UniProtKB - Q62673 (PLK1_RAT)
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Protein
Serine/threonine-protein kinase PLK1
Gene
Plk1
Organism
Rattus norvegicus (Rat)
Status
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, WEE1 and HNRNPU. 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. Regulates mitotic progression by phosphorylating RIOK2 (By similarity).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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 82 | ATPPROSITE-ProRule annotation | 1 | |
Binding sitei | 131 | ATP; via carbonyl oxygenPROSITE-ProRule annotation | 1 | |
Active sitei | 176 | Proton acceptorPROSITE-ProRule annotation | 1 | |
Binding sitei | 194 | ATPPROSITE-ProRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 59 – 67 | ATPPROSITE-ProRule annotation | 9 | |
Nucleotide bindingi | 178 – 181 | ATPPROSITE-ProRule annotation | 4 |
GO - Molecular functioni
- anaphase-promoting complex binding Source: RGD
- ATP binding Source: RGD
- identical protein binding Source: RGD
- magnesium ion binding Source: RGD
- microtubule binding Source: UniProtKB
- protein kinase activity Source: RGD
- protein kinase binding Source: RGD
- protein serine/threonine kinase activity Source: UniProtKB
GO - Biological processi
- centrosome cycle Source: UniProtKB
- establishment of protein localization Source: RGD
- female meiosis chromosome segregation Source: RGD
- G2/M transition of mitotic cell cycle Source: UniProtKB
- homologous chromosome segregation Source: RGD
- microtubule bundle formation Source: UniProtKB
- mitotic cell cycle Source: UniProtKB
- mitotic cytokinesis Source: UniProtKB
- mitotic sister chromatid segregation Source: UniProtKB
- mitotic spindle assembly checkpoint Source: UniProtKB
- negative regulation of apoptotic process Source: UniProtKB
- negative regulation of cyclin-dependent protein serine/threonine kinase activity Source: RGD
- negative regulation of transcription by RNA polymerase II Source: UniProtKB
- nuclear envelope disassembly Source: UniProtKB
- peptidyl-serine phosphorylation Source: RGD
- polar body extrusion after meiotic divisions Source: RGD
- positive regulation of peptidyl-threonine phosphorylation Source: RGD
- positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
- positive regulation of proteolysis Source: RGD
- positive regulation of ubiquitin protein ligase activity Source: UniProtKB
- positive regulation of ubiquitin-protein transferase activity Source: UniProtKB
- protein destabilization Source: RGD
- protein localization to chromatin Source: UniProtKB
- protein localization to nuclear envelope Source: UniProtKB
- protein phosphorylation Source: MGI
- protein ubiquitination Source: RGD
- regulation of cytokinesis Source: RGD
- regulation of mitotic cell cycle Source: RGD
- regulation of mitotic metaphase/anaphase transition Source: RGD
- regulation of mitotic spindle assembly Source: RGD
- regulation of protein binding Source: RGD
- response to antibiotic Source: RGD
- signal transduction involved in G2 DNA damage checkpoint Source: UniProtKB
- synaptonemal complex disassembly Source: RGD
Keywordsi
Molecular function | Kinase, Serine/threonine-protein kinase, Transferase |
Biological process | Cell cycle, Cell division, Mitosis |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
BRENDAi | 2.7.11.21. 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 |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 3352. Plk1. |
Subcellular locationi
Keywords - Cellular componenti
Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, NucleusPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000086558 | 1 – 603 | Serine/threonine-protein kinase PLK1Add BLAST | 603 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Cross-linki | 19 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity | ||
Modified residuei | 103 | PhosphoserineBy similarity | 1 | |
Modified residuei | 137 | PhosphoserineBy similarity | 1 | |
Modified residuei | 210 | Phosphothreonine; by AURKABy similarity | 1 | |
Modified residuei | 214 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 269 | Phosphoserine; by autocatalysisBy similarity | 1 | |
Modified residuei | 335 | Phosphoserine; by autocatalysisBy similarity | 1 | |
Cross-linki | 338 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Modified residuei | 375 | PhosphoserineBy similarity | 1 | |
Modified residuei | 450 | PhosphoserineBy similarity | 1 | |
Cross-linki | 492 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity | ||
Modified residuei | 498 | PhosphothreonineBy similarity | 1 |
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 conjugationProteomic databases
PaxDbi | Q62673. |
PRIDEi | Q62673. |
PTM databases
iPTMneti | Q62673. |
PhosphoSitePlusi | Q62673. |
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. Interacts with HNRNPU; this interaction induces phosphorylation of HNRNPU in mitosis. Interacts (via its N-terminus) with RIOK2 (By similarity).By similarity
GO - Molecular functioni
- anaphase-promoting complex binding Source: RGD
- identical protein binding Source: RGD
- microtubule binding Source: UniProtKB
- protein kinase binding Source: RGD
Protein-protein interaction databases
STRINGi | 10116.ENSRNOP00000025629. |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 53 – 305 | Protein kinasePROSITE-ProRule annotationAdd BLAST | 253 | |
Domaini | 417 – 480 | POLO box 1PROSITE-ProRule annotationAdd BLAST | 64 | |
Domaini | 515 – 584 | POLO box 2PROSITE-ProRule annotationAdd BLAST | 70 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 194 – 221 | Activation loopBy similarityAdd BLAST | 28 | |
Regioni | 493 – 507 | LinkerBy similarityAdd BLAST | 15 | |
Regioni | 538 – 540 | Important for interaction with phosphorylated proteinsBy similarity | 3 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 337 – 340 | D-box that targets the protein for proteasomal degradation in anaphaseBy similarity | 4 |
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
RepeatPhylogenomic databases
eggNOGi | KOG0575. Eukaryota. ENOG410XQBP. LUCA. |
HOGENOMi | HOG000248546. |
HOVERGENi | HBG001843. |
InParanoidi | Q62673. |
KOi | K06631. |
Family and domain databases
CDDi | cd13118. POLO_box_1. 1 hit. cd13117. POLO_box_2. 1 hit. cd14187. STKc_PLK1. 1 hit. |
Gene3Di | 3.30.1120.30. 3 hits. |
InterProi | View protein in InterPro IPR011009. Kinase-like_dom_sf. IPR033702. PLK1_cat. IPR033701. POLO_box_1. IPR033695. POLO_box_2. IPR000959. POLO_box_dom. IPR036947. POLO_box_dom_sf. IPR000719. Prot_kinase_dom. IPR017441. Protein_kinase_ATP_BS. IPR008271. Ser/Thr_kinase_AS. |
Pfami | View protein in Pfam PF00069. Pkinase. 1 hit. PF00659. POLO_box. 2 hits. |
SMARTi | View protein in SMART SM00220. S_TKc. 1 hit. |
SUPFAMi | SSF56112. SSF56112. 1 hit. |
PROSITEi | View 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. |
i Sequence
Sequence statusi: Complete.
Q62673-1 [UniParc]FASTAAdd to basket
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 27 | A → V in AAA18885 (Ref. 1) Curated | 1 | |
Sequence conflicti | 32 | G → V in AAA18885 (Ref. 1) Curated | 1 | |
Sequence conflicti | 45 | M → V in AAA18885 (Ref. 1) Curated | 1 | |
Sequence conflicti | 51 | R → Q in AAA18885 (Ref. 1) Curated | 1 | |
Sequence conflicti | 80 | P → A in AAH83926 (PubMed:15489334).Curated | 1 | |
Sequence conflicti | 102 | I → T in AAA18885 (Ref. 1) Curated | 1 | |
Sequence conflicti | 109 | A → E in AAA18885 (Ref. 1) Curated | 1 | |
Sequence conflicti | 291 | T → A in AAA18885 (Ref. 1) Curated | 1 | |
Sequence conflicti | 543 – 544 | LC → RG in AAA18885 (Ref. 1) Curated | 2 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U10188 mRNA. Translation: AAA18885.1. BC083926 mRNA. Translation: AAH83926.1. |
RefSeqi | NP_058796.1. NM_017100.1. |
UniGenei | Rn.11034. |
Genome annotation databases
GeneIDi | 25515. |
KEGGi | rno:25515. |
UCSCi | RGD:3352. rat. |
Similar proteinsi
Entry informationi
Entry namei | PLK1_RAT | |
Accessioni | Q62673Primary (citable) accession number: Q62673 Secondary accession number(s): F1LNH6, Q5XHX4 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 11, 2001 |
Last sequence update: | December 14, 2011 | |
Last modified: | March 28, 2018 | |
This is version 158 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |