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Protein

Serine/threonine-protein kinase PLK1

Gene

Plk1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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 (By similarity). 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 (PubMed:25533956). 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 (By similarity).By similarity2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.21. 3474.
ReactomeiR-MMU-156711. Polo-like kinase mediated events.
R-MMU-162658. Golgi Cisternae Pericentriolar Stack Reorganization.
R-MMU-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-MMU-176412. Phosphorylation of the APC/C.
R-MMU-176417. Phosphorylation of Emi1.
R-MMU-2299718. Condensation of Prophase Chromosomes.
R-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2500257. Resolution of Sister Chromatid Cohesion.
R-MMU-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-MMU-2980767. Activation of NIMA Kinases NEK9, NEK6, NEK7.
R-MMU-380259. Loss of Nlp from mitotic centrosomes.
R-MMU-380270. Recruitment of mitotic centrosome proteins and complexes.
R-MMU-5620912. Anchoring of the basal body to the plasma membrane.
R-MMU-5663220. RHO GTPases Activate Formins.
R-MMU-68877. Mitotic Prometaphase.
R-MMU-68881. Mitotic Metaphase/Anaphase Transition.
R-MMU-68884. Mitotic Telophase/Cytokinesis.
R-MMU-69273. Cyclin A/B1 associated events during G2/M transition.
R-MMU-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-MMU-8854518. AURKA Activation by TPX2.

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
Serine/threonine-protein kinase 13
Short name:
STPK13
Gene namesi
Name:Plk1
Synonyms:Plk
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:97621. Plk1.

Subcellular locationi

  • Nucleus By similarity
  • Chromosomecentromerekinetochore 1 Publication
  • Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity
  • Cytoplasmcytoskeletonspindle By similarity
  • Midbody By similarity

  • Note: 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).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Nucleus

Pathology & Biotechi

Disruption phenotypei

Lethality: homozygous embryos do not develop beyond the eight cell stage. Heterozygous mice are healthy and fertile but frequently develop tumors, most frequently lung-invading and liver-invading lymphomas. Analysis of chromosome spreads of spleen-derived cells from 6-month-old mice show aneuploidy.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi82K → M: Abolishes activity. 1 Publication1
Mutagenesisi194D → N or R: Abolishes activity. 1 Publication1
Mutagenesisi206E → D: No change in activity. 1 Publication1
Mutagenesisi206E → V: Decreases activity three-fold. 1 Publication1
Mutagenesisi210T → E: Increases activity four-fold. 1 Publication1
Mutagenesisi210T → V: Decreases activity three-fold. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000865572 – 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

EPDiQ07832.
PaxDbiQ07832.
PeptideAtlasiQ07832.
PRIDEiQ07832.

PTM databases

iPTMnetiQ07832.
PhosphoSitePlusiQ07832.

Expressioni

Tissue specificityi

Newborn and adult spleen, fetal and newborn kidney, liver, brain, thymus and adult bone marrow, thymus, ovary and testes.

Developmental stagei

In the thymus, levels increased during fetal development, were highest in newborn animals and decreased in the adult. In the testes, the PLK levels were higher in the adult than in prepubescent mice while in the ovary, the levels were higher in the prepubescent mice. Accumulates to a maximum during the G2 and M phases, declines to a nearly undetectable level following mitosis and throughout G1 phase, and then begins to accumulate again during S phase.

Gene expression databases

BgeeiENSMUSG00000030867.
CleanExiMM_PLK1.
ExpressionAtlasiQ07832. baseline and differential.
GenevisibleiQ07832. MM.

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) (By similarity). Part of an astrin (SPAG5)-kinastrin (SKAP) complex containing KNSTRN, SPAG5, PLK1, DYNLL1 and SGO2 (By similarity). Interacts with BIRC6/bruce (By similarity). Interacts with CDK1-phosphorylated DCTN6 during mitotic prometaphase; the interaction facilitates recruitment to kinetochores (By similarity). 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 CEP68; the interaction phosphorylates CEP68. Interacts (via POLO-box domain) with DCTN1 (By similarity).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi202250. 29 interactors.
DIPiDIP-56722N.
IntActiQ07832. 28 interactors.
MINTiMINT-4596676.
STRINGi10090.ENSMUSP00000033154.

Structurei

Secondary structure

1603
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi369 – 386Combined sources18
Beta strandi391 – 394Combined sources4
Helixi397 – 400Combined sources4
Helixi403 – 405Combined sources3
Beta strandi411 – 416Combined sources6
Turni418 – 420Combined sources3
Beta strandi421 – 427Combined sources7
Beta strandi432 – 436Combined sources5
Beta strandi441 – 444Combined sources4
Beta strandi448 – 454Combined sources7
Beta strandi460 – 467Combined sources8
Helixi470 – 472Combined sources3
Helixi473 – 489Combined sources17
Turni493 – 496Combined sources4
Beta strandi511 – 516Combined sources6
Beta strandi518 – 525Combined sources8
Beta strandi530 – 534Combined sources5
Turni535 – 537Combined sources3
Beta strandi540 – 544Combined sources5
Turni545 – 548Combined sources4
Beta strandi549 – 553Combined sources5
Beta strandi559 – 563Combined sources5
Helixi564 – 570Combined sources7
Helixi574 – 592Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5DMSX-ray1.90A/C367-603[»]
5DMVX-ray2.50C367-603[»]
5DNJX-ray2.30A367-603[»]
ProteinModelPortaliQ07832.
SMRiQ07832.
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
Contains 2 POLO box domains.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0575. Eukaryota.
ENOG410XQBP. LUCA.
GeneTreeiENSGT00530000062954.
HOGENOMiHOG000248546.
HOVERGENiHBG001843.
InParanoidiQ07832.
KOiK06631.
OMAiKRYMTEH.
OrthoDBiEOG091G0D89.
PhylomeDBiQ07832.
TreeFamiTF101089.

