the spindle checkpoint.";
Cell 128:101-114(2007).
[33]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=17617734; DOI=10.4161/cc.6.13.4442;
Pouwels J., Kukkonen A.M., Lan W., Daum J.R., Gorbsky G.J.,
Stukenberg T., Kallio M.J.;
"Shugoshin 1 plays a central role in kinetochore assembly and is
required for kinetochore targeting of Plk1.";
Cell Cycle 6:1579-1585(2007).
[34]
INTERACTION WITH TTDN1.
PubMed=17310276; DOI=10.1007/s00018-007-6501-8;
Zhang Y., Tian Y., Chen Q., Chen D., Zhai Z., Shu H.-B.;
"TTDN1 is a Plk1-interacting protein involved in maintenance of cell
cycle integrity.";
Cell. Mol. Life Sci. 64:632-640(2007).
[35]
FUNCTION IN PHOSPHORYLATION OF BUB1B.
PubMed=17376779; DOI=10.1074/jbc.M611053200;
Matsumura S., Toyoshima F., Nishida E.;
"Polo-like kinase 1 facilitates chromosome alignment during
prometaphase through BubR1.";
J. Biol. Chem. 282:15217-15227(2007).
[36]
INVOLVEMENT IN CANCER.
PubMed=17943598; DOI=10.1080/10428190701615918;
Liu L., Zhang M., Zou P.;
"Expression of PLK1 and survivin in diffuse large B-cell lymphoma.";
Leuk. Lymphoma 48:2179-2183(2007).
[37]
FUNCTION IN PHOSPHORYLATION OF PRC1, AND DOMAIN POLO BOX.
PubMed=17351640; DOI=10.1038/ncb1557;
Neef R., Gruneberg U., Kopajtich R., Li X., Nigg E.A., Sillje H.,
Barr F.A.;
"Choice of Plk1 docking partners during mitosis and cytokinesis is
controlled by the activation state of Cdk1.";
Nat. Cell Biol. 9:436-444(2007).
[38]
INTERACTION WITH CYLD, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17495026; DOI=10.1073/pnas.0703268104;
Stegmeier F., Sowa M.E., Nalepa G., Gygi S.P., Harper J.W.,
Elledge S.J.;
"The tumor suppressor CYLD regulates entry into mitosis.";
Proc. Natl. Acad. Sci. U.S.A. 104:8869-8874(2007).
[39]
FUNCTION IN PHOSPHORYLATION OF HSF1, INTERACTION WITH HSF1, AND
SUBCELLULAR LOCATION.
PubMed=18794143; DOI=10.1158/0008-5472.CAN-08-0129;
Lee Y.J., Kim E.H., Lee J.S., Jeoung D., Bae S., Kwon S.H., Lee Y.S.;
"HSF1 as a mitotic regulator: phosphorylation of HSF1 by Plk1 is
essential for mitotic progression.";
Cancer Res. 68:7550-7560(2008).
[40]
UBIQUITINATION BY THE APC/C COMPLEX, INTERACTION WITH FZR1, AND
MUTAGENESIS OF ARG-337 AND LEU-340.
PubMed=18662541; DOI=10.1016/j.cell.2008.05.043;
Bassermann F., Frescas D., Guardavaccaro D., Busino L.,
Peschiaroli A., Pagano M.;
"The Cdc14B-Cdh1-Plk1 axis controls the G2 DNA-damage-response
checkpoint.";
Cell 134:256-267(2008).
[41]
INTERACTION WITH BIRC6/BRUCE.
PubMed=18329369; DOI=10.1016/j.cell.2008.01.012;
Pohl C., Jentsch S.;
"Final stages of cytokinesis and midbody ring formation are controlled
by BRUCE.";
Cell 132:832-845(2008).
[42]
FUNCTION IN PHOSPHORYLATION OF TP73.
PubMed=18418051; DOI=10.4161/cc.7.9.5777;
Soond S.M., Barry S.P., Melino G., Knight R.A., Latchman D.S.,
Stephanou A.;
"p73-mediated transcriptional activity is negatively regulated by
polo-like kinase 1.";
Cell Cycle 7:1214-1223(2008).
[43]
FUNCTION, AND INTERACTION WITH PHOSPHORYLATED BORA.
PubMed=18521620; DOI=10.1007/s00412-008-0165-5;
Chan E.H., Santamaria A., Sillje H.H., Nigg E.A.;
"Plk1 regulates mitotic Aurora A function through betaTrCP-dependent
degradation of hBora.";
Chromosoma 117:457-469(2008).
[44]
FUNCTION IN PHOSPHORYLATION OF SGO1, AND INTERACTION WITH SGO1.
PubMed=18331714; DOI=10.1016/j.devcel.2007.12.007;
Wang X., Yang Y., Duan Q., Jiang N., Huang Y., Darzynkiewicz Z.,
Dai W.;
"sSgo1, a major splice variant of Sgo1, functions in centriole
cohesion where it is regulated by Plk1.";
Dev. Cell 14:331-341(2008).
[45]
FUNCTION IN PHOSPHORYLATION OF PPP1R12A, PHOSPHORYLATION AT THR-210,
DEPHOSPHORYLATION BY PPP1C, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
HIS-538 AND LYS-540.
PubMed=18477460; DOI=10.1016/j.devcel.2008.02.013;
Yamashiro S., Yamakita Y., Totsukawa G., Goto H., Kaibuchi K., Ito M.,
Hartshorne D.J., Matsumura F.;
"Myosin phosphatase-targeting subunit 1 regulates mitosis by
antagonizing polo-like kinase 1.";
Dev. Cell 14:787-797(2008).
[46]
FUNCTION IN PHOSPHORYLATION OF TP73, AND MUTAGENESIS OF LYS-82.
PubMed=18174154; DOI=10.1074/jbc.M710608200;
Koida N., Ozaki T., Yamamoto H., Ono S., Koda T., Ando K., Okoshi R.,
Kamijo T., Omura K., Nakagawara A.;
"Inhibitory role of Plk1 in the regulation of p73-dependent apoptosis
through physical interaction and phosphorylation.";
J. Biol. Chem. 283:8555-8563(2008).
[47]
INTERACTION WITH FAM29A.
PubMed=19029337; DOI=10.1083/jcb.200807046;
Zhu H., Coppinger J.A., Jang C.-Y., Yates J.R. III, Fang G.;
"FAM29A promotes microtubule amplification via recruitment of the
NEDD1-gamma-tubulin complex to the mitotic spindle.";
J. Cell Biol. 183:835-848(2008).
[48]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-6; SER-103; THR-210;
THR-214; SER-375; SER-450 AND THR-498, 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).
[49]
FUNCTION IN PHOSPHORYLATION OF FOXM1, AND MUTAGENESIS OF LYS-82 AND
THR-210.
PubMed=19160488; DOI=10.1038/ncb1767;
Fu Z., Malureanu L., Huang J., Wang W., Li H., van Deursen J.M.,
Tindall D.J., Chen J.;
"Plk1-dependent phosphorylation of FoxM1 regulates a transcriptional
programme required for mitotic progression.";
Nat. Cell Biol. 10:1076-1082(2008).
[50]
FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT THR-210 BY AURKA,
SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-82; SER-137; ASP-176 AND
THR-210, AND ACTIVE SITE.
PubMed=18615013; DOI=10.1038/nature07185;
Macurek L., Lindqvist A., Lim D., Lampson M.A., Klompmaker R.,
Freire R., Clouin C., Taylor S.S., Yaffe M.B., Medema R.H.;
"Polo-like kinase-1 is activated by aurora A to promote checkpoint
recovery.";
Nature 455:119-123(2008).
[51]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-210 AND THR-214, 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).
[52]
INTERACTION WITH SLX4.
PubMed=19596235; DOI=10.1016/j.cell.2009.06.030;
Svendsen J.M., Smogorzewska A., Sowa M.E., O'Connell B.C., Gygi S.P.,
Elledge S.J., Harper J.W.;
"Mammalian BTBD12/SLX4 assembles a Holliday junction resolvase and is
required for DNA repair.";
Cell 138:63-77(2009).
[53]
FUNCTION IN PHOSPHORYLATION OF TOPORS, AND INTERACTION WITH TOPORS.
PubMed=19473992; DOI=10.1074/jbc.C109.001560;
Yang X., Li H., Zhou Z., Wang W.H., Deng A., Andrisani O., Liu X.;
"Plk1-mediated phosphorylation of Topors regulates p53 stability.";
J. Biol. Chem. 284:18588-18592(2009).
[54]
FUNCTION AS NEDD1 KINASE.
PubMed=19509060; DOI=10.1242/jcs.042747;
Zhang X., Chen Q., Feng J., Hou J., Yang F., Liu J., Jiang Q.,
Zhang C.;
"Sequential phosphorylation of Nedd1 by Cdk1 and Plk1 is required for
targeting of the gammaTuRC to the centrosome.";
J. Cell Sci. 122:2240-2251(2009).
[55]
FUNCTION, INTERACTION WITH KIF2A, AND SUBCELLULAR LOCATION.
PubMed=19351716; DOI=10.1242/jcs.044321;
Jang C.Y., Coppinger J.A., Seki A., Yates J.R. III, Fang G.;
"Plk1 and Aurora A regulate the depolymerase activity and the cellular
localization of Kif2a.";
J. Cell Sci. 122:1334-1341(2009).
[56]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-210 AND THR-214, 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).
[57]
FUNCTION IN PHOSPHORYLATION OF RACGAP1, INTERACTION WITH PRC1, AND
SUBCELLULAR LOCATION.
PubMed=19468300; DOI=10.1371/journal.pbio.1000110;
Wolfe B.A., Takaki T., Petronczki M., Glotzer M.;
"Polo-like kinase 1 directs assembly of the HsCyk-4 RhoGAP/Ect2 RhoGEF
complex to initiate cleavage furrow formation.";
PLoS Biol. 7:E1000110-E1000110(2009).
[58]
FUNCTION IN PHOSPHORYLATION OF RACGAP1, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF CYS-67; LEU-130; HIS-538 AND LYS-540.
PubMed=19468302; DOI=10.1371/journal.pbio.1000111;
Burkard M.E., Maciejowski J., Rodriguez-Bravo V., Repka M.,
Lowery D.M., Clauser K.R., Zhang C., Shokat K.M., Carr S.A.,
Yaffe M.B., Jallepalli P.V.;
"Plk1 self-organization and priming phosphorylation of HsCYK-4 at the
spindle midzone regulate the onset of division in human cells.";
PLoS Biol. 7:E1000111-E1000111(2009).
[59]
REVIEW ON FUNCTION, AND REVIEW ON ENZYME REGULATION.
PubMed=20671765; DOI=10.1038/nrd3184;
Strebhardt K.;
"Multifaceted polo-like kinases: drug targets and antitargets for
cancer therapy.";
Nat. Rev. Drug Discov. 9:643-660(2010).
[60]
FUNCTION IN PHOSPHORYLATION OF DCTN1, AND INTERACTION WITH DCTN1.
PubMed=20679239; DOI=10.1073/pnas.1006615107;
Li H., Liu X.S., Yang X., Song B., Wang Y., Liu X.;
"Polo-like kinase 1 phosphorylation of p150Glued facilitates nuclear
envelope breakdown during prophase.";
Proc. Natl. Acad. Sci. U.S.A. 107:14633-14638(2010).
[61]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-210, 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).
[62]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[63]
FUNCTION IN PHOSPHORYLATION OF RIOK2, AND MUTAGENESIS OF LYS-82.
PubMed=21880710; DOI=10.1074/jbc.M111.250175;
Liu T., Deng M., Li J., Tong X., Wei Q., Ye X.;
"Phosphorylation of right open reading frame 2 (Rio2) protein kinase
by polo-like kinase 1 regulates mitotic progression.";
J. Biol. Chem. 286:36352-36360(2011).
[64]
IDENTIFICATION IN A COMPLEX WITH KNSTRN; SPAG5; DYNLL1 AND SGO2.
PubMed=21402792; DOI=10.1083/jcb.201008023;
Dunsch A.K., Linnane E., Barr F.A., Gruneberg U.;
"The astrin-kinastrin/SKAP complex localizes to microtubule plus ends
and facilitates chromosome alignment.";
J. Cell Biol. 192:959-968(2011).
[65]
INTERACTION WITH FRY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
ASP-194.
PubMed=22753416; DOI=10.1074/jbc.M112.378968;
Ikeda M., Chiba S., Ohashi K., Mizuno K.;
"Furry protein promotes Aurora A-mediated polo-like kinase 1
activation.";
J. Biol. Chem. 287:27670-27681(2012).
[66]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[67]
INTERACTION WITH FOPNL, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
LYS-82; TRP-414; VAL-415 AND LEU-427.
PubMed=24018379; DOI=10.1038/cr.2013.127;
Shen M., Cai Y., Yang Y., Yan X., Liu X., Zhou T.;
"Centrosomal protein FOR20 is essential for S-phase progression by
recruiting Plk1 to centrosomes.";
Cell Res. 23:1284-1295(2013).
[68]
INTERACTION WITH DCTN6, AND SUBCELLULAR LOCATION.
PubMed=23455152; DOI=10.1038/emboj.2013.30;
Yeh T.Y., Kowalska A.K., Scipioni B.R., Cheong F.K., Zheng M.,
Derewenda U., Derewenda Z.S., Schroer T.A.;
"Dynactin helps target Polo-like kinase 1 to kinetochores via its
left-handed beta-helical p27 subunit.";
EMBO J. 32:1023-1035(2013).
[69]
FUNCTION IN PHOSPHORYLATION OF MISP.
PubMed=23509069; DOI=10.1083/jcb.201207050;
Zhu M., Settele F., Kotak S., Sanchez-Pulido L., Ehret L.,
Ponting C.P., Goenczy P., Hoffmann I.;
"MISP is a novel Plk1 substrate required for proper spindle
orientation and mitotic progression.";
J. Cell Biol. 200:773-787(2013).
[70]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-210, 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).
[71]
FUNCTION, SUBCELLULAR LOCATION, UBIQUITINATION AT LYS-9 AND LYS-492,
AND MUTAGENESIS OF LYS-492.
PubMed=23455478; DOI=10.1038/ncb2695;
Beck J., Maerki S., Posch M., Metzger T., Persaud A., Scheel H.,
Hofmann K., Rotin D., Pedrioli P., Swedlow J.R., Peter M., Sumara I.;
"Ubiquitylation-dependent localization of PLK1 in mitosis.";
Nat. Cell Biol. 15:430-439(2013).
[72]
INTERACTION WITH HNRNPU, AND FUNCTION IN PHOSPHORYLATION OF HNRNPU.
PubMed=25986610; DOI=10.1128/MCB.01312-14;
Douglas P., Ye R., Morrice N., Britton S., Trinkle-Mulcahy L.,
Lees-Miller S.P.;
"Phosphorylation of SAF-A/hnRNP-U serine 59 by polo-like kinase 1 is
required for mitosis.";
Mol. Cell. Biol. 35:2699-2713(2015).
[73]
FUNCTION, AND INTERACTION WITH CEP68.
PubMed=25503564; DOI=10.1038/ncb3076;
Pagan J.K., Marzio A., Jones M.J., Saraf A., Jallepalli P.V.,
Florens L., Washburn M.P., Pagano M.;
"Degradation of Cep68 and PCNT cleavage mediate Cep215 removal from
the PCM to allow centriole separation, disengagement and licensing.";
Nat. Cell Biol. 17:31-43(2015).
[74]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-338, 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).
[75]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 367-603 IN COMPLEX WITH
PHOSPHORYLATED PEPTIDE, FUNCTION, SUBCELLULAR LOCATION, DOMAIN POLO
BOX, INTERACTION WITH CDC25C, AND MUTAGENESIS OF HIS-538 AND LYS-540.
PubMed=14532005; DOI=10.1016/S0092-8674(03)00725-6;
Elia A.E., Rellos P., Haire L.F., Chao J.W., Ivins F.J., Hoepker K.,
Mohammad D., Cantley L.C., Smerdon S.J., Yaffe M.B.;
"The molecular basis for phosphodependent substrate targeting and
regulation of Plks by the Polo-box domain.";
Cell 115:83-95(2003).
[76]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 367-603 IN COMPLEX WITH
PHOSPHORYLATED PEPTIDE.
PubMed=14592974; DOI=10.1093/emboj/cdg558;
Cheng K.Y., Lowe E.D., Sinclair J., Nigg E.A., Johnson L.N.;
"The crystal structure of the human polo-like kinase-1 polo box domain
and its phospho-peptide complex.";
EMBO J. 22:5757-5768(2003).
[77]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 13-345 OF MUTANT VAL-210 IN
COMPLEXES WITH ATP ANALOGS, AND MUTAGENESIS OF THR-210.
PubMed=17461553; DOI=10.1021/bi602474j;
Kothe M., Kohls D., Low S., Coli R., Cheng A.C., Jacques S.L.,
Johnson T.L., Lewis C., Loh C., Nonomiya J., Sheils A.L.,
Verdries K.A., Wynn T.A., Kuhn C., Ding Y.H.;
"Structure of the catalytic domain of human polo-like kinase 1.";
Biochemistry 46:5960-5971(2007).
[78]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 37-330 IN COMPLEX WITH
SYNTHETIC INHIBITOR BI 2536.
PubMed=18005335; DOI=10.1111/j.1747-0285.2007.00594.x;
Kothe M., Kohls D., Low S., Coli R., Rennie G.R., Feru F., Kuhn C.,
Ding Y.H.;
"Selectivity-determining residues in Plk1.";
Chem. Biol. Drug Des. 70:540-546(2007).
[79]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 365-603 IN COMPLEX WITH
CDC25C, SUBCELLULAR LOCATION, INTERACTION WITH CDC25C, ENZYME
REGULATION, AND MUTAGENESIS OF TRP-414.
PubMed=17307877; DOI=10.1073/pnas.0609131104;
Garcia-Alvarez B., de Carcer G., Ibanez S., Bragado-Nilsson E.,
Montoya G.;
"Molecular and structural basis of polo-like kinase 1 substrate
recognition: Implications in centrosomal localization.";
Proc. Natl. Acad. Sci. U.S.A. 104:3107-3112(2007).
[80]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 33-345 IN COMPLEX WITH A
DARPIN.
PubMed=18391401; DOI=10.1107/S0907444907068217;
Bandeiras T.M., Hillig R.C., Matias P.M., Eberspaecher U.,
Fanghanel J., Thomaz M., Miranda S., Crusius K., Putter V.,
Amstutz P., Gulotti-Georgieva M., Binz H.K., Holz C., Schmitz A.A.,
Lang C., Donner P., Egner U., Carrondo M.A., Muller-Tiemann B.;
"Structure of wild-type Plk-1 kinase domain in complex with a
selective DARPin.";
Acta Crystallogr. D 64:339-353(2008).
[81]
X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 371-603 IN COMPLEX WITH
PHOSPHOPEPTIDE, FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH
PHOSPHORYLATED CENPU.
PubMed=19597481; DOI=10.1038/nsmb.1628;
Yun S.M., Moulaei T., Lim D., Bang J.K., Park J.E., Shenoy S.R.,
Liu F., Kang Y.H., Liao C., Soung N.K., Lee S., Yoon D.Y., Lim Y.,
Lee D.H., Otaka A., Appella E., McMahon J.B., Nicklaus M.C.,
Burke T.R. Jr., Yaffe M.B., Wlodawer A., Lee K.S.;
"Structural and functional analyses of minimal phosphopeptides
targeting the polo-box domain of polo-like kinase 1.";
Nat. Struct. Mol. Biol. 16:876-882(2009).
[82]
VARIANTS [LARGE SCALE ANALYSIS] LEU-12; PHE-261; VAL-332; HIS-463 AND
HIS-518.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Serine/threonine-protein kinase that performs several
important functions throughout M phase of the cell cycle,
including the regulation of centrosome maturation and spindle
assembly, the removal of cohesins from chromosome arms, the
inactivation of anaphase-promoting complex/cyclosome (APC/C)
inhibitors, and the regulation of mitotic exit and cytokinesis.
Polo-like kinase proteins acts by binding and phosphorylating
proteins are that already phosphorylated on a specific motif
recognized by the POLO box domains. Phosphorylates BORA,
BUB1B/BUBR1, CCNB1, CDC25C, CEP55, ECT2, ERCC6L, FBXO5/EMI1,
FOXM1, KIF20A/MKLP2, CENPU, NEDD1, NINL, NPM1, NUDC, PKMYT1/MYT1,
KIZ, PPP1R12A/MYPT1, PRC1, RACGAP1/CYK4, SGO1, STAG2/SA2, TEX14,
TOPORS, p73/TP73, TPT1, WEE1 and HNRNPU. Plays a key role in
centrosome functions and the assembly of bipolar spindles by
phosphorylating KIZ, NEDD1 and NINL. NEDD1 phosphorylation
promotes subsequent targeting of the gamma-tubulin ring complex
(gTuRC) to the centrosome, an important step for spindle
formation. Phosphorylation of NINL component of the centrosome
leads to NINL dissociation from other centrosomal proteins.
Involved in mitosis exit and cytokinesis by phosphorylating CEP55,
ECT2, KIF20A/MKLP2, CENPU, PRC1 and RACGAP1. Recruited at the
central spindle by phosphorylating and docking PRC1 and
KIF20A/MKLP2; creates its own docking sites on PRC1 and
KIF20A/MKLP2 by mediating phosphorylation of sites subsequently
recognized by the POLO box domains. Phosphorylates RACGAP1,
thereby creating a docking site for the Rho GTP exchange factor
ECT2 that is essential for the cleavage furrow formation. Promotes
the central spindle recruitment of ECT2. Plays a central role in
G2/M transition of mitotic cell cycle by phosphorylating CCNB1,
CDC25C, FOXM1, CENPU, PKMYT1/MYT1, PPP1R12A/MYPT1 and WEE1. Part
of a regulatory circuit that promotes the activation of CDK1 by
phosphorylating the positive regulator CDC25C and inhibiting the
negative regulators WEE1 and PKMYT1/MYT1. Also acts by mediating
phosphorylation of cyclin-B1 (CCNB1) on centrosomes in prophase.
Phosphorylates FOXM1, a key mitotic transcription regulator,
leading to enhance FOXM1 transcriptional activity. Involved in
kinetochore functions and sister chromatid cohesion by
phosphorylating BUB1B/BUBR1, FBXO5/EMI1 and STAG2/SA2. PLK1 is
high on non-attached kinetochores suggesting a role of PLK1 in
kinetochore attachment or in spindle assembly checkpoint (SAC)
regulation. Required for kinetochore localization of BUB1B.
Regulates the dissociation of cohesin from chromosomes by
phosphorylating cohesin subunits such as STAG2/SA2. Phosphorylates
SGO1: required for spindle pole localization of isoform 3 of SGO1
and plays a role in regulating its centriole cohesion function.
Mediates phosphorylation of FBXO5/EMI1, a negative regulator of
the APC/C complex during prophase, leading to FBXO5/EMI1
ubiquitination and degradation by the proteasome. Acts as a
negative regulator of p53 family members: phosphorylates TOPORS,
leading to inhibit the sumoylation of p53/TP53 and simultaneously
enhance the ubiquitination and subsequent degradation of p53/TP53.
Phosphorylates the transactivation domain of the transcription
factor p73/TP73, leading to inhibit p73/TP73-mediated
transcriptional activation and pro-apoptotic functions.
Phosphorylates BORA, and thereby promotes the degradation of BORA.
Contributes to the regulation of AURKA function. Also required for
recovery after DNA damage checkpoint and entry into mitosis.
Phosphorylates MISP, leading to stabilization of cortical and
astral microtubule attachments required for proper spindle
positioning (PubMed:8991084, PubMed:11202906, PubMed:12207013,
PubMed:12447691, PubMed:12524548, PubMed:12738781,
PubMed:12852856, PubMed:12939256, PubMed:14532005,
PubMed:14734534, PubMed:15070733, PubMed:15148369,
PubMed:15469984, PubMed:16198290, PubMed:16247472,
PubMed:16980960, PubMed:17081991, PubMed:17351640,
PubMed:17376779, PubMed:17617734, PubMed:18174154,
PubMed:18331714, PubMed:18418051, PubMed:18477460,
PubMed:18521620, PubMed:18615013, PubMed:19160488,
PubMed:19351716, PubMed:19468300, PubMed:19468302,
PubMed:19473992, PubMed:19509060, PubMed:19597481,
PubMed:23455478, PubMed:23509069). Together with MEIKIN, acts as a
regulator of kinetochore function during meiosis I: required both
for mono-orientation of kinetochores on sister chromosomes and
protection of centromeric cohesin from separase-mediated cleavage
(By similarity). Phosphorylates CEP68 and is required for its
degradation (PubMed:25503564). Regulates nuclear envelope
breakdown during prophase by phosphorylating DCTN1 resulting in
its localization in the nuclear envelope (PubMed:20679239).
Phosphorylates the heat shock transcription factor HSF1, promoting
HSF1 nuclear translocation upon heat shock (PubMed:15661742).
Phosphorylates HSF1 also in the early mitotic period; this
phosphorylation regulates HSF1 localization to the spindle pole,
the recruitment of the SCF(BTRC) ubiquitin ligase complex
induicing HSF1 degradation, and hence mitotic progression
(PubMed:18794143). Regulates mitotic progression by
phosphorylating RIOK2 (PubMed:21880710).
{ECO:0000250|UniProtKB:Q5F2C3, ECO:0000269|PubMed:11202906,
ECO:0000269|PubMed:12207013, ECO:0000269|PubMed:12447691,
ECO:0000269|PubMed:12524548, ECO:0000269|PubMed:12738781,
ECO:0000269|PubMed:12852856, ECO:0000269|PubMed:12939256,
ECO:0000269|PubMed:14532005, ECO:0000269|PubMed:14734534,
ECO:0000269|PubMed:15070733, ECO:0000269|PubMed:15148369,
ECO:0000269|PubMed:15469984, ECO:0000269|PubMed:15661742,
ECO:0000269|PubMed:16198290, ECO:0000269|PubMed:16247472,
ECO:0000269|PubMed:16980960, ECO:0000269|PubMed:17081991,
ECO:0000269|PubMed:17351640, ECO:0000269|PubMed:17376779,
ECO:0000269|PubMed:17617734, ECO:0000269|PubMed:18174154,
ECO:0000269|PubMed:18331714, ECO:0000269|PubMed:18418051,
ECO:0000269|PubMed:18477460, ECO:0000269|PubMed:18521620,
ECO:0000269|PubMed:18615013, ECO:0000269|PubMed:18794143,
ECO:0000269|PubMed:19160488, ECO:0000269|PubMed:19351716,
ECO:0000269|PubMed:19468300, ECO:0000269|PubMed:19468302,
ECO:0000269|PubMed:19473992, ECO:0000269|PubMed:19509060,
ECO:0000269|PubMed:19597481, ECO:0000269|PubMed:20679239,
ECO:0000269|PubMed:21880710, ECO:0000269|PubMed:23455478,
ECO:0000269|PubMed:23509069, ECO:0000269|PubMed:25503564,
ECO:0000269|PubMed:25986610, ECO:0000269|PubMed:8991084}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:11202906, ECO:0000269|PubMed:12207013,
ECO:0000269|PubMed:21880710}.
-!- ENZYME REGULATION: Activated by phosphorylation of Thr-210 by
AURKA; phosphorylation by AURKA is enhanced by BORA. Once
activated, activity is stimulated by binding target proteins.
Binding of target proteins has no effect on the non-activated
kinase. Several inhibitors targeting PLKs are currently in
development and are under investigation in a growing number of
clinical trials, such as BI 2536, an ATP-competitive PLK1
inhibitor or BI 6727, a dihydropteridinone that specifically
inhibits the catalytic activity of PLK1.
{ECO:0000269|PubMed:17307877, ECO:0000269|PubMed:18615013}.
-!- SUBUNIT: Interacts with CEP170 and EVI5. Interacts and
phosphorylates ERCC6L. Interacts with FAM29A. Interacts with
SLX4/BTBD12 and TTDN1. Interacts with BUB1B. Interacts (via POLO-
box domain) with the phosphorylated form of BUB1, CENPU and
CDC25C. Interacts with isoform 3 of SGO1. Interacts with BORA,
KIF2A and AURKA. Interacts with TOPORS and CYLD. Interacts with
ECT2; the interaction is stimulated upon phosphorylation of ECT2
on 'Thr-444'. Interacts with PRC1. Interacts with KIF20A/MKLP2
(when phosphorylated), leading to the recruitment at the central
spindle. Interacts (via POLO box domains) with PPP1R12A/MYPT1
(when previously phosphorylated by CDK1). Part of an astrin
(SPAG5)-kinastrin (SKAP) complex containing KNSTRN, SPAG5, PLK1,
DYNLL1 and SGO2. Interacts with BIRC6/bruce. Interacts with CDK1-
phosphorylated FRY; this interaction occurs in mitotic cells, but
not in interphase cells. FRY interaction facilitates AURKA-
mediated PLK1 phosphorylation. Interacts with CDK1-phosphorylated
DCTN6 during mitotic prometaphase; the interaction facilitates
recruitment to kinetochores. Interacts with CEP68; the interaction
phosphorylates CEP68 (PubMed:25503564). Interacts (via POLO-box
domain) with DCTN1 (PubMed:20679239). Interacts with FOPNL in
later G1, S, G2 and M phases of the cell cycle; this interaction
recruits PLK1 to centrosomes, a step required for S phase
progression (PubMed:24018379). Interacts with HSF1; this
interaction increases upon heat shock but does not modulate
neither HSF1 homotrimerization nor DNA-binding activities
(PubMed:15661742, PubMed:18794143). Interacts with HNRNPU; this
interaction induces phosphorylation of HNRNPU in mitosis
(PubMed:25986610). Interacts (via its N-terminus) to RIOK2
(PubMed:21880710). {ECO:0000269|PubMed:12939256,
ECO:0000269|PubMed:14532005, ECO:0000269|PubMed:14592974,
ECO:0000269|PubMed:15616186, ECO:0000269|PubMed:15661742,
ECO:0000269|PubMed:16247472, ECO:0000269|PubMed:16439210,
ECO:0000269|PubMed:16760428, ECO:0000269|PubMed:17218258,
ECO:0000269|PubMed:17307877, ECO:0000269|PubMed:17310276,
ECO:0000269|PubMed:17495026, ECO:0000269|PubMed:18005335,
ECO:0000269|PubMed:18329369, ECO:0000269|PubMed:18331714,
ECO:0000269|PubMed:18391401, ECO:0000269|PubMed:18521620,
ECO:0000269|PubMed:18662541, ECO:0000269|PubMed:18794143,
ECO:0000269|PubMed:19029337, ECO:0000269|PubMed:19351716,
ECO:0000269|PubMed:19468300, ECO:0000269|PubMed:19473992,
ECO:0000269|PubMed:19596235, ECO:0000269|PubMed:19597481,
ECO:0000269|PubMed:20679239, ECO:0000269|PubMed:21402792,
ECO:0000269|PubMed:21880710, ECO:0000269|PubMed:22753416,
ECO:0000269|PubMed:23455152, ECO:0000269|PubMed:24018379,
ECO:0000269|PubMed:25503564, ECO:0000269|PubMed:25986610}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-476768, EBI-476768;
Q99IB8:- (xeno); NbExp=4; IntAct=EBI-476768, EBI-6927873;
O14965:AURKA; NbExp=4; IntAct=EBI-476768, EBI-448680;
Q9Y2T1:AXIN2; NbExp=2; IntAct=EBI-476768, EBI-4400025;
Q9NR09:BIRC6; NbExp=4; IntAct=EBI-476768, EBI-1765160;
P54132:BLM; NbExp=4; IntAct=EBI-476768, EBI-621372;
Q6PGQ7:BORA; NbExp=3; IntAct=EBI-476768, EBI-719836;
P30307:CDC25C; NbExp=5; IntAct=EBI-476768, EBI-974439;
Q99741:CDC6; NbExp=6; IntAct=EBI-476768, EBI-374862;
Q71F23-1:CENPU; NbExp=5; IntAct=EBI-476768, EBI-15793375;
Q76N32:CEP68; NbExp=2; IntAct=EBI-476768, EBI-9051024;
O96017:CHEK2; NbExp=7; IntAct=EBI-476768, EBI-1180783;
Q60838:Dvl2 (xeno); NbExp=12; IntAct=EBI-476768, EBI-641940;
P23588:EIF4B; NbExp=3; IntAct=EBI-476768, EBI-970310;
Q2NKX8:ERCC6L; NbExp=3; IntAct=EBI-476768, EBI-1042535;
O60447:EVI5; NbExp=3; IntAct=EBI-476768, EBI-852291;
Q13158:FADD; NbExp=9; IntAct=EBI-476768, EBI-494804;
Q9NYZ3:GTSE1; NbExp=6; IntAct=EBI-476768, EBI-2511327;
P08107:HSPA1B; NbExp=5; IntAct=EBI-476768, EBI-629985;
O95251:KAT7; NbExp=6; IntAct=EBI-476768, EBI-473199;
P49736:MCM2; NbExp=2; IntAct=EBI-476768, EBI-374819;
P33993:MCM7; NbExp=4; IntAct=EBI-476768, EBI-355924;
Q00987:MDM2; NbExp=7; IntAct=EBI-476768, EBI-389668;
P23804:Mdm2 (xeno); NbExp=2; IntAct=EBI-476768, EBI-641788;
Q8TD19:NEK9; NbExp=5; IntAct=EBI-476768, EBI-1044009;
O75665:OFD1; NbExp=4; IntAct=EBI-476768, EBI-716327;
Q8IXK0:PHC2; NbExp=2; IntAct=EBI-476768, EBI-713786;
Q9H0H5:RACGAP1; NbExp=4; IntAct=EBI-476768, EBI-717233;
Q8IY92:SLX4; NbExp=7; IntAct=EBI-476768, EBI-2370740;
Q92844:TANK; NbExp=3; IntAct=EBI-476768, EBI-356349;
P04637:TP53; NbExp=6; IntAct=EBI-476768, EBI-366083;
Q12888:TP53BP1; NbExp=5; IntAct=EBI-476768, EBI-396540;
P70399-1:Tp53bp1 (xeno); NbExp=2; IntAct=EBI-476768, EBI-15790796;
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere,
kinetochore. Cytoplasm, cytoskeleton, microtubule organizing
center, centrosome {ECO:0000269|PubMed:24018379}. Cytoplasm,
cytoskeleton, spindle {ECO:0000269|PubMed:18794143}. Midbody.
Note=localization at the centrosome starts at the G1/S transition
(PubMed:24018379). During early stages of mitosis, the
phosphorylated form is detected on centrosomes and kinetochores.
Localizes to the outer kinetochore. Presence of SGO1 and
interaction with the phosphorylated form of BUB1 is required for
the kinetochore localization. Localizes onto the central spindle
by phosphorylating and docking at midzone proteins KIF20A/MKLP2
and PRC1. Colocalizes with FRY to separating centrosomes and
spindle poles from prophase to metaphase in mitosis, but not in
other stages of the cell cycle. Localization to the centrosome is
required for S phase progression (PubMed:24018379). Colocalizes
with HSF1 at the spindle poles during prometaphase
(PubMed:18794143). {ECO:0000269|PubMed:18794143,
ECO:0000269|PubMed:24018379}.
-!- TISSUE SPECIFICITY: Placenta and colon.
-!- DEVELOPMENTAL STAGE: Accumulates to a maximum during the G2 and M
phases, declines to a nearly undetectable level following mitosis
and throughout G1 phase, and then begins to accumulate again
during S phase.
-!- INDUCTION: By growth-stimulating agents.
-!- DOMAIN: The POLO box domains act as phosphopeptide-binding module
that recognize and bind serine-[phosphothreonine/phosphoserine]-
(proline/X) motifs. PLK1 recognizes and binds docking proteins
that are already phosphorylated on these motifs, and then
phosphorylates them. PLK1 can also create its own docking sites by
mediating phosphorylation of serine-
[phosphothreonine/phosphoserine]-(proline/X) motifs subsequently
recognized by the POLO box domains. {ECO:0000269|PubMed:12939256,
ECO:0000269|PubMed:14532005, ECO:0000269|PubMed:14734534,
ECO:0000269|PubMed:17351640}.
-!- PTM: Catalytic activity is enhanced by phosphorylation of Thr-210.
Phosphorylation at Thr-210 is first detected on centrosomes in the
G2 phase of the cell cycle, peaks in prometaphase and gradually
disappears from centrosomes during anaphase. Dephosphorylation at
Thr-210 at centrosomes is probably mediated by protein phosphatase
1C (PP1C), via interaction with PPP1R12A/MYPT1.
Autophosphorylation and phosphorylation of Ser-137 may not be
significant for the activation of PLK1 during mitosis, but may
enhance catalytic activity during recovery after DNA damage
checkpoint. Phosphorylated in vitro by STK10.
{ECO:0000269|PubMed:12207013, ECO:0000269|PubMed:12442251,
ECO:0000269|PubMed:12639966, ECO:0000269|PubMed:18477460,
ECO:0000269|PubMed:18615013}.
-!- PTM: Ubiquitinated by the anaphase promoting complex/cyclosome
(APC/C) in anaphase and following DNA damage, leading to its
degradation by the proteasome. Ubiquitination is mediated via its
interaction with FZR1/CDH1. Ubiquitination and subsequent
degradation prevents entry into mitosis and is essential to
maintain an efficient G2 DNA damage checkpoint. Monoubiquitination
at Lys-492 by the BCR(KLHL22) ubiquitin ligase complex does not
lead to degradation: it promotes PLK1 dissociation from
phosphoreceptor proteins and subsequent removal from kinetochores,
allowing silencing of the spindle assembly checkpoint (SAC) and
chromosome segregation. {ECO:0000269|PubMed:18662541,
ECO:0000269|PubMed:23455478}.
-!- DISEASE: Note=Defects in PLK1 are associated with some cancers,
such as gastric, thyroid or B-cell lymphomas. Expression is cancer
increased in tumor tissues with a poor prognosis, suggesting a
role in malignant transformations and carcinogenesis.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. CDC5/Polo subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PLK1ID41747ch16p12.html";
-----------------------------------------------------------------------
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EMBL; U01038; AAA56634.1; -; mRNA.
EMBL; L19559; AAA36659.1; -; mRNA.
EMBL; X73458; CAA51837.1; -; mRNA.
EMBL; X75932; CAA53536.1; -; mRNA.
EMBL; BC002369; AAH02369.1; -; mRNA.
EMBL; BC003002; AAH03002.1; -; mRNA.
EMBL; BC014846; AAH14846.1; -; mRNA.
EMBL; X90725; CAA62260.1; -; Genomic_DNA.
EMBL; U78073; AAB36946.1; -; Genomic_DNA.
CCDS; CCDS10616.1; -.
PIR; S34130; S34130.
RefSeq; NP_005021.2; NM_005030.5.
UniGene; Hs.592049; -.
PDB; 1Q4K; X-ray; 2.30 A; A/B/C=345-603.
PDB; 1Q4O; X-ray; 2.20 A; A/B=367-603.
PDB; 1UMW; X-ray; 1.90 A; A/B=367-603.
PDB; 2OGQ; X-ray; 1.95 A; A=365-603.
PDB; 2OJX; X-ray; 2.85 A; A=365-603.
PDB; 2OU7; X-ray; 2.40 A; A=13-345.
PDB; 2OWB; X-ray; 2.10 A; A=13-345.
PDB; 2RKU; X-ray; 1.95 A; A=37-330.
PDB; 2V5Q; X-ray; 2.30 A; A/B=33-345.
PDB; 2YAC; X-ray; 2.20 A; A=36-345.
PDB; 3BZI; X-ray; 2.10 A; A=365-603.
PDB; 3C5L; X-ray; 2.33 A; A=373-593.
PDB; 3FC2; X-ray; 2.45 A; A=13-345.
PDB; 3FVH; X-ray; 1.58 A; A=371-603.
PDB; 3HIH; X-ray; 1.70 A; A/B=371-593.
PDB; 3HIK; X-ray; 1.77 A; A=367-603.
PDB; 3KB7; X-ray; 2.50 A; A=36-345.
PDB; 3P2W; X-ray; 1.66 A; A=371-594.
PDB; 3P2Z; X-ray; 1.79 A; A=371-594.
PDB; 3P34; X-ray; 1.40 A; A=371-594.
PDB; 3P35; X-ray; 2.09 A; A/B/C=371-594.
PDB; 3P36; X-ray; 1.59 A; A=371-594.
PDB; 3P37; X-ray; 2.38 A; A/B/C=371-594.
PDB; 3Q1I; X-ray; 1.40 A; A=371-594.
PDB; 3RQ7; X-ray; 1.55 A; A=371-603.
PDB; 3THB; X-ray; 2.50 A; A=13-345.
PDB; 4A4L; X-ray; 2.35 A; A=36-345.
PDB; 4A4O; X-ray; 2.70 A; A=36-345.
PDB; 4DFW; X-ray; 1.55 A; A=367-603.
PDB; 4E67; X-ray; 2.10 A; A=371-594.
PDB; 4E9C; X-ray; 1.70 A; A=371-594.
PDB; 4E9D; X-ray; 2.75 A; A=371-594.
PDB; 4H5X; X-ray; 1.95 A; A/B=367-603.
PDB; 4H71; X-ray; 1.93 A; A/B=367-603.
PDB; 4HAB; X-ray; 2.65 A; A/B/C=371-593.
PDB; 4HCO; X-ray; 2.75 A; A/B=367-603.
PDB; 4HY2; X-ray; 2.00 A; A=371-595.
PDB; 4J52; X-ray; 2.30 A; A=38-330.
PDB; 4J53; X-ray; 2.50 A; A=38-330.
PDB; 4LKL; X-ray; 1.58 A; A=372-593.
PDB; 4LKM; X-ray; 2.00 A; A/C=371-601.
PDB; 4O56; X-ray; 1.80 A; A=367-603.
PDB; 4O6W; X-ray; 1.45 A; A=371-603.
PDB; 4O9W; X-ray; 1.69 A; A=373-594.
PDB; 4RCP; X-ray; 1.60 A; A=372-599.
PDB; 4WHH; X-ray; 1.90 A; A=371-603.
PDB; 4WHK; X-ray; 1.80 A; A=371-603.
PDB; 4WHL; X-ray; 2.71 A; A=371-603.
PDB; 4X9R; X-ray; 1.40 A; A=371-603.
PDB; 4X9V; X-ray; 1.43 A; A=371-603.
PDB; 4X9W; X-ray; 1.80 A; A=371-603.
PDB; 5J19; X-ray; 2.00 A; A/B=367-594.
PDB; 5NEI; X-ray; 2.68 A; A=371-603.
PDB; 5NMM; X-ray; 2.02 A; A=371-603.
PDB; 5NN1; X-ray; 1.78 A; A=371-603.
PDB; 5NN2; X-ray; 1.81 A; A=371-594.
PDB; 5TA6; X-ray; 2.50 A; A=13-345.
PDB; 5TA8; X-ray; 2.60 A; A=13-345.
PDBsum; 1Q4K; -.
PDBsum; 1Q4O; -.
PDBsum; 1UMW; -.
PDBsum; 2OGQ; -.
PDBsum; 2OJX; -.
PDBsum; 2OU7; -.
PDBsum; 2OWB; -.
PDBsum; 2RKU; -.
PDBsum; 2V5Q; -.
PDBsum; 2YAC; -.
PDBsum; 3BZI; -.
PDBsum; 3C5L; -.
PDBsum; 3FC2; -.
PDBsum; 3FVH; -.
PDBsum; 3HIH; -.
PDBsum; 3HIK; -.
PDBsum; 3KB7; -.
PDBsum; 3P2W; -.
PDBsum; 3P2Z; -.
PDBsum; 3P34; -.
PDBsum; 3P35; -.
PDBsum; 3P36; -.
PDBsum; 3P37; -.
PDBsum; 3Q1I; -.
PDBsum; 3RQ7; -.
PDBsum; 3THB; -.
PDBsum; 4A4L; -.
PDBsum; 4A4O; -.
PDBsum; 4DFW; -.
PDBsum; 4E67; -.
PDBsum; 4E9C; -.
PDBsum; 4E9D; -.
PDBsum; 4H5X; -.
PDBsum; 4H71; -.
PDBsum; 4HAB; -.
PDBsum; 4HCO; -.
PDBsum; 4HY2; -.
PDBsum; 4J52; -.
PDBsum; 4J53; -.
PDBsum; 4LKL; -.
PDBsum; 4LKM; -.
PDBsum; 4O56; -.
PDBsum; 4O6W; -.
PDBsum; 4O9W; -.
PDBsum; 4RCP; -.
PDBsum; 4WHH; -.
PDBsum; 4WHK; -.
PDBsum; 4WHL; -.
PDBsum; 4X9R; -.
PDBsum; 4X9V; -.
PDBsum; 4X9W; -.
PDBsum; 5J19; -.
PDBsum; 5NEI; -.
PDBsum; 5NMM; -.
PDBsum; 5NN1; -.
PDBsum; 5NN2; -.
PDBsum; 5TA6; -.
PDBsum; 5TA8; -.
DisProt; DP00428; -.
ProteinModelPortal; P53350; -.
SMR; P53350; -.
BioGrid; 111362; 261.
DIP; DIP-29696N; -.
ELM; P53350; -.
IntAct; P53350; 184.
MINT; P53350; -.
STRING; 9606.ENSP00000300093; -.
BindingDB; P53350; -.
ChEMBL; CHEMBL3024; -.
GuidetoPHARMACOLOGY; 2168; -.
iPTMnet; P53350; -.
PhosphoSitePlus; P53350; -.
BioMuta; PLK1; -.
DMDM; 1709658; -.
EPD; P53350; -.
MaxQB; P53350; -.
PaxDb; P53350; -.
PeptideAtlas; P53350; -.
PRIDE; P53350; -.
DNASU; 5347; -.
Ensembl; ENST00000300093; ENSP00000300093; ENSG00000166851.
GeneID; 5347; -.
KEGG; hsa:5347; -.
UCSC; uc002dlz.2; human.
CTD; 5347; -.
DisGeNET; 5347; -.
EuPathDB; HostDB:ENSG00000166851.14; -.
GeneCards; PLK1; -.
HGNC; HGNC:9077; PLK1.
HPA; HPA051638; -.
HPA; HPA053229; -.
MIM; 602098; gene.
neXtProt; NX_P53350; -.
OpenTargets; ENSG00000166851; -.
PharmGKB; PA33410; -.
eggNOG; KOG0575; Eukaryota.
eggNOG; ENOG410XQBP; LUCA.
GeneTree; ENSGT00530000062954; -.
HOGENOM; HOG000248546; -.
HOVERGEN; HBG001843; -.
InParanoid; P53350; -.
KO; K06631; -.
OMA; FEVDTWS; -.
OrthoDB; EOG091G0D89; -.
PhylomeDB; P53350; -.
TreeFam; TF101089; -.
BRENDA; 2.7.11.21; 2681.
Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
Reactome; R-HSA-156711; Polo-like kinase mediated events.
Reactome; R-HSA-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
Reactome; R-HSA-176412; Phosphorylation of the APC/C.
Reactome; R-HSA-176417; Phosphorylation of Emi1.
Reactome; R-HSA-2299718; Condensation of Prophase Chromosomes.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-HSA-2980767; Activation of NIMA Kinases NEK9, NEK6, NEK7.
Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
Reactome; R-HSA-68877; Mitotic Prometaphase.
Reactome; R-HSA-68881; Mitotic Metaphase/Anaphase Transition.
Reactome; R-HSA-68884; Mitotic Telophase/Cytokinesis.
Reactome; R-HSA-69273; Cyclin A/B1/B2 associated events during G2/M transition.
Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
Reactome; R-HSA-8854518; AURKA Activation by TPX2.
SignaLink; P53350; -.
SIGNOR; P53350; -.
ChiTaRS; PLK1; human.
EvolutionaryTrace; P53350; -.
GeneWiki; PLK1; -.
GenomeRNAi; 5347; -.
PRO; PR:P53350; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000166851; -.
CleanEx; HS_PLK1; -.
ExpressionAtlas; P53350; baseline and differential.
Genevisible; P53350; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0000785; C:chromatin; IEA:Ensembl.
GO; GO:0000942; C:condensed nuclear chromosome outer kinetochore; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
GO; GO:0015630; C:microtubule cytoskeleton; IDA:BHF-UCL.
GO; GO:0030496; C:midbody; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005819; C:spindle; IDA:UniProtKB.
GO; GO:0051233; C:spindle midzone; IDA:UniProtKB.
GO; GO:0000922; C:spindle pole; IDA:BHF-UCL.
GO; GO:0000795; C:synaptonemal complex; IEA:Ensembl.
GO; GO:0010997; F:anaphase-promoting complex binding; IPI:UniProtKB.
GO; GO:0005524; F:ATP binding; IMP:CAFA.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0016301; F:kinase activity; TAS:Reactome.
GO; GO:0000287; F:magnesium ion binding; IMP:CAFA.
GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0007098; P:centrosome cycle; IMP:UniProtKB.
GO; GO:0097711; P:ciliary basal body-plasma membrane docking; TAS:Reactome.
GO; GO:0045184; P:establishment of protein localization; IMP:MGI.
GO; GO:0016321; P:female meiosis chromosome segregation; IEA:Ensembl.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IDA:UniProtKB.
GO; GO:0045143; P:homologous chromosome segregation; IEA:Ensembl.
GO; GO:0001578; P:microtubule bundle formation; IDA:UniProtKB.
GO; GO:0000278; P:mitotic cell cycle; IDA:UniProtKB.
GO; GO:0000281; P:mitotic cytokinesis; IDA:UniProtKB.
GO; GO:0007077; P:mitotic nuclear envelope disassembly; TAS:Reactome.
GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:UniProtKB.
GO; GO:0007094; P:mitotic spindle assembly checkpoint; IMP:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IMP:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
GO; GO:0051081; P:nuclear envelope disassembly; IMP:UniProtKB.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:UniProtKB.
GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IMP:BHF-UCL.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; TAS:Reactome.
GO; GO:0045862; P:positive regulation of proteolysis; IDA:UniProtKB.
GO; GO:1904668; P:positive regulation of ubiquitin protein ligase activity; IDA:UniProtKB.
GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; IMP:UniProtKB.
GO; GO:0031648; P:protein destabilization; IDA:UniProtKB.
GO; GO:0071168; P:protein localization to chromatin; IDA:UniProtKB.
GO; GO:0090435; P:protein localization to nuclear envelope; IMP:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
GO; GO:0051726; P:regulation of cell cycle; TAS:Reactome.
GO; GO:1902749; P:regulation of cell cycle G2/M phase transition; TAS:Reactome.
GO; GO:0032465; P:regulation of cytokinesis; IDA:UniProtKB.
GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:UniProtKB.
GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IMP:BHF-UCL.
GO; GO:1901673; P:regulation of mitotic spindle assembly; IDA:CACAO.
GO; GO:0043393; P:regulation of protein binding; IMP:BHF-UCL.
GO; GO:0072425; P:signal transduction involved in G2 DNA damage checkpoint; IDA:UniProtKB.
GO; GO:0007062; P:sister chromatid cohesion; TAS:Reactome.
GO; GO:0070194; P:synaptonemal complex disassembly; IEA:Ensembl.
CDD; cd13118; POLO_box_1; 1.
CDD; cd13117; POLO_box_2; 1.
CDD; cd14187; STKc_PLK1; 1.
Gene3D; 3.30.1120.30; -; 3.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR033702; PLK1_cat.
InterPro; IPR033701; POLO_box_1.
InterPro; IPR033695; POLO_box_2.
InterPro; IPR000959; POLO_box_dom.
InterPro; IPR036947; POLO_box_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
Pfam; PF00659; POLO_box; 2.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50078; POLO_BOX; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Cell cycle; Cell division;
Centromere; Chromosome; Complete proteome; Cytoplasm; Cytoskeleton;
Isopeptide bond; Kinase; Kinetochore; Mitosis; Nucleotide-binding;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Serine/threonine-protein kinase; Transferase; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 603 Serine/threonine-protein kinase PLK1.
/FTId=PRO_0000086556.
DOMAIN 53 305 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 417 480 POLO box 1. {ECO:0000255|PROSITE-
ProRule:PRU00154}.
DOMAIN 515 584 POLO box 2. {ECO:0000255|PROSITE-
ProRule:PRU00154}.
NP_BIND 59 67 ATP.
NP_BIND 178 181 ATP.
REGION 194 221 Activation loop.
REGION 493 507 Linker.
REGION 538 540 Important for interaction with
phosphorylated proteins. {ECO:0000250}.
MOTIF 337 340 D-box that targets the protein for
proteasomal degradation in anaphase.
ACT_SITE 176 176 Proton acceptor.
{ECO:0000269|PubMed:18615013}.
BINDING 82 82 ATP.
BINDING 131 131 ATP; via carbonyl oxygen.
BINDING 194 194 ATP.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 6 6 Phosphothreonine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 103 103 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 137 137 Phosphoserine.
{ECO:0000305|PubMed:12207013}.
MOD_RES 210 210 Phosphothreonine; by AURKA.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:12207013,
ECO:0000269|PubMed:18477460,
ECO:0000269|PubMed:18615013}.
MOD_RES 214 214 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195}.
MOD_RES 269 269 Phosphoserine; by autocatalysis.
{ECO:0000250}.
MOD_RES 335 335 Phosphoserine.
{ECO:0000269|PubMed:12442251}.
MOD_RES 375 375 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 450 450 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 498 498 Phosphothreonine.
{ECO:0000244|PubMed:18691976}.
CROSSLNK 19 19 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:18662541}.
CROSSLNK 338 338 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 492 492 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:23455478}.
VARIANT 12 12 R -> L (in a lung squamous cell carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041018.
VARIANT 261 261 L -> F (in dbSNP:rs35056440).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041019.
VARIANT 297 297 N -> D (in dbSNP:rs16972799).
/FTId=VAR_051659.
VARIANT 332 332 L -> V (in dbSNP:rs45489499).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041020.
VARIANT 463 463 L -> H (in dbSNP:rs45569335).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041021.
VARIANT 518 518 R -> H (in dbSNP:rs56027600).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041022.
VARIANT 595 595 S -> L (in dbSNP:rs34001032).
/FTId=VAR_051660.
VARIANT 599 599 R -> H (in dbSNP:rs34954545).
/FTId=VAR_051661.
MUTAGEN 67 67 C->V: In analog-sensitive mutant;
enlarged catalytic pocket to accommodate
purine analogs; when associated with G-
130. {ECO:0000269|PubMed:19468302}.
MUTAGEN 82 82 K->M: Loss of kinase activity. No effect
on S-phase progression.
{ECO:0000269|PubMed:12207013,
ECO:0000269|PubMed:12447691,
ECO:0000269|PubMed:18174154,
ECO:0000269|PubMed:24018379}.
MUTAGEN 82 82 K->R: Loss of kinase activity. No effect
on RIOK2-binding.
{ECO:0000269|PubMed:18615013,
ECO:0000269|PubMed:19160488,
ECO:0000269|PubMed:21880710}.
MUTAGEN 130 130 L->G: In analog-sensitive mutant;
enlarged catalytic pocket to accommodate
purine analogs; when associated with V-
67. {ECO:0000269|PubMed:19468302}.
MUTAGEN 137 137 S->A: No change in activity. Increases
activity and restores recovery after DNA
damage checkpoint; when associated with
D-210. {ECO:0000269|PubMed:12207013,
ECO:0000269|PubMed:18615013}.
MUTAGEN 137 137 S->D: Increases activity. Results in a
block in G1/S.
{ECO:0000269|PubMed:12207013,
ECO:0000269|PubMed:18615013}.
MUTAGEN 176 176 D->N: Abolishes kinase activity.
{ECO:0000269|PubMed:18615013}.
MUTAGEN 194 194 D->A: Does not interfere with FRY-
binding. {ECO:0000269|PubMed:22753416}.
MUTAGEN 210 210 T->A: Abolishes activity. Abolishes
checkpoint recovery.
{ECO:0000269|PubMed:12207013,
ECO:0000269|PubMed:12447691,
ECO:0000269|PubMed:17461553,
ECO:0000269|PubMed:18615013,
ECO:0000269|PubMed:19160488}.
MUTAGEN 210 210 T->D: Increases activity and restores
recovery after DNA damage checkpoint.
{ECO:0000269|PubMed:12207013,
ECO:0000269|PubMed:12447691,
ECO:0000269|PubMed:17461553,
ECO:0000269|PubMed:18615013,
ECO:0000269|PubMed:19160488}.
MUTAGEN 210 210 T->V: Reduced catalytic activity, but no
effect on affinity for ATP.
{ECO:0000269|PubMed:12207013,
ECO:0000269|PubMed:12447691,
ECO:0000269|PubMed:17461553,
ECO:0000269|PubMed:18615013,
ECO:0000269|PubMed:19160488}.
MUTAGEN 337 337 R->A: Interferes with ubiquitination and
subsequent proteasomal degradation in
anaphase; when associated with A-340.
{ECO:0000269|PubMed:14734534,
ECO:0000269|PubMed:18662541}.
MUTAGEN 340 340 L->A: Interferes with ubiquitination and
subsequent proteasomal degradation in
anaphase; when associated with A-337.
{ECO:0000269|PubMed:14734534,
ECO:0000269|PubMed:18662541}.
MUTAGEN 414 414 W->F: Abolishes interaction with CDC25C
and reduces centrosomal localization.
{ECO:0000269|PubMed:17307877}.
MUTAGEN 414 414 W->F: No effect on centrosomal
localization, nor on S-phase progression;
when asscociated with A-427. Loss of
centrosomal localization and of S-phase
progression; when associated with A- 415
and A-427. {ECO:0000269|PubMed:24018379}.
MUTAGEN 415 415 V->A: Loss of centrosomal localization
and of S-phase progression; when
associated with A- 414 and A-427.
{ECO:0000269|PubMed:24018379}.
MUTAGEN 427 427 L->A: No effect on centrosomal
localization, nor on S-phase progression;
when associated with A-414. Loss of
centrosomal localization and of S-phase
progression; when associated with A- 414
and A-415. {ECO:0000269|PubMed:24018379}.
MUTAGEN 492 492 K->R: Severe mitotic defects leading to
prometaphase delay. Increased
localization at kinetochores leading to
increased levels of phosphorylated BUBR1.
{ECO:0000269|PubMed:23455478}.
MUTAGEN 538 538 H->A: In pincer mutant; loss of
centrosomal location and decreased
interaction with phosphorylated CDC25C
and BUB1; when associated with M-540.
{ECO:0000269|PubMed:14532005,
ECO:0000269|PubMed:16760428,
ECO:0000269|PubMed:18477460,
ECO:0000269|PubMed:19468302}.
MUTAGEN 540 540 K->M: In pincer mutant; loss of
centrosomal location and decreased
interaction with phosphorylated CDC25C
and BUB1; when associated with A-538.
{ECO:0000269|PubMed:14532005,
ECO:0000269|PubMed:16760428,
ECO:0000269|PubMed:18477460,
ECO:0000269|PubMed:19468302}.
CONFLICT 2 2 S -> T (in Ref. 1; AAA56634).
{ECO:0000305}.
CONFLICT 11 11 A -> P (in Ref. 1; AAA56634).
{ECO:0000305}.
CONFLICT 58 58 F -> L (in Ref. 1; AAA56634).
{ECO:0000305}.
CONFLICT 60 60 G -> S (in Ref. 1; AAA56634).
{ECO:0000305}.
CONFLICT 73 73 A -> V (in Ref. 2; AAA36659 and 7;
AAB36946). {ECO:0000305}.
CONFLICT 123 123 N -> T (in Ref. 6; CAA62260).
{ECO:0000305}.
CONFLICT 141 141 L -> P (in Ref. 4; CAA53536).
{ECO:0000305}.
CONFLICT 227 227 G -> E (in Ref. 4; CAA53536).
{ECO:0000305}.
CONFLICT 301 301 N -> G (in Ref. 2; AAA36659).
{ECO:0000305}.
CONFLICT 495 495 A -> G (in Ref. 2; AAA36659).
{ECO:0000305}.
CONFLICT 501 501 E -> Q (in Ref. 2; AAA36659).
{ECO:0000305}.
STRAND 42 46 {ECO:0000244|PDB:2RKU}.
TURN 47 50 {ECO:0000244|PDB:2RKU}.
STRAND 51 62 {ECO:0000244|PDB:2RKU}.
STRAND 65 72 {ECO:0000244|PDB:2RKU}.
TURN 73 75 {ECO:0000244|PDB:2RKU}.
STRAND 78 85 {ECO:0000244|PDB:2RKU}.
HELIX 86 88 {ECO:0000244|PDB:2RKU}.
HELIX 92 106 {ECO:0000244|PDB:2RKU}.
STRAND 116 121 {ECO:0000244|PDB:2RKU}.
STRAND 123 131 {ECO:0000244|PDB:2RKU}.
HELIX 138 145 {ECO:0000244|PDB:2RKU}.
HELIX 150 169 {ECO:0000244|PDB:2RKU}.
HELIX 179 181 {ECO:0000244|PDB:2RKU}.
STRAND 182 184 {ECO:0000244|PDB:2RKU}.
STRAND 190 192 {ECO:0000244|PDB:2RKU}.
HELIX 220 223 {ECO:0000244|PDB:2RKU}.
STRAND 224 226 {ECO:0000244|PDB:2V5Q}.
HELIX 231 246 {ECO:0000244|PDB:2RKU}.
HELIX 256 264 {ECO:0000244|PDB:2RKU}.
HELIX 276 285 {ECO:0000244|PDB:2RKU}.
HELIX 290 292 {ECO:0000244|PDB:2RKU}.
HELIX 296 301 {ECO:0000244|PDB:2RKU}.
HELIX 303 306 {ECO:0000244|PDB:2RKU}.
HELIX 316 319 {ECO:0000244|PDB:2RKU}.
HELIX 367 370 {ECO:0000244|PDB:5J19}.
HELIX 374 386 {ECO:0000244|PDB:4X9R}.
HELIX 389 391 {ECO:0000244|PDB:4X9R}.
STRAND 392 394 {ECO:0000244|PDB:3P34}.
HELIX 397 400 {ECO:0000244|PDB:4X9R}.
HELIX 403 405 {ECO:0000244|PDB:4X9R}.
STRAND 411 417 {ECO:0000244|PDB:4X9R}.
TURN 418 421 {ECO:0000244|PDB:4X9R}.
STRAND 422 427 {ECO:0000244|PDB:4X9R}.
STRAND 432 436 {ECO:0000244|PDB:4X9R}.
STRAND 441 444 {ECO:0000244|PDB:4X9R}.
STRAND 448 454 {ECO:0000244|PDB:4X9R}.
STRAND 460 464 {ECO:0000244|PDB:4X9R}.
TURN 465 467 {ECO:0000244|PDB:3Q1I}.
HELIX 470 472 {ECO:0000244|PDB:4X9R}.
HELIX 473 488 {ECO:0000244|PDB:4X9R}.
TURN 493 496 {ECO:0000244|PDB:4X9R}.
TURN 503 505 {ECO:0000244|PDB:3P34}.
STRAND 511 516 {ECO:0000244|PDB:4X9R}.
STRAND 518 525 {ECO:0000244|PDB:4X9R}.
TURN 526 528 {ECO:0000244|PDB:4WHL}.
STRAND 530 534 {ECO:0000244|PDB:4X9R}.
TURN 535 537 {ECO:0000244|PDB:4X9R}.
STRAND 540 544 {ECO:0000244|PDB:4X9R}.
TURN 545 548 {ECO:0000244|PDB:4X9R}.
STRAND 549 553 {ECO:0000244|PDB:4X9R}.
STRAND 559 563 {ECO:0000244|PDB:4X9R}.
HELIX 564 570 {ECO:0000244|PDB:4X9R}.
HELIX 574 591 {ECO:0000244|PDB:4X9R}.
STRAND 593 595 {ECO:0000244|PDB:4O56}.
STRAND 598 602 {ECO:0000244|PDB:4O56}.
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


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