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UniProtKB - Q62673 (PLK1_RAT)

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Protein

Serine/threonine-protein kinase PLK1

Gene

Plk1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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 and WEE1. 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. 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. Phosphorylates CEP68 and is required for its degradation. Regulates nuclear envelope breakdown during prophase by phosphorylating DCTN1 resulting in its localization in the nuclear envelope. Phosphorylates the heat shock transcription factor HSF1, promoting HSF1 nuclear translocation upon heat shock. 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.By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.By similarity

Enzyme regulationi

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 (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei82ATPPROSITE-ProRule annotation1
Binding sitei131ATP; via carbonyl oxygenPROSITE-ProRule annotation1
Active sitei176Proton acceptorPROSITE-ProRule annotation1
Binding sitei194ATPPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi59 – 67ATPPROSITE-ProRule annotation9
Nucleotide bindingi178 – 181ATPPROSITE-ProRule annotation4

GO - Molecular functioni

Complete GO annotation...

GO - Biological processi

Complete GO annotation...

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processCell cycle, Cell division, Mitosis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.21. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase PLK1 (EC:2.7.11.21)
Alternative name(s):
Polo-like kinase 1
Short name:
PLK-1
Gene namesi
Name:Plk1
Synonyms:Plk
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3352. Plk1.

Subcellular locationi

  • Nucleus By similarity
  • Chromosome › centromere › kinetochore By similarity
  • Cytoplasm › cytoskeleton › microtubule organizing center › centrosome By similarity
  • Cytoplasm › cytoskeleton › spindle By similarity
  • Midbody By similarity

    • Note: localization at the centrosome starts at the G1/S transition (By similarity). 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 (By similarity). Colocalizes with FRY to separating centrosomes and spindle poles from prophase to metaphase in mitosis, but not in other stages of the cell cycle (By similarity). Localization to the centrosome is required for S phase progression (By similarity). Colocalizes with HSF1 at the spindle poles during prometaphase (By similarity).By similarity

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • condensed chromosome kinetochore Source: UniProtKB-SubCell
  • cytoplasm Source: RGD
  • kinetochore Source: UniProtKB
  • midbody Source: UniProtKB
  • nucleus Source: RGD
  • spindle Source: UniProtKB
  • spindle midzone Source: RGD
  • spindle pole Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000865582 – 603Serine/threonine-protein kinase PLK1Add BLAST602

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki19Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei103PhosphoserineBy similarity1
Modified residuei210Phosphothreonine; by AURKABy similarity1
Modified residuei214PhosphothreonineBy similarity1
Modified residuei269Phosphoserine; by autocatalysisBy similarity1
Modified residuei335Phosphoserine; by autocatalysisBy similarity1
Modified residuei375PhosphoserineBy similarity1
Modified residuei450PhosphoserineBy similarity1
Cross-linki492Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei498PhosphothreonineBy similarity1

Post-translational modificationi

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 (By similarity).By similarity
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 (By similarity).By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ62673.
PRIDEiQ62673.

PTM databases

iPTMnetiQ62673.
PhosphoSitePlusiQ62673.

Expressioni

Gene expression databases

BgeeiENSRNOG00000018815.

Interactioni

Subunit structurei

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. Interacts (via POLO-box domain) with DCTN1. 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. Interacts with HSF1; this interaction increases upon heat shock but does not modulate neither HSF1 homotrimerization nor DNA-binding activities.By similarity

GO - Molecular functioni

Complete GO annotation...

Protein-protein interaction databases

MINTiMINT-4565080.
STRINGi10116.ENSRNOP00000025629.

Structurei

3D structure databases

SMRiQ62673.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini53 – 305Protein kinasePROSITE-ProRule annotationAdd BLAST253
Domaini417 – 480POLO box 1PROSITE-ProRule annotationAdd BLAST64
Domaini515 – 584POLO box 2PROSITE-ProRule annotationAdd BLAST70

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni194 – 221Activation loopBy similarityAdd BLAST28
Regioni493 – 507LinkerBy similarityAdd BLAST15
Regioni538 – 540Important for interaction with phosphorylated proteinsBy similarity3

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi337 – 340D-box that targets the protein for proteasomal degradation in anaphaseBy similarity4

Domaini

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 (By similarity).By similarity

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC5/Polo subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0575. Eukaryota.
ENOG410XQBP. LUCA.
HOGENOMiHOG000248546.
HOVERGENiHBG001843.
InParanoidiQ62673.
KOiK06631.

Family and domain databases

CDDicd13118. POLO_box_1. 1 hit.
cd13117. POLO_box_2. 1 hit.
cd14187. STKc_PLK1. 1 hit.
Gene3Di3.30.1120.30. 2 hits.
InterProiView protein in InterPro
IPR011009. Kinase-like_dom.
IPR033702. PLK1_cat.
IPR033701. POLO_box_1.
IPR033695. POLO_box_2.
IPR000959. POLO_box_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
PfamiView protein in Pfam
PF00069. Pkinase. 1 hit.
PF00659. POLO_box. 2 hits.
SMARTiView protein in SMART
SM00220. S_TKc. 1 hit.
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiView protein in PROSITE
PS50078. POLO_BOX. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q62673-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNAAAKAGKL ARAPADLGKG GVPGDAAPGA PGAAPLAKEI PEVLMDPRSR 
        60         70         80         90        100
RQYVRGRFLG KGGFAKCFEI SDSDTKEVFP GKIVPKSLLL KPHQKEKMSM 
       110        120        130        140        150
EISIHRSLAH QHVVGFHGFF EDSDFVFVVL ELCRRRSLLE LHKRRKALTE 
       160        170        180        190        200
PEARYYLRQI VLGCQYLHRN QVIHRDLKLG NLFLNEDLEV KIGDFGLATK 
       210        220        230        240        250
VEYEGERKKT LCGTPNYIAP EVLSKKGHSF EVDVWSIGCI MYTLLVGKPP 
       260        270        280        290        300
FETSCLKETY LRIKKNEYSI PKHINPVAAS LIQKMLQTDP TARPTIHELL 
       310        320        330        340        350
NDEFFTSGYI PARLPITCLT IPPRFSIAPS SLDPSNRKPL TVLNKGVENP 
       360        370        380        390        400
LPDRPREKEE PVVRETNEAI ECHLSDLLQQ LTSVNASKPS ERGLVRQEEA 
       410        420        430        440        450
EDPACIPIFW VSKWVDYSDK YGLGYQLCDN SVGVLFNDST RLILYNDGDS 
       460        470        480        490        500
LQYIERDGTE SYLTVSSHPN SLMKKITLLN YFRNYMSEHL LKAGANITPR 
       510        520        530        540        550
EGDELARLPY LRTWFRTRSA IILHLSNGTV QINFFQDHTK LILCPLMAAV 
       560        570        580        590        600
TYINEKRDFR TYRLSLLEEY GCCKELASRL RYARTMVDKL LSSRSACNRL 

KAS
Length:603
Mass (Da):68,291
Last modified:December 14, 2011 - v2
Checksum:iD756DD742CB14F6E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti27A → V in AAA18885 (Ref. 1) Curated1
Sequence conflicti32G → V in AAA18885 (Ref. 1) Curated1
Sequence conflicti45M → V in AAA18885 (Ref. 1) Curated1
Sequence conflicti51R → Q in AAA18885 (Ref. 1) Curated1
Sequence conflicti80P → A in AAH83926 (PubMed:15489334).Curated1
Sequence conflicti102I → T in AAA18885 (Ref. 1) Curated1
Sequence conflicti109A → E in AAA18885 (Ref. 1) Curated1
Sequence conflicti291T → A in AAA18885 (Ref. 1) Curated1
Sequence conflicti543 – 544LC → RG in AAA18885 (Ref. 1) Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10188 mRNA. Translation: AAA18885.1.
BC083926 mRNA. Translation: AAH83926.1.
RefSeqiNP_058796.1. NM_017100.1.
UniGeneiRn.11034.

Genome annotation databases

GeneIDi25515.
KEGGirno:25515.
UCSCiRGD:3352. rat.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiPLK1_RAT
AccessioniPrimary (citable) accession number: Q62673
Secondary accession number(s): F1LNH6, Q5XHX4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: December 14, 2011
Last modified: June 7, 2017
This is version 151 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families