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Q9NYY3

- PLK2_HUMAN

UniProt

Q9NYY3 - PLK2_HUMAN

Protein

Serine/threonine-protein kinase PLK2

Gene

PLK2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 3 (02 Aug 2002)
      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-239. Once activated, activity is stimulated by binding target proteins By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei111 – 1111ATPPROSITE-ProRule annotation
    Active sitei205 – 2051Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi88 – 969ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    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 checkpoint Source: UniProtKB
    6. mitotic spindle organization Source: UniProtKB
    7. negative regulation of apoptotic process Source: UniProtKB
    8. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    9. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: Ensembl
    10. protein phosphorylation Source: UniProtKB
    11. Rap protein signal transduction Source: UniProtKB
    12. Ras protein signal transduction Source: UniProtKB
    13. regulation of centriole replication Source: UniProtKB
    14. 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. 2681.
    SignaLinkiQ9NYY3.

    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
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:19699. PLK2.

    Subcellular locationi

    Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole 2 Publications. 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.

    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

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi210 – 2101N → A: Loss of kinase activity. 1 Publication
    Mutagenesisi503 – 5031W → F: Impairs localization to the centrosome and centriole duplication; when associated with A-629 and M-631. 1 Publication
    Mutagenesisi629 – 6291H → A: Impairs localization to the centrosome and centriole duplication; when associated with F-503 and M-631. 1 Publication
    Mutagenesisi631 – 6311K → M: Impairs localization to the centrosome and centriole duplication; when associated with F-503 and A-631. 1 Publication

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    PharmGKBiPA134940798.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 685685Serine/threonine-protein kinase PLK2PRO_0000086561Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei239 – 2391PhosphothreonineBy similarity

    Post-translational modificationi

    Catalytic activity is enhanced by phosphorylation of Thr-239.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9NYY3.
    PaxDbiQ9NYY3.
    PRIDEiQ9NYY3.

    PTM databases

    PhosphoSiteiQ9NYY3.

    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

    BgeeiQ9NYY3.
    CleanExiHS_PLK2.
    GenevestigatoriQ9NYY3.

    Organism-specific databases

    HPAiCAB009624.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CENPJQ9HC773EBI-721354,EBI-946194

    Protein-protein interaction databases

    BioGridi115988. 11 interactions.
    DIPiDIP-48943N.
    IntActiQ9NYY3. 8 interactions.
    MINTiMINT-1397390.
    STRINGi9606.ENSP00000274289.

    Structurei

    Secondary structure

    1
    685
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi72 – 743
    Turni76 – 783
    Beta strandi81 – 9111
    Beta strandi94 – 1018
    Turni102 – 1054
    Beta strandi106 – 1149
    Helixi115 – 1184
    Helixi121 – 13414
    Beta strandi145 – 1506
    Beta strandi152 – 1598
    Helixi167 – 1748
    Helixi179 – 19820
    Helixi208 – 2103
    Beta strandi211 – 2133
    Beta strandi219 – 2213
    Helixi224 – 2263
    Turni233 – 2353
    Helixi249 – 2524
    Helixi259 – 27517
    Helixi286 – 2883
    Helixi289 – 2935
    Helixi305 – 31410
    Helixi319 – 3213
    Helixi325 – 3295
    Helixi332 – 3354
    Helixi345 – 3484

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4I5MX-ray1.80A57-360[»]
    4I5PX-ray1.74A57-360[»]
    4I6BX-ray1.80A57-360[»]
    4I6FX-ray2.90A57-360[»]
    4I6HX-ray1.91A57-360[»]
    ProteinModelPortaliQ9NYY3.
    SMRiQ9NYY3. Positions 71-354, 503-680.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini82 – 334253Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini510 – 57364POLO box 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini606 – 67772POLO box 2PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi57 – 648Poly-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.
    InParanoidiQ9NYY3.
    KOiK08861.
    OMAiRHEFFLQ.
    OrthoDBiEOG78M01K.
    PhylomeDBiQ9NYY3.
    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.

    Q9NYY3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MELLRTITYQ PAASTKMCEQ ALGKGCGADS KKKRPPQPPE ESQPPQSQAQ    50
    VPPAAPHHHH HHSHSGPEIS RIIVDPTTGK RYCRGKVLGK GGFAKCYEMT 100
    DLTNNKVYAA KIIPHSRVAK PHQREKIDKE IELHRILHHK HVVQFYHYFE 150
    DKENIYILLE YCSRRSMAHI LKARKVLTEP EVRYYLRQIV SGLKYLHEQE 200
    ILHRDLKLGN FFINEAMELK VGDFGLAARL EPLEHRRRTI CGTPNYLSPE 250
    VLNKQGHGCE SDIWALGCVM YTMLLGRPPF ETTNLKETYR CIREARYTMP 300
    SSLLAPAKHL IASMLSKNPE DRPSLDDIIR HDFFLQGFTP DRLSSSCCHT 350
    VPDFHLSSPA KNFFKKAAAA LFGGKKDKAR YIDTHNRVSK EDEDIYKLRH 400
    DLKKTSITQQ PSKHRTDEEL QPPTTTVARS GTPAVENKQQ IGDAIRMIVR 450
    GTLGSCSSSS ECLEDSTMGS VADTVARVLR GCLENMPEAD CIPKEQLSTS 500
    FQWVTKWVDY SNKYGFGYQL SDHTVGVLFN NGAHMSLLPD KKTVHYYAEL 550
    GQCSVFPATD APEQFISQVT VLKYFSHYME ENLMDGGDLP SVTDIRRPRL 600
    YLLQWLKSDK ALMMLFNDGT FQVNFYHDHT KIIICSQNEE YLLTYINEDR 650
    ISTTFRLTTL LMSGCSSELK NRMEYALNML LQRCN 685
    Length:685
    Mass (Da):78,237
    Last modified:August 2, 2002 - v3
    Checksum:i6429F6EFD830B333
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti28 – 281A → G in AAC14573. (PubMed:11696980)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti14 – 141S → T in an ovarian Endometrioid carcinoma sample; somatic mutation. 1 Publication
    VAR_041023
    Natural varianti92 – 921G → S in a lung adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_041024
    Natural varianti436 – 4361E → K.1 Publication
    Corresponds to variant rs55768901 [ dbSNP | Ensembl ].
    VAR_041025
    Natural varianti487 – 4871P → L.1 Publication
    Corresponds to variant rs55645589 [ dbSNP | Ensembl ].
    VAR_041026

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.3. human.

    Polymorphism databases

    DMDMi22096374.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS3974.1.
    RefSeqi NP_001239155.1. NM_001252226.1.
    NP_006613.2. NM_006622.3.
    UniGenei Hs.398157.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4I5M X-ray 1.80 A 57-360 [» ]
    4I5P X-ray 1.74 A 57-360 [» ]
    4I6B X-ray 1.80 A 57-360 [» ]
    4I6F X-ray 2.90 A 57-360 [» ]
    4I6H X-ray 1.91 A 57-360 [» ]
    ProteinModelPortali Q9NYY3.
    SMRi Q9NYY3. Positions 71-354, 503-680.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115988. 11 interactions.
    DIPi DIP-48943N.
    IntActi Q9NYY3. 8 interactions.
    MINTi MINT-1397390.
    STRINGi 9606.ENSP00000274289.

    Chemistry

    BindingDBi Q9NYY3.
    ChEMBLi CHEMBL5938.
    GuidetoPHARMACOLOGYi 2169.

    PTM databases

    PhosphoSitei Q9NYY3.

    Polymorphism databases

    DMDMi 22096374.

    Proteomic databases

    MaxQBi Q9NYY3.
    PaxDbi Q9NYY3.
    PRIDEi Q9NYY3.

    Protocols and materials databases

    DNASUi 10769.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000274289 ; ENSP00000274289 ; ENSG00000145632 .
    GeneIDi 10769.
    KEGGi hsa:10769.
    UCSCi uc003jrn.3. human.

    Organism-specific databases

    CTDi 10769.
    GeneCardsi GC05M057749.
    HGNCi HGNC:19699. PLK2.
    HPAi CAB009624.
    MIMi 607023. gene.
    neXtProti NX_Q9NYY3.
    PharmGKBi PA134940798.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000248546.
    HOVERGENi HBG001843.
    InParanoidi Q9NYY3.
    KOi K08861.
    OMAi RHEFFLQ.
    OrthoDBi EOG78M01K.
    PhylomeDBi Q9NYY3.
    TreeFami TF101089.

    Enzyme and pathway databases

    BRENDAi 2.7.11.21. 2681.
    SignaLinki Q9NYY3.

    Miscellaneous databases

    GeneWikii PLK2.
    GenomeRNAii 10769.
    NextBioi 40893.
    PROi Q9NYY3.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9NYY3.
    CleanExi HS_PLK2.
    Genevestigatori Q9NYY3.

    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 the human homologue of the early-growth response gene Snk, encoding a serum-inducible kinase."
      Liby K., Wu H., Ouyang B., Wu S., Chen J., Dai W.
      DNA Seq. 11:527-533(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    2. "Identification and characterization of human serum-inducible kinase (SNK), a novel member of the polo-kinase family of cell cycle regulators: potential implication for regulation of vascular smooth muscle proliferation."
      Anderson K.M., Nerurkar S.S., Hansbury M.J., Fornwald J., Scott G., Bouzyk M., Mui P., Imbrugia C.S., Carlson K., Marshall L.A., Roshak A.K.
      Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Colon.
    3. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Skin.
    5. Fidler C., Boultwood J., Wang Jabs E., Wainscoat J.S.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 110-408.
    6. "Radiation-inducible hSNK gene is transcriptionally regulated by p53 binding homology element in human thyroid cells."
      Shimizu-Yoshida Y., Sugiyama K., Rogounovitch T., Ohtsuru A., Namba H., Saenko V., Yamashita S.
      Biochem. Biophys. Res. Commun. 289:491-498(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    7. "Polo-like kinase-2 is required for centriole duplication in mammalian cells."
      Warnke S., Kemmler S., Hames R.S., Tsai H.L., Hoffmann-Rohrer U., Fry A.M., Hoffmann I.
      Curr. Biol. 14:1200-1207(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    8. "Transcriptional silencing of Polo-like kinase 2 (SNK/PLK2) is a frequent event in B-cell malignancies."
      Syed N., Smith P., Sullivan A., Spender L.C., Dyer M., Karran L., O'Nions J., Allday M., Hoffmann I., Crawford D., Griffin B., Farrell P.J., Crook T.
      Blood 107:250-256(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOWN-REGULATION IN B-CELL LYMPHOMAS.
    9. "Plk2 regulated centriole duplication is dependent on its localization to the centrioles and a functional polo-box domain."
      Cizmecioglu O., Warnke S., Arnold M., Duensing S., Hoffmann I.
      Cell Cycle 7:3548-3555(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASN-210; TRP-503; HIS-629 AND LYS-631.
    10. Cited for: INDUCTION.
    11. "PLK2 phosphorylation is critical for CPAP function in procentriole formation during the centrosome cycle."
      Chang J., Cizmecioglu O., Hoffmann I., Rhee K.
      EMBO J. 29:2395-2406(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF CENPJ.
    12. "Polo-like kinase 2-dependent phosphorylation of NPM/B23 on serine 4 triggers centriole duplication."
      Krause A., Hoffmann I.
      PLoS ONE 5:E9849-E9849(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF NPM.
    13. "Polo-like kinase 2 (SNK/PLK2) is a novel epigenetically regulated gene in acute myeloid leukemia and myelodysplastic syndromes: genetic and epigenetic interactions."
      Benetatos L., Dasoula A., Hatzimichael E., Syed N., Voukelatou M., Dranitsaris G., Bourantas K.L., Crook T.
      Ann. Hematol. 90:1037-1045(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOWN-REGULATION IN ACUTE MYELOID LEUKEMIA.
    14. "Multifaceted polo-like kinases: drug targets and antitargets for cancer therapy."
      Strebhardt K.
      Nat. Rev. Drug Discov. 9:643-660(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    15. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] THR-14; SER-92; LYS-436 AND LEU-487.

    Entry informationi

    Entry nameiPLK2_HUMAN
    AccessioniPrimary (citable) accession number: Q9NYY3
    Secondary accession number(s): O60679, Q96CV7, Q9UE61
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: August 2, 2002
    Last modified: October 1, 2014
    This is version 135 of the entry and version 3 of the sequence. [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

    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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    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 and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3