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Protein

Serine/threonine-protein kinase PLK2

Gene

Plk2

Organism
Mus musculus (Mouse)
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

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Activated by phosphorylation of Thr-236. Once activated, activity is stimulated by binding target proteins (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei108ATPCurated1
Active sitei202Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi85 – 93ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

  • G1/S transition of mitotic cell cycle Source: UniProtKB
  • long term synaptic depression Source: UniProtKB
  • long-term synaptic potentiation Source: UniProtKB
  • memory Source: UniProtKB
  • mitotic cell cycle Source: MGI
  • mitotic cell cycle checkpoint Source: UniProtKB
  • mitotic spindle organization Source: UniProtKB
  • negative regulation of angiogenesis Source: BHF-UCL
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of apoptotic process in bone marrow Source: BHF-UCL
  • negative regulation of cellular senescence Source: BHF-UCL
  • negative regulation of dendritic spine development Source: Ensembl
  • peptidyl-serine phosphorylation Source: MGI
  • positive regulation of autophagy Source: MGI
  • positive regulation of cell migration involved in sprouting angiogenesis Source: BHF-UCL
  • positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: Ensembl
  • positive regulation of protein binding Source: Ensembl
  • positive regulation of protein catabolic process Source: MGI
  • protein phosphorylation Source: UniProtKB
  • Rap protein signal transduction Source: UniProtKB
  • Ras protein signal transduction Source: UniProtKB
  • regulation of centriole replication Source: UniProtKB
  • regulation of synaptic plasticity Source: UniProtKB

Keywordsi

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

Enzyme and pathway databases

BRENDAi2.7.11.21 3474
ReactomeiR-MMU-6804115 TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain

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
Serine/threonine-protein kinase SNK
Serum-inducible kinase
Gene namesi
Name:Plk2
Synonyms:Snk
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:1099790 Plk2

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

Disruption phenotypei

Embryos display a delay in skeletal development and retarded growth. Embryonic fibroblasts proliferated slowly and displayed a delayed entry into S phase. Mice display loss of dendritic spines and impaired memory formation.2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi108K → M in DN mutant; Loss of kinase activity; leading to disrupted Ras and Rap protein signaling, altered spine morphology and aberrant memory formation in mice. 2 Publications1
Mutagenesisi236T → D or V: Does not significantely affect kinase activity. 2 Publications1
Mutagenesisi236T → E: Mimicks phosphorylation state, leading to increased activity. 2 Publications1

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000865621 – 682Serine/threonine-protein kinase PLK2Add BLAST682

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei236Phosphothreonine1 Publication1

Post-translational modificationi

Catalytic activity is enhanced by phosphorylation of Thr-236.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP53351
PRIDEiP53351

PTM databases

iPTMnetiP53351
PhosphoSitePlusiP53351

Expressioni

Tissue specificityi

Brain, lung and heart.1 Publication

Developmental stagei

Expressed in early G1, during G0-G1 transition as well as in cycling cells.1 Publication

Inductioni

Directly regulated by p53/TP53. Induced by serum and phorbol ester.2 Publications

Gene expression databases

BgeeiENSMUSG00000021701
CleanExiMM_PLK2
ExpressionAtlasiP53351 baseline and differential
GenevisibleiP53351 MM

Interactioni

Subunit structurei

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi203368, 10 interactors
IntActiP53351, 9 interactors
STRINGi10090.ENSMUSP00000022212

Structurei

3D structure databases

ProteinModelPortaliP53351
SMRiP53351
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini79 – 331Protein kinasePROSITE-ProRule annotationAdd BLAST253
Domaini507 – 570POLO box 1PROSITE-ProRule annotationAdd BLAST64
Domaini603 – 674POLO box 2PROSITE-ProRule annotationAdd BLAST72

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi54 – 59Poly-His6

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
InParanoidiP53351
KOiK08861
OMAiNGTHMSL
OrthoDBiEOG091G0D89
PhylomeDBiP53351
TreeFamiTF101089

Family and domain databases

CDDicd13118 POLO_box_1, 1 hit
cd13117 POLO_box_2, 1 hit
Gene3Di3.30.1120.30, 3 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

Sequencei

Sequence statusi: Complete.

P53351-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELLRTITYQ PAAGTKMCEQ ALGKACGGDS KKKRPQQPSE DGQPQAQVTP
60 70 80 90 100
AAPHHHHHHS HSGPEISRII VDPTTGKRYC RGKVLGKGGF AKCYEMTDLT
110 120 130 140 150
NNKVYAAKII PHSRVAKPHQ REKIDKEIEL HRLLHHKHVV QFYHYFEDKE
160 170 180 190 200
NIYILLEYCS RRSMAHILKA RKVLTEPEVR YYLRQIVSGL KYLHEQEILH
210 220 230 240 250
RDLKLGNFFI NEAMELKVGD FGLAARLEPL EHRRRTICGT PNYLSPEVLN
260 270 280 290 300
KQGHGCESDI WALGCVMYTM LLGRPPFETT NLKETYRCIR EARYTMPSSL
310 320 330 340 350
LAPAKHLIAS MLSKNPEDRP SLDDIIRHDF FLQGFTPDRL SSSCCHTVPD
360 370 380 390 400
FHLSSPAKNF FKKAAAALFG GKKDKARYND THNKVSKEDE DIYKLRHDLK
410 420 430 440 450
KVSITQQPSK HRADEEPQPP PTTVARSGTS AVENKQQIGD AIRMIVRGTL
460 470 480 490 500
GSCSSSSECL EDSTMGSVAD TVARVLRGCL ENMPEADCIP KEQLSTSFQW
510 520 530 540 550
VTKWVDYSNK YGFGYQLSDH TVGVLFNNGA HMSLLPDKKT VHYYAELGQC
560 570 580 590 600
SVFPATDAPE QFISQVTVLK YFSHYMEENL MDGGDLPSVT DIRRPRLYLL
610 620 630 640 650
QWLKSDKALM MLFNDGTFQV NFYHDHTKII ICNQSEEYLL TYINEDRIST
660 670 680
TFRLTTLLMS GCSLELKNRM EYALNMLLQR CN
Length:682
Mass (Da):77,812
Last modified:October 1, 1996 - v1
Checksum:i586DEABFD7208A9D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96163 mRNA No translation available.
CCDSiCCDS26767.1
PIRiA44493
RefSeqiNP_690017.2, NM_152804.2
UniGeneiMm.380

Genome annotation databases

EnsembliENSMUST00000022212; ENSMUSP00000022212; ENSMUSG00000021701
GeneIDi20620
KEGGimmu:20620
UCSCiuc007rvs.2 mouse

Similar proteinsi

Entry informationi

Entry nameiPLK2_MOUSE
AccessioniPrimary (citable) accession number: P53351
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 25, 2018
This is version 150 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health