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Q07832

- PLK1_MOUSE

UniProt

Q07832 - PLK1_MOUSE

Protein

Serine/threonine-protein kinase PLK1

Gene

Plk1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
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    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, SGOL1, 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 SGOL1: required for spindle pole localization of isoform 3 of SGOL1 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.By similarity

    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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei82 – 821ATPPROSITE-ProRule annotation
    Binding sitei131 – 1311ATP; via carbonyl oxygenPROSITE-ProRule annotation
    Active sitei176 – 1761Proton acceptorPROSITE-ProRule annotation
    Binding sitei194 – 1941ATPPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi59 – 679ATPPROSITE-ProRule annotation
    Nucleotide bindingi178 – 1814ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. microtubule binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. activation of mitotic anaphase-promoting complex activity Source: UniProtKB
    2. centrosome organization Source: UniProtKB
    3. establishment of protein localization Source: MGI
    4. G2/M transition of mitotic cell cycle Source: UniProtKB
    5. G2 DNA damage checkpoint Source: UniProtKB
    6. microtubule bundle formation Source: UniProtKB
    7. mitotic cytokinesis Source: UniProtKB
    8. mitotic nuclear division Source: UniProtKB
    9. mitotic sister chromatid segregation Source: UniProtKB
    10. mitotic spindle assembly checkpoint Source: UniProtKB
    11. negative regulation of apoptotic process Source: UniProtKB
    12. negative regulation of cyclin-dependent protein serine/threonine kinase activity Source: Ensembl
    13. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    14. peptidyl-serine phosphorylation Source: Ensembl
    15. polar body extrusion after meiotic divisions Source: Ensembl
    16. positive regulation of peptidyl-threonine phosphorylation Source: Ensembl
    17. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
    18. positive regulation of ubiquitin-protein transferase activity Source: UniProtKB
    19. protein destabilization Source: Ensembl
    20. protein localization to chromatin Source: UniProtKB
    21. protein phosphorylation Source: UniProtKB
    22. protein ubiquitination Source: Ensembl
    23. regulation of protein binding Source: Ensembl
    24. response to antibiotic Source: Ensembl

    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

    ReactomeiREACT_196580. Condensation of Prophase Chromosomes.
    REACT_196635. Regulation of PLK1 Activity at G2/M Transition.
    REACT_196645. Activation of NIMA Kinases NEK9, NEK6, NEK7.
    REACT_198961. Resolution of Sister Chromatid Cohesion.
    REACT_204224. Phosphorylation of Emi1.
    REACT_205250. Phosphorylation of the APC/C.
    REACT_206803. Cyclin A/B1 associated events during G2/M transition.
    REACT_207679. Separation of Sister Chromatids.
    REACT_226135. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.

    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
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:97621. Plk1.

    Subcellular locationi

    Nucleus By similarity. Chromosomecentromerekinetochore By similarity. 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 SGOL1 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

    1. centrosome Source: UniProtKB
    2. condensed nuclear chromosome outer kinetochore Source: Ensembl
    3. cytoplasm Source: UniProtKB-KW
    4. kinetochore Source: UniProtKB
    5. midbody Source: UniProtKB
    6. nucleus Source: UniProtKB
    7. spindle Source: UniProtKB
    8. spindle microtubule Source: Ensembl
    9. spindle midzone Source: UniProtKB
    10. spindle pole Source: MGI

    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)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi82 – 821K → M: Abolishes activity. 1 Publication
    Mutagenesisi194 – 1941D → N or R: Abolishes activity. 1 Publication
    Mutagenesisi206 – 2061E → D: No change in activity. 1 Publication
    Mutagenesisi206 – 2061E → V: Decreases activity three-fold. 1 Publication
    Mutagenesisi210 – 2101T → E: Increases activity four-fold. 1 Publication
    Mutagenesisi210 – 2101T → V: Decreases activity three-fold. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 603602Serine/threonine-protein kinase PLK1PRO_0000086557Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki19 – 19Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei103 – 1031PhosphoserineBy similarity
    Modified residuei210 – 2101Phosphothreonine; by AURKABy similarity
    Modified residuei214 – 2141PhosphothreonineBy similarity
    Modified residuei269 – 2691Phosphoserine; by autocatalysisBy similarity
    Modified residuei335 – 3351Phosphoserine; by autocatalysisBy similarity
    Modified residuei375 – 3751PhosphoserineBy similarity
    Modified residuei450 – 4501PhosphoserineBy similarity
    Cross-linki492 – 492Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei498 – 4981PhosphothreonineBy similarity

    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

    PaxDbiQ07832.
    PRIDEiQ07832.

    PTM databases

    PhosphoSiteiQ07832.

    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

    ArrayExpressiQ07832.
    BgeeiQ07832.
    CleanExiMM_PLK1.
    GenevestigatoriQ07832.

    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 SGOL1. 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 SGOL2 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.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi202250. 30 interactions.
    IntActiQ07832. 27 interactions.
    MINTiMINT-4596676.

    Structurei

    3D structure databases

    ProteinModelPortaliQ07832.
    SMRiQ07832. Positions 39-328, 372-594.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini53 – 305253Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini417 – 48064POLO box 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini515 – 58470POLO box 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni194 – 22128Activation loopBy similarityAdd
    BLAST
    Regioni493 – 50715LinkerBy similarityAdd
    BLAST
    Regioni538 – 5403Important for interaction with phosphorylated proteinsBy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi337 – 3404D-box that targets the protein for proteasomal degradation in anaphaseBy similarity

    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

    eggNOGiCOG0515.
    HOGENOMiHOG000248546.
    HOVERGENiHBG001843.
    InParanoidiQ07832.
    KOiK06631.
    OMAiLCKKGHS.
    OrthoDBiEOG78M01K.
    PhylomeDBiQ07832.
    TreeFamiTF101089.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000959. POLO_box_duplicated_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    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

    MNAAAKAGKL ARAPADLGKG GVPGDAVPGA PVAAPLAKEI PEVLVDPRSR    50
    RQYVRGRFLG KGGFAKCFEI SDADTKEVFA GKIVPKSLLL KPHQKEKMSM 100
    EISIHRSLAH QHVVGFHDFF EDSDFVFVVL ELCRRRSLLE LHKRRKALTE 150
    PEARYYLRQI VLGCQYLHRN QVIHRDLKLG NLFLNEDLEV KIGDFGLATK 200
    VEYEGERKKT LCGTPNYIAP EVLSKKGHSF EVDVWSIGCI MYTLLVGKPP 250
    FETSCLKETY LRIKKNEYSI PKHINPVAAS LIQKMLQTDP TARPTIHELL 300
    NDEFFTSGYI PARLPITCLT IPPRFSIAPS SLDPSSRKPL KVLNKGVENP 350
    LPDRPREKEE PVVRETNEAI ECHLSDLLQQ LTSVNASKPS ERGLVRQEEA 400
    EDPACIPIFW VSKWVDYSDK YGLGYQLCDN SVGVLFNDST RLILYNDGDS 450
    LQYIERDGTE SYLTVSSHPN SLMKKITLLN YFRNYMSEHL LKAGANITPR 500
    EGDELARLPY LRTWFRTRSA IILHLSNGTV QINFFQDHTK LILCPLMAAV 550
    TYINEKRDFQ TYRLSLLEEY GCCKELASRL RYARTMVDKL LSSRSASNRL 600
    KAS 603
    Length:603
    Mass (Da):68,301
    Last modified:October 1, 1996 - v2
    Checksum:i1B980646366EFA10
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti4 – 41A → V in AAA39948. (PubMed:8099445)Curated
    Sequence conflicti15 – 151A → T in AAA39948. (PubMed:8099445)Curated
    Sequence conflicti23 – 231P → L in AAA39948. (PubMed:8099445)Curated
    Sequence conflicti27 – 271V → A in AAA39948. (PubMed:8099445)Curated
    Sequence conflicti29 – 291G → S in AAA39948. (PubMed:8099445)Curated
    Sequence conflicti41 – 411P → L in AAA39948. (PubMed:8099445)Curated
    Sequence conflicti54 – 541V → I in AAA39948. (PubMed:8099445)Curated
    Sequence conflicti495 – 4951A → R in AAA39948. (PubMed:8099445)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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_011121.3.
    UniGeneiMm.16525.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L06144 mRNA. Translation: AAA39948.1 .
    U01063 mRNA. Translation: AAA56635.1 .
    L19558 mRNA. Translation: AAA16071.1 .
    BC006880 mRNA. Translation: AAH06880.1 .
    CCDSi CCDS21812.1.
    PIRi A47545.
    A54596.
    RefSeqi NP_035251.3. NM_011121.3.
    UniGenei Mm.16525.

    3D structure databases

    ProteinModelPortali Q07832.
    SMRi Q07832. Positions 39-328, 372-594.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202250. 30 interactions.
    IntActi Q07832. 27 interactions.
    MINTi MINT-4596676.

    PTM databases

    PhosphoSitei Q07832.

    Proteomic databases

    PaxDbi Q07832.
    PRIDEi Q07832.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000033154 ; ENSMUSP00000033154 ; ENSMUSG00000030867 .
    GeneIDi 18817.
    KEGGi mmu:18817.
    UCSCi uc009joo.2. mouse.

    Organism-specific databases

    CTDi 5347.
    MGIi MGI:97621. Plk1.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000248546.
    HOVERGENi HBG001843.
    InParanoidi Q07832.
    KOi K06631.
    OMAi LCKKGHS.
    OrthoDBi EOG78M01K.
    PhylomeDBi Q07832.
    TreeFami TF101089.

    Enzyme and pathway databases

    Reactomei REACT_196580. Condensation of Prophase Chromosomes.
    REACT_196635. Regulation of PLK1 Activity at G2/M Transition.
    REACT_196645. Activation of NIMA Kinases NEK9, NEK6, NEK7.
    REACT_198961. Resolution of Sister Chromatid Cohesion.
    REACT_204224. Phosphorylation of Emi1.
    REACT_205250. Phosphorylation of the APC/C.
    REACT_206803. Cyclin A/B1 associated events during G2/M transition.
    REACT_207679. Separation of Sister Chromatids.
    REACT_226135. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.

    Miscellaneous databases

    NextBioi 295174.
    PROi Q07832.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q07832.
    Bgeei Q07832.
    CleanExi MM_PLK1.
    Genevestigatori Q07832.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000959. POLO_box_duplicated_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    PF00659. POLO_box. 2 hits.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS50078. POLO_BOX. 2 hits.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and cloning of a protein kinase-encoding mouse gene, Plk, related to the polo gene of Drosophila."
      Clay F.J., McEwen S.J., Bertoncello I., Wilks A.F., Dunn A.R.
      Proc. Natl. Acad. Sci. U.S.A. 90:4882-4886(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6.
      Tissue: Bone marrow.
    2. "Cloning and characterization of human and murine homologues of the Drosophila polo serine-threonine kinase."
      Hamanaka R., Maloid S., Smith M.R., O'Connell C.D., Longo D.L., Ferris D.K.
      Cell Growth Differ. 5:249-257(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6 X CBA.
      Tissue: Thymus.
    3. "Cell cycle- and terminal differentiation-associated regulation of the mouse mRNA encoding a conserved mitotic protein kinase."
      Lake R.J., Jelinek W.R.
      Mol. Cell. Biol. 13:7793-7801(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Testis.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: FVB/N.
      Tissue: Mammary gland.
    5. "Plk is a functional homolog of Saccharomyces cerevisiae Cdc5, and elevated Plk activity induces multiple septation structures."
      Lee K.S., Erikson R.L.
      Mol. Cell. Biol. 17:3408-3417(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF LYS-82; ASP-194; GLU-206 AND THR-210.
    6. "Polo-like kinase 1 is essential for early embryonic development and tumor suppression."
      Lu L.Y., Wood J.L., Minter-Dykhouse K., Ye L., Saunders T.L., Yu X., Chen J.
      Mol. Cell. Biol. 28:6870-6876(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    7. "Furry protein promotes Aurora A-mediated polo-like kinase 1 activation."
      Ikeda M., Chiba S., Ohashi K., Mizuno K.
      J. Biol. Chem. 287:27670-27681(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FRY.
    8. "Tex14, a plk1-regulated protein, is required for kinetochore-microtubule attachment and regulation of the spindle assembly checkpoint."
      Mondal G., Ohashi A., Yang L., Rowley M., Couch F.J.
      Mol. Cell 45:680-695(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF TEX14.

    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: October 1, 2014
    This is version 146 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

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3