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P53351

- PLK2_MOUSE

UniProt

P53351 - PLK2_MOUSE

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Protein
Serine/threonine-protein kinase PLK2
Gene
Plk2, Snk
Organism
Mus musculus (Mouse)
Status
Reviewed - 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-236. Once activated, activity is stimulated by binding target proteins By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei108 – 1081ATP Inferred
Active sitei202 – 2021Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi85 – 939ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein serine/threonine kinase activity Source: UniProtKB
  3. signal transducer activity Source: Ensembl

GO - Biological processi

  1. G1/S transition of mitotic cell cycle Source: UniProtKB
  2. Rap protein signal transduction Source: UniProtKB
  3. Ras protein signal transduction Source: UniProtKB
  4. long term synaptic depression Source: UniProtKB
  5. long-term synaptic potentiation Source: UniProtKB
  6. memory Source: UniProtKB
  7. mitotic cell cycle Source: MGI
  8. mitotic cell cycle checkpoint Source: UniProtKB
  9. mitotic spindle organization Source: UniProtKB
  10. negative regulation of apoptotic process Source: UniProtKB
  11. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
  12. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: Ensembl
  13. protein phosphorylation Source: UniProtKB
  14. regulation of centriole replication Source: UniProtKB
  15. regulation of synaptic plasticity Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.21. 3474.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 13

Organism-specific databases

MGIiMGI:1099790. Plk2.

Subcellular locationi

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.

GO - Cellular componenti

  1. centriole Source: UniProtKB
  2. centrosome Source: UniProtKB
  3. dendrite Source: UniProtKB
  4. intracellular Source: UniProtKB
Complete GO annotation...

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi108 – 1081K → 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 Publications
Mutagenesisi236 – 2361T → D or V: Does not significantely affect kinase activity. 2 Publications
Mutagenesisi236 – 2361T → E: Mimicks phosphorylation state, leading to increased activity. 2 Publications

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 682682Serine/threonine-protein kinase PLK2
PRO_0000086562Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei236 – 2361Phosphothreonine1 Publication

Post-translational modificationi

Catalytic activity is enhanced by phosphorylation of Thr-236.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP53351.

PTM databases

PhosphoSiteiP53351.

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

ArrayExpressiP53351.
BgeeiP53351.
CleanExiMM_PLK2.
GenevestigatoriP53351.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi203368. 1 interaction.
IntActiP53351. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP53351.
SMRiP53351. Positions 68-351, 500-677.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini79 – 331253Protein kinase
Add
BLAST
Domaini507 – 57064POLO box 1
Add
BLAST
Domaini603 – 67472POLO box 2
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi54 – 596Poly-His

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.

Sequence similaritiesi

Contains 2 POLO box domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000248546.
HOVERGENiHBG001843.
InParanoidiP53351.
KOiK08861.
OMAiRHEFFLQ.
OrthoDBiEOG78M01K.
PhylomeDBiP53351.
TreeFamiTF101089.

Family and domain databases

InterProiIPR011009. 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]
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.

P53351-1 [UniParc]FASTAAdd to Basket

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MELLRTITYQ PAAGTKMCEQ ALGKACGGDS KKKRPQQPSE DGQPQAQVTP    50
AAPHHHHHHS HSGPEISRII VDPTTGKRYC RGKVLGKGGF AKCYEMTDLT 100
NNKVYAAKII PHSRVAKPHQ REKIDKEIEL HRLLHHKHVV QFYHYFEDKE 150
NIYILLEYCS RRSMAHILKA RKVLTEPEVR YYLRQIVSGL KYLHEQEILH 200
RDLKLGNFFI NEAMELKVGD FGLAARLEPL EHRRRTICGT PNYLSPEVLN 250
KQGHGCESDI WALGCVMYTM LLGRPPFETT NLKETYRCIR EARYTMPSSL 300
LAPAKHLIAS MLSKNPEDRP SLDDIIRHDF FLQGFTPDRL SSSCCHTVPD 350
FHLSSPAKNF FKKAAAALFG GKKDKARYND THNKVSKEDE DIYKLRHDLK 400
KVSITQQPSK HRADEEPQPP PTTVARSGTS AVENKQQIGD AIRMIVRGTL 450
GSCSSSSECL EDSTMGSVAD TVARVLRGCL ENMPEADCIP KEQLSTSFQW 500
VTKWVDYSNK YGFGYQLSDH TVGVLFNNGA HMSLLPDKKT VHYYAELGQC 550
SVFPATDAPE QFISQVTVLK YFSHYMEENL MDGGDLPSVT DIRRPRLYLL 600
QWLKSDKALM MLFNDGTFQV NFYHDHTKII ICNQSEEYLL TYINEDRIST 650
TFRLTTLLMS GCSLELKNRM EYALNMLLQR CN 682
Length:682
Mass (Da):77,812
Last modified:October 1, 1996 - v1
Checksum:i586DEABFD7208A9D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M96163 mRNA. No translation available.
CCDSi CCDS26767.1.
PIRi A44493.
RefSeqi NP_690017.2. NM_152804.2.
UniGenei Mm.380.

3D structure databases

ProteinModelPortali P53351.
SMRi P53351. Positions 68-351, 500-677.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 203368. 1 interaction.
IntActi P53351. 1 interaction.

PTM databases

PhosphoSitei P53351.

Proteomic databases

PRIDEi P53351.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000022212 ; ENSMUSP00000022212 ; ENSMUSG00000021701 .
GeneIDi 20620.
KEGGi mmu:20620.
UCSCi uc007rvs.2. mouse.

Organism-specific databases

CTDi 10769.
MGIi MGI:1099790. Plk2.

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000248546.
HOVERGENi HBG001843.
InParanoidi P53351.
KOi K08861.
OMAi RHEFFLQ.
OrthoDBi EOG78M01K.
PhylomeDBi P53351.
TreeFami TF101089.

Enzyme and pathway databases

BRENDAi 2.7.11.21. 3474.

Miscellaneous databases

NextBioi 299009.
PROi P53351.
SOURCEi Search...

Gene expression databases

ArrayExpressi P53351.
Bgeei P53351.
CleanExi MM_PLK2.
Genevestigatori P53351.

Family and domain databases

InterProi IPR011009. 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 ]
Pfami PF00069. Pkinase. 1 hit.
PF00659. POLO_box. 2 hits.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS50078. POLO_BOX. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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. 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.

Entry informationi

Entry nameiPLK2_MOUSE
AccessioniPrimary (citable) accession number: P53351
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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