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Protein

Serine/threonine-protein kinase PLK1

Gene

PLK1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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, WEE1 and HNRNPU. 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). Regulates nuclear envelope breakdown during prophase by phosphorylating DCTN1 resulting in its localization in the nuclear envelope (PubMed:20679239). Phosphorylates the heat shock transcription factor HSF1, promoting HSF1 nuclear translocation upon heat shock (PubMed:15661742). Phosphorylates HSF1 also in the early mitotic period; this phosphorylation regulates HSF1 localization to the spindle pole, the recruitment of the SCF(BTRC) ubiquitin ligase complex induicing HSF1 degradation, and hence mitotic progression (PubMed:18794143). Regulates mitotic progression by phosphorylating RIOK2 (PubMed:21880710).By similarity41 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.3 Publications

Activity 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)DescriptionActionsGraphical viewLength
Binding sitei82ATP1
Binding sitei131ATP; via carbonyl oxygen1
Active sitei176Proton acceptor1 Publication1
Binding sitei194ATP1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi59 – 67ATP9
Nucleotide bindingi178 – 181ATP4

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processCell cycle, Cell division, Mitosis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.21 2681
ReactomeiR-HSA-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
R-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-380284 Loss of proteins required for interphase microtubule organization from the centrosome
R-HSA-380320 Recruitment of NuMA to mitotic centrosomes
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/B2 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

Protein family/group databases

MoonDBiP53350 Curated

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase PLK1 (EC:2.7.11.213 Publications)
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

EuPathDBiHostDB:ENSG00000166851.14
HGNCiHGNC:9077 PLK1
MIMi602098 gene
neXtProtiNX_P53350

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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)DescriptionActionsGraphical viewLength
Mutagenesisi67C → V in analog-sensitive mutant; enlarged catalytic pocket to accommodate purine analogs; when associated with G-130. 1 Publication1
Mutagenesisi82K → M: Loss of kinase activity. No effect on S-phase progression. 4 Publications1
Mutagenesisi82K → R: Loss of kinase activity. No effect on RIOK2-binding. 3 Publications1
Mutagenesisi130L → G in analog-sensitive mutant; enlarged catalytic pocket to accommodate purine analogs; when associated with V-67. 1 Publication1
Mutagenesisi137S → A: No change in activity. Increases activity and restores recovery after DNA damage checkpoint; when associated with D-210. 2 Publications1
Mutagenesisi137S → D: Increases activity. Results in a block in G1/S. 2 Publications1
Mutagenesisi176D → N: Abolishes kinase activity. 1 Publication1
Mutagenesisi194D → A: Does not interfere with FRY-binding. 1 Publication1
Mutagenesisi210T → A: Abolishes activity. Abolishes checkpoint recovery. 5 Publications1
Mutagenesisi210T → D: Increases activity and restores recovery after DNA damage checkpoint. 5 Publications1
Mutagenesisi210T → V: Reduced catalytic activity, but no effect on affinity for ATP. 5 Publications1
Mutagenesisi337R → A: Interferes with ubiquitination and subsequent proteasomal degradation in anaphase; when associated with A-340. 2 Publications1
Mutagenesisi340L → A: Interferes with ubiquitination and subsequent proteasomal degradation in anaphase; when associated with A-337. 2 Publications1
Mutagenesisi414W → F: Abolishes interaction with CDC25C and reduces centrosomal localization. 1 Publication1
Mutagenesisi414W → F: No effect on centrosomal localization, nor on S-phase progression; when asscociated with A-427. Loss of centrosomal localization and of S-phase progression; when associated with A- 415 and A-427. 1 Publication1
Mutagenesisi415V → A: Loss of centrosomal localization and of S-phase progression; when associated with A- 414 and A-427. 1 Publication1
Mutagenesisi427L → A: No effect on centrosomal localization, nor on S-phase progression; when associated with A-414. Loss of centrosomal localization and of S-phase progression; when associated with A- 414 and A-415. 1 Publication1
Mutagenesisi492K → R: Severe mitotic defects leading to prometaphase delay. Increased localization at kinetochores leading to increased levels of phosphorylated BUBR1. 1 Publication1
Mutagenesisi538H → A in pincer mutant; loss of centrosomal location and decreased interaction with phosphorylated CDC25C and BUB1; when associated with M-540. 4 Publications1
Mutagenesisi540K → M in pincer mutant; loss of centrosomal location and decreased interaction with phosphorylated CDC25C and BUB1; when associated with A-538. 4 Publications1

Organism-specific databases

DisGeNETi5347
OpenTargetsiENSG00000166851
PharmGKBiPA33410

Chemistry databases

ChEMBLiCHEMBL3024
GuidetoPHARMACOLOGYi2168

Polymorphism and mutation databases

BioMutaiPLK1
DMDMi1709658

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000865562 – 603Serine/threonine-protein kinase PLK1Add BLAST602

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei6PhosphothreonineCombined sources1
Cross-linki19Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei103PhosphoserineCombined sources1
Modified residuei137Phosphoserine1 Publication1
Modified residuei210Phosphothreonine; by AURKACombined sources3 Publications1
Modified residuei214PhosphothreonineCombined sources1
Modified residuei269Phosphoserine; by autocatalysisBy similarity1
Modified residuei335Phosphoserine1 Publication1
Cross-linki338Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei375PhosphoserineCombined sources1
Modified residuei450PhosphoserineCombined sources1
Cross-linki492Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei498PhosphothreonineCombined sources1

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
ProteomicsDBi56569

PTM databases

iPTMnetiP53350
PhosphoSitePlusiP53350

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 Expressed in 110 organ(s), highest expression level in testis
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). Interacts (via POLO-box domain) with DCTN1 (PubMed:20679239). Interacts with FOPNL in later G1, S, G2 and M phases of the cell cycle; this interaction recruits PLK1 to centrosomes, a step required for S phase progression (PubMed:24018379). Interacts with HSF1; this interaction increases upon heat shock but does not modulate neither HSF1 homotrimerization nor DNA-binding activities (PubMed:15661742, PubMed:18794143). Interacts with HNRNPU; this interaction induces phosphorylation of HNRNPU in mitosis (PubMed:25986610). Interacts (via its N-terminus) to RIOK2 (PubMed:21880710). Interacts with KLHL22 (PubMed:24067371, PubMed:23455478).35 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi111362, 261 interactors
DIPiDIP-29696N
ELMiP53350
IntActiP53350, 185 interactors
MINTiP53350
STRINGi9606.ENSP00000300093

Chemistry databases

BindingDBiP53350

Structurei

Secondary structure

1603
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

DisProtiDP00428
ProteinModelPortaliP53350
SMRiP53350
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53350

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini53 – 305Protein kinasePROSITE-ProRule annotationAdd BLAST253
Domaini417 – 480POLO box 1PROSITE-ProRule annotationAdd BLAST64
Domaini515 – 584POLO box 2PROSITE-ProRule annotationAdd BLAST70

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni194 – 221Activation loopAdd BLAST28
Regioni493 – 507LinkerAdd BLAST15
Regioni538 – 540Important for interaction with phosphorylated proteinsBy similarity3

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi337 – 340D-box that targets the protein for proteasomal degradation in anaphase4

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0575 Eukaryota
ENOG410XQBP LUCA
GeneTreeiENSGT00530000062954
HOGENOMiHOG000248546
HOVERGENiHBG001843
InParanoidiP53350
KOiK06631
OMAiFEVDTWS
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
InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR033702 PLK1_cat
IPR033701 POLO_box_1
IPR033695 POLO_box_2
IPR000959 POLO_box_dom
IPR036947 POLO_box_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF00069 Pkinase, 1 hit
PF00659 POLO_box, 2 hits
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS50078 POLO_BOX, 2 hits
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
I3L387I3L387_HUMAN
Serine/threonine-protein kinase PLK...
PLK1
173Annotation score:
I3L2H5I3L2H5_HUMAN
Serine/threonine-protein kinase PLK...
PLK1
105Annotation score:
I3L309I3L309_HUMAN
Serine/threonine-protein kinase PLK...
PLK1
58Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti2S → T in AAA56634 (PubMed:8018557).Curated1
Sequence conflicti11A → P in AAA56634 (PubMed:8018557).Curated1
Sequence conflicti58F → L in AAA56634 (PubMed:8018557).Curated1
Sequence conflicti60G → S in AAA56634 (PubMed:8018557).Curated1
Sequence conflicti73A → V in AAA36659 (PubMed:7902533).Curated1
Sequence conflicti73A → V in AAB36946 (PubMed:9083047).Curated1
Sequence conflicti123N → T in CAA62260 (PubMed:7478607).Curated1
Sequence conflicti141L → P in CAA53536 (PubMed:8127874).Curated1
Sequence conflicti227G → E in CAA53536 (PubMed:8127874).Curated1
Sequence conflicti301N → G in AAA36659 (PubMed:7902533).Curated1
Sequence conflicti495A → G in AAA36659 (PubMed:7902533).Curated1
Sequence conflicti501E → Q in AAA36659 (PubMed:7902533).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04101812R → L in a lung squamous cell carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_041019261L → F1 PublicationCorresponds to variant dbSNP:rs35056440Ensembl.1
Natural variantiVAR_051659297N → D. Corresponds to variant dbSNP:rs16972799Ensembl.1
Natural variantiVAR_041020332L → V1 PublicationCorresponds to variant dbSNP:rs45489499Ensembl.1
Natural variantiVAR_041021463L → H1 PublicationCorresponds to variant dbSNP:rs45569335Ensembl.1
Natural variantiVAR_041022518R → H1 PublicationCorresponds to variant dbSNP:rs56027600Ensembl.1
Natural variantiVAR_051660595S → L. Corresponds to variant dbSNP:rs34001032Ensembl.1
Natural variantiVAR_051661599R → H. Corresponds to variant dbSNP:rs34954545Ensembl.1

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

Similar proteinsi

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
PDB 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[»]
5NEIX-ray2.68A371-603[»]
5NFUX-ray1.81A371-602[»]
5NJEX-ray1.98A371-603[»]
5NMMX-ray2.02A371-603[»]
5NN1X-ray1.78A371-603[»]
5NN2X-ray1.81A371-594[»]
5TA6X-ray2.50A13-345[»]
5TA8X-ray2.60A13-345[»]
6AX4X-ray1.45A371-603[»]
DisProtiDP00428
ProteinModelPortaliP53350
SMRiP53350
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111362, 261 interactors
DIPiDIP-29696N
ELMiP53350
IntActiP53350, 185 interactors
MINTiP53350
STRINGi9606.ENSP00000300093

Chemistry databases

BindingDBiP53350
ChEMBLiCHEMBL3024
GuidetoPHARMACOLOGYi2168

Protein family/group databases

MoonDBiP53350 Curated

PTM databases

iPTMnetiP53350
PhosphoSitePlusiP53350

Polymorphism and mutation databases

BioMutaiPLK1
DMDMi1709658

Proteomic databases

EPDiP53350
MaxQBiP53350
PaxDbiP53350
PeptideAtlasiP53350
PRIDEiP53350
ProteomicsDBi56569

Protocols and materials databases

DNASUi5347
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5347
DisGeNETi5347
EuPathDBiHostDB:ENSG00000166851.14
GeneCardsiPLK1
HGNCiHGNC:9077 PLK1
HPAiHPA051638
HPA053229
MIMi602098 gene
neXtProtiNX_P53350
OpenTargetsiENSG00000166851
PharmGKBiPA33410
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BRENDAi2.7.11.21 2681
ReactomeiR-HSA-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
R-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-380284 Loss of proteins required for interphase microtubule organization from the centrosome
R-HSA-380320 Recruitment of NuMA to mitotic centrosomes
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/B2 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
PROiPR:P53350
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000166851 Expressed in 110 organ(s), highest expression level in testis
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
InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR033702 PLK1_cat
IPR033701 POLO_box_1
IPR033695 POLO_box_2
IPR000959 POLO_box_dom
IPR036947 POLO_box_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF00069 Pkinase, 1 hit
PF00659 POLO_box, 2 hits
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS50078 POLO_BOX, 2 hits
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiPLK1_HUMAN
AccessioniPrimary (citable) accession number: P53350
Secondary accession number(s): Q15153, Q99746
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 7, 2018
This is version 212 of the entry and version 1 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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