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Serine/threonine-protein kinase PLK1 (EC 2.7.11.21) (Plx1) (Polo-like kinase 1) (PLK-1)

 PLK1_XENLA              Reviewed;         598 AA.
P70032; Q7ZWQ6;
21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
23-MAY-2018, entry version 129.
RecName: Full=Serine/threonine-protein kinase PLK1;
EC=2.7.11.21;
AltName: Full=Plx1;
AltName: Full=Polo-like kinase 1;
Short=PLK-1;
Name=plk1; Synonyms=plx1;
Xenopus laevis (African clawed frog).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
Xenopus.
NCBI_TaxID=8355;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
TISSUE=Oocyte;
PubMed=8703070; DOI=10.1126/science.273.5280.1377;
Kumagai A., Dunphy W.G.;
"Purification and molecular cloning of Plx1, a Cdc25-regulatory kinase
from Xenopus egg extracts.";
Science 273:1377-1380(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Embryo;
NIH - Xenopus Gene Collection (XGC) project;
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[3]
PHOSPHORYLATION BY STK10, FUNCTION, AND MUTAGENESIS OF ASN-172.
PubMed=9831560; DOI=10.1126/science.282.5394.1701;
Qian Y.W., Erikson E., Maller J.L.;
"Purification and cloning of a protein kinase that phosphorylates and
activates the polo-like kinase Plx1.";
Science 282:1701-1704(1998).
[4]
FUNCTION, PHOSPHORYLATION AT THR-201, ENZYME REGULATION, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF SER-128; THR-140; THR-201; THR-205 AND
SER-227.
PubMed=10567586; DOI=10.1128/MCB.19.12.8625;
Qian Y.W., Erikson E., Maller J.L.;
"Mitotic effects of a constitutively active mutant of the Xenopus
polo-like kinase Plx1.";
Mol. Cell. Biol. 19:8625-8632(1999).
[5]
FUNCTION, PHOSPHORYLATION AT THR-10; SER-25; SER-26; THR-201; SER-260;
SER-326 AND SER-340, IDENTIFICATION BY MASS SPECTROMETRY, AND
MUTAGENESIS OF SER-128; ASN-172; THR-201 AND SER-340.
PubMed=11994303; DOI=10.1074/jbc.M202855200;
Kelm O., Wind M., Lehmann W.D., Nigg E.A.;
"Cell cycle-regulated phosphorylation of the Xenopus polo-like kinase
Plx1.";
J. Biol. Chem. 277:25247-25256(2002).
[6]
FUNCTION IN PHOSPHORYLATION OF STAG2.
PubMed=11931760; DOI=10.1016/S1097-2765(02)00473-2;
Sumara I., Vorlaufer E., Stukenberg P.T., Kelm O., Redemann N.,
Nigg E.A., Peters J.-M.;
"The dissociation of cohesin from chromosomes in prophase is regulated
by Polo-like kinase.";
Mol. Cell 9:515-525(2002).
[7]
FUNCTION.
PubMed=15964272; DOI=10.1016/j.cub.2005.05.026;
Ahonen L.J., Kallio M.J., Daum J.R., Bolton M., Manke I.A.,
Yaffe M.B., Stukenberg P.T., Gorbsky G.J.;
"Polo-like kinase 1 creates the tension-sensing 3F3/2 phosphoepitope
and modulates the association of spindle-checkpoint proteins at
kinetochores.";
Curr. Biol. 15:1078-1089(2005).
[8]
FUNCTION IN PHOSPHORYLATION OF PKMYT1.
PubMed=15692562; DOI=10.1038/sj.emboj.7600567;
Inoue D., Sagata N.;
"The Polo-like kinase Plx1 interacts with and inhibits Myt1 after
fertilization of Xenopus eggs.";
EMBO J. 24:1057-1067(2005).
[9]
INTERACTION WITH TPX2, AND FUNCTION.
PubMed=19556869; DOI=10.4161/cc.8.15.9086;
Eckerdt F., Pascreau G., Phistry M., Lewellyn A.L.,
DePaoli-Roach A.A., Maller J.L.;
"Phosphorylation of TPX2 by Plx1 enhances activation of Aurora A.";
Cell Cycle 8:2413-2419(2009).
[10]
FUNCTION, AND INTERACTION WITH KIF2A.
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).
-!- 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 cdc25,
pkmyt1/myt1, stag2/sa2, tpx2. Plays multiple essential roles
during mitosis. Phosphorylates the N-terminal domain of cdc25,
which leads to cyclin b-cdc2 activation and mitotic entry. Also
required for organization of bipolar spindles, and for exit from
mitosis. Involved in kinetochore functions and sister chromatid
cohesion by phosphorylating stag2/sa2.
{ECO:0000269|PubMed:10567586, ECO:0000269|PubMed:11931760,
ECO:0000269|PubMed:11994303, ECO:0000269|PubMed:15692562,
ECO:0000269|PubMed:15964272, ECO:0000269|PubMed:19351716,
ECO:0000269|PubMed:19556869, ECO:0000269|PubMed:8703070,
ECO:0000269|PubMed:9831560}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Activated by phosphorylation of Thr-201.
{ECO:0000269|PubMed:10567586}.
-!- SUBUNIT: Interacts with plk1 and kif2a.
{ECO:0000269|PubMed:19351716, ECO:0000269|PubMed:19556869}.
-!- INTERACTION:
Q90Z80:fbxo5-a; NbExp=2; IntAct=EBI-3511304, EBI-7161111;
Q91876:mcm7-a; NbExp=3; IntAct=EBI-3511304, EBI-876852;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10567586}.
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
{ECO:0000269|PubMed:10567586}. Cytoplasm, cytoskeleton, spindle
{ECO:0000269|PubMed:10567586}. Midbody {ECO:0000250}.
Note=localization at the centrosome starts at the G1/S transition
(By similarity). Localized at centrosomes at prophase, spindles at
metaphase, and at the midbody during cytokinesis. Localization to
the centrosome is required for S phase progression (By
similarity). {ECO:0000250|UniProtKB:P53350}.
-!- INDUCTION: By growth-stimulating agents. {ECO:0000250}.
-!- 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 (By similarity). {ECO:0000250}.
-!- PTM: Activated by phosphorylation on Thr-201 during M phase.
Phosphorylated by stk10, leading to activation during oocyte
maturation. {ECO:0000269|PubMed:10567586,
ECO:0000269|PubMed:11994303, ECO:0000269|PubMed:9831560}.
-!- PTM: Ubiquitinated by the anaphase promoting complex/cyclosome
(APC/C) in anaphase and following DNA damage, leading to its
degradation by the proteasome. Protein levels are down-regulated
by proteasomal degradation in anaphase (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; U58205; AAC60017.1; -; mRNA.
EMBL; BC046839; AAH46839.1; -; mRNA.
RefSeq; NP_001080788.1; NM_001087319.1.
UniGene; Xl.28141; -.
ProteinModelPortal; P70032; -.
SMR; P70032; -.
BioGrid; 98723; 8.
DIP; DIP-42603N; -.
IntAct; P70032; 11.
MINT; P70032; -.
BindingDB; P70032; -.
ChEMBL; CHEMBL4519; -.
iPTMnet; P70032; -.
PRIDE; P70032; -.
GeneID; 380481; -.
KEGG; xla:380481; -.
CTD; 380481; -.
Xenbase; XB-GENE-941545; plk1.
HOVERGEN; HBG001843; -.
KO; K06631; -.
PRO; PR:P70032; -.
GO; GO:0005813; C:centrosome; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
GO; GO:0030496; C:midbody; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005819; C:spindle; ISS:UniProtKB.
GO; GO:0051233; C:spindle midzone; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0007098; P:centrosome cycle; ISS:UniProtKB.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISS:UniProtKB.
GO; GO:0001578; P:microtubule bundle formation; ISS:UniProtKB.
GO; GO:0000278; P:mitotic cell cycle; ISS:UniProtKB.
GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0001556; P:oocyte maturation; IDA:UniProtKB.
GO; GO:1904668; P:positive regulation of ubiquitin protein ligase activity; ISS:UniProtKB.
GO; GO:0071168; P:protein localization to chromatin; ISS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
GO; GO:0072425; P:signal transduction involved in G2 DNA damage checkpoint; ISS:UniProtKB.
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;
ATP-binding; Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
Kinase; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein; Repeat;
Serine/threonine-protein kinase; Transferase; Ubl conjugation.
CHAIN 1 598 Serine/threonine-protein kinase PLK1.
/FTId=PRO_0000086559.
DOMAIN 44 296 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 411 474 POLO box 1. {ECO:0000255|PROSITE-
ProRule:PRU00154}.
DOMAIN 509 578 POLO box 2. {ECO:0000255|PROSITE-
ProRule:PRU00154}.
NP_BIND 50 58 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 169 172 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 185 212 Activation loop. {ECO:0000250}.
REGION 487 501 Linker. {ECO:0000250}.
REGION 532 534 Important for interaction with
phosphorylated proteins. {ECO:0000250}.
MOTIF 328 331 D-box that targets the protein for
proteasomal degradation in anaphase.
{ECO:0000250}.
ACT_SITE 167 167 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 73 73 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 122 122 ATP; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU00159}.
BINDING 185 185 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 10 10 Phosphothreonine; by PKA; in vitro.
{ECO:0000269|PubMed:11994303}.
MOD_RES 25 25 Phosphoserine.
{ECO:0000305|PubMed:11994303}.
MOD_RES 26 26 Phosphoserine.
{ECO:0000305|PubMed:11994303}.
MOD_RES 201 201 Phosphothreonine; by PKA.
{ECO:0000269|PubMed:10567586,
ECO:0000269|PubMed:11994303}.
MOD_RES 260 260 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:11994303}.
MOD_RES 326 326 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:11994303}.
MOD_RES 340 340 Phosphoserine; by CDK1.
{ECO:0000269|PubMed:11994303}.
MUTAGEN 128 128 S->A: No effect on activity.
{ECO:0000269|PubMed:10567586,
ECO:0000269|PubMed:11994303}.
MUTAGEN 128 128 S->D: Increases activity.
{ECO:0000269|PubMed:10567586,
ECO:0000269|PubMed:11994303}.
MUTAGEN 140 140 T->D: No effect on activity.
{ECO:0000269|PubMed:10567586}.
MUTAGEN 172 172 N->A: Abolishes activity.
{ECO:0000269|PubMed:11994303,
ECO:0000269|PubMed:9831560}.
MUTAGEN 201 201 T->A: Abolishes activity.
{ECO:0000269|PubMed:10567586,
ECO:0000269|PubMed:11994303}.
MUTAGEN 201 201 T->D: Increases activity.
{ECO:0000269|PubMed:10567586,
ECO:0000269|PubMed:11994303}.
MUTAGEN 201 201 T->V: Abolishes activity.
{ECO:0000269|PubMed:10567586,
ECO:0000269|PubMed:11994303}.
MUTAGEN 205 205 T->D: No effect on activity.
{ECO:0000269|PubMed:10567586}.
MUTAGEN 227 227 S->D: No effect on activity.
{ECO:0000269|PubMed:10567586}.
MUTAGEN 340 340 S->A: No effect on activity.
{ECO:0000269|PubMed:11994303}.
MUTAGEN 340 340 S->D: No effect on activity.
{ECO:0000269|PubMed:11994303}.
CONFLICT 348 348 A -> V (in Ref. 2; AAH46839).
{ECO:0000305}.
SEQUENCE 598 AA; 68212 MW; 2467195911F225E6 CRC64;
MAQVAGKKLT VAPEAAKPPG IPGSSSAVKE IPEILVDPRT RRRYLRGRFL GKGGFAKCYE
ITDLESREVF AGKIVPKTML LKPHQKDKMT MEIAIQRSLD HRHVVGFHGF FEDNDFVYVV
LELCRRRSLL ELHKRRKAVT EPEARYYLKQ TISGCQYLHS NRVIHRDLKL GNLFLNDEME
VKIGDFGLAT KVEYDGERKK TLCGTPNYIA PEVLGKKGHS FEVDIWSIGC IMYTLLVGKP
PFETSCLKET YMRIKKNEYS IPKHINPVAA ALIQKMLRSD PTSRPTIDDL LNDEFFTSGY
IPSRLPTTCL TVPPRFSIAP STIDQSLRKP LTAINKGQDS PLVEKQVAPA KEEEMQQPEF
TEPADCYLSE MLQQLTCLNA VKPSERALIR QEEAEDPASI PIFWISKWVD YSDKYGLGYQ
LCDNSVGVLF NDSTRLIMYN DGDSLQYIER NNTESYLNVR SYPTTLTKKI TLLKYFRNYM
SEHLLKAGAN TTPREGDELA RLPFLRTWFR TRSAIILHLS NGTVQINFFQ DHTKIILCPL
MAAVSYIDEK REFRTYKLSL IQEFGCCKEL ASRLRYARTM VEKLQSSKSA VAHVKASA


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