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O97143

- PLK4_DROME

UniProt

O97143 - PLK4_DROME

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Protein

Serine/threonine-protein kinase PLK4

Gene
SAK, CG7186
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 431ATP By similarity
Active sitei138 – 1381Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi20 – 289ATP By similarity

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
Complete GO annotation...

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

GO - Cellular componenti

  1. centriole Source: FlyBase
Complete GO annotation...

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 267254Protein kinaseAdd
BLAST
Domaini665 – 73470POLO boxAdd
BLAST

Sequence similaritiesi

Contains 1 POLO box domain.

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

Sequence conflict

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

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 130 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

Similar proteinsi