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O97143 (PLK4_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:SAK
ORF Names:CG7186
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length769 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.6 Ref.7

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole Ref.5 Ref.8.

Post-translational modification

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. Ref.8 Ref.9

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC5/Polo subfamily.

Contains 1 POLO box domain.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMUbl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcentriole replication

Inferred from direct assay PubMed 21145506. Source: FlyBase

male meiosis

Inferred from mutant phenotype PubMed 18196975. Source: FlyBase

mitotic spindle organization

Inferred from mutant phenotype PubMed 17412918. Source: FlyBase

peptidyl-tyrosine phosphorylation

Inferred from electronic annotation. Source: GOC

positive regulation of protein catabolic process

Inferred from mutant phenotype PubMed 21987638. Source: FlyBase

protein autophosphorylation

Inferred from direct assay PubMed 21987638. Source: FlyBase

regulation of centriole replication

Inferred from direct assay Ref.8. Source: FlyBase

regulation of protein stability

Inferred from mutant phenotype PubMed 21987638. Source: FlyBase

sperm axoneme assembly

Inferred from mutant phenotype Ref.5. Source: FlyBase

syncytial blastoderm mitotic cell cycle

Inferred from mutant phenotype PubMed 18196975. Source: FlyBase

   Cellular_componentcentriole

Inferred from direct assay PubMed 17475495PubMed 21145506. Source: FlyBase

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein serine/threonine kinase activity

Inferred from direct assay PubMed 21987638. Source: FlyBase

protein tyrosine kinase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 769769Serine/threonine-protein kinase PLK4
PRO_0000385291

Regions

Domain14 – 267254Protein kinase
Domain665 – 73470POLO box
Nucleotide binding20 – 289ATP By similarity

Sites

Active site1381Proton acceptor By similarity
Binding site431ATP By similarity

Experimental info

Mutagenesis2931S → A in SAK-ND; impairs interaction with SCF(Slimb) ubiquitin ligase complex and subsequent ubiquitination; when associated with A-297. Ref.9
Mutagenesis2971T → A in SAK-ND; impairs interaction with SCF(Slimb) ubiquitin ligase complex and subsequent ubiquitination; when associated with A-292. Ref.9
Sequence conflict1451L → V in AAO45202. Ref.4

Secondary structure

................................... 769
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O97143 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: F050BF60A5D94AA4

FASTA76985,887
        10         20         30         40         50         60 
MLSNRAFGET IEDYEVQHLL GKGGFATVYK ARCLHTHQDV AIKMIDKKLI QGTGLTNRVR 

        70         80         90        100        110        120 
QEVEIHSRLK HPSVLQLYTF FQDANYVYLV LELAHNGELH RYMNHIARPF TETEAASILK 

       130        140        150        160        170        180 
QVVAGLLYLH SHNIMHRDIS LSNLLLSREM HVKIADFGLA TQLKRPDERH MTMCGTPNYI 

       190        200        210        220        230        240 
SPEVVSRTSH GLPADVWSVG CMLYTLLVGR PPFETDAVQS TLNKVVMSEY IMPAHLSYEA 

       250        260        270        280        290        300 
QDLINKLLKK LPHERITLEA VLCHPFMLKC SNGGHSAPGA LNVFSQSMES GDSGIITFAS 

       310        320        330        340        350        360 
SDSRNSQQIR SVENSGPQQV LPQIREEFKQ VHHKLPYEQT GLFGQASTGL AEPNWPGAAK 

       370        380        390        400        410        420 
SSAFCMEAGN VPNSKQASLK EDRISVPPLN TKRLLPTRYK TKNAIMSILR NGEVVLEFLK 

       430        440        450        460        470        480 
FRPTYNEDRI NDICRISDDG QRIIIYQPDP GRGLPVREQP PDLQIPSGDC VYNYDNLPSK 

       490        500        510        520        530        540 
HWKKYIYGAR FVGLVKSKTP KVTYFSTLGK CQLMETMTDF EIRFYSGAKL LKTPSEGLKV 

       550        560        570        580        590        600 
YDRNGMLLSD YSCSESRSLI EHGNECFTHC VNISNALEVA QTKDNSCFPV TIGRRPITDV 

       610        620        630        640        650        660 
QPAQRLDGLR DTTNIAFSTP KSNQGSINFS LSTISSTRNT SDFGTNCSRS NMLAAHQNIP 

       670        680        690        700        710        720 
IKRINVPEIG IATELSHGVV QVQFYDGSVV SVIPSMQGGG ITYTQPNGTS THFGKGDDLP 

       730        740        750        760 
FPVRDRVGQI PNIQLKLKTA PLLGSGRKTD YNNAMTPKTT TPYYNRMLL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
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]"SAK/PLK4 is required for centriole duplication and flagella development."
Bettencourt-Dias M., Rodrigues-Martins A., Carpenter L., Riparbelli M., Lehmann L., Gatt M.K., Carmo N., Balloux F., Callaini G., Glover D.M.
Curr. Biol. 15:2199-2207(2005) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF106952 mRNA. Translation: AAD19607.1.
AE014296 Genomic DNA. Translation: AAF51737.1.
BT004846 mRNA. Translation: AAO45202.1.
BT044561 mRNA. Translation: ACI15756.1.
RefSeqNP_649324.1. NM_141067.3.
UniGeneDm.3240.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4G7NX-ray2.30A/B382-602[»]
ProteinModelPortalO97143.
SMRO97143. Positions 8-335, 382-596.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid65629. 62 interactions.
DIPDIP-49071N.
IntActO97143. 52 interactions.
MINTMINT-7952919.
STRING7227.FBpp0078042.

Proteomic databases

PaxDbO97143.
PRIDEO97143.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0078387; FBpp0078042; FBgn0026371.
GeneID40384.
KEGGdme:Dmel_CG7186.
UCSCCG7186-RA. d. melanogaster.

Organism-specific databases

CTD40384.
FlyBaseFBgn0026371. SAK.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00530000062954.
InParanoidO97143.
KOK08863.
OMAKNAIMSI.
OrthoDBEOG7NCV33.
PhylomeDBO97143.

Enzyme and pathway databases

SignaLinkO97143.

Gene expression databases

BgeeO97143.

Family and domain databases

InterProIPR011009. 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]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50078. POLO_BOX. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPLK4. drosophila.
GenomeRNAi40384.
NextBio818499.
PROO97143.

Entry information

Entry namePLK4_DROME
AccessionPrimary (citable) accession number: O97143
Secondary accession number(s): Q86NL8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: May 1, 1999
Last modified: March 19, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase