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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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. DR Genevisible; Q07832; MM. 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 //