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Protein

Serine/threonine-protein kinase PLK2

Gene

PLK2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

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

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Activity 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

GO - Biological processi

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

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

EuPathDBiHostDB:ENSG00000145632.14
HGNCiHGNC:19699 PLK2
MIMi607023 gene
neXtProtiNX_Q9NYY3

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

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
ProteomicsDBi83299

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 Expressed in 226 organ(s), highest expression level in frontal cortex
CleanExiHS_PLK2
ExpressionAtlasiQ9NYY3 baseline and differential
GenevisibleiQ9NYY3 HS

Organism-specific databases

HPAiCAB009624
HPA069329

Interactioni

Subunit structurei

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

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi115988, 51 interactors
DIPiDIP-48943N
IntActiQ9NYY3, 28 interactors
MINTiQ9NYY3
STRINGi9606.ENSP00000274289

Chemistry databases

BindingDBiQ9NYY3

Structurei

Secondary structure

1685
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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
InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
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.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A087WUH9A0A087WUH9_HUMAN
Serine/threonine-protein kinase PLK
PLK2
671Annotation score:

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 → K1 PublicationCorresponds to variant dbSNP:rs55768901Ensembl.1
Natural variantiVAR_041026487P → L1 PublicationCorresponds to variant dbSNP:rs55645589Ensembl.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

Similar proteinsi

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, 51 interactors
DIPiDIP-48943N
IntActiQ9NYY3, 28 interactors
MINTiQ9NYY3
STRINGi9606.ENSP00000274289

Chemistry databases

BindingDBiQ9NYY3
ChEMBLiCHEMBL5938
GuidetoPHARMACOLOGYi2169

PTM databases

iPTMnetiQ9NYY3
PhosphoSitePlusiQ9NYY3

Polymorphism and mutation databases

BioMutaiPLK2
DMDMi22096374

Proteomic databases

MaxQBiQ9NYY3
PaxDbiQ9NYY3
PeptideAtlasiQ9NYY3
PRIDEiQ9NYY3
ProteomicsDBi83299

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
EuPathDBiHostDB:ENSG00000145632.14
GeneCardsiPLK2
HGNCiHGNC:19699 PLK2
HPAiCAB009624
HPA069329
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

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
PROiPR:Q9NYY3
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000145632 Expressed in 226 organ(s), highest expression level in frontal cortex
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
InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
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 nameiPLK2_HUMAN
AccessioniPrimary (citable) accession number: Q9NYY3
Secondary accession number(s): O60679, Q96CV7, Q9UE61
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: August 2, 2002
Last modified: November 7, 2018
This is version 170 of the entry and version 3 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 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 chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  7. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
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