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P53350

- PLK1_HUMAN

UniProt

P53350 - PLK1_HUMAN

Protein

Serine/threonine-protein kinase PLK1

Gene

PLK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 169 (01 Oct 2014)
      Sequence version 1 (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.35 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    Activated by phosphorylation of Thr-210 by AURKA; phosphorylation by AURKA is enhanced by BORA. Once activated, activity is stimulated by binding target proteins. Binding of target proteins has no effect on the non-activated kinase. Several inhibitors targeting PLKs are currently in development and are under investigation in a growing number of clinical trials, such as BI 2536, an ATP-competitive PLK1 inhibitor or BI 6727, a dihydropteridinone that specifically inhibits the catalytic activity of PLK1.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei82 – 821ATP
    Binding sitei131 – 1311ATP; via carbonyl oxygen
    Active sitei176 – 1761Proton acceptor
    Binding sitei194 – 1941ATP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi59 – 679ATP
    Nucleotide bindingi178 – 1814ATP

    GO - Molecular functioni

    1. anaphase-promoting complex binding Source: UniProtKB
    2. ATP binding Source: UniProtKB-KW
    3. kinase activity Source: Reactome
    4. microtubule binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. protein kinase activity Source: UniProtKB
    7. protein kinase binding Source: UniProtKB
    8. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. activation of mitotic anaphase-promoting complex activity Source: UniProtKB
    2. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
    3. cell proliferation Source: ProtInc
    4. centrosome organization Source: UniProtKB
    5. cytokinesis Source: UniProtKB
    6. establishment of protein localization Source: MGI
    7. G2/M transition of mitotic cell cycle Source: UniProtKB
    8. G2 DNA damage checkpoint Source: UniProtKB
    9. metaphase/anaphase transition of mitotic cell cycle Source: Reactome
    10. microtubule bundle formation Source: UniProtKB
    11. mitotic cell cycle Source: Reactome
    12. mitotic cytokinesis Source: UniProtKB
    13. mitotic nuclear division Source: UniProtKB
    14. mitotic nuclear envelope disassembly Source: Reactome
    15. mitotic sister chromatid segregation Source: UniProtKB
    16. mitotic spindle assembly checkpoint Source: UniProtKB
    17. negative regulation of apoptotic process Source: UniProtKB
    18. negative regulation of cyclin-dependent protein serine/threonine kinase activity Source: BHF-UCL
    19. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    20. peptidyl-serine phosphorylation Source: UniProtKB
    21. polar body extrusion after meiotic divisions Source: Ensembl
    22. positive regulation of peptidyl-threonine phosphorylation Source: BHF-UCL
    23. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
    24. positive regulation of proteolysis Source: UniProtKB
    25. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    26. positive regulation of ubiquitin-protein transferase activity Source: UniProtKB
    27. protein destabilization Source: UniProtKB
    28. protein localization to chromatin Source: UniProtKB
    29. protein phosphorylation Source: UniProtKB
    30. protein ubiquitination Source: UniProtKB
    31. regulation of cell cycle Source: Reactome
    32. regulation of mitotic cell cycle Source: UniProtKB
    33. regulation of mitotic metaphase/anaphase transition Source: BHF-UCL
    34. regulation of protein binding Source: BHF-UCL
    35. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    36. 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

    BRENDAi2.7.11.21. 2681.
    ReactomeiREACT_1006. Polo-like kinase mediated events.
    REACT_1016. Mitotic Metaphase/Anaphase Transition.
    REACT_1100. Golgi Cisternae Pericentriolar Stack Reorganization.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_160122. Activation of NIMA Kinases NEK9, NEK6, NEK7.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    REACT_172744. Condensation of Prophase Chromosomes.
    REACT_1857. Cyclin A/B1 associated events during G2/M transition.
    REACT_1932. Mitotic Telophase/Cytokinesis.
    REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    REACT_682. Mitotic Prometaphase.
    REACT_6875. Phosphorylation of Emi1.
    REACT_6904. Phosphorylation of the APC/C.
    SignaLinkiP53350.

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:9077. PLK1.

    Subcellular locationi

    Nucleus. Chromosomecentromerekinetochore. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletonspindle. Midbody
    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. Colocalizes with FRY to separating centrosomes and spindle poles from prophase to metaphase in mitosis, but not in other stages of the cell cycle.

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. condensed nuclear chromosome outer kinetochore Source: BHF-UCL
    3. cytoplasm Source: HPA
    4. cytosol Source: Reactome
    5. kinetochore Source: UniProtKB
    6. microtubule cytoskeleton Source: BHF-UCL
    7. midbody Source: UniProtKB
    8. nucleolus Source: HPA
    9. nucleoplasm Source: Reactome
    10. nucleus Source: UniProtKB
    11. spindle Source: UniProtKB
    12. spindle midzone Source: UniProtKB
    13. spindle pole Source: BHF-UCL

    Keywords - Cellular componenti

    Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Defects in PLK1 are associated with some cancers, such as gastric, thyroid or B-cell lymphomas. Expression is cancer increased in tumor tissues with a poor prognosis, suggesting a role in malignant transformations and carcinogenesis.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi67 – 671C → V in analog-sensitive mutant; enlarged catalytic pocket to accommodate purine analogs; when associated with G-130. 1 Publication
    Mutagenesisi82 – 821K → M or R: Kinase defective mutant, abolishes activity. 5 Publications
    Mutagenesisi130 – 1301L → G in analog-sensitive mutant; enlarged catalytic pocket to accommodate purine analogs; when associated with V-67. 1 Publication
    Mutagenesisi137 – 1371S → A: No change in activity. Increases activity and restores recovery after DNA damage checkpoint; when associated with D-210. 2 Publications
    Mutagenesisi137 – 1371S → D: Increases activity. Results in a block in G1/S. 2 Publications
    Mutagenesisi176 – 1761D → N: Abolishes kinase activity. 1 Publication
    Mutagenesisi194 – 1941D → A: Does not interfere with FRY-binding. 1 Publication
    Mutagenesisi210 – 2101T → A: Abolishes activity. Abolishes checkpoint recovery. 5 Publications
    Mutagenesisi210 – 2101T → D: Increases activity and restores recovery after DNA damage checkpoint. 5 Publications
    Mutagenesisi210 – 2101T → V: Reduced catalytic activity, but no effect on affinity for ATP. 5 Publications
    Mutagenesisi337 – 3371R → A: Interferes with ubiquitination and subsequent proteasomal degradation in anaphase; when associated with A-340. 2 Publications
    Mutagenesisi340 – 3401L → A: Interferes with ubiquitination and subsequent proteasomal degradation in anaphase; when associated with A-337. 2 Publications
    Mutagenesisi414 – 4141W → F: Abolishes interaction with CDC25C and reduces centrosomal localization. 1 Publication
    Mutagenesisi492 – 4921K → R: Severe mitotic defects leading to prometaphase delay. Increased localization at kinetochores leading to increased levels of phosphorylated BUBR1. 1 Publication
    Mutagenesisi538 – 5381H → A in pincer mutant; loss of centrosomal location and decreased interaction with phosphorylated CDC25C and BUB1; when associated with M-540. 4 Publications
    Mutagenesisi540 – 5401K → M in pincer mutant; loss of centrosomal location and decreased interaction with phosphorylated CDC25C and BUB1; when associated with A-538. 4 Publications

    Organism-specific databases

    PharmGKBiPA33410.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 603602Serine/threonine-protein kinase PLK1PRO_0000086556Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei6 – 61Phosphothreonine2 Publications
    Cross-linki19 – 19Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei103 – 1031Phosphoserine2 Publications
    Modified residuei137 – 1371Phosphoserine2 Publications
    Modified residuei210 – 2101Phosphothreonine; by AURKA8 Publications
    Modified residuei214 – 2141Phosphothreonine4 Publications
    Modified residuei269 – 2691Phosphoserine; by autocatalysisBy similarity
    Modified residuei335 – 3351Phosphoserine2 Publications
    Modified residuei375 – 3751Phosphoserine2 Publications
    Modified residuei450 – 4501Phosphoserine2 Publications
    Cross-linki492 – 492Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
    Modified residuei498 – 4981Phosphothreonine2 Publications

    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 STK10.9 Publications
    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.2 Publications

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP53350.
    PaxDbiP53350.
    PRIDEiP53350.

    PTM databases

    PhosphoSiteiP53350.

    Expressioni

    Tissue specificityi

    Placenta and colon.

    Developmental stagei

    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.

    Inductioni

    By growth-stimulating agents.

    Gene expression databases

    ArrayExpressiP53350.
    BgeeiP53350.
    CleanExiHS_PLK1.
    GenevestigatoriP53350.

    Organism-specific databases

    HPAiHPA051638.
    HPA053229.

    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). Part of an astrin (SPAG5)-kinastrin (SKAP) complex containing KNSTRN, SPAG5, PLK1, DYNLL1 and SGOL2. Interacts with BIRC6/bruce. Interacts with CDK1-phosphorylated FRY; this interaction occurs in mitotic cells, but not in interphase cells. FRY interaction facilitates AURKA-mediated PLK1 phosphorylation. Interacts with CDK1-phosphorylated DCTN6 during mitotic prometaphase; the interaction facilitates recruitment to kinetochores.26 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Q99IB84EBI-476768,EBI-6927873From a different organism.
    BIRC6Q9NR093EBI-476768,EBI-1765160
    CHEK2O960176EBI-476768,EBI-1180783
    Dvl2Q6083812EBI-476768,EBI-641940From a different organism.
    EIF4BP235883EBI-476768,EBI-970310
    EVI5O604472EBI-476768,EBI-852291
    FADDQ131589EBI-476768,EBI-494804
    GTSE1Q9NYZ36EBI-476768,EBI-2511327
    HSPA1BP081075EBI-476768,EBI-629985
    MCM7P339934EBI-476768,EBI-355924
    MDM2Q009877EBI-476768,EBI-389668
    Mdm2P238042EBI-476768,EBI-641788From a different organism.
    NEK9Q8TD195EBI-476768,EBI-1044009
    OFD1O756652EBI-476768,EBI-716327
    PHC2Q8IXK02EBI-476768,EBI-713786
    SLX4Q8IY926EBI-476768,EBI-2370740
    TANKQ928443EBI-476768,EBI-356349
    TP53P046376EBI-476768,EBI-366083

    Protein-protein interaction databases

    BioGridi111362. 155 interactions.
    DIPiDIP-29696N.
    IntActiP53350. 109 interactions.
    MINTiMINT-86316.
    STRINGi9606.ENSP00000300093.

    Structurei

    Secondary structure

    1
    603
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi42 – 465
    Turni47 – 504
    Beta strandi51 – 6212
    Beta strandi65 – 728
    Turni73 – 753
    Beta strandi78 – 858
    Helixi86 – 883
    Helixi92 – 10615
    Beta strandi116 – 1216
    Beta strandi123 – 1319
    Helixi138 – 1458
    Helixi150 – 16920
    Helixi179 – 1813
    Beta strandi182 – 1843
    Beta strandi190 – 1923
    Helixi220 – 2234
    Beta strandi224 – 2263
    Helixi231 – 24616
    Helixi256 – 2649
    Helixi276 – 28510
    Helixi290 – 2923
    Helixi296 – 3016
    Helixi303 – 3064
    Helixi316 – 3194
    Helixi373 – 38614
    Helixi389 – 3913
    Beta strandi392 – 3943
    Helixi397 – 4004
    Helixi403 – 4053
    Beta strandi411 – 4166
    Turni418 – 4203
    Beta strandi421 – 4277
    Beta strandi432 – 4365
    Beta strandi441 – 4444
    Beta strandi448 – 4547
    Beta strandi460 – 4678
    Helixi470 – 4723
    Helixi473 – 48917
    Turni493 – 4964
    Turni503 – 5053
    Beta strandi511 – 5166
    Beta strandi518 – 5258
    Beta strandi530 – 5345
    Turni535 – 5373
    Beta strandi540 – 5445
    Turni545 – 5484
    Beta strandi549 – 5535
    Beta strandi559 – 5635
    Helixi564 – 5707
    Helixi574 – 59118

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Q4KX-ray2.30A/B/C345-603[»]
    1Q4OX-ray2.20A/B367-603[»]
    1UMWX-ray1.90A/B367-603[»]
    2OGQX-ray1.95A365-603[»]
    2OJXX-ray2.85A365-603[»]
    2OU7X-ray2.40A13-345[»]
    2OWBX-ray2.10A13-345[»]
    2RKUX-ray1.95A37-330[»]
    2V5QX-ray2.30A/B33-345[»]
    2YACX-ray2.20A36-345[»]
    3BZIX-ray2.10A365-603[»]
    3C5LX-ray2.33A373-593[»]
    3FC2X-ray2.45A13-345[»]
    3FVHX-ray1.58A371-603[»]
    3HIHX-ray1.70A/B371-593[»]
    3HIKX-ray1.77A367-603[»]
    3KB7X-ray2.50A36-345[»]
    3P2WX-ray1.66A371-594[»]
    3P2ZX-ray1.79A371-594[»]
    3P34X-ray1.40A371-594[»]
    3P35X-ray2.09A/B/C371-594[»]
    3P36X-ray1.59A371-594[»]
    3P37X-ray2.38A/B/C371-594[»]
    3Q1IX-ray1.40A371-594[»]
    3RQ7X-ray1.55A371-603[»]
    3THBX-ray2.50A13-345[»]
    4A4LX-ray2.35A36-345[»]
    4A4OX-ray2.70A36-345[»]
    4DFWX-ray1.55A367-603[»]
    4E67X-ray2.10A371-594[»]
    4E9CX-ray1.70A371-594[»]
    4E9DX-ray2.75A371-594[»]
    4H5XX-ray1.95A/B367-603[»]
    4H71X-ray1.93A/B367-603[»]
    4HABX-ray2.65A/B/C371-593[»]
    4HCOX-ray2.75A/B367-603[»]
    4HY2X-ray2.00A371-595[»]
    4J52X-ray2.30A38-330[»]
    4J53X-ray2.50A38-330[»]
    4LKLX-ray1.58A372-593[»]
    4LKMX-ray2.00A/C371-601[»]
    4MLUX-ray1.45A371-603[»]
    DisProtiDP00428.
    ProteinModelPortaliP53350.
    SMRiP53350. Positions 37-330, 371-592.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP53350.

    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 loopAdd
    BLAST
    Regioni493 – 50715LinkerAdd
    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 anaphase

    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.4 Publications

    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.
    InParanoidiP53350.
    KOiK06631.
    OMAiLCKKGHS.
    OrthoDBiEOG78M01K.
    PhylomeDBiP53350.
    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.

    P53350-1 [UniParc]FASTAAdd to Basket

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    MSAAVTAGKL ARAPADPGKA GVPGVAAPGA PAAAPPAKEI PEVLVDPRSR    50
    RRYVRGRFLG KGGFAKCFEI SDADTKEVFA GKIVPKSLLL KPHQREKMSM 100
    EISIHRSLAH QHVVGFHGFF EDNDFVFVVL ELCRRRSLLE LHKRRKALTE 150
    PEARYYLRQI VLGCQYLHRN RVIHRDLKLG NLFLNEDLEV KIGDFGLATK 200
    VEYDGERKKT LCGTPNYIAP EVLSKKGHSF EVDVWSIGCI MYTLLVGKPP 250
    FETSCLKETY LRIKKNEYSI PKHINPVAAS LIQKMLQTDP TARPTINELL 300
    NDEFFTSGYI PARLPITCLT IPPRFSIAPS SLDPSNRKPL TVLNKGLENP 350
    LPERPREKEE PVVRETGEVV DCHLSDMLQQ LHSVNASKPS ERGLVRQEEA 400
    EDPACIPIFW VSKWVDYSDK YGLGYQLCDN SVGVLFNDST RLILYNDGDS 450
    LQYIERDGTE SYLTVSSHPN SLMKKITLLK YFRNYMSEHL LKAGANITPR 500
    EGDELARLPY LRTWFRTRSA IILHLSNGSV QINFFQDHTK LILCPLMAAV 550
    TYIDEKRDFR TYRLSLLEEY GCCKELASRL RYARTMVDKL LSSRSASNRL 600
    KAS 603
    Length:603
    Mass (Da):68,255
    Last modified:October 1, 1996 - v1
    Checksum:i178C2F13C10E8206
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21S → T in AAA56634. (PubMed:8018557)Curated
    Sequence conflicti11 – 111A → P in AAA56634. (PubMed:8018557)Curated
    Sequence conflicti58 – 581F → L in AAA56634. (PubMed:8018557)Curated
    Sequence conflicti60 – 601G → S in AAA56634. (PubMed:8018557)Curated
    Sequence conflicti73 – 731A → V in AAA36659. (PubMed:7902533)Curated
    Sequence conflicti73 – 731A → V in AAB36946. (PubMed:9083047)Curated
    Sequence conflicti123 – 1231N → T in CAA62260. (PubMed:7478607)Curated
    Sequence conflicti141 – 1411L → P in CAA53536. (PubMed:8127874)Curated
    Sequence conflicti227 – 2271G → E in CAA53536. (PubMed:8127874)Curated
    Sequence conflicti301 – 3011N → G in AAA36659. (PubMed:7902533)Curated
    Sequence conflicti495 – 4951A → G in AAA36659. (PubMed:7902533)Curated
    Sequence conflicti501 – 5011E → Q in AAA36659. (PubMed:7902533)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti12 – 121R → L in a lung squamous cell carcinoma sample; somatic mutation. 1 Publication
    VAR_041018
    Natural varianti261 – 2611L → F.1 Publication
    Corresponds to variant rs35056440 [ dbSNP | Ensembl ].
    VAR_041019
    Natural varianti297 – 2971N → D.
    Corresponds to variant rs16972799 [ dbSNP | Ensembl ].
    VAR_051659
    Natural varianti332 – 3321L → V.1 Publication
    Corresponds to variant rs45489499 [ dbSNP | Ensembl ].
    VAR_041020
    Natural varianti463 – 4631L → H.1 Publication
    Corresponds to variant rs45569335 [ dbSNP | Ensembl ].
    VAR_041021
    Natural varianti518 – 5181R → H.1 Publication
    Corresponds to variant rs56027600 [ dbSNP | Ensembl ].
    VAR_041022
    Natural varianti595 – 5951S → L.
    Corresponds to variant rs34001032 [ dbSNP | Ensembl ].
    VAR_051660
    Natural varianti599 – 5991R → H.
    Corresponds to variant rs34954545 [ dbSNP | Ensembl ].
    VAR_051661

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U01038 mRNA. Translation: AAA56634.1.
    L19559 mRNA. Translation: AAA36659.1.
    X73458 mRNA. Translation: CAA51837.1.
    X75932 mRNA. Translation: CAA53536.1.
    BC002369 mRNA. Translation: AAH02369.1.
    BC003002 mRNA. Translation: AAH03002.1.
    BC014846 mRNA. Translation: AAH14846.1.
    X90725 Genomic DNA. Translation: CAA62260.1.
    U78073 Genomic DNA. Translation: AAB36946.1.
    CCDSiCCDS10616.1.
    PIRiS34130.
    RefSeqiNP_005021.2. NM_005030.3.
    UniGeneiHs.592049.

    Genome annotation databases

    EnsembliENST00000300093; ENSP00000300093; ENSG00000166851.
    GeneIDi5347.
    KEGGihsa:5347.
    UCSCiuc002dlz.1. human.

    Polymorphism databases

    DMDMi1709658.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U01038 mRNA. Translation: AAA56634.1 .
    L19559 mRNA. Translation: AAA36659.1 .
    X73458 mRNA. Translation: CAA51837.1 .
    X75932 mRNA. Translation: CAA53536.1 .
    BC002369 mRNA. Translation: AAH02369.1 .
    BC003002 mRNA. Translation: AAH03002.1 .
    BC014846 mRNA. Translation: AAH14846.1 .
    X90725 Genomic DNA. Translation: CAA62260.1 .
    U78073 Genomic DNA. Translation: AAB36946.1 .
    CCDSi CCDS10616.1.
    PIRi S34130.
    RefSeqi NP_005021.2. NM_005030.3.
    UniGenei Hs.592049.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Q4K X-ray 2.30 A/B/C 345-603 [» ]
    1Q4O X-ray 2.20 A/B 367-603 [» ]
    1UMW X-ray 1.90 A/B 367-603 [» ]
    2OGQ X-ray 1.95 A 365-603 [» ]
    2OJX X-ray 2.85 A 365-603 [» ]
    2OU7 X-ray 2.40 A 13-345 [» ]
    2OWB X-ray 2.10 A 13-345 [» ]
    2RKU X-ray 1.95 A 37-330 [» ]
    2V5Q X-ray 2.30 A/B 33-345 [» ]
    2YAC X-ray 2.20 A 36-345 [» ]
    3BZI X-ray 2.10 A 365-603 [» ]
    3C5L X-ray 2.33 A 373-593 [» ]
    3FC2 X-ray 2.45 A 13-345 [» ]
    3FVH X-ray 1.58 A 371-603 [» ]
    3HIH X-ray 1.70 A/B 371-593 [» ]
    3HIK X-ray 1.77 A 367-603 [» ]
    3KB7 X-ray 2.50 A 36-345 [» ]
    3P2W X-ray 1.66 A 371-594 [» ]
    3P2Z X-ray 1.79 A 371-594 [» ]
    3P34 X-ray 1.40 A 371-594 [» ]
    3P35 X-ray 2.09 A/B/C 371-594 [» ]
    3P36 X-ray 1.59 A 371-594 [» ]
    3P37 X-ray 2.38 A/B/C 371-594 [» ]
    3Q1I X-ray 1.40 A 371-594 [» ]
    3RQ7 X-ray 1.55 A 371-603 [» ]
    3THB X-ray 2.50 A 13-345 [» ]
    4A4L X-ray 2.35 A 36-345 [» ]
    4A4O X-ray 2.70 A 36-345 [» ]
    4DFW X-ray 1.55 A 367-603 [» ]
    4E67 X-ray 2.10 A 371-594 [» ]
    4E9C X-ray 1.70 A 371-594 [» ]
    4E9D X-ray 2.75 A 371-594 [» ]
    4H5X X-ray 1.95 A/B 367-603 [» ]
    4H71 X-ray 1.93 A/B 367-603 [» ]
    4HAB X-ray 2.65 A/B/C 371-593 [» ]
    4HCO X-ray 2.75 A/B 367-603 [» ]
    4HY2 X-ray 2.00 A 371-595 [» ]
    4J52 X-ray 2.30 A 38-330 [» ]
    4J53 X-ray 2.50 A 38-330 [» ]
    4LKL X-ray 1.58 A 372-593 [» ]
    4LKM X-ray 2.00 A/C 371-601 [» ]
    4MLU X-ray 1.45 A 371-603 [» ]
    DisProti DP00428.
    ProteinModelPortali P53350.
    SMRi P53350. Positions 37-330, 371-592.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111362. 155 interactions.
    DIPi DIP-29696N.
    IntActi P53350. 109 interactions.
    MINTi MINT-86316.
    STRINGi 9606.ENSP00000300093.

    Chemistry

    BindingDBi P53350.
    ChEMBLi CHEMBL3024.
    GuidetoPHARMACOLOGYi 2168.

    PTM databases

    PhosphoSitei P53350.

    Polymorphism databases

    DMDMi 1709658.

    Proteomic databases

    MaxQBi P53350.
    PaxDbi P53350.
    PRIDEi P53350.

    Protocols and materials databases

    DNASUi 5347.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000300093 ; ENSP00000300093 ; ENSG00000166851 .
    GeneIDi 5347.
    KEGGi hsa:5347.
    UCSCi uc002dlz.1. human.

    Organism-specific databases

    CTDi 5347.
    GeneCardsi GC16P023712.
    HGNCi HGNC:9077. PLK1.
    HPAi HPA051638.
    HPA053229.
    MIMi 602098. gene.
    neXtProti NX_P53350.
    PharmGKBi PA33410.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000248546.
    HOVERGENi HBG001843.
    InParanoidi P53350.
    KOi K06631.
    OMAi LCKKGHS.
    OrthoDBi EOG78M01K.
    PhylomeDBi P53350.
    TreeFami TF101089.

    Enzyme and pathway databases

    BRENDAi 2.7.11.21. 2681.
    Reactomei REACT_1006. Polo-like kinase mediated events.
    REACT_1016. Mitotic Metaphase/Anaphase Transition.
    REACT_1100. Golgi Cisternae Pericentriolar Stack Reorganization.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_160122. Activation of NIMA Kinases NEK9, NEK6, NEK7.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    REACT_172744. Condensation of Prophase Chromosomes.
    REACT_1857. Cyclin A/B1 associated events during G2/M transition.
    REACT_1932. Mitotic Telophase/Cytokinesis.
    REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    REACT_682. Mitotic Prometaphase.
    REACT_6875. Phosphorylation of Emi1.
    REACT_6904. Phosphorylation of the APC/C.
    SignaLinki P53350.

    Miscellaneous databases

    ChiTaRSi PLK1. human.
    EvolutionaryTracei P53350.
    GeneWikii PLK1.
    GenomeRNAii 5347.
    NextBioi 20722.
    PROi P53350.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P53350.
    Bgeei P53350.
    CleanExi HS_PLK1.
    Genevestigatori P53350.

    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. "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].
      Tissue: Placenta.
    2. "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].
    3. "Cell cycle analysis and chromosomal localization of human Plk1, a putative homologue of the mitotic kinases Drosophila polo and Saccharomyces cerevisiae Cdc5."
      Golsteyn R.M., Schultz S.J., Bartek J., Ziemiecki A., Ried T., Nigg E.A.
      J. Cell Sci. 107:1509-1517(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Induction and down-regulation of PLK, a human serine/threonine kinase expressed in proliferating cells and tumors."
      Holtrich U., Wolf G., Braeuninger A., Karn T., Boehme B., Ruebsamen-Waigmann H., Strebhardt K.
      Proc. Natl. Acad. Sci. U.S.A. 91:1736-1740(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Lung.
    5. "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].
      Tissue: Colon and Lung.
    6. "Identification and functional characterization of the human and murine polo-like kinase (Plk) promoter."
      Brauninger A., Strebhardt K., Rubsamen-Waigmann H.
      Oncogene 11:1793-1800(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-136.
    7. "Cell cycle regulation of the human polo-like kinase (PLK) promoter."
      Uchiumi T., Longo D.L., Ferris D.K.
      J. Biol. Chem. 272:9166-9174(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-136.
    8. "Antibody microinjection reveals an essential role for human polo-like kinase 1 (Plk1) in the functional maturation of mitotic centrosomes."
      Lane H.A., Nigg E.A.
      J. Cell Biol. 135:1701-1713(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CENTROSOME MATURATION, SUBCELLULAR LOCATION.
    9. "The human polo-like kinase, PLK, regulates cdc2/cyclin B through phosphorylation and activation of the cdc25C phosphatase."
      Roshak A.K., Capper E.A., Imburgia C., Fornwald J., Scott G., Marshall L.A.
      Cell. Signal. 12:405-411(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF CDC25C.
    10. "Phosphorylation of threonine 210 and the role of serine 137 in the regulation of mammalian polo-like kinase."
      Jang Y.-J., Ma S., Terada Y., Erikson R.L.
      J. Biol. Chem. 277:44115-44120(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT SER-137 AND THR-210, MUTAGENESIS OF LYS-82; SER-137 AND THR-210.
    11. "Cooperative phosphorylation including the activity of polo-like kinase 1 regulates the subcellular localization of cyclin B1."
      Yuan J., Eckerdt F., Bereiter-Hahn J., Kurunci-Csacsko E., Kaufmann M., Strebhardt K.
      Oncogene 21:8282-8292(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF CCNB1, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-82 AND THR-210.
    12. "Identification of phosphorylation sites in the polo-like kinases Plx1 and Plk1 by a novel strategy based on element and electrospray high resolution mass spectrometry."
      Wind M., Kelm O., Nigg E.A., Lehmann W.D.
      Proteomics 2:1516-1523(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-335.
    13. "Polo-like kinase 1 regulates Nlp, a centrosome protein involved in microtubule nucleation."
      Casenghi M., Meraldi P., Weinhart U., Duncan P.I., Korner R., Nigg E.A.
      Dev. Cell 5:113-125(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF NINL.
    14. "Stk10, a new member of the polo-like kinase kinase family highly expressed in hematopoietic tissue."
      Walter S.A., Cutler R.E. Jr., Martinez R., Gishizky M., Hill R.J.
      J. Biol. Chem. 278:18221-18228(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY STK10.
    15. "Identification of a consensus motif for Plk (Polo-like kinase) phosphorylation reveals Myt1 as a Plk1 substrate."
      Nakajima H., Toyoshima-Morimoto F., Taniguchi E., Nishida E.
      J. Biol. Chem. 278:25277-25280(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF PKMYT1.
    16. "Phosphorylation of mitotic kinesin-like protein 2 by polo-like kinase 1 is required for cytokinesis."
      Neef R., Preisinger C., Sutcliffe J., Kopajtich R., Nigg E.A., Mayer T.U., Barr F.A.
      J. Cell Biol. 162:863-875(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF KIF20A, DOMAIN POLO BOX, SUBCELLULAR LOCATION, INTERACTION WITH KIF20A.
    17. "Active cyclin B1-Cdk1 first appears on centrosomes in prophase."
      Jackman M., Lindon C., Nigg E.A., Pines J.
      Nat. Cell Biol. 5:143-148(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF CCNB1, SUBCELLULAR LOCATION.
    18. "Ordered proteolysis in anaphase inactivates Plk1 to contribute to proper mitotic exit in human cells."
      Lindon C., Pines J.
      J. Cell Biol. 164:233-241(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PROTEASOMAL DEGRADATION, DOMAIN D-BOX MOTIF, MUTAGENESIS OF ARG-337 AND LEU-340.
    19. "Plk1 regulates activation of the anaphase promoting complex by phosphorylating and triggering SCFbetaTrCP-dependent destruction of the APC inhibitor Emi1."
      Hansen D.V., Loktev A.V., Ban K.H., Jackson P.K.
      Mol. Biol. Cell 15:5623-5634(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF FBXO5.
    20. "M-phase kinases induce phospho-dependent ubiquitination of somatic Wee1 by SCFbeta-TrCP."
      Watanabe N., Arai H., Nishihara Y., Taniguchi M., Watanabe N., Hunter T., Osada H.
      Proc. Natl. Acad. Sci. U.S.A. 101:4419-4424(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF WEE1.
    21. "Role of Polo-like kinase in the degradation of early mitotic inhibitor 1, a regulator of the anaphase promoting complex/cyclosome."
      Moshe Y., Boulaire J., Pagano M., Hershko A.
      Proc. Natl. Acad. Sci. U.S.A. 101:7937-7942(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF FBXO5.
    22. "Cdk1/Erk2- and Plk1-dependent phosphorylation of a centrosome protein, Cep55, is required for its recruitment to midbody and cytokinesis."
      Fabbro M., Zhou B.-B., Takahashi M., Sarcevic B., Lal P., Graham M.E., Gabrielli B.G., Robinson P.J., Nigg E.A., Ono Y., Khanna K.K.
      Dev. Cell 9:477-488(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF CEP55.
    23. "The forkhead-associated domain protein Cep170 interacts with Polo-like kinase 1 and serves as a marker for mature centrioles."
      Guarguaglini G., Duncan P.I., Stierhof Y.D., Holmstroem T., Duensing S., Nigg E.A.
      Mol. Biol. Cell 16:1095-1107(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CEP170.
    24. "The evi5 oncogene regulates cyclin accumulation by stabilizing the anaphase-promoting complex inhibitor emi1."
      Eldridge A.G., Loktev A.V., Hansen D.V., Verschuren E.W., Reimann J.D.R., Jackson P.K.
      Cell 124:367-380(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EVI5.
    25. "Phosphorylation- and polo-box-dependent binding of Plk1 to Bub1 is required for the kinetochore localization of Plk1."
      Qi W., Tang Z., Yu H.
      Mol. Biol. Cell 17:3705-3716(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH BUB1 AND BUB1B, MUTAGENESIS OF HIS-538 AND LYS-540.
    26. "The Plk1 target Kizuna stabilizes mitotic centrosomes to ensure spindle bipolarity."
      Oshimori N., Ohsugi M., Yamamoto T.
      Nat. Cell Biol. 8:1095-1101(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF KIZ.
    27. "Phosphorylation of the cytokinesis regulator ECT2 at G2/M phase stimulates association of the mitotic kinase Plk1 and accumulation of GTP-bound RhoA."
      Niiya F., Tatsumoto T., Lee K.S., Miki T.
      Oncogene 25:827-837(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF ECT2, INTERACTION WITH ECT2.
    28. "Self-regulated Plk1 recruitment to kinetochores by the Plk1-PBIP1 interaction is critical for proper chromosome segregation."
      Kang Y.H., Park J.-E., Yu L.-R., Soung N.-K., Yun S.-M., Bang J.K., Seong Y.-S., Yu H., Garfield S., Veenstra T.D., Lee K.S.
      Mol. Cell 24:409-422(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF CENPU.
    29. "Expression of polo-like kinase 1 (PLK1) protein predicts the survival of patients with gastric carcinoma."
      Kanaji S., Saito H., Tsujitani S., Matsumoto S., Tatebe S., Kondo A., Ozaki M., Ito H., Ikeguchi M.
      Oncology 70:126-133(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN CANCER.
    30. Cited for: INVOLVEMENT IN CANCER.
    31. "PICH, a centromere-associated SNF2 family ATPase, is regulated by Plk1 and required for the spindle checkpoint."
      Baumann C., Koerner R., Hofmann K., Nigg E.A.
      Cell 128:101-114(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ERCC6L.
    32. "Shugoshin 1 plays a central role in kinetochore assembly and is required for kinetochore targeting of Plk1."
      Pouwels J., Kukkonen A.M., Lan W., Daum J.R., Gorbsky G.J., Stukenberg T., Kallio M.J.
      Cell Cycle 6:1579-1585(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    33. "TTDN1 is a Plk1-interacting protein involved in maintenance of cell cycle integrity."
      Zhang Y., Tian Y., Chen Q., Chen D., Zhai Z., Shu H.-B.
      Cell. Mol. Life Sci. 64:632-640(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TTDN1.
    34. "Polo-like kinase 1 facilitates chromosome alignment during prometaphase through BubR1."
      Matsumura S., Toyoshima F., Nishida E.
      J. Biol. Chem. 282:15217-15227(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF BUB1B.
    35. "Expression of PLK1 and survivin in diffuse large B-cell lymphoma."
      Liu L., Zhang M., Zou P.
      Leuk. Lymphoma 48:2179-2183(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN CANCER.
    36. "Choice of Plk1 docking partners during mitosis and cytokinesis is controlled by the activation state of Cdk1."
      Neef R., Gruneberg U., Kopajtich R., Li X., Nigg E.A., Sillje H., Barr F.A.
      Nat. Cell Biol. 9:436-444(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF PRC1, DOMAIN POLO BOX.
    37. Cited for: INTERACTION WITH CYLD, IDENTIFICATION BY MASS SPECTROMETRY.
    38. "The Cdc14B-Cdh1-Plk1 axis controls the G2 DNA-damage-response checkpoint."
      Bassermann F., Frescas D., Guardavaccaro D., Busino L., Peschiaroli A., Pagano M.
      Cell 134:256-267(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION BY THE APC/C COMPLEX, INTERACTION WITH FZR1, MUTAGENESIS OF ARG-337 AND LEU-340.
    39. "Final stages of cytokinesis and midbody ring formation are controlled by BRUCE."
      Pohl C., Jentsch S.
      Cell 132:832-845(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BIRC6/BRUCE.
    40. "p73-mediated transcriptional activity is negatively regulated by polo-like kinase 1."
      Soond S.M., Barry S.P., Melino G., Knight R.A., Latchman D.S., Stephanou A.
      Cell Cycle 7:1214-1223(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF TP73.
    41. "Plk1 regulates mitotic Aurora A function through betaTrCP-dependent degradation of hBora."
      Chan E.H., Santamaria A., Sillje H.H., Nigg E.A.
      Chromosoma 117:457-469(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PHOSPHORYLATED BORA.
    42. "sSgo1, a major splice variant of Sgo1, functions in centriole cohesion where it is regulated by Plk1."
      Wang X., Yang Y., Duan Q., Jiang N., Huang Y., Darzynkiewicz Z., Dai W.
      Dev. Cell 14:331-341(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF SGOL1, INTERACTION WITH SGOL1.
    43. "Myosin phosphatase-targeting subunit 1 regulates mitosis by antagonizing polo-like kinase 1."
      Yamashiro S., Yamakita Y., Totsukawa G., Goto H., Kaibuchi K., Ito M., Hartshorne D.J., Matsumura F.
      Dev. Cell 14:787-797(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF PPP1R12A, PHOSPHORYLATION AT THR-210, DEPHOSPHORYLATION BY PPP1C, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-538 AND LYS-540.
    44. "Inhibitory role of Plk1 in the regulation of p73-dependent apoptosis through physical interaction and phosphorylation."
      Koida N., Ozaki T., Yamamoto H., Ono S., Koda T., Ando K., Okoshi R., Kamijo T., Omura K., Nakagawara A.
      J. Biol. Chem. 283:8555-8563(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF TP73, MUTAGENESIS OF LYS-82.
    45. "FAM29A promotes microtubule amplification via recruitment of the NEDD1-gamma-tubulin complex to the mitotic spindle."
      Zhu H., Coppinger J.A., Jang C.-Y., Yates J.R. III, Fang G.
      J. Cell Biol. 183:835-848(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FAM29A.
    46. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-6; SER-103; THR-210; THR-214; SER-375; SER-450 AND THR-498, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    47. "Plk1-dependent phosphorylation of FoxM1 regulates a transcriptional programme required for mitotic progression."
      Fu Z., Malureanu L., Huang J., Wang W., Li H., van Deursen J.M., Tindall D.J., Chen J.
      Nat. Cell Biol. 10:1076-1082(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF FOXM1, MUTAGENESIS OF LYS-82 AND THR-210.
    48. "Polo-like kinase-1 is activated by aurora A to promote checkpoint recovery."
      Macurek L., Lindqvist A., Lim D., Lampson M.A., Klompmaker R., Freire R., Clouin C., Taylor S.S., Yaffe M.B., Medema R.H.
      Nature 455:119-123(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT THR-210 BY AURKA, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-82; SER-137; ASP-176 AND THR-210.
    49. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-210 AND THR-214, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    50. "Mammalian BTBD12/SLX4 assembles a Holliday junction resolvase and is required for DNA repair."
      Svendsen J.M., Smogorzewska A., Sowa M.E., O'Connell B.C., Gygi S.P., Elledge S.J., Harper J.W.
      Cell 138:63-77(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SLX4.
    51. "Plk1-mediated phosphorylation of Topors regulates p53 stability."
      Yang X., Li H., Zhou Z., Wang W.H., Deng A., Andrisani O., Liu X.
      J. Biol. Chem. 284:18588-18592(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF TOPORS, INTERACTION WITH TOPORS.
    52. "Sequential phosphorylation of Nedd1 by Cdk1 and Plk1 is required for targeting of the gammaTuRC to the centrosome."
      Zhang X., Chen Q., Feng J., Hou J., Yang F., Liu J., Jiang Q., Zhang C.
      J. Cell Sci. 122:2240-2251(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS NEDD1 KINASE.
    53. "Plk1 and Aurora A regulate the depolymerase activity and the cellular localization of Kif2a."
      Jang C.Y., Coppinger J.A., Seki A., Yates J.R. III, Fang G.
      J. Cell Sci. 122:1334-1341(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH KIF2A, SUBCELLULAR LOCATION.
    54. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-210 AND THR-214, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    55. "Polo-like kinase 1 directs assembly of the HsCyk-4 RhoGAP/Ect2 RhoGEF complex to initiate cleavage furrow formation."
      Wolfe B.A., Takaki T., Petronczki M., Glotzer M.
      PLoS Biol. 7:E1000110-E1000110(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF RACGAP1, INTERACTION WITH PRC1, SUBCELLULAR LOCATION.
    56. "Plk1 self-organization and priming phosphorylation of HsCYK-4 at the spindle midzone regulate the onset of division in human cells."
      Burkard M.E., Maciejowski J., Rodriguez-Bravo V., Repka M., Lowery D.M., Clauser K.R., Zhang C., Shokat K.M., Carr S.A., Yaffe M.B., Jallepalli P.V.
      PLoS Biol. 7:E1000111-E1000111(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF RACGAP1, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-67; LEU-130; HIS-538 AND LYS-540.
    57. "Multifaceted polo-like kinases: drug targets and antitargets for cancer therapy."
      Strebhardt K.
      Nat. Rev. Drug Discov. 9:643-660(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION, REVIEW ON ENZYME REGULATION.
    58. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-210, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    59. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    60. "The astrin-kinastrin/SKAP complex localizes to microtubule plus ends and facilitates chromosome alignment."
      Dunsch A.K., Linnane E., Barr F.A., Gruneberg U.
      J. Cell Biol. 192:959-968(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH KNSTRN; SPAG5; DYNLL1 AND SGOL2.
    61. "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, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-194.
    62. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    63. "Dynactin helps target Polo-like kinase 1 to kinetochores via its left-handed beta-helical p27 subunit."
      Yeh T.Y., Kowalska A.K., Scipioni B.R., Cheong F.K., Zheng M., Derewenda U., Derewenda Z.S., Schroer T.A.
      EMBO J. 32:1023-1035(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DCTN6, SUBCELLULAR LOCATION.
    64. "MISP is a novel Plk1 substrate required for proper spindle orientation and mitotic progression."
      Zhu M., Settele F., Kotak S., Sanchez-Pulido L., Ehret L., Ponting C.P., Goenczy P., Hoffmann I.
      J. Cell Biol. 200:773-787(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF MISP.
    65. Cited for: FUNCTION, SUBCELLULAR LOCATION, UBIQUITINATION AT LYS-9 AND LYS-492, MUTAGENESIS OF LYS-492.
    66. "The molecular basis for phosphodependent substrate targeting and regulation of Plks by the Polo-box domain."
      Elia A.E., Rellos P., Haire L.F., Chao J.W., Ivins F.J., Hoepker K., Mohammad D., Cantley L.C., Smerdon S.J., Yaffe M.B.
      Cell 115:83-95(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 367-603 IN COMPLEX WITH PHOSPHORYLATED PEPTIDE, FUNCTION, SUBCELLULAR LOCATION, DOMAIN POLO BOX, INTERACTION WITH CDC25C, MUTAGENESIS OF HIS-538 AND LYS-540.
    67. "The crystal structure of the human polo-like kinase-1 polo box domain and its phospho-peptide complex."
      Cheng K.Y., Lowe E.D., Sinclair J., Nigg E.A., Johnson L.N.
      EMBO J. 22:5757-5768(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 367-603 IN COMPLEX WITH PHOSPHORYLATED PEPTIDE.
    68. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 13-345 OF MUTANT VAL-210 IN COMPLEXES WITH ATP ANALOGS, MUTAGENESIS OF THR-210.
    69. Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 37-330 IN COMPLEX WITH SYNTHETIC INHIBITOR BI 2536.
    70. "Molecular and structural basis of polo-like kinase 1 substrate recognition: Implications in centrosomal localization."
      Garcia-Alvarez B., de Carcer G., Ibanez S., Bragado-Nilsson E., Montoya G.
      Proc. Natl. Acad. Sci. U.S.A. 104:3107-3112(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 365-603 IN COMPLEX WITH CDC25C, SUBCELLULAR LOCATION, INTERACTION WITH CDC25C, ENZYME REGULATION, MUTAGENESIS OF TRP-414.
    71. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 33-345 IN COMPLEX WITH A DARPIN.
    72. Cited for: X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 371-603 IN COMPLEX WITH PHOSPHOPEPTIDE, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PHOSPHORYLATED CENPU.
    73. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-12; PHE-261; VAL-332; HIS-463 AND HIS-518.

    Entry informationi

    Entry nameiPLK1_HUMAN
    AccessioniPrimary (citable) accession number: P53350
    Secondary accession number(s): Q15153, Q99746
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 169 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3