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P53350

- PLK1_HUMAN

UniProt

P53350 - PLK1_HUMAN

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Protein
Serine/threonine-protein kinase PLK1
Gene
PLK1, PLK
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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. ATP binding Source: UniProtKB-KW
  2. anaphase-promoting complex binding Source: UniProtKB
  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
Complete GO annotation...

GO - Biological processi

  1. G2 DNA damage checkpoint Source: UniProtKB
  2. G2/M transition of mitotic cell cycle Source: UniProtKB
  3. activation of mitotic anaphase-promoting complex activity Source: UniProtKB
  4. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
  5. cell proliferation Source: ProtInc
  6. centrosome organization Source: UniProtKB
  7. cytokinesis Source: UniProtKB
  8. establishment of protein localization Source: MGI
  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
Complete GO annotation...

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.17 Publications

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
Complete GO annotation...

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 PLK1
PRO_0000086556Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei6 – 61Phosphothreonine1 Publication
Cross-linki19 – 19Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residuei103 – 1031Phosphoserine1 Publication
Modified residuei137 – 1371Phosphoserine Inferred
Modified residuei210 – 2101Phosphothreonine; by AURKA7 Publications
Modified residuei214 – 2141Phosphothreonine3 Publications
Modified residuei269 – 2691Phosphoserine; by autocatalysis By similarity
Modified residuei335 – 3351Phosphoserine1 Publication
Modified residuei375 – 3751Phosphoserine1 Publication
Modified residuei450 – 4501Phosphoserine1 Publication
Cross-linki492 – 492Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei498 – 4981Phosphothreonine1 Publication

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 STK10.5 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.3 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.2 Publications

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.23 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. 154 interactions.
DIPiDIP-29696N.
IntActiP53350. 108 interactions.
MINTiMINT-86316.
STRINGi9606.ENSP00000300093.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP53350.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini53 – 305253Protein kinase
Add
BLAST
Domaini417 – 48064POLO box 1
Add
BLAST
Domaini515 – 58470POLO box 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni194 – 22128Activation loop
Add
BLAST
Regioni493 – 50715Linker
Add
BLAST
Regioni538 – 5403Important for interaction with phosphorylated proteins By 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

Contains 2 POLO box domains.

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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21S → T in AAA56634. 1 Publication
Sequence conflicti11 – 111A → P in AAA56634. 1 Publication
Sequence conflicti58 – 581F → L in AAA56634. 1 Publication
Sequence conflicti60 – 601G → S in AAA56634. 1 Publication
Sequence conflicti73 – 731A → V in AAA36659. 1 Publication
Sequence conflicti73 – 731A → V in AAB36946. 1 Publication
Sequence conflicti123 – 1231N → T in CAA62260. 1 Publication
Sequence conflicti141 – 1411L → P in CAA53536. 1 Publication
Sequence conflicti227 – 2271G → E in CAA53536. 1 Publication
Sequence conflicti301 – 3011N → G in AAA36659. 1 Publication
Sequence conflicti495 – 4951A → G in AAA36659. 1 Publication
Sequence conflicti501 – 5011E → Q in AAA36659. 1 Publication

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...

Protein-protein interaction databases

BioGridi 111362. 154 interactions.
DIPi DIP-29696N.
IntActi P53350. 108 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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 168 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

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