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Protein

Serine/threonine-protein kinase PLK1

Gene

PLK1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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, SGO1, 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 SGO1: required for spindle pole localization of isoform 3 of SGO1 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 (PubMed:8991084, PubMed:11202906, PubMed:12207013, PubMed:12447691, PubMed:12524548, PubMed:12738781, PubMed:12852856, PubMed:12939256, PubMed:14532005, PubMed:14734534, PubMed:15070733, PubMed:15148369, PubMed:15469984, PubMed:16198290, PubMed:16247472, PubMed:16980960, PubMed:17081991, PubMed:17351640, PubMed:17376779, PubMed:17617734, PubMed:18174154, PubMed:18331714, PubMed:18418051, PubMed:18477460, PubMed:18521620, PubMed:18615013, PubMed:19160488, PubMed:19351716, PubMed:19468300, PubMed:19468302, PubMed:19473992, PubMed:19509060, PubMed:19597481, PubMed:23455478, PubMed:23509069). Together with MEIKIN, acts as a regulator of kinetochore function during meiosis I: required both for mono-orientation of kinetochores on sister chromosomes and protection of centromeric cohesin from separase-mediated cleavage (By similarity). Phosphorylates CEP68 and is required for its degradation (PubMed:25503564).By similarity36 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

  • anaphase-promoting complex binding Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • kinase activity Source: Reactome
  • microtubule binding Source: UniProtKB
  • protein kinase activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  • anaphase-promoting complex-dependent catabolic process Source: Reactome
  • cell proliferation Source: ProtInc
  • centrosome organization Source: UniProtKB
  • cytokinesis Source: UniProtKB
  • establishment of protein localization Source: MGI
  • female meiosis chromosome segregation Source: Ensembl
  • G2/M transition of mitotic cell cycle Source: UniProtKB
  • G2 DNA damage checkpoint Source: UniProtKB
  • homologous chromosome segregation Source: Ensembl
  • microtubule bundle formation Source: UniProtKB
  • mitotic cytokinesis Source: UniProtKB
  • mitotic nuclear division Source: UniProtKB
  • mitotic nuclear envelope disassembly Source: Reactome
  • mitotic sister chromatid segregation Source: UniProtKB
  • mitotic spindle assembly checkpoint Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of cyclin-dependent protein serine/threonine kinase activity Source: BHF-UCL
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • peptidyl-serine phosphorylation Source: UniProtKB
  • positive regulation of peptidyl-threonine phosphorylation Source: BHF-UCL
  • positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
  • positive regulation of protein localization to nucleus Source: Reactome
  • positive regulation of proteolysis Source: UniProtKB
  • positive regulation of ubiquitin protein ligase activity Source: UniProtKB
  • positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition Source: Reactome
  • positive regulation of ubiquitin-protein transferase activity Source: UniProtKB
  • protein destabilization Source: UniProtKB
  • protein localization to chromatin Source: UniProtKB
  • protein phosphorylation Source: UniProtKB
  • protein ubiquitination Source: UniProtKB
  • protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: Reactome
  • regulation of cell cycle Source: Reactome
  • regulation of cell cycle G2/M phase transition Source: Reactome
  • regulation of mitotic cell cycle Source: UniProtKB
  • regulation of mitotic metaphase/anaphase transition Source: BHF-UCL
  • regulation of mitotic spindle assembly Source: CACAO
  • regulation of protein binding Source: BHF-UCL
  • regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  • sister chromatid cohesion Source: Reactome
  • synaptonemal complex disassembly 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.
ReactomeiR-HSA-156711. Polo-like kinase mediated events.
R-HSA-162658. Golgi Cisternae Pericentriolar Stack Reorganization.
R-HSA-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-HSA-176412. Phosphorylation of the APC/C.
R-HSA-176417. Phosphorylation of Emi1.
R-HSA-2299718. Condensation of Prophase Chromosomes.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-2980767. Activation of NIMA Kinases NEK9, NEK6, NEK7.
R-HSA-380259. Loss of Nlp from mitotic centrosomes.
R-HSA-380270. Recruitment of mitotic centrosome proteins and complexes.
R-HSA-5620912. Anchoring of the basal body to the plasma membrane.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-68877. Mitotic Prometaphase.
R-HSA-68881. Mitotic Metaphase/Anaphase Transition.
R-HSA-68884. Mitotic Telophase/Cytokinesis.
R-HSA-69273. Cyclin A/B1 associated events during G2/M transition.
R-HSA-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-HSA-8854518. AURKA Activation by TPX2.
SignaLinkiP53350.
SIGNORiP53350.

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
Proteomesi
  • UP000005640 Componenti: 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 SGO1 and interaction with the phosphorylated form of BUB1 is required for the kinetochore localization. Localizes onto the central spindle by phosphorylating and docking at midzone proteins KIF20A/MKLP2 and PRC1. Colocalizes with FRY to separating centrosomes and spindle poles from prophase to metaphase in mitosis, but not in other stages of the cell cycle.

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • chromatin Source: Ensembl
  • condensed nuclear chromosome outer kinetochore Source: BHF-UCL
  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • kinetochore Source: UniProtKB
  • microtubule cytoskeleton Source: BHF-UCL
  • midbody Source: UniProtKB
  • nucleolus Source: HPA
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • spindle Source: UniProtKB
  • spindle midzone Source: UniProtKB
  • spindle pole Source: BHF-UCL
  • synaptonemal complex Source: Ensembl
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.

Chemistry

ChEMBLiCHEMBL3024.
GuidetoPHARMACOLOGYi2168.

Polymorphism and mutation databases

BioMutaiPLK1.
DMDMi1709658.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 603602Serine/threonine-protein kinase PLK1PRO_0000086556Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei6 – 61PhosphothreonineCombined sources
Cross-linki19 – 19Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei103 – 1031PhosphoserineCombined sources
Modified residuei137 – 1371Phosphoserine1 Publication
Modified residuei210 – 2101Phosphothreonine; by AURKACombined sources3 Publications
Modified residuei214 – 2141PhosphothreonineCombined sources
Modified residuei269 – 2691Phosphoserine; by autocatalysisBy similarity
Modified residuei335 – 3351Phosphoserine1 Publication
Modified residuei375 – 3751PhosphoserineCombined sources
Modified residuei450 – 4501PhosphoserineCombined sources
Cross-linki492 – 492Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei498 – 4981PhosphothreonineCombined sources

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.2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP53350.
MaxQBiP53350.
PaxDbiP53350.
PeptideAtlasiP53350.
PRIDEiP53350.

PTM databases

iPTMnetiP53350.
PhosphoSiteiP53350.

Expressioni

Tissue specificityi

Placenta and colon.

Developmental stagei

Accumulates to a maximum during the G2 and M phases, declines to a nearly undetectable level following mitosis and throughout G1 phase, and then begins to accumulate again during S phase.

Inductioni

By growth-stimulating agents.

Gene expression databases

BgeeiENSG00000166851.
CleanExiHS_PLK1.
ExpressionAtlasiP53350. baseline and differential.
GenevisibleiP53350. HS.

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 SGO1. 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 SGO2. 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. Interacts with CEP68; the interaction phosphorylates CEP68 (PubMed:25503564).27 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q99IB84EBI-476768,EBI-6927873From a different organism.
BIRC6Q9NR094EBI-476768,EBI-1765160
CHEK2O960176EBI-476768,EBI-1180783
Dvl2Q6083812EBI-476768,EBI-641940From a different organism.
EIF4BP235883EBI-476768,EBI-970310
ERCC6LQ2NKX83EBI-476768,EBI-1042535
EVI5O604473EBI-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
OFD1O756654EBI-476768,EBI-716327
PHC2Q8IXK02EBI-476768,EBI-713786
SLX4Q8IY927EBI-476768,EBI-2370740
TANKQ928443EBI-476768,EBI-356349
TP53P046376EBI-476768,EBI-366083

GO - Molecular functioni

  • anaphase-promoting complex binding Source: UniProtKB
  • microtubule binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111362. 229 interactions.
DIPiDIP-29696N.
IntActiP53350. 147 interactions.
MINTiMINT-86316.
STRINGi9606.ENSP00000300093.

Chemistry

BindingDBiP53350.

Structurei

Secondary structure

1
603
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi42 – 465Combined sources
Turni47 – 504Combined sources
Beta strandi51 – 6212Combined sources
Beta strandi65 – 728Combined sources
Turni73 – 753Combined sources
Beta strandi78 – 858Combined sources
Helixi86 – 883Combined sources
Helixi92 – 10615Combined sources
Beta strandi116 – 1216Combined sources
Beta strandi123 – 1319Combined sources
Helixi138 – 1458Combined sources
Helixi150 – 16920Combined sources
Helixi179 – 1813Combined sources
Beta strandi182 – 1843Combined sources
Beta strandi190 – 1923Combined sources
Helixi220 – 2234Combined sources
Beta strandi224 – 2263Combined sources
Helixi231 – 24616Combined sources
Helixi256 – 2649Combined sources
Helixi276 – 28510Combined sources
Helixi290 – 2923Combined sources
Helixi296 – 3016Combined sources
Helixi303 – 3064Combined sources
Helixi316 – 3194Combined sources
Helixi374 – 38613Combined sources
Helixi389 – 3913Combined sources
Beta strandi392 – 3943Combined sources
Helixi397 – 4004Combined sources
Helixi403 – 4053Combined sources
Beta strandi411 – 4177Combined sources
Turni418 – 4214Combined sources
Beta strandi422 – 4276Combined sources
Beta strandi432 – 4365Combined sources
Beta strandi441 – 4444Combined sources
Beta strandi448 – 4547Combined sources
Beta strandi460 – 4645Combined sources
Turni465 – 4673Combined sources
Helixi470 – 4723Combined sources
Helixi473 – 48816Combined sources
Turni493 – 4964Combined sources
Turni503 – 5053Combined sources
Beta strandi511 – 5166Combined sources
Beta strandi518 – 5258Combined sources
Turni526 – 5283Combined sources
Beta strandi530 – 5345Combined sources
Turni535 – 5373Combined sources
Beta strandi540 – 5445Combined sources
Turni545 – 5484Combined sources
Beta strandi549 – 5535Combined sources
Beta strandi559 – 5635Combined sources
Helixi564 – 5707Combined sources
Helixi574 – 59118Combined sources
Beta strandi593 – 5953Combined sources
Beta strandi598 – 6025Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4O56X-ray1.80A367-603[»]
4O6WX-ray1.45A371-603[»]
4O9WX-ray1.69A373-594[»]
4RCPX-ray1.60A372-599[»]
4WHHX-ray1.90A371-603[»]
4WHKX-ray1.80A371-603[»]
4WHLX-ray2.71A371-603[»]
4X9RX-ray1.40A371-603[»]
4X9VX-ray1.43A371-603[»]
4X9WX-ray1.80A371-603[»]
5J19X-ray2.00A/B367-594[»]
DisProtiDP00428.
ProteinModelPortaliP53350.
SMRiP53350. Positions 37-330, 371-592.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53350.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini53 – 305253Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini417 – 48064POLO box 1PROSITE-ProRule annotationAdd
BLAST
Domaini515 – 58470POLO box 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni194 – 22128Activation loopAdd
BLAST
Regioni493 – 50715LinkerAdd
BLAST
Regioni538 – 5403Important for interaction with phosphorylated proteinsBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi337 – 3404D-box that targets the protein for proteasomal degradation in anaphase

