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O97143

- PLK4_DROME

UniProt

O97143 - PLK4_DROME

Protein

Serine/threonine-protein kinase PLK4

Gene

SAK

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the mother centriole cylinder, using mother centriole as a platform, leading to the recruitment of centriole biogenesis proteins such as Sas-6. When overexpressed, it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Centrosome amplification following overexpression can initiate tumorigenesis, highlighting the importance of centrosome regulation in cancers.3 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei43 – 431ATPPROSITE-ProRule annotation
    Active sitei138 – 1381Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi20 – 289ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein kinase activity Source: FlyBase
    3. protein serine/threonine kinase activity Source: FlyBase
    4. protein tyrosine kinase activity Source: InterPro

    GO - Biological processi

    1. centriole replication Source: FlyBase
    2. centrosome duplication Source: FlyBase
    3. centrosome organization Source: FlyBase
    4. male meiosis Source: FlyBase
    5. mitotic spindle organization Source: FlyBase
    6. positive regulation of protein catabolic process Source: FlyBase
    7. protein autophosphorylation Source: FlyBase
    8. protein phosphorylation Source: FlyBase
    9. regulation of centriole replication Source: FlyBase
    10. regulation of protein stability Source: FlyBase
    11. sperm axoneme assembly Source: FlyBase
    12. syncytial blastoderm mitotic cell cycle Source: FlyBase

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiO97143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase PLK4 (EC:2.7.11.21)
    Alternative name(s):
    Polo-like kinase 4
    Short name:
    PLK-4
    Serine/threonine-protein kinase SAK
    Gene namesi
    Name:SAK
    ORF Names:CG7186
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3L

    Organism-specific databases

    FlyBaseiFBgn0026371. SAK.

    Subcellular locationi

    Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole 3 Publications
    Note: Colocalizes with Sas-4 and Patronin at the microtubule organizing center.

    GO - Cellular componenti

    1. centriole Source: FlyBase

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi293 – 2931S → A in SAK-ND; impairs interaction with SCF(Slimb) ubiquitin ligase complex and subsequent ubiquitination; when associated with A-297. 1 Publication
    Mutagenesisi297 – 2971T → A in SAK-ND; impairs interaction with SCF(Slimb) ubiquitin ligase complex and subsequent ubiquitination; when associated with A-292. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 769769Serine/threonine-protein kinase PLK4PRO_0000385291Add
    BLAST

    Post-translational modificationi

    Ubiquitinated by the SCF(Slimb) ubiquitin ligase complex; leading to its degradation by the proteasome during interphase and regulating centriole number and ensuring the block to centriole reduplication.2 Publications

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    PaxDbiO97143.
    PRIDEiO97143.

    Expressioni

    Gene expression databases

    BgeeiO97143.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    BioGridi65629. 62 interactions.
    DIPiDIP-49071N.
    IntActiO97143. 52 interactions.
    MINTiMINT-7952919.
    STRINGi7227.FBpp0078042.

    Structurei

    Secondary structure

    1
    769
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi397 – 4004
    Beta strandi402 – 4087
    Beta strandi414 – 4218
    Turni423 – 4253
    Beta strandi426 – 43611
    Beta strandi442 – 4465
    Turni449 – 4524
    Helixi468 – 4703
    Beta strandi471 – 4733
    Turni474 – 4763
    Helixi479 – 4813
    Helixi482 – 49615
    Beta strandi499 – 5057
    Beta strandi507 – 5148
    Beta strandi520 – 5245
    Beta strandi529 – 5335
    Turni534 – 5363
    Beta strandi537 – 5415
    Helixi554 – 57825
    Beta strandi589 – 5935

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4G7NX-ray2.30A/B382-602[»]
    ProteinModelPortaliO97143.
    SMRiO97143. Positions 8-335, 382-596.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini14 – 267254Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini665 – 73470POLO boxPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC5/Polo subfamily.PROSITE-ProRule annotation
    Contains 1 POLO box domain.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00530000062954.
    InParanoidiO97143.
    KOiK08863.
    OMAiKNAIMSI.
    OrthoDBiEOG7NCV33.
    PhylomeDBiO97143.

    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.
    IPR008266. Tyr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS50078. POLO_BOX. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O97143-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLSNRAFGET IEDYEVQHLL GKGGFATVYK ARCLHTHQDV AIKMIDKKLI    50
    QGTGLTNRVR QEVEIHSRLK HPSVLQLYTF FQDANYVYLV LELAHNGELH 100
    RYMNHIARPF TETEAASILK QVVAGLLYLH SHNIMHRDIS LSNLLLSREM 150
    HVKIADFGLA TQLKRPDERH MTMCGTPNYI SPEVVSRTSH GLPADVWSVG 200
    CMLYTLLVGR PPFETDAVQS TLNKVVMSEY IMPAHLSYEA QDLINKLLKK 250
    LPHERITLEA VLCHPFMLKC SNGGHSAPGA LNVFSQSMES GDSGIITFAS 300
    SDSRNSQQIR SVENSGPQQV LPQIREEFKQ VHHKLPYEQT GLFGQASTGL 350
    AEPNWPGAAK SSAFCMEAGN VPNSKQASLK EDRISVPPLN TKRLLPTRYK 400
    TKNAIMSILR NGEVVLEFLK FRPTYNEDRI NDICRISDDG QRIIIYQPDP 450
    GRGLPVREQP PDLQIPSGDC VYNYDNLPSK HWKKYIYGAR FVGLVKSKTP 500
    KVTYFSTLGK CQLMETMTDF EIRFYSGAKL LKTPSEGLKV YDRNGMLLSD 550
    YSCSESRSLI EHGNECFTHC VNISNALEVA QTKDNSCFPV TIGRRPITDV 600
    QPAQRLDGLR DTTNIAFSTP KSNQGSINFS LSTISSTRNT SDFGTNCSRS 650
    NMLAAHQNIP IKRINVPEIG IATELSHGVV QVQFYDGSVV SVIPSMQGGG 700
    ITYTQPNGTS THFGKGDDLP FPVRDRVGQI PNIQLKLKTA PLLGSGRKTD 750
    YNNAMTPKTT TPYYNRMLL 769
    Length:769
    Mass (Da):85,887
    Last modified:May 1, 1999 - v1
    Checksum:iF050BF60A5D94AA4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti145 – 1451L → V in AAO45202. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF106952 mRNA. Translation: AAD19607.1.
    AE014296 Genomic DNA. Translation: AAF51737.1.
    BT004846 mRNA. Translation: AAO45202.1.
    BT044561 mRNA. Translation: ACI15756.1.
    RefSeqiNP_649324.1. NM_141067.3.
    UniGeneiDm.3240.

    Genome annotation databases

    EnsemblMetazoaiFBtr0078387; FBpp0078042; FBgn0026371.
    GeneIDi40384.
    KEGGidme:Dmel_CG7186.
    UCSCiCG7186-RA. d. melanogaster.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF106952 mRNA. Translation: AAD19607.1 .
    AE014296 Genomic DNA. Translation: AAF51737.1 .
    BT004846 mRNA. Translation: AAO45202.1 .
    BT044561 mRNA. Translation: ACI15756.1 .
    RefSeqi NP_649324.1. NM_141067.3.
    UniGenei Dm.3240.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4G7N X-ray 2.30 A/B 382-602 [» ]
    ProteinModelPortali O97143.
    SMRi O97143. Positions 8-335, 382-596.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 65629. 62 interactions.
    DIPi DIP-49071N.
    IntActi O97143. 52 interactions.
    MINTi MINT-7952919.
    STRINGi 7227.FBpp0078042.

    Proteomic databases

    PaxDbi O97143.
    PRIDEi O97143.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0078387 ; FBpp0078042 ; FBgn0026371 .
    GeneIDi 40384.
    KEGGi dme:Dmel_CG7186.
    UCSCi CG7186-RA. d. melanogaster.

    Organism-specific databases

    CTDi 40384.
    FlyBasei FBgn0026371. SAK.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00530000062954.
    InParanoidi O97143.
    KOi K08863.
    OMAi KNAIMSI.
    OrthoDBi EOG7NCV33.
    PhylomeDBi O97143.

    Enzyme and pathway databases

    SignaLinki O97143.

    Miscellaneous databases

    ChiTaRSi PLK4. drosophila.
    GenomeRNAii 40384.
    NextBioi 818499.
    PROi O97143.

    Gene expression databases

    Bgeei O97143.

    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.
    IPR008266. Tyr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS50078. POLO_BOX. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Hudson J.W., Dennis J.W.
      Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    3. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    4. Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.
      Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Embryo.
    5. Cited for: FUNCTION, SUBCELLULAR LOCATION.
    6. "Revisiting the role of the mother centriole in centriole biogenesis."
      Rodrigues-Martins A., Riparbelli M., Callaini G., Glover D.M., Bettencourt-Dias M.
      Science 316:1046-1050(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Centrosome amplification can initiate tumorigenesis in flies."
      Basto R., Brunk K., Vinadogrova T., Peel N., Franz A., Khodjakov A., Raff J.W.
      Cell 133:1032-1042(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "The SCF Slimb ubiquitin ligase regulates Plk4/Sak levels to block centriole reduplication."
      Rogers G.C., Rusan N.M., Roberts D.M., Peifer M., Rogers S.L.
      J. Cell Biol. 184:225-239(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, UBIQUITINATION.
    9. "The SCF/Slimb ubiquitin ligase limits centrosome amplification through degradation of SAK/PLK4."
      Cunha-Ferreira I., Rodrigues-Martins A., Bento I., Riparbelli M., Zhang W., Laue E., Callaini G., Glover D.M., Bettencourt-Dias M.
      Curr. Biol. 19:43-49(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, MUTAGENESIS OF SER-293 AND THR-297.
    10. "Patronin regulates the microtubule network by protecting microtubule minus ends."
      Goodwin S.S., Vale R.D.
      Cell 143:263-274(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiPLK4_DROME
    AccessioniPrimary (citable) accession number: O97143
    Secondary accession number(s): Q86NL8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 22, 2009
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 131 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3