PLK1_XENLA
ID PLK1_XENLA Reviewed; 598 AA.
AC P70032; Q7ZWQ6;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Serine/threonine-protein kinase PLK1;
DE EC=2.7.11.21;
DE AltName: Full=Plx1;
DE AltName: Full=Polo-like kinase 1;
DE Short=PLK-1;
GN Name=plk1; Synonyms=plx1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Oocyte;
RX PubMed=8703070; DOI=10.1126/science.273.5280.1377;
RA Kumagai A., Dunphy W.G.;
RT "Purification and molecular cloning of Plx1, a Cdc25-regulatory kinase from
RT Xenopus egg extracts.";
RL Science 273:1377-1380(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION BY STK10, FUNCTION, AND MUTAGENESIS OF ASN-172.
RX PubMed=9831560; DOI=10.1126/science.282.5394.1701;
RA Qian Y.W., Erikson E., Maller J.L.;
RT "Purification and cloning of a protein kinase that phosphorylates and
RT activates the polo-like kinase Plx1.";
RL Science 282:1701-1704(1998).
RN [4]
RP FUNCTION, PHOSPHORYLATION AT THR-201, ACTIVITY REGULATION, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF SER-128; THR-140; THR-201; THR-205 AND
RP SER-227.
RX PubMed=10567586; DOI=10.1128/mcb.19.12.8625;
RA Qian Y.W., Erikson E., Maller J.L.;
RT "Mitotic effects of a constitutively active mutant of the Xenopus polo-like
RT kinase Plx1.";
RL Mol. Cell. Biol. 19:8625-8632(1999).
RN [5]
RP FUNCTION, PHOSPHORYLATION AT THR-10; SER-25; SER-26; THR-201; SER-260;
RP SER-326 AND SER-340, IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS
RP OF SER-128; ASN-172; THR-201 AND SER-340.
RX PubMed=11994303; DOI=10.1074/jbc.m202855200;
RA Kelm O., Wind M., Lehmann W.D., Nigg E.A.;
RT "Cell cycle-regulated phosphorylation of the Xenopus polo-like kinase
RT Plx1.";
RL J. Biol. Chem. 277:25247-25256(2002).
RN [6]
RP FUNCTION IN PHOSPHORYLATION OF STAG2.
RX PubMed=11931760; DOI=10.1016/s1097-2765(02)00473-2;
RA Sumara I., Vorlaufer E., Stukenberg P.T., Kelm O., Redemann N., Nigg E.A.,
RA Peters J.-M.;
RT "The dissociation of cohesin from chromosomes in prophase is regulated by
RT Polo-like kinase.";
RL Mol. Cell 9:515-525(2002).
RN [7]
RP FUNCTION.
RX PubMed=15964272; DOI=10.1016/j.cub.2005.05.026;
RA Ahonen L.J., Kallio M.J., Daum J.R., Bolton M., Manke I.A., Yaffe M.B.,
RA Stukenberg P.T., Gorbsky G.J.;
RT "Polo-like kinase 1 creates the tension-sensing 3F3/2 phosphoepitope and
RT modulates the association of spindle-checkpoint proteins at kinetochores.";
RL Curr. Biol. 15:1078-1089(2005).
RN [8]
RP FUNCTION IN PHOSPHORYLATION OF PKMYT1.
RX PubMed=15692562; DOI=10.1038/sj.emboj.7600567;
RA Inoue D., Sagata N.;
RT "The Polo-like kinase Plx1 interacts with and inhibits Myt1 after
RT fertilization of Xenopus eggs.";
RL EMBO J. 24:1057-1067(2005).
RN [9]
RP INTERACTION WITH FBXO5.
RX PubMed=17159919; DOI=10.1038/sj.embor.7400853;
RA Bernis C., Vigneron S., Burgess A., Labbe J.C., Fesquet D., Castro A.,
RA Lorca T.;
RT "Pin1 stabilizes Emi1 during G2 phase by preventing its association with
RT SCF(betatrcp).";
RL EMBO Rep. 8:91-98(2007).
RN [10]
RP INTERACTION WITH TPX2, AND FUNCTION.
RX PubMed=19556869; DOI=10.4161/cc.8.15.9086;
RA Eckerdt F., Pascreau G., Phistry M., Lewellyn A.L., DePaoli-Roach A.A.,
RA Maller J.L.;
RT "Phosphorylation of TPX2 by Plx1 enhances activation of Aurora A.";
RL Cell Cycle 8:2413-2419(2009).
RN [11]
RP FUNCTION, AND INTERACTION WITH KIF2A.
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).
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. Polo-like kinase proteins acts by binding
CC and phosphorylating proteins are that already phosphorylated on a
CC specific motif recognized by the POLO box domains. Phosphorylates
CC cdc25, pkmyt1/myt1, stag2/sa2, tpx2. Plays multiple essential roles
CC during mitosis. Phosphorylates the N-terminal domain of cdc25, which
CC leads to cyclin b-cdc2 activation and mitotic entry. Also required for
CC organization of bipolar spindles, and for exit from mitosis. Involved
CC in kinetochore functions and sister chromatid cohesion by
CC phosphorylating stag2/sa2. {ECO:0000269|PubMed:10567586,
CC ECO:0000269|PubMed:11931760, ECO:0000269|PubMed:11994303,
CC ECO:0000269|PubMed:15692562, ECO:0000269|PubMed:15964272,
CC ECO:0000269|PubMed:19351716, ECO:0000269|PubMed:19556869,
CC ECO:0000269|PubMed:8703070, ECO:0000269|PubMed:9831560}.
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 -!- 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;
CC -!- ACTIVITY REGULATION: Activated by phosphorylation of Thr-201.
CC {ECO:0000269|PubMed:10567586}.
CC -!- SUBUNIT: Interacts with plk1 and kif2a. Interacts with fbxo5
CC (PubMed:17159919). {ECO:0000269|PubMed:17159919,
CC ECO:0000269|PubMed:19351716, ECO:0000269|PubMed:19556869}.
CC -!- INTERACTION:
CC P70032; Q90Z80: fbxo5-a; NbExp=2; IntAct=EBI-3511304, EBI-7161111;
CC P70032; Q91876: mcm7-a; NbExp=3; IntAct=EBI-3511304, EBI-876852;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10567586}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:10567586}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:10567586}. Midbody {ECO:0000250}. Note=localization
CC at the centrosome starts at the G1/S transition (By similarity).
CC Localized at centrosomes at prophase, spindles at metaphase, and at the
CC midbody during cytokinesis. Localization to the centrosome is required
CC for S phase progression (By similarity).
CC {ECO:0000250|UniProtKB:P53350}.
CC -!- INDUCTION: By growth-stimulating agents. {ECO:0000250}.
CC -!- DOMAIN: The POLO box domains act as phosphopeptide-binding module that
CC recognize and bind serine-[phosphothreonine/phosphoserine]-(proline/X)
CC motifs. plk1 recognizes and binds docking proteins that are already
CC phosphorylated on these motifs, and then phosphorylates them (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Activated by phosphorylation on Thr-201 during M phase.
CC Phosphorylated by stk10, leading to activation during oocyte
CC maturation. {ECO:0000269|PubMed:10567586, ECO:0000269|PubMed:11994303,
CC ECO:0000269|PubMed:9831560}.
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. Protein levels are down-regulated by proteasomal
CC degradation in anaphase (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; U58205; AAC60017.1; -; mRNA.
DR EMBL; BC046839; AAH46839.1; -; mRNA.
DR RefSeq; NP_001080788.1; NM_001087319.1.
DR AlphaFoldDB; P70032; -.
DR SMR; P70032; -.
DR BioGRID; 98723; 11.
DR DIP; DIP-42603N; -.
DR IntAct; P70032; 11.
DR MINT; P70032; -.
DR BindingDB; P70032; -.
DR ChEMBL; CHEMBL4519; -.
DR iPTMnet; P70032; -.
DR PRIDE; P70032; -.
DR DNASU; 380481; -.
DR GeneID; 380481; -.
DR KEGG; xla:380481; -.
DR CTD; 380481; -.
DR Xenbase; XB-GENE-941545; plk1.S.
DR OrthoDB; 507604at2759; -.
DR PRO; PR:P70032; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 380481; Expressed in egg cell and 16 other tissues.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0051233; C:spindle midzone; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0007098; P:centrosome cycle; ISS:UniProtKB.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0001578; P:microtubule bundle formation; ISS:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0001556; P:oocyte maturation; IDA:UniProtKB.
DR GO; GO:1904668; P:positive regulation of ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0071168; P:protein localization to chromatin; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
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; -; 2.
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 Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00659; POLO_box; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Kinase;
KW Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Transferase; Ubl conjugation.
FT CHAIN 1..598
FT /note="Serine/threonine-protein kinase PLK1"
FT /id="PRO_0000086559"
FT DOMAIN 44..296
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 411..474
FT /note="POLO box 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT DOMAIN 509..578
FT /note="POLO box 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..212
FT /note="Activation loop"
FT /evidence="ECO:0000250"
FT REGION 487..501
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 532..534
FT /note="Important for interaction with phosphorylated
FT proteins"
FT /evidence="ECO:0000250"
FT MOTIF 328..331
FT /note="D-box that targets the protein for proteasomal
FT degradation in anaphase"
FT /evidence="ECO:0000250"
FT ACT_SITE 167
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 50..58
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 169..172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 10
FT /note="Phosphothreonine; by PKA; in vitro"
FT /evidence="ECO:0000269|PubMed:11994303"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:11994303"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:11994303"
FT MOD_RES 201
FT /note="Phosphothreonine; by PKA"
FT /evidence="ECO:0000269|PubMed:10567586,
FT ECO:0000269|PubMed:11994303"
FT MOD_RES 260
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:11994303"
FT MOD_RES 326
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:11994303"
FT MOD_RES 340
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:11994303"
FT MUTAGEN 128
FT /note="S->A: No effect on activity."
FT /evidence="ECO:0000269|PubMed:10567586,
FT ECO:0000269|PubMed:11994303"
FT MUTAGEN 128
FT /note="S->D: Increases activity."
FT /evidence="ECO:0000269|PubMed:10567586,
FT ECO:0000269|PubMed:11994303"
FT MUTAGEN 140
FT /note="T->D: No effect on activity."
FT /evidence="ECO:0000269|PubMed:10567586"
FT MUTAGEN 172
FT /note="N->A: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:11994303,
FT ECO:0000269|PubMed:9831560"
FT MUTAGEN 201
FT /note="T->A: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:10567586,
FT ECO:0000269|PubMed:11994303"
FT MUTAGEN 201
FT /note="T->D: Increases activity."
FT /evidence="ECO:0000269|PubMed:10567586,
FT ECO:0000269|PubMed:11994303"
FT MUTAGEN 201
FT /note="T->V: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:10567586,
FT ECO:0000269|PubMed:11994303"
FT MUTAGEN 205
FT /note="T->D: No effect on activity."
FT /evidence="ECO:0000269|PubMed:10567586"
FT MUTAGEN 227
FT /note="S->D: No effect on activity."
FT /evidence="ECO:0000269|PubMed:10567586"
FT MUTAGEN 340
FT /note="S->A: No effect on activity."
FT /evidence="ECO:0000269|PubMed:11994303"
FT MUTAGEN 340
FT /note="S->D: No effect on activity."
FT /evidence="ECO:0000269|PubMed:11994303"
FT CONFLICT 348
FT /note="A -> V (in Ref. 2; AAH46839)"
FT /evidence="ECO:0000305"
SQ 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