Domaini

The POLO box domains act as phosphopeptide-binding module that recognize and bind serine-[phosphothreonine/phosphoserine]-(proline/X) motifs. PLK1 recognizes and binds docking proteins that are already phosphorylated on these motifs, and then phosphorylates them. PLK1 can also create its own docking sites by mediating phosphorylation of serine-[phosphothreonine/phosphoserine]-(proline/X) motifs subsequently recognized by the POLO box domains.4 Publications

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC5/Polo subfamily.PROSITE-ProRule annotation
Contains 2 POLO box domains.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0575. Eukaryota.
ENOG410XQBP. LUCA.
GeneTreeiENSGT00530000062954.
HOGENOMiHOG000248546.
HOVERGENiHBG001843.
InParanoidiP53350.
KOiK06631.
OMAiKRYMTEH.
OrthoDBiEOG091G0D89.
PhylomeDBiP53350.
TreeFamiTF101089.

Family and domain databases

CDDicd13118. POLO_box_1. 1 hit.
cd13117. POLO_box_2. 1 hit.
cd14187. STKc_PLK1. 1 hit.
Gene3Di3.30.1120.30. 2 hits.
InterProiIPR011009. Kinase-like_dom.
IPR033702. PLK1_cat.
IPR033701. POLO_box_1.
IPR033695. POLO_box_2.
IPR000959. POLO_box_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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

« Hide

        10         20         30         40         50
MSAAVTAGKL ARAPADPGKA GVPGVAAPGA PAAAPPAKEI PEVLVDPRSR
60 70 80 90 100
RRYVRGRFLG KGGFAKCFEI SDADTKEVFA GKIVPKSLLL KPHQREKMSM
110 120 130 140 150
EISIHRSLAH QHVVGFHGFF EDNDFVFVVL ELCRRRSLLE LHKRRKALTE
160 170 180 190 200
PEARYYLRQI VLGCQYLHRN RVIHRDLKLG NLFLNEDLEV KIGDFGLATK
210 220 230 240 250
VEYDGERKKT LCGTPNYIAP EVLSKKGHSF EVDVWSIGCI MYTLLVGKPP
260 270 280 290 300
FETSCLKETY LRIKKNEYSI PKHINPVAAS LIQKMLQTDP TARPTINELL
310 320 330 340 350
NDEFFTSGYI PARLPITCLT IPPRFSIAPS SLDPSNRKPL TVLNKGLENP
360 370 380 390 400
LPERPREKEE PVVRETGEVV DCHLSDMLQQ LHSVNASKPS ERGLVRQEEA
410 420 430 440 450
EDPACIPIFW VSKWVDYSDK YGLGYQLCDN SVGVLFNDST RLILYNDGDS
460 470 480 490 500
LQYIERDGTE SYLTVSSHPN SLMKKITLLK YFRNYMSEHL LKAGANITPR
510 520 530 540 550
EGDELARLPY LRTWFRTRSA IILHLSNGSV QINFFQDHTK LILCPLMAAV
560 570 580 590 600
TYIDEKRDFR TYRLSLLEEY GCCKELASRL RYARTMVDKL LSSRSASNRL

KAS
Length:603
Mass (Da):68,255
Last modified:October 1, 1996 - v1
Checksum:i178C2F13C10E8206
GO

Experimental Info

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

Natural variant

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_005030.5.
UniGeneiHs.592049.

Genome annotation databases

EnsembliENST00000300093; ENSP00000300093; ENSG00000166851.
GeneIDi5347.
KEGGihsa:5347.
UCSCiuc002dlz.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_005030.5.
UniGeneiHs.592049.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4O56X-ray1.80A367-603[»]
4O6WX-ray1.45A371-603[»]
4O9WX-ray1.69A373-594[»]
4RCPX-ray1.60A372-599[»]
4WHHX-ray1.90A371-603[»]
4WHKX-ray1.80A371-603[»]
4WHLX-ray2.71A371-603[»]
4X9RX-ray1.40A371-603[»]
4X9VX-ray1.43A371-603[»]
4X9WX-ray1.80A371-603[»]
5J19X-ray2.00A/B367-594[»]
DisProtiDP00428.
ProteinModelPortaliP53350.
SMRiP53350. Positions 37-330, 371-592.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111362. 229 interactions.
DIPiDIP-29696N.
IntActiP53350. 147 interactions.
MINTiMINT-86316.
STRINGi9606.ENSP00000300093.

Chemistry

BindingDBiP53350.
ChEMBLiCHEMBL3024.
GuidetoPHARMACOLOGYi2168.

PTM databases

iPTMnetiP53350.
PhosphoSiteiP53350.

Polymorphism and mutation databases

BioMutaiPLK1.
DMDMi1709658.

Proteomic databases

EPDiP53350.
MaxQBiP53350.
PaxDbiP53350.
PeptideAtlasiP53350.
PRIDEiP53350.

Protocols and materials databases

DNASUi5347.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000300093; ENSP00000300093; ENSG00000166851.
GeneIDi5347.
KEGGihsa:5347.
UCSCiuc002dlz.2. human.

Organism-specific databases

CTDi5347.
GeneCardsiPLK1.
HGNCiHGNC:9077. PLK1.
HPAiHPA051638.
HPA053229.
MIMi602098. gene.
neXtProtiNX_P53350.
PharmGKBiPA33410.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0575. Eukaryota.
ENOG410XQBP. LUCA.
GeneTreeiENSGT00530000062954.
HOGENOMiHOG000248546.
HOVERGENiHBG001843.
InParanoidiP53350.
KOiK06631.
OMAiKRYMTEH.
OrthoDBiEOG091G0D89.
PhylomeDBiP53350.
TreeFamiTF101089.

Enzyme and pathway databases

BRENDAi2.7.11.21. 2681.
ReactomeiR-HSA-156711. Polo-like kinase mediated events.
R-HSA-162658. Golgi Cisternae Pericentriolar Stack Reorganization.
R-HSA-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-HSA-176412. Phosphorylation of the APC/C.
R-HSA-176417. Phosphorylation of Emi1.
R-HSA-2299718. Condensation of Prophase Chromosomes.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-2980767. Activation of NIMA Kinases NEK9, NEK6, NEK7.
R-HSA-380259. Loss of Nlp from mitotic centrosomes.
R-HSA-380270. Recruitment of mitotic centrosome proteins and complexes.
R-HSA-5620912. Anchoring of the basal body to the plasma membrane.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-68877. Mitotic Prometaphase.
R-HSA-68881. Mitotic Metaphase/Anaphase Transition.
R-HSA-68884. Mitotic Telophase/Cytokinesis.
R-HSA-69273. Cyclin A/B1 associated events during G2/M transition.
R-HSA-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-HSA-8854518. AURKA Activation by TPX2.
SignaLinkiP53350.
SIGNORiP53350.

Miscellaneous databases

ChiTaRSiPLK1. human.
EvolutionaryTraceiP53350.
GeneWikiiPLK1.
GenomeRNAii5347.
PROiP53350.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000166851.
CleanExiHS_PLK1.
ExpressionAtlasiP53350. baseline and differential.
GenevisibleiP53350. HS.

Family and domain databases

CDDicd13118. POLO_box_1. 1 hit.
cd13117. POLO_box_2. 1 hit.
cd14187. STKc_PLK1. 1 hit.
Gene3Di3.30.1120.30. 2 hits.
InterProiIPR011009. Kinase-like_dom.
IPR033702. PLK1_cat.
IPR033701. POLO_box_1.
IPR033695. POLO_box_2.
IPR000959. POLO_box_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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]
ProtoNetiSearch...

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 7, 2016
This is version 189 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.