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.
InterProiIPR011009. 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.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
PF00659. POLO_box. 2 hits.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50078. POLO_BOX. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q07832-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNAAAKAGKL ARAPADLGKG GVPGDAVPGA PVAAPLAKEI PEVLVDPRSR
60 70 80 90 100
RQYVRGRFLG KGGFAKCFEI SDADTKEVFA GKIVPKSLLL KPHQKEKMSM
110 120 130 140 150
EISIHRSLAH QHVVGFHDFF 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 SLDPSSRKPL KVLNKGVENP
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
TYINEKRDFQ TYRLSLLEEY GCCKELASRL RYARTMVDKL LSSRSASNRL

KAS
Length:603
Mass (Da):68,301
Last modified:October 1, 1996 - v2
Checksum:i1B980646366EFA10
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti4A → V in AAA39948 (PubMed:8099445).Curated1
Sequence conflicti15A → T in AAA39948 (PubMed:8099445).Curated1
Sequence conflicti23P → L in AAA39948 (PubMed:8099445).Curated1
Sequence conflicti27V → A in AAA39948 (PubMed:8099445).Curated1
Sequence conflicti29G → S in AAA39948 (PubMed:8099445).Curated1
Sequence conflicti41P → L in AAA39948 (PubMed:8099445).Curated1
Sequence conflicti54V → I in AAA39948 (PubMed:8099445).Curated1
Sequence conflicti495A → R in AAA39948 (PubMed:8099445).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06144 mRNA. Translation: AAA39948.1.
U01063 mRNA. Translation: AAA56635.1.
L19558 mRNA. Translation: AAA16071.1.
BC006880 mRNA. Translation: AAH06880.1.
CCDSiCCDS21812.1.
PIRiA47545.
A54596.
RefSeqiNP_035251.3. NM_011121.4.
UniGeneiMm.16525.

Genome annotation databases

EnsembliENSMUST00000033154; ENSMUSP00000033154; ENSMUSG00000030867.
GeneIDi18817.
KEGGimmu:18817.
UCSCiuc009joo.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06144 mRNA. Translation: AAA39948.1.
U01063 mRNA. Translation: AAA56635.1.
L19558 mRNA. Translation: AAA16071.1.
BC006880 mRNA. Translation: AAH06880.1.
CCDSiCCDS21812.1.
PIRiA47545.
A54596.
RefSeqiNP_035251.3. NM_011121.4.
UniGeneiMm.16525.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5DMSX-ray1.90A/C367-603[»]
5DMVX-ray2.50C367-603[»]
5DNJX-ray2.30A367-603[»]
ProteinModelPortaliQ07832.
SMRiQ07832.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202250. 29 interactors.
DIPiDIP-56722N.
IntActiQ07832. 28 interactors.
MINTiMINT-4596676.
STRINGi10090.ENSMUSP00000033154.

PTM databases

iPTMnetiQ07832.
PhosphoSitePlusiQ07832.

Proteomic databases

EPDiQ07832.
PaxDbiQ07832.
PeptideAtlasiQ07832.
PRIDEiQ07832.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033154; ENSMUSP00000033154; ENSMUSG00000030867.
GeneIDi18817.
KEGGimmu:18817.
UCSCiuc009joo.2. mouse.

Organism-specific databases

CTDi5347.
MGIiMGI:97621. Plk1.

Phylogenomic databases

eggNOGiKOG0575. Eukaryota.
ENOG410XQBP. LUCA.
GeneTreeiENSGT00530000062954.
HOGENOMiHOG000248546.
HOVERGENiHBG001843.
InParanoidiQ07832.
KOiK06631.
OMAiKRYMTEH.
OrthoDBiEOG091G0D89.
PhylomeDBiQ07832.
TreeFamiTF101089.

Enzyme and pathway databases

BRENDAi2.7.11.21. 3474.
ReactomeiR-MMU-156711. Polo-like kinase mediated events.
R-MMU-162658. Golgi Cisternae Pericentriolar Stack Reorganization.
R-MMU-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-MMU-176412. Phosphorylation of the APC/C.
R-MMU-176417. Phosphorylation of Emi1.
R-MMU-2299718. Condensation of Prophase Chromosomes.
R-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2500257. Resolution of Sister Chromatid Cohesion.
R-MMU-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-MMU-2980767. Activation of NIMA Kinases NEK9, NEK6, NEK7.
R-MMU-380259. Loss of Nlp from mitotic centrosomes.
R-MMU-380270. Recruitment of mitotic centrosome proteins and complexes.
R-MMU-5620912. Anchoring of the basal body to the plasma membrane.
R-MMU-5663220. RHO GTPases Activate Formins.
R-MMU-68877. Mitotic Prometaphase.
R-MMU-68881. Mitotic Metaphase/Anaphase Transition.
R-MMU-68884. Mitotic Telophase/Cytokinesis.
R-MMU-69273. Cyclin A/B1 associated events during G2/M transition.
R-MMU-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-MMU-8854518. AURKA Activation by TPX2.

Miscellaneous databases

PROiQ07832.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000030867.
CleanExiMM_PLK1.
ExpressionAtlasiQ07832. baseline and differential.
GenevisibleiQ07832. MM.

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.
InterProiIPR011009. 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.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
PF00659. POLO_box. 2 hits.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50078. POLO_BOX. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPLK1_MOUSE
AccessioniPrimary (citable) accession number: Q07832
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: October 1, 1996
Last modified: November 30, 2016
This is version 171 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. SIMILARITY comments
    Index of protein domains and families

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.