PLK1_XENTR
ID PLK1_XENTR Reviewed; 598 AA.
AC P62205;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 129.
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;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays multiple essential roles during mitosis. Phosphorylates
CC the N-terminal domain of cdc25, which leads to cyclin b-cdc2 activation
CC and mitotic entry. Also required for organization of bipolar spindles,
CC and for exit from mitosis. Phosphorylates tpx2 (By similarity).
CC {ECO:0000250}.
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 -!- SUBUNIT: Interacts with plk1 and kif2a. Interacts with fbxo5.
CC {ECO:0000250|UniProtKB:P70032}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000250}. Midbody {ECO:0000250}.
CC Note=Localized at centrosomes at prophase, spindles at metaphase, and
CC at the midbody during cytokinesis. {ECO:0000250}.
CC -!- PTM: Activated by phosphorylation on Thr-201 during M phase.
CC {ECO:0000250}.
CC -!- PTM: Protein levels are down-regulated by proteasomal degradation in
CC anaphase. {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; BC067963; AAH67963.1; -; mRNA.
DR RefSeq; NP_998844.1; NM_213679.2.
DR AlphaFoldDB; P62205; -.
DR SMR; P62205; -.
DR STRING; 8364.ENSXETP00000022754; -.
DR PaxDb; P62205; -.
DR DNASU; 407937; -.
DR Ensembl; ENSXETT00000022754; ENSXETP00000022754; ENSXETG00000010344.
DR GeneID; 407937; -.
DR KEGG; xtr:407937; -.
DR CTD; 5347; -.
DR Xenbase; XB-GENE-941540; plk1.
DR eggNOG; KOG0575; Eukaryota.
DR HOGENOM; CLU_000288_46_1_1; -.
DR InParanoid; P62205; -.
DR OrthoDB; 507604at2759; -.
DR PhylomeDB; P62205; -.
DR Reactome; R-XTR-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-XTR-156711; Polo-like kinase mediated events.
DR Reactome; R-XTR-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
DR Reactome; R-XTR-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-XTR-176412; Phosphorylation of the APC/C.
DR Reactome; R-XTR-176417; Phosphorylation of Emi1.
DR Reactome; R-XTR-2467813; Separation of Sister Chromatids.
DR Reactome; R-XTR-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-XTR-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-XTR-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-XTR-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-XTR-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-XTR-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-XTR-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-XTR-5663220; RHO GTPases Activate Formins.
DR Reactome; R-XTR-68881; Mitotic Metaphase/Anaphase Transition.
DR Reactome; R-XTR-68884; Mitotic Telophase/Cytokinesis.
DR Reactome; R-XTR-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-XTR-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-XTR-8854518; AURKA Activation by TPX2.
DR Reactome; R-XTR-9648025; EML4 and NUDC in mitotic spindle formation.
DR Proteomes; UP000008143; Chromosome 9.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000010344; Expressed in 2-cell stage embryo and 8 other 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:0000922; C:spindle pole; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000278; P:mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0071168; P:protein localization to chromatin; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0032465; P:regulation of cytokinesis; IBA:GO_Central.
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 2: Evidence at transcript 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.
FT CHAIN 1..598
FT /note="Serine/threonine-protein kinase PLK1"
FT /id="PRO_0000086560"
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..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..212
FT /note="Activation loop"
FT /evidence="ECO:0000250"
FT REGION 336..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 201
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 260
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 326
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 598 AA; 68121 MW; 854393ADF42C6C9F CRC64;
MAQVAGKKLT VAPEAGKPPG IPGSSSSVKE IPEILVDPRT RRRYLRGRFL GKGGFAKCYE
ITDLESREVF AGKIVPKTML LKPHQKDKMT MEIAIQRSLD HRHVVGFHGF FEDNDFVYVV
LELCRRRSLL ELHKRRKAVT EPEARYYLKQ TILGCQYLHS NRVIHRDLKL GNLFLNDEME
VKIGDFGLAT KVEYDGERKK TLCGTPNYIA PEVLGKKGHS FEVDIWSIGC IMYTLLVGKP
PFETSCLKET YMRIKKNEYS VPKHINPMAT ALIQKMLRSE PTSRPTIDDL LNDEFFTTGY
IPSRLPTTCL TVPPRFSIAP STIDQSLRKP LTAINKGQDS PLVEKQSVPA KEEEMQQPES
TEPADCYLSE MLQQLTCVNA VKPSERAVIR QEEAEDPASV PIFWVSKWVD YSDKYGLGYQ
LCDNSVGVLF NDSTRLIMYN DGDSLQYIER NNSESYLNVR SYPAALTKKI TLLKYFRNYM
SEHLLKAGAN ITPREGDELA RLPFLRTWFR TRSAIILHLS NGTVQINFFQ DHTKIILCPL
MAAVSYIDEK REFHTYKLSL IQEFGCCKEL ASRLRYARTM VEKLQSSKSG VAHVKASA
