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Reviewed, UniProtKB/Swiss-Prot O00444 (PLK4_HUMAN)

Last modified July 7, 2009. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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
    Serine/threonine-protein kinase 18
Gene names
Name: PLK4
Synonyms: SAK, STK18
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length970 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

May play a role in cell proliferation.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Post-translational modification

Tyrosine-phosphorylated by TEC. Ref.2 Ref.4

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SFNP319471EBI-746202,EBI-476295

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 970970Serine/threonine-protein kinase PLK4
PRO_0000086567

Regions

Domain12 – 265254Protein kinase
Domain892 – 95665POLO box
Nucleotide binding18 – 269ATP By similarity

Sites

Active site1361Proton acceptor By similarity
Binding site411ATP By similarity

Amino acid modifications

Modified residue4011Phosphoserine Ref.4
Modified residue4211Phosphoserine Ref.4
Modified residue4991Phosphoserine Ref.4
Modified residue5921Phosphoserine Ref.4
Modified residue6711Phosphoserine Ref.4
Modified residue8171Phosphoserine Ref.4

Natural variations

Natural variant861Y → C: dbSNP rs34156294. Ref.5
VAR_041027
Natural variant1461R → H: dbSNP rs35232579. Ref.5
VAR_041028
Natural variant2261A → T Ref.5
VAR_041029
Natural variant2321S → T: dbSNP rs3811740. Ref.2 Ref.5 Ref.1
VAR_019632
Natural variant3171P → L Ref.5
VAR_041030
Natural variant4491N → D Ref.5
VAR_041031
Natural variant5191W → S Ref.5
VAR_041032
Natural variant8301E → D: dbSNP rs17012739. Ref.2 Ref.5 Ref.1
VAR_041033

Experimental info

Sequence conflict341T → S in BAB69958. Ref.2
Sequence conflict581Q → K in CAA73575. Ref.1
Sequence conflict3871S → R in BAB69958. Ref.2
Sequence conflict6961V → L in BAB69958. Ref.2
Sequence conflict7681Y → F in CAA73575. Ref.1
Sequence conflict8421A → D in BAB69958. Ref.2

Secondary structure

..................................... 970
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O00444-1 [UniParc].

Last modified November 13, 2007. Version 3.
Checksum: 4D56F5FD983211A6

FASTA970108,972
        10         20         30         40         50         60 
MATCIGEKIE DFKVGNLLGK GSFAGVYRAE SIHTGLEVAI KMIDKKAMYK AGMVQRVQNE 

        70         80         90        100        110        120 
VKIHCQLKHP SILELYNYFE DSNYVYLVLE MCHNGEMNRY LKNRVKPFSE NEARHFMHQI 

       130        140        150        160        170        180 
ITGMLYLHSH GILHRDLTLS NLLLTRNMNI KIADFGLATQ LKMPHEKHYT LCGTPNYISP 

       190        200        210        220        230        240 
EIATRSAHGL ESDVWSLGCM FYTLLIGRPP FDTDTVKNTL NKVVLADYEM PSFLSIEAKD 

       250        260        270        280        290        300 
LIHQLLRRNP ADRLSLSSVL DHPFMSRNSS TKSKDLGTVE DSIDSGHATI STAITASSST 

       310        320        330        340        350        360 
SISGSLFDKR RLLIGQPLPN KMTVFPKNKS STDFSSSGDG NSFYTQWGNQ ETSNSGRGRV 

       370        380        390        400        410        420 
IQDAEERPHS RYLRRAYSSD RSGTSNSQSQ AKTYTMERCH SAEMLSVSKR SGGGENEERY 

       430        440        450        460        470        480 
SPTDNNANIF NFFKEKTSSS SGSFERPDNN QALSNHLCPG KTPFPFADPT PQTETVQQWF 

       490        500        510        520        530        540 
GNLQINAHLR KTTEYDSISP NRDFQGHPDL QKDTSKNAWT DTKVKKNSDA SDNAHSVKQQ 

       550        560        570        580        590        600 
NTMKYMTALH SKPEIIQQEC VFGSDPLSEQ SKTRGMEPPW GYQNRTLRSI TSPLVAHRLK 

       610        620        630        640        650        660 
PIRQKTKKAV VSILDSEEVC VELVKEYASQ EYVKEVLQIS SDGNTITIYY PNGGRGFPLA 

       670        680        690        700        710        720 
DRPPSPTDNI SRYSFDNLPE KYWRKYQYAS RFVQLVRSKS PKITYFTRYA KCILMENSPG 

       730        740        750        760        770        780 
ADFEVWFYDG VKIHKTEDFI QVIEKTGKSY TLKSESEVNS LKEEIKMYMD HANEGHRICL 

       790        800        810        820        830        840 
ALESIISEEE RKTRSAPFFP IIIGRKPGST SSPKALSPPP SVDSNYPTRE RASFNRMVMH 

       850        860        870        880        890        900 
SAASPTQAPI LNPSMVTNEG LGLTTTASGT DISSNSLKDC LPKSAQLLKS VFVKNVGWAT 

       910        920        930        940        950        960 
QLTSGAVWVQ FNDGSQLVVQ AGVSSISYTS PNGQTTRYGE NEKLPDYIKQ KLQCLSSILL 

       970 
MFSNPTPNFH 

« Hide

References

« Hide 'large scale' references
[1]"Human SAK related to the PLK/polo family of cell cycle kinases shows high mRNA expression in testis."
Karn T., Holtrich U., Wolf G., Hock B., Strebhardt K., Ruebsamen-Waigmann H.
Oncol. Rep. 4:505-510(1997)
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS THR-232 AND ASP-830.
Tissue: Lung.
[2]"Sak serine-threonine kinase acts as an effector of Tec tyrosine kinase."
Yamashita Y., Kajigaya S., Yoshida K., Ueno S., Ota J., Ohmine K., Ueda M., Miyazato A., Ohya K., Kitamura T., Ozawa K., Mano H.
J. Biol. Chem. 276:39012-39020(2001) [PubMed: 11489907] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION BY TEC, VARIANTS THR-232 AND ASP-830.
Tissue: Blood.
[3]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[4]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401; SER-421; SER-499; SER-592; SER-671 AND SER-817, MASS SPECTROMETRY.
[5]"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. expand/collapse author list , 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: 17344846] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] CYS-86; HIS-146; THR-226; THR-232; LEU-317; ASP-449; SER-519 AND ASP-830.
+Additional computationally mapped references.

Cross-references

Sequence databases

Y13115 mRNA. Translation: CAA73575.1.
AB006972 mRNA. Translation: BAB69958.1.
BC036023 mRNA. Translation: AAH36023.1.
IPIIPI00410344.
RefSeqNP_055079.3.
UniGeneHs.172052

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
3COKX-ray2.25A/B2-275[»]
SMRO00444. Positions 890-964.
ModBaseSearch...

Protein-protein interaction databases

IntActO00444. 9 interactions.

PTM databases

PhosphoSiteO00444.

Proteomic databases

PRIDEO00444.

Genome annotation databases

EnsemblENSG00000142731. Homo sapiens. [Contig view]
GeneID10733.
KEGGhsa:10733.
UCSCuc003ifo.1. human.

Organism-specific databases

GeneCardsGC04P129021.
HGNCHGNC:11397. PLK4.
MIM605031. gene.
PharmGKBPA36205.
GenAtlasSearch...

Phylogenomic databases

HOGENOMO00444.
HOVERGENO00444.
OMAO00444. YTLKSES.

Enzyme and pathway databases

BRENDA2.7.11.21. 247.
ReactomeREACT_152. Cell Cycle, Mitotic.

Gene expression databases

ArrayExpressO00444.
BgeeO00444.
CleanExHS_PLK4.
GermOnlineENSG00000142731. Homo sapiens.

Family and domain databases

InterProIPR000959. POLO_box_duplicated.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR015114. Sak_Polo.
IPR017442. Se/Thr_pkinase-rel.
IPR002290. Ser_thr_pkinase.
IPR008266. Tyr_pkinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
PF09024. Sak_Polo. 1 hit.
[Graphical view]
ProDomPD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
PROSITEPS50078. POLO_BOX. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

BindingDBO00444.
NextBio40744.
SOURCESearch...

Entry information

Entry namePLK4_HUMAN
AccessionPrimary (citable) accession number: O00444
Secondary accession number(s): Q8IYF0, Q96Q95
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: November 13, 2007
Last modified: July 7, 2009
This is version 76 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents