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   02-SEP-2026, entry version 160.
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 act by binding
CC       and phosphorylating proteins that are 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=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC         H(+); 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=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; 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       recognizes and binds serine-[phosphothreonine/phosphoserine]-
CC       (proline/X) motifs. plk1 recognizes and binds docking proteins that are
CC       already phosphorylated on these motifs, and then phosphorylates them
CC       (By 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; 13.
DR   DIP; DIP-42603N; -.
DR   IntAct; P70032; 11.
DR   MINT; P70032; -.
DR   BindingDB; P70032; -.
DR   ChEMBL; CHEMBL4519; -.
DR   iPTMnet; P70032; -.
DR   DNASU; 380481; -.
DR   GeneID; 380481; -.
DR   KEGG; xla:380481; -.
DR   AGR; Xenbase:XB-GENE-941545; -.
DR   CTD; 380481; -.
DR   Xenbase; XB-GENE-941545; plk1.S.
DR   OrthoDB; 408964at2759; -.
DR   PRO; PR:P70032; -.
DR   Proteomes; UP000186698; Chromosome 9_10S.
DR   Bgee; 380481; Expressed in egg cell and 16 other cell types or tissues.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0000922; C:spindle pole; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:1903673; P:mitotic cleavage furrow formation; 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:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:2000042; P:negative regulation of double-strand break repair via homologous recombination; 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:0045842; P:positive regulation of mitotic metaphase/anaphase transition; ISS:UniProtKB.
DR   GO; GO:0071168; P:protein localization to chromatin; ISS:UniProtKB.
DR   CDD; cd13118; POLO_box_1; 1.
DR   CDD; cd13117; POLO_box_2; 1.
DR   CDD; cd14187; STKc_PLK1; 1.
DR   FunFam; 1.10.510.10:FF:000727; Serine/threonine-protein kinase PLK; 1.
DR   FunFam; 3.30.1120.30:FF:000003; Serine/threonine-protein kinase PLK; 1.
DR   FunFam; 3.30.200.20:FF:000284; Serine/threonine-protein kinase PLK; 1.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR   Gene3D; 3.30.1120.30; POLO box domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR033702; PLK1_cat.
DR   InterPro; IPR033701; POLO_box_1.
DR   InterPro; IPR033695; POLO_box_2.
DR   InterPro; IPR000959; POLO_box_dom.
DR   InterPro; IPR036947; POLO_box_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24345; SERINE/THREONINE-PROTEIN KINASE PLK; 1.
DR   PANTHER; PTHR24345:SF93; SERINE_THREONINE-PROTEIN KINASE PLK1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00659; POLO_box; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF82615; Polo-box domain; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50078; POLO_BOX; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
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          404..482
FT                   /note="POLO box 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT   DOMAIN          504..586
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
//