O97143 (PLK4_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	SAK
ORF Names:	CG7186

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	769 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Cytoplasm › cytoskeleton › centrosome › centriole 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 component	Cytoplasm Cytoskeleton
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	centriole replication Inferred from mutant phenotype Ref.5. Source: FlyBase mitotic spindle organization Inferred from mutant phenotype. Source: FlyBase regulation of centriole replication Inferred from direct assay Ref.8. Source: FlyBase sperm axoneme assembly Inferred from mutant phenotype Ref.5. Source: FlyBase
Cellular component	centriole Inferred from direct assay. Source: FlyBase
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW protein tyrosine kinase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 769	769	Serine/threonine-protein kinase PLK4		PRO_0000385291
Regions
	Domain	14 – 267	254	Protein kinase
	Domain	665 – 734	70	POLO box
	Nucleotide binding	20 – 28	9	ATP By similarity
Sites
	Active site	138	1	Proton acceptor By similarity
	Binding site	43	1	ATP By similarity
Experimental info
	Mutagenesis	293	1	S → A in SAK-ND; impairs interaction with SCF(Slimb) ubiquitin ligase complex and subsequent ubiquitination; when associated with A-297. Ref.9
	Mutagenesis	297	1	T → A in SAK-ND; impairs interaction with SCF(Slimb) ubiquitin ligase complex and subsequent ubiquitination; when associated with A-292. Ref.9
	Sequence conflict	145	1	L → V in AAO45202. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	O97143 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: F050BF60A5D94AA4	FASTA	769	85,887
	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

References

	« Hide 'large scale' referencesShow '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. , 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: 10731132] [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. , 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: 12537572] [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: 16326102] [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: 17463247] [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: 18555779] [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: 19171756] [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: 19084407] [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.
RefSeq	NP_649324.1. NM_141067.2.
UniGene	Dm.3240.
3D structure databases
HSSP	HSSP built from PDB template 2AC3 based on UniProtKB Q9HBH9.
ProteinModelPortal	O97143.
SMR	O97143. Positions 6-268, 663-738.
ModBase	Search...
Protein-protein interaction databases
IntAct	O97143. 52 interactions.
STRING	O97143.
Proteomic databases
PRIDE	O97143.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0078387; FBpp0078042; FBgn0026371.
GeneID	40384.
KEGG	dme:Dmel_CG7186.
NMPDR	fig|7227.3.peg.10930.
UCSC	CG7186-RA. d. melanogaster.
Organism-specific databases
CTD	40384.
FlyBase	FBgn0026371. SAK.
Phylogenomic databases
eggNOG	inNOG07994.
GeneTree	EMGT00050000001100.
InParanoid	O97143.
OMA	IMHRDIS.
OrthoDB	EOG4RR4ZG.
PhylomeDB	O97143.
Gene expression databases
ArrayExpress	O97143.
Bgee	O97143.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000959. POLO_box_duplicated_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_kinase-like_dom. IPR002290. Ser/Thr_kinase_dom. IPR008266. Tyr_kinase_AS. [Graphical view]
KO	K08863.
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS50078. POLO_BOX. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	818499.

Entry information

Entry name

PLK4_DROME

Accession

Primary (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:	January 25, 2012
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project