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P53351

- PLK2_MOUSE

UniProt

P53351 - PLK2_MOUSE

Protein

Serine/threonine-protein kinase PLK2

Gene

Plk2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei108 – 1081ATPCurated
    Active sitei202 – 2021Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi85 – 939ATPPROSITE-ProRule annotation

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

    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

    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 PLK2PRO_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-236.1 Publication

    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.By similarity

    Protein-protein interaction databases

    BioGridi203368. 1 interaction.
    IntActiP53351. 1 interaction.

    Structurei

    3D structure databases

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

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini79 – 331253Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini507 – 57064POLO box 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini603 – 67472POLO box 2PROSITE-ProRule annotationAdd
    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.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

    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: October 1, 2014
    This is version 122 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