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P53350 (PLK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 164. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:PLK1
Synonyms:PLK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length603 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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, PLK1S1/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 PLK1S1/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 3of 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. Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.26 Ref.27 Ref.28 Ref.32 Ref.34 Ref.36 Ref.40 Ref.41 Ref.42 Ref.43 Ref.44 Ref.47 Ref.48 Ref.51 Ref.52 Ref.53 Ref.55 Ref.56 Ref.64 Ref.65 Ref.66 Ref.72

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

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. Ref.48 Ref.70

Subunit structure

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 3of 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. Ref.16 Ref.23 Ref.24 Ref.25 Ref.27 Ref.31 Ref.33 Ref.37 Ref.38 Ref.39 Ref.41 Ref.42 Ref.45 Ref.50 Ref.51 Ref.53 Ref.55 Ref.60 Ref.61 Ref.63 Ref.66 Ref.70 Ref.72

Subcellular location

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. Ref.8 Ref.11 Ref.16 Ref.17 Ref.25 Ref.32 Ref.43 Ref.48 Ref.53 Ref.55 Ref.56 Ref.61 Ref.63 Ref.65 Ref.66 Ref.70 Ref.72

Tissue specificity

Placenta and colon.

Developmental stage

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.

Induction

By growth-stimulating agents. Ref.48 Ref.70

Domain

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. Ref.16 Ref.18 Ref.36 Ref.66

Post-translational modification

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. Ref.10 Ref.12 Ref.14 Ref.43 Ref.48

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. Ref.18 Ref.38 Ref.65

Involvement in disease

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.

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC5/Polo subfamily.

Contains 2 POLO box domains.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCentromere
Chromosome
Cytoplasm
Cytoskeleton
Kinetochore
Nucleus
   Coding sequence diversityPolymorphism
   DomainRepeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2 DNA damage checkpoint

Inferred from direct assay Ref.38. Source: UniProtKB

G2/M transition of mitotic cell cycle

Inferred from direct assay Ref.47. Source: UniProtKB

activation of mitotic anaphase-promoting complex activity

Inferred from direct assay Ref.21. Source: UniProtKB

anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process

Traceable author statement. Source: Reactome

cell proliferation

Traceable author statement Ref.4. Source: ProtInc

centrosome organization

Inferred from mutant phenotype Ref.43Ref.8. Source: UniProtKB

cytokinesis

Inferred from direct assay Ref.36. Source: UniProtKB

metaphase/anaphase transition of mitotic cell cycle

Traceable author statement. Source: Reactome

microtubule bundle formation

Inferred from direct assay Ref.16. Source: UniProtKB

mitosis

Inferred from direct assay Ref.48. Source: UniProtKB

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic cytokinesis

Inferred from direct assay Ref.56. Source: UniProtKB

mitotic nuclear envelope disassembly

Traceable author statement. Source: Reactome

mitotic sister chromatid segregation

Inferred from mutant phenotype Ref.65. Source: UniProtKB

mitotic spindle assembly checkpoint

Inferred from mutant phenotype Ref.65. Source: UniProtKB

negative regulation of apoptotic process

Inferred from mutant phenotype Ref.44. Source: UniProtKB

negative regulation of cyclin-dependent protein serine/threonine kinase activity

Inferred from mutant phenotype PubMed 21041660. Source: BHF-UCL

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype Ref.44. Source: UniProtKB

peptidyl-serine phosphorylation

Inferred from direct assay PubMed 16885022. Source: UniProtKB

polar body extrusion after meiotic divisions

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-threonine phosphorylation

Inferred from mutant phenotype PubMed 21041660. Source: BHF-UCL

positive regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype Ref.51. Source: UniProtKB

positive regulation of proteolysis

Inferred from direct assay PubMed 16885022. Source: UniProtKB

positive regulation of ubiquitin-protein ligase activity

Inferred from mutant phenotype Ref.51. Source: UniProtKB

positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

protein destabilization

Inferred from direct assay PubMed 16885022. Source: UniProtKB

protein localization to chromatin

Inferred from direct assay PubMed 21111234. Source: UniProtKB

protein phosphorylation

Inferred from direct assay Ref.55. Source: UniProtKB

protein ubiquitination

Inferred from direct assay PubMed 16885022. Source: UniProtKB

regulation of cell cycle

Traceable author statement. Source: Reactome

regulation of mitotic cell cycle

Inferred from mutant phenotype Ref.37. Source: UniProtKB

regulation of mitotic metaphase/anaphase transition

Inferred from mutant phenotype PubMed 21041660. Source: BHF-UCL

regulation of protein binding

Inferred from mutant phenotype PubMed 21041660. Source: BHF-UCL

regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

response to antibiotic

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcentrosome

Inferred from direct assay Ref.17Ref.43Ref.48PubMed 21399614Ref.65Ref.8. Source: UniProtKB

condensed nuclear chromosome outer kinetochore

Inferred from direct assay PubMed 18195732. Source: BHF-UCL

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

kinetochore

Inferred from direct assay Ref.32Ref.43Ref.48Ref.65. Source: UniProtKB

midbody

Inferred from direct assay Ref.55. Source: UniProtKB

nucleolus

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.48. Source: UniProtKB

spindle

Inferred from direct assay Ref.16Ref.36. Source: UniProtKB

spindle microtubule

Inferred from direct assay PubMed 21041660. Source: BHF-UCL

spindle midzone

Inferred from direct assay Ref.56. Source: UniProtKB

spindle pole

Inferred from direct assay PubMed 21041660. Source: BHF-UCL

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

anaphase-promoting complex binding

Inferred from physical interaction Ref.38. Source: UniProtKB

kinase activity

Traceable author statement. Source: Reactome

microtubule binding

Inferred from direct assay Ref.16. Source: UniProtKB

protein kinase activity

Inferred from direct assay Ref.50. Source: UniProtKB

protein kinase binding

Inferred from physical interaction Ref.14Ref.48. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from direct assay Ref.17Ref.16Ref.21Ref.36Ref.44Ref.43Ref.47Ref.55Ref.56. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.62
Chain2 – 603602Serine/threonine-protein kinase PLK1
PRO_0000086556

Regions

Domain53 – 305253Protein kinase
Domain417 – 48064POLO box 1
Domain515 – 58470POLO box 2
Nucleotide binding59 – 679ATP
Nucleotide binding178 – 1814ATP
Region194 – 22128Activation loop
Region493 – 50715Linker
Region538 – 5403Important for interaction with phosphorylated proteins By similarity
Motif337 – 3404D-box that targets the protein for proteasomal degradation in anaphase

Sites

Active site1761Proton acceptor
Binding site821ATP
Binding site1311ATP; via carbonyl oxygen
Binding site1941ATP

Amino acid modifications

Modified residue21N-acetylserine Ref.62
Modified residue61Phosphothreonine Ref.46
Modified residue1031Phosphoserine Ref.46
Modified residue1371Phosphoserine Probable
Modified residue2101Phosphothreonine; by AURKA Ref.10 Ref.43 Ref.46 Ref.48 Ref.49 Ref.54 Ref.58
Modified residue2141Phosphothreonine Ref.46 Ref.49 Ref.54
Modified residue2691Phosphoserine; by autocatalysis By similarity
Modified residue3351Phosphoserine Ref.12
Modified residue3751Phosphoserine Ref.46
Modified residue4501Phosphoserine Ref.46
Modified residue4981Phosphothreonine Ref.46
Cross-link19Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link492Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.65

Natural variations

Natural variant121R → L in a lung squamous cell carcinoma sample; somatic mutation. Ref.73
VAR_041018
Natural variant2611L → F. Ref.73
Corresponds to variant rs35056440 [ dbSNP | Ensembl ].
VAR_041019
Natural variant2971N → D.
Corresponds to variant rs16972799 [ dbSNP | Ensembl ].
VAR_051659
Natural variant3321L → V. Ref.73
Corresponds to variant rs45489499 [ dbSNP | Ensembl ].
VAR_041020
Natural variant4631L → H. Ref.73
Corresponds to variant rs45569335 [ dbSNP | Ensembl ].
VAR_041021
Natural variant5181R → H. Ref.73
Corresponds to variant rs56027600 [ dbSNP | Ensembl ].
VAR_041022
Natural variant5951S → L.
Corresponds to variant rs34001032 [ dbSNP | Ensembl ].
VAR_051660
Natural variant5991R → H.
Corresponds to variant rs34954545 [ dbSNP | Ensembl ].
VAR_051661

Experimental info

Mutagenesis671C → V in analog-sensitive mutant; enlarged catalytic pocket to accommodate purine analogs; when associated with G-130. Ref.56
Mutagenesis821K → M or R: Kinase defective mutant, abolishes activity. Ref.10 Ref.11 Ref.44 Ref.47 Ref.48
Mutagenesis1301L → G in analog-sensitive mutant; enlarged catalytic pocket to accommodate purine analogs; when associated with V-67. Ref.56
Mutagenesis1371S → A: No change in activity. Increases activity and restores recovery after DNA damage checkpoint; when associated with D-210. Ref.10 Ref.48
Mutagenesis1371S → D: Increases activity. Results in a block in G1/S. Ref.10 Ref.48
Mutagenesis1761D → N: Abolishes kinase activity. Ref.48
Mutagenesis1941D → A: Does not interfere with FRY-binding. Ref.61
Mutagenesis2101T → A: Abolishes activity. Abolishes checkpoint recovery. Ref.10 Ref.11 Ref.47 Ref.48 Ref.68
Mutagenesis2101T → D: Increases activity and restores recovery after DNA damage checkpoint. Ref.10 Ref.11 Ref.47 Ref.48 Ref.68
Mutagenesis2101T → V: Reduced catalytic activity, but no effect on affinity for ATP. Ref.10 Ref.11 Ref.47 Ref.48 Ref.68
Mutagenesis3371R → A: Interferes with ubiquitination and subsequent proteasomal degradation in anaphase; when associated with A-340. Ref.18 Ref.38
Mutagenesis3401L → A: Interferes with ubiquitination and subsequent proteasomal degradation in anaphase; when associated with A-337. Ref.18 Ref.38
Mutagenesis4141W → F: Abolishes interaction with CDC25C and reduces centrosomal localization. Ref.70
Mutagenesis4921K → R: Severe mitotic defects leading to prometaphase delay. Increased localization at kinetochores leading to increased levels of phosphorylated BUBR1. Ref.65
Mutagenesis5381H → A in pincer mutant; loss of centrosomal location and decreased interaction with phosphorylated CDC25C and BUB1; when associated with M-540. Ref.25 Ref.43 Ref.56 Ref.66
Mutagenesis5401K → M in pincer mutant; loss of centrosomal location and decreased interaction with phosphorylated CDC25C and BUB1; when associated with A-538. Ref.25 Ref.43 Ref.56 Ref.66
Sequence conflict21S → T in AAA56634. Ref.1
Sequence conflict111A → P in AAA56634. Ref.1
Sequence conflict581F → L in AAA56634. Ref.1
Sequence conflict601G → S in AAA56634. Ref.1
Sequence conflict731A → V in AAA36659. Ref.2
Sequence conflict731A → V in AAB36946. Ref.7
Sequence conflict1231N → T in CAA62260. Ref.6
Sequence conflict1411L → P in CAA53536. Ref.4
Sequence conflict2271G → E in CAA53536. Ref.4
Sequence conflict3011N → G in AAA36659. Ref.2
Sequence conflict4951A → G in AAA36659. Ref.2
Sequence conflict5011E → Q in AAA36659. Ref.2

Secondary structure

........................................................................................ 603
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P53350 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 178C2F13C10E8206

FASTA60368,255
        10         20         30         40         50         60 
MSAAVTAGKL ARAPADPGKA GVPGVAAPGA PAAAPPAKEI PEVLVDPRSR RRYVRGRFLG 

        70         80         90        100        110        120 
KGGFAKCFEI SDADTKEVFA GKIVPKSLLL KPHQREKMSM EISIHRSLAH QHVVGFHGFF 

       130        140        150        160        170        180 
EDNDFVFVVL ELCRRRSLLE LHKRRKALTE PEARYYLRQI VLGCQYLHRN RVIHRDLKLG 

       190        200        210        220        230        240 
NLFLNEDLEV KIGDFGLATK VEYDGERKKT LCGTPNYIAP EVLSKKGHSF EVDVWSIGCI 

       250        260        270        280        290        300 
MYTLLVGKPP FETSCLKETY LRIKKNEYSI PKHINPVAAS LIQKMLQTDP TARPTINELL 

       310        320        330        340        350        360 
NDEFFTSGYI PARLPITCLT IPPRFSIAPS SLDPSNRKPL TVLNKGLENP LPERPREKEE 

       370        380        390        400        410        420 
PVVRETGEVV DCHLSDMLQQ LHSVNASKPS ERGLVRQEEA EDPACIPIFW VSKWVDYSDK 

       430        440        450        460        470        480 
YGLGYQLCDN SVGVLFNDST RLILYNDGDS LQYIERDGTE SYLTVSSHPN SLMKKITLLK 

       490        500        510        520        530        540 
YFRNYMSEHL LKAGANITPR EGDELARLPY LRTWFRTRSA IILHLSNGSV QINFFQDHTK 

       550        560        570        580        590        600 
LILCPLMAAV TYIDEKRDFR TYRLSLLEEY GCCKELASRL RYARTMVDKL LSSRSASNRL 


KAS 

« Hide

References

« Hide 'large scale' references
[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 PLK1S1.
[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]"A cell proliferation and chromosomal instability signature in anaplastic thyroid carcinoma."
Salvatore G., Nappi T.C., Salerno P., Jiang Y., Garbi C., Ugolini C., Miccoli P., Basolo F., Castellone M.D., Cirafici A.M., Melillo R.M., Fusco A., Bittner M.L., Santoro M.
Cancer Res. 67:10148-10158(2007) [PubMed] [Europe PMC] [Abstract]
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]"The tumor suppressor CYLD regulates entry into mitosis."
Stegmeier F., Sowa M.E., Nalepa G., Gygi S.P., Harper J.W., Elledge S.J.
Proc. Natl. Acad. Sci. U.S.A. 104:8869-8874(2007) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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]"Ubiquitylation-dependent localization of PLK1 in mitosis."
Beck J., Maerki S., Posch M., Metzger T., Persaud A., Scheel H., Hofmann K., Rotin D., Pedrioli P., Swedlow J.R., Peter M., Sumara I.
Nat. Cell Biol. 15:430-439(2013) [PubMed] [Europe PMC] [Abstract]
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]"Structure of the catalytic domain of human polo-like kinase 1."
Kothe M., Kohls D., Low S., Coli R., Cheng A.C., Jacques S.L., Johnson T.L., Lewis C., Loh C., Nonomiya J., Sheils A.L., Verdries K.A., Wynn T.A., Kuhn C., Ding Y.H.
Biochemistry 46:5960-5971(2007) [PubMed] [Europe PMC] [Abstract]
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]"Selectivity-determining residues in Plk1."
Kothe M., Kohls D., Low S., Coli R., Rennie G.R., Feru F., Kuhn C., Ding Y.H.
Chem. Biol. Drug Des. 70:540-546(2007) [PubMed] [Europe PMC] [Abstract]
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]"Structure of wild-type Plk-1 kinase domain in complex with a selective DARPin."
Bandeiras T.M., Hillig R.C., Matias P.M., Eberspaecher U., Fanghanel J., Thomaz M., Miranda S., Crusius K., Putter V., Amstutz P., Gulotti-Georgieva M., Binz H.K., Holz C., Schmitz A.A., Lang C., Donner P., Egner U., Carrondo M.A., Muller-Tiemann B.
Acta Crystallogr. D 64:339-353(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 33-345 IN COMPLEX WITH A DARPIN.
[72]"Structural and functional analyses of minimal phosphopeptides targeting the polo-box domain of polo-like kinase 1."
Yun S.M., Moulaei T., Lim D., Bang J.K., Park J.E., Shenoy S.R., Liu F., Kang Y.H., Liao C., Soung N.K., Lee S., Yoon D.Y., Lim Y., Lee D.H., Otaka A., Appella E., McMahon J.B., Nicklaus M.C. expand/collapse author list , Burke T.R. Jr., Yaffe M.B., Wlodawer A., Lee K.S.
Nat. Struct. Mol. Biol. 16:876-882(2009) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS34130.
RefSeqNP_005021.2. NM_005030.3.
UniGeneHs.592049.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
DisProtDP00428.
ProteinModelPortalP53350.
SMRP53350. Positions 37-330, 371-592.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111362. 153 interactions.
DIPDIP-29696N.
IntActP53350. 108 interactions.
MINTMINT-86316.
STRING9606.ENSP00000300093.

Chemistry

BindingDBP53350.
ChEMBLCHEMBL3024.
GuidetoPHARMACOLOGY2168.

PTM databases

PhosphoSiteP53350.

Polymorphism databases

DMDM1709658.

Proteomic databases

PaxDbP53350.
PRIDEP53350.

Protocols and materials databases

DNASU5347.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000300093; ENSP00000300093; ENSG00000166851.
GeneID5347.
KEGGhsa:5347.
UCSCuc002dlz.1. human.

Organism-specific databases

CTD5347.
GeneCardsGC16P023712.
HGNCHGNC:9077. PLK1.
HPAHPA051638.
HPA053229.
MIM602098. gene.
neXtProtNX_P53350.
PharmGKBPA33410.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000248546.
HOVERGENHBG001843.
InParanoidP53350.
KOK06631.
OMALCKKGHS.
OrthoDBEOG78M01K.
PhylomeDBP53350.
TreeFamTF101089.

Enzyme and pathway databases

BRENDA2.7.11.21. 2681.
ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
SignaLinkP53350.

Gene expression databases

ArrayExpressP53350.
BgeeP53350.
CleanExHS_PLK1.
GenevestigatorP53350.

Family and domain databases

InterProIPR011009. 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]
PfamPF00069. Pkinase. 1 hit.
PF00659. POLO_box. 2 hits.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50078. POLO_BOX. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPLK1. human.
EvolutionaryTraceP53350.
GeneWikiPLK1.
GenomeRNAi5347.
NextBio20722.
PROP53350.
SOURCESearch...

Entry information

Entry namePLK1_HUMAN
AccessionPrimary (citable) accession number: P53350
Secondary accession number(s): Q15153, Q99746
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 164 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM