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Protein

Serine/threonine-protein kinase PLK2

Gene

PLK2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Tumor suppressor serine/threonine-protein kinase involved in synaptic plasticity, centriole duplication and G1/S phase transition. Polo-like kinases act by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates CENPJ, NPM1, RAPGEF2, RASGRF1, SNCA, SIPA1L1 and SYNGAP1. Plays a key role in synaptic plasticity and memory by regulating the Ras and Rap protein signaling: required for overactivity-dependent spine remodeling by phosphorylating the Ras activator RASGRF1 and the Rap inhibitor SIPA1L1 leading to their degradation by the proteasome. Conversely, phosphorylates the Rap activator RAPGEF2 and the Ras inhibitor SYNGAP1, promoting their activity. Also regulates synaptic plasticity independently of kinase activity, via its interaction with NSF that disrupts the interaction between NSF and the GRIA2 subunit of AMPARs, leading to a rapid rundown of AMPAR-mediated current that occludes long term depression. Required for procentriole formation and centriole duplication by phosphorylating CENPJ and NPM1, respectively. Its induction by p53/TP53 suggests that it may participate in the mitotic checkpoint following stress.4 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Activated by phosphorylation of Thr-239. Once activated, activity is stimulated by binding target proteins (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei111ATPPROSITE-ProRule annotation1
Active sitei205Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi88 – 96ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent protein binding Source: ParkinsonsUK-UCL
  • protein serine/threonine kinase activity Source: UniProtKB
  • signal transducer activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS07267-MONOMER.
BRENDAi2.7.11.21. 2681.
ReactomeiR-HSA-6804115. TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
SignaLinkiQ9NYY3.
SIGNORiQ9NYY3.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase PLK2 (EC:2.7.11.21)
Alternative name(s):
Polo-like kinase 2
Short name:
PLK-2
Short name:
hPlk2
Serine/threonine-protein kinase SNK
Short name:
hSNK
Serum-inducible kinase
Gene namesi
Name:PLK2
Synonyms:SNK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:19699. PLK2.

Subcellular locationi

GO - Cellular componenti

  • centriole Source: UniProtKB
  • centrosome Source: UniProtKB
  • chromatin Source: Ensembl
  • cytoplasm Source: ParkinsonsUK-UCL
  • cytosol Source: Reactome
  • dendrite Source: UniProtKB
  • intracellular Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi210N → A: Loss of kinase activity. 1 Publication1
Mutagenesisi503W → F: Impairs localization to the centrosome and centriole duplication; when associated with A-629 and M-631. 1 Publication1
Mutagenesisi629H → A: Impairs localization to the centrosome and centriole duplication; when associated with F-503 and M-631. 1 Publication1
Mutagenesisi631K → M: Impairs localization to the centrosome and centriole duplication; when associated with F-503 and A-631. 1 Publication1

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

DisGeNETi10769.
OpenTargetsiENSG00000145632.
PharmGKBiPA134940798.

Chemistry databases

ChEMBLiCHEMBL5938.
GuidetoPHARMACOLOGYi2169.

Polymorphism and mutation databases

BioMutaiPLK2.
DMDMi22096374.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000865611 – 685Serine/threonine-protein kinase PLK2Add BLAST685

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei239PhosphothreonineBy similarity1

Post-translational modificationi

Catalytic activity is enhanced by phosphorylation of Thr-239.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9NYY3.
PaxDbiQ9NYY3.
PeptideAtlasiQ9NYY3.
PRIDEiQ9NYY3.

PTM databases

iPTMnetiQ9NYY3.
PhosphoSitePlusiQ9NYY3.

Expressioni

Tissue specificityi

Expressed at higher level in the fetal lung, kidney, spleen and heart.1 Publication

Inductioni

Directly regulated by p53/TP53. Negatively regulated by miR-126.2 Publications

Gene expression databases

BgeeiENSG00000145632.
CleanExiHS_PLK2.
ExpressionAtlasiQ9NYY3. baseline and differential.
GenevisibleiQ9NYY3. HS.

Organism-specific databases

HPAiCAB009624.

Interactioni

Subunit structurei

Interacts with NSF; causing NSF dissociation from GRIA2. Interacts with CIB1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC20BQ86Y333EBI-721354,EBI-10260504
CENPJQ9HC773EBI-721354,EBI-946194

GO - Molecular functioni

  • ATP-dependent protein binding Source: ParkinsonsUK-UCL

Protein-protein interaction databases

BioGridi115988. 47 interactors.
DIPiDIP-48943N.
IntActiQ9NYY3. 23 interactors.
MINTiMINT-1397390.
STRINGi9606.ENSP00000274289.

Chemistry databases

BindingDBiQ9NYY3.

Structurei

Secondary structure

1685
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi72 – 74Combined sources3
Turni76 – 78Combined sources3
Beta strandi81 – 91Combined sources11
Beta strandi94 – 101Combined sources8
Turni102 – 105Combined sources4
Beta strandi106 – 114Combined sources9
Helixi115 – 118Combined sources4
Helixi121 – 134Combined sources14
Beta strandi145 – 150Combined sources6
Beta strandi152 – 159Combined sources8
Helixi167 – 174Combined sources8
Helixi179 – 198Combined sources20
Helixi208 – 210Combined sources3
Beta strandi211 – 213Combined sources3
Beta strandi219 – 221Combined sources3
Helixi224 – 226Combined sources3
Turni233 – 235Combined sources3
Helixi249 – 252Combined sources4
Helixi259 – 275Combined sources17
Helixi286 – 288Combined sources3
Helixi289 – 293Combined sources5
Helixi305 – 314Combined sources10
Helixi319 – 321Combined sources3
Helixi325 – 329Combined sources5
Helixi332 – 335Combined sources4
Helixi345 – 348Combined sources4
Helixi471 – 485Combined sources15
Beta strandi490 – 492Combined sources3
Beta strandi504 – 510Combined sources7
Turni511 – 514Combined sources4
Beta strandi515 – 520Combined sources6
Beta strandi525 – 529Combined sources5
Beta strandi534 – 537Combined sources4
Beta strandi541 – 547Combined sources7
Beta strandi553 – 558Combined sources6
Helixi563 – 582Combined sources20
Beta strandi602 – 616Combined sources15
Beta strandi621 – 625Combined sources5
Turni626 – 628Combined sources3
Beta strandi631 – 646Combined sources16
Beta strandi652 – 656Combined sources5
Helixi657 – 663Combined sources7
Helixi667 – 680Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4I5MX-ray1.80A57-360[»]
4I5PX-ray1.74A57-360[»]
4I6BX-ray1.80A57-360[»]
4I6FX-ray2.90A57-360[»]
4I6HX-ray1.91A57-360[»]
4RS6X-ray2.60A/B451-685[»]
4XB0X-ray2.70A/B468-685[»]
ProteinModelPortaliQ9NYY3.
SMRiQ9NYY3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini82 – 334Protein kinasePROSITE-ProRule annotationAdd BLAST253
Domaini510 – 573POLO box 1PROSITE-ProRule annotationAdd BLAST64
Domaini606 – 677POLO box 2PROSITE-ProRule annotationAdd BLAST72

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi57 – 64Poly-His8

Domaini

The POLO box domains act as phosphopeptide-binding module that recognize and bind serine-[phosphothreonine/phosphoserine]-(proline/X) motifs. PLK2 recognizes and binds docking proteins that are already phosphorylated on these motifs, and then phosphorylates them (By similarity).By similarity

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.
InParanoidiQ9NYY3.
KOiK08861.
OMAiNGTHMSL.
OrthoDBiEOG091G0D89.
PhylomeDBiQ9NYY3.
TreeFamiTF101089.

Family and domain databases

CDDicd13118. POLO_box_1. 1 hit.
cd13117. POLO_box_2. 1 hit.
Gene3Di3.30.1120.30. 2 hits.
InterProiIPR011009. Kinase-like_dom.
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.

Q9NYY3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELLRTITYQ PAASTKMCEQ ALGKGCGADS KKKRPPQPPE ESQPPQSQAQ
60 70 80 90 100
VPPAAPHHHH HHSHSGPEIS RIIVDPTTGK RYCRGKVLGK GGFAKCYEMT
110 120 130 140 150
DLTNNKVYAA KIIPHSRVAK PHQREKIDKE IELHRILHHK HVVQFYHYFE
160 170 180 190 200
DKENIYILLE YCSRRSMAHI LKARKVLTEP EVRYYLRQIV SGLKYLHEQE
210 220 230 240 250
ILHRDLKLGN FFINEAMELK VGDFGLAARL EPLEHRRRTI CGTPNYLSPE
260 270 280 290 300
VLNKQGHGCE SDIWALGCVM YTMLLGRPPF ETTNLKETYR CIREARYTMP
310 320 330 340 350
SSLLAPAKHL IASMLSKNPE DRPSLDDIIR HDFFLQGFTP DRLSSSCCHT
360 370 380 390 400
VPDFHLSSPA KNFFKKAAAA LFGGKKDKAR YIDTHNRVSK EDEDIYKLRH
410 420 430 440 450
DLKKTSITQQ PSKHRTDEEL QPPTTTVARS GTPAVENKQQ IGDAIRMIVR
460 470 480 490 500
GTLGSCSSSS ECLEDSTMGS VADTVARVLR GCLENMPEAD CIPKEQLSTS
510 520 530 540 550
FQWVTKWVDY SNKYGFGYQL SDHTVGVLFN NGAHMSLLPD KKTVHYYAEL
560 570 580 590 600
GQCSVFPATD APEQFISQVT VLKYFSHYME ENLMDGGDLP SVTDIRRPRL
610 620 630 640 650
YLLQWLKSDK ALMMLFNDGT FQVNFYHDHT KIIICSQNEE YLLTYINEDR
660 670 680
ISTTFRLTTL LMSGCSSELK NRMEYALNML LQRCN
Length:685
Mass (Da):78,237
Last modified:August 2, 2002 - v3
Checksum:i6429F6EFD830B333
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti28A → G in AAC14573 (PubMed:11696980).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04102314S → T in an ovarian Endometrioid carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_04102492G → S in a lung adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_041025436E → K.1 PublicationCorresponds to variant rs55768901dbSNPEnsembl.1
Natural variantiVAR_041026487P → L.1 PublicationCorresponds to variant rs55645589dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF059617 mRNA. Translation: AAC14573.1.
AF223574 mRNA. Translation: AAF62897.1.
U85755 mRNA. Translation: AAD00575.1.
AC008814 Genomic DNA. No translation available.
BC013879 mRNA. Translation: AAH13879.1.
CCDSiCCDS3974.1.
RefSeqiNP_001239155.1. NM_001252226.1.
NP_006613.2. NM_006622.3.
UniGeneiHs.398157.

Genome annotation databases

EnsembliENST00000274289; ENSP00000274289; ENSG00000145632.
GeneIDi10769.
KEGGihsa:10769.
UCSCiuc003jrn.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF059617 mRNA. Translation: AAC14573.1.
AF223574 mRNA. Translation: AAF62897.1.
U85755 mRNA. Translation: AAD00575.1.
AC008814 Genomic DNA. No translation available.
BC013879 mRNA. Translation: AAH13879.1.
CCDSiCCDS3974.1.
RefSeqiNP_001239155.1. NM_001252226.1.
NP_006613.2. NM_006622.3.
UniGeneiHs.398157.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4I5MX-ray1.80A57-360[»]
4I5PX-ray1.74A57-360[»]
4I6BX-ray1.80A57-360[»]
4I6FX-ray2.90A57-360[»]
4I6HX-ray1.91A57-360[»]
4RS6X-ray2.60A/B451-685[»]
4XB0X-ray2.70A/B468-685[»]
ProteinModelPortaliQ9NYY3.
SMRiQ9NYY3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115988. 47 interactors.
DIPiDIP-48943N.
IntActiQ9NYY3. 23 interactors.
MINTiMINT-1397390.
STRINGi9606.ENSP00000274289.

Chemistry databases

BindingDBiQ9NYY3.
ChEMBLiCHEMBL5938.
GuidetoPHARMACOLOGYi2169.

PTM databases

iPTMnetiQ9NYY3.
PhosphoSitePlusiQ9NYY3.

Polymorphism and mutation databases

BioMutaiPLK2.
DMDMi22096374.

Proteomic databases

MaxQBiQ9NYY3.
PaxDbiQ9NYY3.
PeptideAtlasiQ9NYY3.
PRIDEiQ9NYY3.

Protocols and materials databases

DNASUi10769.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000274289; ENSP00000274289; ENSG00000145632.
GeneIDi10769.
KEGGihsa:10769.
UCSCiuc003jrn.4. human.

Organism-specific databases

CTDi10769.
DisGeNETi10769.
GeneCardsiPLK2.
HGNCiHGNC:19699. PLK2.
HPAiCAB009624.
MIMi607023. gene.
neXtProtiNX_Q9NYY3.
OpenTargetsiENSG00000145632.
PharmGKBiPA134940798.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0575. Eukaryota.
ENOG410XQBP. LUCA.
GeneTreeiENSGT00530000062954.
HOGENOMiHOG000248546.
HOVERGENiHBG001843.
InParanoidiQ9NYY3.
KOiK08861.
OMAiNGTHMSL.
OrthoDBiEOG091G0D89.
PhylomeDBiQ9NYY3.
TreeFamiTF101089.

Enzyme and pathway databases

BioCyciZFISH:HS07267-MONOMER.
BRENDAi2.7.11.21. 2681.
ReactomeiR-HSA-6804115. TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
SignaLinkiQ9NYY3.
SIGNORiQ9NYY3.

Miscellaneous databases

GeneWikiiPLK2.
GenomeRNAii10769.
PROiQ9NYY3.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000145632.
CleanExiHS_PLK2.
ExpressionAtlasiQ9NYY3. baseline and differential.
GenevisibleiQ9NYY3. HS.

Family and domain databases

CDDicd13118. POLO_box_1. 1 hit.
cd13117. POLO_box_2. 1 hit.
Gene3Di3.30.1120.30. 2 hits.
InterProiIPR011009. Kinase-like_dom.
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 nameiPLK2_HUMAN
AccessioniPrimary (citable) accession number: Q9NYY3
Secondary accession number(s): O60679, Q96CV7, Q9UE61
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: August 2, 2002
Last modified: November 2, 2016
This is version 158 of the entry and version 3 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

Miscellaneous

There are indications that PLK2 might act as a tumor suppressor: PLK2 is significantly down-regulated in a wide range of acute myeloid leukemias (AMLs) and B-cell lymphomas due to aberrant cytosine methylation in the CpG island located at the 5' of the PLK2 gene (PubMed:16160013, PubMed:21340720). Moreover, miR-126, a microRNA that negatively regulates PLK2 is up-regulated in AMLs, suggesting that PLK2 down-regulation by miR-126 could also contribute to leukemogenesis (PubMed:18832181).3 Publications

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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.