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P53351 (PLK2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Plk2
Synonyms:Snk
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length682 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.3 Ref.5 Ref.6

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

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

Subunit structure

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

Subcellular location

Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole By similarity. Cell projectiondendrite By similarity. Note: Localizes to centrosomes during early G1 phase where it only associates to the mother centriole and then distributes equally to both mother and daughter centrioles at the onset of S phase By similarity.

Tissue specificity

Brain, lung and heart. Ref.1

Developmental stage

Expressed in early G1, during G0-G1 transition as well as in cycling cells. Ref.2

Induction

Directly regulated by p53/TP53. Induced by serum and phorbol ester. Ref.1 Ref.3

Domain

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.

Post-translational modification

Catalytic activity is enhanced by phosphorylation of Thr-236.

Disruption phenotype

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. Ref.4 Ref.6

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC5/Polo subfamily.

Contains 2 POLO box domains.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Cellular componentCell projection
Cytoplasm
Cytoskeleton
   DiseaseTumor suppressor
   DomainRepeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG1/S transition of mitotic cell cycle

Inferred from sequence or structural similarity. Source: UniProtKB

Rap protein signal transduction

Inferred from sequence or structural similarity. Source: UniProtKB

Ras protein signal transduction

Inferred from sequence or structural similarity. Source: UniProtKB

long term synaptic depression

Inferred from sequence or structural similarity. Source: UniProtKB

long-term synaptic potentiation

Inferred from sequence or structural similarity. Source: UniProtKB

memory

Inferred from mutant phenotype Ref.6. Source: UniProtKB

mitotic cell cycle

Inferred from mutant phenotype Ref.4. Source: MGI

mitotic cell cycle checkpoint

Inferred from mutant phenotype Ref.3. Source: UniProtKB

mitotic spindle organization

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of apoptotic process

Inferred from mutant phenotype Ref.3. Source: UniProtKB

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from direct assay Ref.3. Source: UniProtKB

regulation of centriole replication

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of synaptic plasticity

Inferred from mutant phenotype Ref.6. Source: UniProtKB

   Cellular_componentcentriole

Inferred from sequence or structural similarity. Source: UniProtKB

centrosome

Inferred from sequence or structural similarity. Source: UniProtKB

dendrite

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein serine/threonine kinase activity

Inferred from direct assay Ref.3. Source: UniProtKB

signal transducer activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 682682Serine/threonine-protein kinase PLK2
PRO_0000086562

Regions

Domain79 – 331253Protein kinase
Domain507 – 57064POLO box 1
Domain603 – 67472POLO box 2
Nucleotide binding85 – 939ATP By similarity
Compositional bias54 – 596Poly-His

Sites

Active site2021Proton acceptor By similarity
Binding site1081ATP Probable

Amino acid modifications

Modified residue2361Phosphothreonine Ref.2

Experimental info

Mutagenesis1081K → 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. Ref.2 Ref.6
Mutagenesis2361T → D or V: Does not significantely affect kinase activity. Ref.2 Ref.3
Mutagenesis2361T → E: Mimicks phosphorylation state, leading to increased activity. Ref.2 Ref.3

Sequences

Sequence LengthMass (Da)Tools
P53351 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 586DEABFD7208A9D

FASTA68277,812
        10         20         30         40         50         60 
MELLRTITYQ PAAGTKMCEQ ALGKACGGDS KKKRPQQPSE DGQPQAQVTP AAPHHHHHHS 

        70         80         90        100        110        120 
HSGPEISRII VDPTTGKRYC RGKVLGKGGF AKCYEMTDLT NNKVYAAKII PHSRVAKPHQ 

       130        140        150        160        170        180 
REKIDKEIEL HRLLHHKHVV QFYHYFEDKE NIYILLEYCS RRSMAHILKA RKVLTEPEVR 

       190        200        210        220        230        240 
YYLRQIVSGL KYLHEQEILH RDLKLGNFFI NEAMELKVGD FGLAARLEPL EHRRRTICGT 

       250        260        270        280        290        300 
PNYLSPEVLN KQGHGCESDI WALGCVMYTM LLGRPPFETT NLKETYRCIR EARYTMPSSL 

       310        320        330        340        350        360 
LAPAKHLIAS MLSKNPEDRP SLDDIIRHDF FLQGFTPDRL SSSCCHTVPD FHLSSPAKNF 

       370        380        390        400        410        420 
FKKAAAALFG GKKDKARYND THNKVSKEDE DIYKLRHDLK KVSITQQPSK HRADEEPQPP 

       430        440        450        460        470        480 
PTTVARSGTS AVENKQQIGD AIRMIVRGTL GSCSSSSECL EDSTMGSVAD TVARVLRGCL 

       490        500        510        520        530        540 
ENMPEADCIP KEQLSTSFQW VTKWVDYSNK YGFGYQLSDH TVGVLFNNGA HMSLLPDKKT 

       550        560        570        580        590        600 
VHYYAELGQC SVFPATDAPE QFISQVTVLK YFSHYMEENL MDGGDLPSVT DIRRPRLYLL 

       610        620        630        640        650        660 
QWLKSDKALM MLFNDGTFQV NFYHDHTKII ICNQSEEYLL TYINEDRIST TFRLTTLLMS 

       670        680 
GCSLELKNRM EYALNMLLQR CN 

« Hide

References

[1]"Identification of an early-growth-response gene encoding a novel putative protein kinase."
Simmons D.L., Neel B.G., Stevens R., Evett G., Erikson R.L.
Mol. Cell. Biol. 12:4164-4169(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
[2]"The serum-inducible protein kinase Snk is a G1 phase polo-like kinase that is inhibited by the calcium- and integrin-binding protein CIB."
Ma S., Liu M.A., Yuan Y.L., Erikson R.L.
Mol. Cancer Res. 1:376-384(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DEVELOPMENTAL STAGE, PHOSPHORYLATION AT THR-236, MUTAGENESIS OF LYS-108 AND THR-236.
[3]"Silencing of the novel p53 target gene Snk/Plk2 leads to mitotic catastrophe in paclitaxel (taxol)-exposed cells."
Burns T.F., Fei P., Scata K.A., Dicker D.T., El-Deiry W.S.
Mol. Cell. Biol. 23:5556-5571(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION, MUTAGENESIS OF THR-236.
[4]"Role of Plk2 (Snk) in mouse development and cell proliferation."
Ma S., Charron J., Erikson R.L.
Mol. Cell. Biol. 23:6936-6943(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[5]"Polo-like kinase 2 (PLK2) phosphorylates alpha-synuclein at serine 129 in central nervous system."
Inglis K.J., Chereau D., Brigham E.F., Chiou S.S., Schobel S., Frigon N.L., Yu M., Caccavello R.J., Nelson S., Motter R., Wright S., Chian D., Santiago P., Soriano F., Ramos C., Powell K., Goldstein J.M., Babcock M. expand/collapse author list , Yednock T., Bard F., Basi G.S., Sham H., Chilcote T.J., McConlogue L., Griswold-Prenner I., Anderson J.P.
J. Biol. Chem. 284:2598-2602(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF SNCA.
[6]"Requirement for Plk2 in orchestrated ras and rap signaling, homeostatic structural plasticity, and memory."
Lee K.J., Lee Y., Rozeboom A., Lee J.Y., Udagawa N., Hoe H.S., Pak D.T.
Neuron 69:957-973(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF LYS-108, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M96163 mRNA. No translation available.
PIRA44493.
RefSeqNP_690017.2. NM_152804.2.
UniGeneMm.380.

3D structure databases

ProteinModelPortalP53351.
SMRP53351. Positions 68-352, 500-677.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203368. 1 interaction.
IntActP53351. 1 interaction.

PTM databases

PhosphoSiteP53351.

Proteomic databases

PRIDEP53351.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022212; ENSMUSP00000022212; ENSMUSG00000021701.
GeneID20620.
KEGGmmu:20620.
UCSCuc007rvs.2. mouse.

Organism-specific databases

CTD10769.
MGIMGI:1099790. Plk2.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000248546.
HOVERGENHBG001843.
InParanoidP53351.
KOK08861.
OMARHEFFLQ.
OrthoDBEOG78M01K.
PhylomeDBP53351.
TreeFamTF101089.

Enzyme and pathway databases

BRENDA2.7.11.21. 3474.

Gene expression databases

ArrayExpressP53351.
BgeeP53351.
CleanExMM_PLK2.
GenevestigatorP53351.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000959. POLO_box_duplicated_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
PF00659. POLO_box. 2 hits.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50078. POLO_BOX. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio299009.
PROP53351.
SOURCESearch...

Entry information

Entry namePLK2_MOUSE
AccessionPrimary (citable) accession number: P53351
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot