ID PLK1_MOUSE Reviewed; 603 AA.
AC Q07832;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 27-MAR-2024, entry version 219.
DE RecName: Full=Serine/threonine-protein kinase PLK1;
DE EC=2.7.11.21 {ECO:0000269|PubMed:22405274};
DE AltName: Full=Polo-like kinase 1;
DE Short=PLK-1;
DE AltName: Full=Serine/threonine-protein kinase 13;
DE Short=STPK13;
GN Name=Plk1; Synonyms=Plk;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=8099445; DOI=10.1073/pnas.90.11.4882;
RA Clay F.J., McEwen S.J., Bertoncello I., Wilks A.F., Dunn A.R.;
RT "Identification and cloning of a protein kinase-encoding mouse gene, Plk,
RT related to the polo gene of Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:4882-4886(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6 X CBA; TISSUE=Thymus;
RX PubMed=8018557;
RA Hamanaka R., Maloid S., Smith M.R., O'Connell C.D., Longo D.L.,
RA Ferris D.K.;
RT "Cloning and characterization of human and murine homologues of the
RT Drosophila polo serine-threonine kinase.";
RL Cell Growth Differ. 5:249-257(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=7902533; DOI=10.1128/mcb.13.12.7793-7801.1993;
RA Lake R.J., Jelinek W.R.;
RT "Cell cycle- and terminal differentiation-associated regulation of the
RT mouse mRNA encoding a conserved mitotic protein kinase.";
RL Mol. Cell. Biol. 13:7793-7801(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP MUTAGENESIS OF LYS-82; ASP-194; GLU-206 AND THR-210.
RX PubMed=9154840; DOI=10.1128/mcb.17.6.3408;
RA Lee K.S., Erikson R.L.;
RT "Plk is a functional homolog of Saccharomyces cerevisiae Cdc5, and elevated
RT Plk activity induces multiple septation structures.";
RL Mol. Cell. Biol. 17:3408-3417(1997).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=18794363; DOI=10.1128/mcb.00392-08;
RA Lu L.Y., Wood J.L., Minter-Dykhouse K., Ye L., Saunders T.L., Yu X.,
RA Chen J.;
RT "Polo-like kinase 1 is essential for early embryonic development and tumor
RT suppression.";
RL Mol. Cell. Biol. 28:6870-6876(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP INTERACTION WITH FRY.
RX PubMed=22753416; DOI=10.1074/jbc.m112.378968;
RA Ikeda M., Chiba S., Ohashi K., Mizuno K.;
RT "Furry protein promotes Aurora A-mediated polo-like kinase 1 activation.";
RL J. Biol. Chem. 287:27670-27681(2012).
RN [9]
RP FUNCTION IN PHOSPHORYLATION OF TEX14.
RX PubMed=22405274; DOI=10.1016/j.molcel.2012.01.013;
RA Mondal G., Ohashi A., Yang L., Rowley M., Couch F.J.;
RT "Tex14, a plk1-regulated protein, is required for kinetochore-microtubule
RT attachment and regulation of the spindle assembly checkpoint.";
RL Mol. Cell 45:680-695(2012).
RN [10]
RP FUNCTION.
RX PubMed=27979967; DOI=10.1074/jbc.m116.765438;
RA Zhang B., Wang G., Xu X., Yang S., Zhuang T., Wang G., Ren H., Cheng S.Y.,
RA Jiang Q., Zhang C.;
RT "DAZ-interacting Protein 1 (Dzip1) Phosphorylation by Polo-like Kinase 1
RT (Plk1) Regulates the Centriolar Satellite Localization of the BBSome
RT Protein during the Cell Cycle.";
RL J. Biol. Chem. 292:1351-1360(2017).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25533956; DOI=10.1038/nature14097;
RA Kim J., Ishiguro K., Nambu A., Akiyoshi B., Yokobayashi S., Kagami A.,
RA Ishiguro T., Pendas A.M., Takeda N., Sakakibara Y., Kitajima T.S.,
RA Tanno Y., Sakuno T., Watanabe Y.;
RT "Meikin is a conserved regulator of meiosis-I-specific kinetochore
RT function.";
RL Nature 517:466-471(2015).
RN [12] {ECO:0007744|PDB:5X3S}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 371-594 IN COMPLEX WITH NEDD9
RP PHOSPHOPEPTIDE, INTERACTION WITH NEDD9, AND MUTAGENESIS OF HIS-538 AND
RP LYS-540.
RX PubMed=29191835; DOI=10.1074/jbc.m117.802587;
RA Lee K.H., Hwang J.A., Kim S.O., Kim J.H., Shin S.C., Kim E.E., Lee K.S.,
RA Rhee K., Jeon B.H., Bang J.K., Cha-Molstad H., Soung N.K., Jang J.H.,
RA Ko S.K., Lee H.G., Ahn J.S., Kwon Y.T., Kim B.Y.;
RT "Phosphorylation of human enhancer filamentation 1 (HEF1) stimulates
RT interaction with Polo-like kinase 1 leading to HEF1 localization to focal
RT adhesions.";
RL J. Biol. Chem. 293:847-862(2018).
CC -!- FUNCTION: Serine/threonine-protein kinase that performs several
CC important functions throughout M phase of the cell cycle, including the
CC regulation of centrosome maturation and spindle assembly, the removal
CC of cohesins from chromosome arms, the inactivation of anaphase-
CC promoting complex/cyclosome (APC/C) inhibitors, and the regulation of
CC mitotic exit and cytokinesis (PubMed:22405274, PubMed:27979967). Polo-
CC like kinase proteins act by binding and phosphorylating proteins that
CC are already phosphorylated on a specific motif recognized by the POLO
CC box domains (By similarity). Phosphorylates BORA, BUB1B/BUBR1, CCNB1,
CC CDC25C, CEP55, ECT2, ERCC6L, FBXO5/EMI1, FOXM1, KIF20A/MKLP2, CENPU,
CC NEDD1, NINL, NPM1, NUDC, PKMYT1/MYT1, KIZ, PPP1R12A/MYPT1, POLQ, PRC1,
CC RACGAP1/CYK4, RAD51, RHNO1, SGO1, STAG2/SA2, TEX14, TOPORS, p73/TP73,
CC TPT1, WEE1 and HNRNPU (PubMed:22405274). Plays a key role in centrosome
CC functions and the assembly of bipolar spindles by phosphorylating KIZ,
CC NEDD1 and NINL (By similarity). NEDD1 phosphorylation promotes
CC subsequent targeting of the gamma-tubulin ring complex (gTuRC) to the
CC centrosome, an important step for spindle formation (By similarity).
CC Phosphorylation of NINL component of the centrosome leads to NINL
CC dissociation from other centrosomal proteins (By similarity). Involved
CC in mitosis exit and cytokinesis by phosphorylating CEP55, ECT2,
CC KIF20A/MKLP2, CENPU, PRC1 and RACGAP1 (By similarity). Recruited at the
CC central spindle by phosphorylating and docking PRC1 and KIF20A/MKLP2;
CC creates its own docking sites on PRC1 and KIF20A/MKLP2 by mediating
CC phosphorylation of sites subsequently recognized by the POLO box
CC domains (By similarity). Phosphorylates RACGAP1, thereby creating a
CC docking site for the Rho GTP exchange factor ECT2 that is essential for
CC the cleavage furrow formation (By similarity). Promotes the central
CC spindle recruitment of ECT2 (By similarity). Plays a central role in
CC G2/M transition of mitotic cell cycle by phosphorylating CCNB1, CDC25C,
CC FOXM1, CENPU, PKMYT1/MYT1, PPP1R12A/MYPT1 and WEE1 (By similarity).
CC Part of a regulatory circuit that promotes the activation of CDK1 by
CC phosphorylating the positive regulator CDC25C and inhibiting the
CC negative regulators WEE1 and PKMYT1/MYT1 (By similarity). Also acts by
CC mediating phosphorylation of cyclin-B1 (CCNB1) on centrosomes in
CC prophase (By similarity). Phosphorylates FOXM1, a key mitotic
CC transcription regulator, leading to enhance FOXM1 transcriptional
CC activity (By similarity). Involved in kinetochore functions and sister
CC chromatid cohesion by phosphorylating BUB1B/BUBR1, FBXO5/EMI1 and
CC STAG2/SA2 (By similarity). PLK1 is high on non-attached kinetochores
CC suggesting a role of PLK1 in kinetochore attachment or in spindle
CC assembly checkpoint (SAC) regulation (By similarity). Required for
CC kinetochore localization of BUB1B (By similarity). Regulates the
CC dissociation of cohesin from chromosomes by phosphorylating cohesin
CC subunits such as STAG2/SA2 (By similarity). Phosphorylates SGO1:
CC required for spindle pole localization of isoform 3 of SGO1 and plays a
CC role in regulating its centriole cohesion function (By similarity).
CC Mediates phosphorylation of FBXO5/EMI1, a negative regulator of the
CC APC/C complex during prophase, leading to FBXO5/EMI1 ubiquitination and
CC degradation by the proteasome (By similarity). Acts as a negative
CC regulator of p53 family members: phosphorylates TOPORS, leading to
CC inhibit the sumoylation of p53/TP53 and simultaneously enhance the
CC ubiquitination and subsequent degradation of p53/TP53 (By similarity).
CC Phosphorylates the transactivation domain of the transcription factor
CC p73/TP73, leading to inhibit p73/TP73-mediated transcriptional
CC activation and pro-apoptotic functions (By similarity). Phosphorylates
CC BORA, and thereby promotes the degradation of BORA (By similarity).
CC Contributes to the regulation of AURKA function (By similarity). Also
CC required for recovery after DNA damage checkpoint and entry into
CC mitosis (By similarity).Phosphorylates MISP, leading to stabilization
CC of cortical and astral microtubule attachments required for proper
CC spindle positioning (By similarity). Together with MEIKIN, acts as a
CC regulator of kinetochore function during meiosis I: required both for
CC mono-orientation of kinetochores on sister chromosomes and protection
CC of centromeric cohesin from separase-mediated cleavage
CC (PubMed:25533956). Phosphorylates CEP68 and is required for its
CC degradation (By similarity). Regulates nuclear envelope breakdown
CC during prophase by phosphorylating DCTN1 resulting in its localization
CC in the nuclear envelope (By similarity). Phosphorylates the heat shock
CC transcription factor HSF1, promoting HSF1 nuclear translocation upon
CC heat shock (By similarity). Phosphorylates HSF1 also in the early
CC mitotic period; this phosphorylation regulates HSF1 localization to the
CC spindle pole, the recruitment of the SCF(BTRC) ubiquitin ligase complex
CC induicing HSF1 degradation, and hence mitotic progression (By
CC similarity). Regulates mitotic progression by phosphorylating RIOK2 (By
CC similarity). Through the phosphorylation of DZIP1 regulates the
CC localization during mitosis of the BBSome, a ciliary protein complex
CC involved in cilium biogenesis (PubMed:27979967). Regulates DNA repair
CC during mitosis by mediating phosphorylation of POLQ and RHNO1, thereby
CC promoting POLQ recruitment to DNA damage sites (By similarity).
CC {ECO:0000250|UniProtKB:P53350, ECO:0000269|PubMed:22405274,
CC ECO:0000269|PubMed:25533956, ECO:0000269|PubMed:27979967}.
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 Evidence={ECO:0000269|PubMed:22405274};
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; Evidence={ECO:0000269|PubMed:22405274};
CC -!- ACTIVITY REGULATION: Activated by phosphorylation of Thr-210 by AURKA;
CC phosphorylation by AURKA is enhanced by BORA. Once activated, activity
CC is stimulated by binding target proteins. Binding of target proteins
CC has no effect on the non-activated kinase. Several inhibitors targeting
CC PLKs are currently in development and are under investigation in a
CC growing number of clinical trials, such as BI 2536, an ATP-competitive
CC PLK1 inhibitor or BI 6727, a dihydropteridinone that specifically
CC inhibits the catalytic activity of PLK1 (By similarity).
CC {ECO:0000250|UniProtKB:P53350}.
CC -!- SUBUNIT: Interacts with CEP170 and EVI5. Interacts and phosphorylates
CC ERCC6L. Interacts with FAM29A. Interacts with SLX4/BTBD12 and TTDN1.
CC Interacts with BUB1B. Interacts (via POLO-box domain) with the
CC phosphorylated form of BUB1, CENPU and CDC25C. Interacts with isoform 3
CC of SGO1. Interacts with BORA, KIF2A and AURKA. Interacts with TOPORS
CC and CYLD. Interacts with ECT2; the interaction is stimulated upon
CC phosphorylation of ECT2 on 'Thr-444'. Interacts with PRC1. Interacts
CC with KIF20A/MKLP2 (when phosphorylated), leading to the recruitment at
CC the central spindle. Interacts (via POLO box domains) with
CC PPP1R12A/MYPT1 (when previously phosphorylated by CDK1) (By
CC similarity). Part of an astrin (SPAG5)-kinastrin (SKAP) complex
CC containing KNSTRN, SPAG5, PLK1, DYNLL1 and SGO2 (By similarity).
CC Interacts with BIRC6/bruce (By similarity). Interacts with CDK1-
CC phosphorylated DCTN6 during mitotic prometaphase; the interaction
CC facilitates recruitment to kinetochores (By similarity). Interacts with
CC CDK1-phosphorylated FRY; this interaction occurs in mitotic cells, but
CC not in interphase cells. FRY interaction facilitates AURKA-mediated
CC PLK1 phosphorylation. Interacts with CEP68; the interaction
CC phosphorylates CEP68. Interacts (via POLO-box domain) with DCTN1 (By
CC similarity). Interacts with CEP20 in later G1, S, G2 and M phases of
CC the cell cycle; this interaction recruits PLK1 to centrosomes, a step
CC required for S phase progression (By similarity). Interacts with HSF1;
CC this interaction increases upon heat shock but does not modulate
CC neither HSF1 homotrimerization nor DNA-binding activities (By
CC similarity). Interacts with HNRNPU; this interaction induces
CC phosphorylation of HNRNPU in mitosis (By similarity). Interacts (via
CC its N-terminus) with RIOK2 (By similarity). Interacts with KLHL22 (By
CC similarity). Interacts (via POLO box domains) with NEDD9/HEF1 (via C-
CC terminus) (PubMed:29191835). Interacts (via RVxF motif) with FIRRM;
CC regulates PLK1 kinase activity (By similarity).
CC {ECO:0000250|UniProtKB:P36873, ECO:0000250|UniProtKB:P53350,
CC ECO:0000269|PubMed:22753416, ECO:0000269|PubMed:29191835}.
CC -!- INTERACTION:
CC Q07832; Q5F2C3: Meikin; NbExp=4; IntAct=EBI-2552999, EBI-20739301;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P53350}.
CC Chromosome, centromere, kinetochore {ECO:0000269|PubMed:25533956}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:P53350}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:P53350}. Midbody {ECO:0000250|UniProtKB:P53350}.
CC Note=localization at the centrosome starts at the G1/S transition (By
CC similarity). During early stages of mitosis, the phosphorylated form is
CC detected on centrosomes and kinetochores. Localizes to the outer
CC kinetochore. Presence of SGO1 and interaction with the phosphorylated
CC form of BUB1 is required for the kinetochore localization. Localizes
CC onto the central spindle by phosphorylating and docking at midzone
CC proteins KIF20A/MKLP2 and PRC1 (By similarity). Colocalizes with FRY to
CC separating centrosomes and spindle poles from prophase to metaphase in
CC mitosis, but not in other stages of the cell cycle (By similarity).
CC Localization to the centrosome is required for S phase progression (By
CC similarity). Colocalizes with HSF1 at the spindle poles during
CC prometaphase (By similarity). {ECO:0000250|UniProtKB:P53350}.
CC -!- TISSUE SPECIFICITY: Newborn and adult spleen, fetal and newborn kidney,
CC liver, brain, thymus and adult bone marrow, thymus, ovary and testes.
CC -!- DEVELOPMENTAL STAGE: In the thymus, levels increased during fetal
CC development, were highest in newborn animals and decreased in the
CC adult. In the testes, the PLK levels were higher in the adult than in
CC prepubescent mice while in the ovary, the levels were higher in the
CC prepubescent mice. Accumulates to a maximum during the G2 and M phases,
CC declines to a nearly undetectable level following mitosis and
CC throughout G1 phase, and then begins to accumulate again during S
CC phase.
CC -!- DOMAIN: The POLO box domains act as phosphopeptide-binding module that
CC recognizes and binds serine-[phosphothreonine/phosphoserine]-
CC (proline/X) motifs. PLK1 recognizes and binds docking proteins that are
CC already phosphorylated on these motifs, and then phosphorylates them.
CC PLK1 can also create its own docking sites by mediating phosphorylation
CC of serine-[phosphothreonine/phosphoserine]-(proline/X) motifs
CC subsequently recognized by the POLO box domains (By similarity).
CC {ECO:0000250|UniProtKB:P53350}.
CC -!- PTM: Catalytic activity is enhanced by phosphorylation of Thr-210.
CC Phosphorylation at Thr-210 is first detected on centrosomes in the G2
CC phase of the cell cycle, peaks in prometaphase and gradually disappears
CC from centrosomes during anaphase. Dephosphorylation at Thr-210 at
CC centrosomes is probably mediated by protein phosphatase 1C (PP1C), via
CC interaction with PPP1R12A/MYPT1. Autophosphorylation and
CC phosphorylation of Ser-137 may not be significant for the activation of
CC PLK1 during mitosis, but may enhance catalytic activity during recovery
CC after DNA damage checkpoint. Phosphorylated in vitro by STK10 (By
CC similarity). {ECO:0000250|UniProtKB:P53350}.
CC -!- PTM: Ubiquitinated by the anaphase promoting complex/cyclosome (APC/C)
CC in anaphase and following DNA damage, leading to its degradation by the
CC proteasome. Ubiquitination is mediated via its interaction with
CC FZR1/CDH1. Ubiquitination and subsequent degradation prevents entry
CC into mitosis and is essential to maintain an efficient G2 DNA damage
CC checkpoint. Monoubiquitination at Lys-492 by the BCR(KLHL22) ubiquitin
CC ligase complex does not lead to degradation: it promotes PLK1
CC dissociation from phosphoreceptor proteins and subsequent removal from
CC kinetochores, allowing silencing of the spindle assembly checkpoint
CC (SAC) and chromosome segregation (By similarity).
CC {ECO:0000250|UniProtKB:P53350}.
CC -!- DISRUPTION PHENOTYPE: Lethality: homozygous embryos do not develop
CC beyond the eight cell stage. Heterozygous mice are healthy and fertile
CC but frequently develop tumors, most frequently lung-invading and liver-
CC invading lymphomas. Analysis of chromosome spreads of spleen-derived
CC cells from 6-month-old mice show aneuploidy.
CC {ECO:0000269|PubMed:18794363}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CDC5/Polo subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; L06144; AAA39948.1; -; mRNA.
DR EMBL; U01063; AAA56635.1; -; mRNA.
DR EMBL; L19558; AAA16071.1; -; mRNA.
DR EMBL; BC006880; AAH06880.1; -; mRNA.
DR CCDS; CCDS21812.1; -.
DR PIR; A47545; A47545.
DR PIR; A54596; A54596.
DR RefSeq; NP_035251.3; NM_011121.4.
DR PDB; 5DMS; X-ray; 1.90 A; A/C=367-603.
DR PDB; 5DMV; X-ray; 2.50 A; C=367-603.
DR PDB; 5DNJ; X-ray; 2.30 A; A=367-603.
DR PDB; 5X3S; X-ray; 2.90 A; A/B=371-594.
DR PDBsum; 5DMS; -.
DR PDBsum; 5DMV; -.
DR PDBsum; 5DNJ; -.
DR PDBsum; 5X3S; -.
DR AlphaFoldDB; Q07832; -.
DR SMR; Q07832; -.
DR BioGRID; 202250; 34.
DR DIP; DIP-56722N; -.
DR IntAct; Q07832; 31.
DR MINT; Q07832; -.
DR STRING; 10090.ENSMUSP00000033154; -.
DR iPTMnet; Q07832; -.
DR PhosphoSitePlus; Q07832; -.
DR EPD; Q07832; -.
DR PaxDb; 10090-ENSMUSP00000033154; -.
DR PeptideAtlas; Q07832; -.
DR ProteomicsDB; 289764; -.
DR Pumba; Q07832; -.
DR Antibodypedia; 12634; 1380 antibodies from 48 providers.
DR DNASU; 18817; -.
DR Ensembl; ENSMUST00000033154.8; ENSMUSP00000033154.7; ENSMUSG00000030867.8.
DR GeneID; 18817; -.
DR KEGG; mmu:18817; -.
DR UCSC; uc009joo.2; mouse.
DR AGR; MGI:97621; -.
DR CTD; 5347; -.
DR MGI; MGI:97621; Plk1.
DR VEuPathDB; HostDB:ENSMUSG00000030867; -.
DR eggNOG; KOG0575; Eukaryota.
DR GeneTree; ENSGT00940000157752; -.
DR HOGENOM; CLU_000288_46_1_1; -.
DR InParanoid; Q07832; -.
DR OMA; IQIHKSM; -.
DR OrthoDB; 5471704at2759; -.
DR PhylomeDB; Q07832; -.
DR TreeFam; TF101089; -.
DR BRENDA; 2.7.11.21; 3474.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-156711; Polo-like kinase mediated events.
DR Reactome; R-MMU-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
DR Reactome; R-MMU-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-MMU-176412; Phosphorylation of the APC/C.
DR Reactome; R-MMU-176417; Phosphorylation of Emi1.
DR Reactome; R-MMU-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-2980767; Activation of NIMA Kinases NEK9, NEK6, NEK7.
DR Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-68881; Mitotic Metaphase/Anaphase Transition.
DR Reactome; R-MMU-68884; Mitotic Telophase/Cytokinesis.
DR Reactome; R-MMU-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR Reactome; R-MMU-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 18817; 30 hits in 79 CRISPR screens.
DR ChiTaRS; Plk1; mouse.
DR PRO; PR:Q07832; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q07832; Protein.
DR Bgee; ENSMUSG00000030867; Expressed in embryonic post-anal tail and 178 other cell types or tissues.
DR ExpressionAtlas; Q07832; baseline and differential.
DR Genevisible; Q07832; MM.
DR GO; GO:0034451; C:centriolar satellite; IDA:MGI.
DR GO; GO:0005814; C:centriole; IDA:MGI.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0000785; C:chromatin; IDA:MGI.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:MGI.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; IDA:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0097431; C:mitotic spindle pole; IDA:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000940; C:outer kinetochore; ISO:MGI.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0005876; C:spindle microtubule; IEA:Ensembl.
DR GO; GO:0051233; C:spindle midzone; ISS:UniProtKB.
DR GO; GO:0000922; C:spindle pole; ISO:MGI.
DR GO; GO:0000795; C:synaptonemal complex; IDA:MGI.
DR GO; GO:0010997; F:anaphase-promoting complex binding; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0000287; F:magnesium ion binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; IDA:CACAO.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:Ensembl.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0007098; P:centrosome cycle; ISS:UniProtKB.
DR GO; GO:0006302; P:double-strand break repair; ISO:MGI.
DR GO; GO:0097681; P:double-strand break repair via alternative nonhomologous end joining; ISO:MGI.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; ISO:MGI.
DR GO; GO:0045184; P:establishment of protein localization; ISO:MGI.
DR GO; GO:0016321; P:female meiosis chromosome segregation; IMP:MGI.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0045143; P:homologous chromosome segregation; IMP:MGI.
DR GO; GO:0001578; P:microtubule bundle formation; ISS:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; ISS:UniProtKB.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0051081; P:nuclear membrane disassembly; ISS:UniProtKB.
DR GO; GO:0040038; P:polar body extrusion after meiotic divisions; ISO:MGI.
DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; ISO:MGI.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0045862; P:positive regulation of proteolysis; ISO:MGI.
DR GO; GO:1904668; P:positive regulation of ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0031648; P:protein destabilization; ISO:MGI.
DR GO; GO:0071168; P:protein localization to chromatin; ISS:UniProtKB.
DR GO; GO:0090435; P:protein localization to nuclear envelope; ISS:UniProtKB.
DR GO; GO:0033365; P:protein localization to organelle; IDA:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IMP:CACAO.
DR GO; GO:0016567; P:protein ubiquitination; ISO:MGI.
DR GO; GO:0032465; P:regulation of cytokinesis; ISO:MGI.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; ISO:MGI.
DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; ISO:MGI.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; ISO:MGI.
DR GO; GO:1904776; P:regulation of protein localization to cell cortex; ISO:MGI.
DR GO; GO:0070194; P:synaptonemal complex disassembly; IMP:MGI.
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; POLO box domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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 PANTHER; PTHR24345; SERINE/THREONINE-PROTEIN KINASE PLK; 1.
DR PANTHER; PTHR24345:SF0; SERINE_THREONINE-PROTEIN KINASE PLK1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00659; POLO_box; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF82615; Polo-box domain; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell cycle; Cell division; Centromere;
KW Chromosome; Cytoplasm; Cytoskeleton; Isopeptide bond; Kinase; Kinetochore;
KW Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Transferase; Ubl conjugation.
FT CHAIN 1..603
FT /note="Serine/threonine-protein kinase PLK1"
FT /id="PRO_0000086557"
FT DOMAIN 53..305
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 410..488
FT /note="POLO box 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT DOMAIN 510..592
FT /note="POLO box 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00154"
FT REGION 194..221
FT /note="Activation loop"
FT /evidence="ECO:0000250"
FT REGION 493..507
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 538..540
FT /note="Important for interaction with phosphorylated
FT proteins"
FT /evidence="ECO:0000250"
FT MOTIF 337..340
FT /note="D-box that targets the protein for proteasomal
FT degradation in anaphase"
FT /evidence="ECO:0000250"
FT ACT_SITE 176
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 59..67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 82
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 178..181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53350"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53350"
FT MOD_RES 210
FT /note="Phosphothreonine; by AURKA"
FT /evidence="ECO:0000250|UniProtKB:P53350"
FT MOD_RES 214
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P53350"
FT MOD_RES 269
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 335
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P53350"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53350"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53350"
FT MOD_RES 498
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P53350"
FT CROSSLNK 19
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P53350"
FT CROSSLNK 338
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P53350"
FT CROSSLNK 492
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P53350"
FT MUTAGEN 82
FT /note="K->M: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:9154840"
FT MUTAGEN 194
FT /note="D->N,R: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:9154840"
FT MUTAGEN 206
FT /note="E->D: No change in activity."
FT /evidence="ECO:0000269|PubMed:9154840"
FT MUTAGEN 206
FT /note="E->V: Decreases activity three-fold."
FT /evidence="ECO:0000269|PubMed:9154840"
FT MUTAGEN 210
FT /note="T->E: Increases activity four-fold."
FT /evidence="ECO:0000269|PubMed:9154840"
FT MUTAGEN 210
FT /note="T->V: Decreases activity three-fold."
FT /evidence="ECO:0000269|PubMed:9154840"
FT MUTAGEN 538
FT /note="H->A: Abolishes interaction with NEDD9; when
FT associated with M-540."
FT /evidence="ECO:0000269|PubMed:29191835"
FT MUTAGEN 540
FT /note="K->M: Abolishes interaction with NEDD9; when
FT associated with A-538."
FT /evidence="ECO:0000269|PubMed:29191835"
FT CONFLICT 4
FT /note="A -> V (in Ref. 1; AAA39948)"
FT /evidence="ECO:0000305"
FT CONFLICT 15
FT /note="A -> T (in Ref. 1; AAA39948)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="P -> L (in Ref. 1; AAA39948)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="V -> A (in Ref. 1; AAA39948)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="G -> S (in Ref. 1; AAA39948)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="P -> L (in Ref. 1; AAA39948)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="V -> I (in Ref. 1; AAA39948)"
FT /evidence="ECO:0000305"
FT CONFLICT 495
FT /note="A -> R (in Ref. 1; AAA39948)"
FT /evidence="ECO:0000305"
FT HELIX 369..386
FT /evidence="ECO:0007829|PDB:5DMS"
FT STRAND 391..394
FT /evidence="ECO:0007829|PDB:5DNJ"
FT HELIX 397..400
FT /evidence="ECO:0007829|PDB:5DMS"
FT HELIX 403..405
FT /evidence="ECO:0007829|PDB:5DMS"
FT STRAND 411..416
FT /evidence="ECO:0007829|PDB:5DMS"
FT TURN 418..420
FT /evidence="ECO:0007829|PDB:5DMS"
FT STRAND 421..427
FT /evidence="ECO:0007829|PDB:5DMS"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:5X3S"
FT STRAND 432..436
FT /evidence="ECO:0007829|PDB:5DMS"
FT STRAND 441..444
FT /evidence="ECO:0007829|PDB:5DMS"
FT STRAND 448..454
FT /evidence="ECO:0007829|PDB:5DMS"
FT STRAND 460..467
FT /evidence="ECO:0007829|PDB:5DMS"
FT HELIX 470..472
FT /evidence="ECO:0007829|PDB:5DMS"
FT HELIX 473..489
FT /evidence="ECO:0007829|PDB:5DMS"
FT TURN 493..496
FT /evidence="ECO:0007829|PDB:5DMS"
FT STRAND 511..516
FT /evidence="ECO:0007829|PDB:5DMS"
FT STRAND 518..525
FT /evidence="ECO:0007829|PDB:5DMS"
FT STRAND 530..534
FT /evidence="ECO:0007829|PDB:5DMS"
FT TURN 535..537
FT /evidence="ECO:0007829|PDB:5DMS"
FT STRAND 540..544
FT /evidence="ECO:0007829|PDB:5DMS"
FT TURN 545..548
FT /evidence="ECO:0007829|PDB:5DMS"
FT STRAND 549..553
FT /evidence="ECO:0007829|PDB:5DMS"
FT STRAND 559..563
FT /evidence="ECO:0007829|PDB:5DMS"
FT HELIX 564..570
FT /evidence="ECO:0007829|PDB:5DMS"
FT HELIX 574..592
FT /evidence="ECO:0007829|PDB:5DMS"
SQ SEQUENCE 603 AA; 68301 MW; 1B980646366EFA10 CRC64;
MNAAAKAGKL ARAPADLGKG GVPGDAVPGA PVAAPLAKEI PEVLVDPRSR RQYVRGRFLG
KGGFAKCFEI SDADTKEVFA GKIVPKSLLL KPHQKEKMSM EISIHRSLAH QHVVGFHDFF
EDSDFVFVVL ELCRRRSLLE LHKRRKALTE PEARYYLRQI VLGCQYLHRN QVIHRDLKLG
NLFLNEDLEV KIGDFGLATK VEYEGERKKT LCGTPNYIAP EVLSKKGHSF EVDVWSIGCI
MYTLLVGKPP FETSCLKETY LRIKKNEYSI PKHINPVAAS LIQKMLQTDP TARPTIHELL
NDEFFTSGYI PARLPITCLT IPPRFSIAPS SLDPSSRKPL KVLNKGVENP LPDRPREKEE
PVVRETNEAI ECHLSDLLQQ LTSVNASKPS ERGLVRQEEA EDPACIPIFW VSKWVDYSDK
YGLGYQLCDN SVGVLFNDST RLILYNDGDS LQYIERDGTE SYLTVSSHPN SLMKKITLLN
YFRNYMSEHL LKAGANITPR EGDELARLPY LRTWFRTRSA IILHLSNGTV QINFFQDHTK
LILCPLMAAV TYINEKRDFQ TYRLSLLEEY GCCKELASRL RYARTMVDKL LSSRSASNRL
KAS
//
