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O00444 (PLK4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·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 18
Serine/threonine-protein kinase Sak
Gene names
Name:PLK4
Synonyms:SAK, STK18
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length970 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 parental centriole cylinder, leading to the recruitment of centriole biogenesis proteins such as SASS6, CENPJ/CPAP, CCP110, CEP135 and gamma-tubulin. When overexpressed, it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Phosphorylates 'Ser-151' of FBXW5 during the G1/S transition, leading to inhibit FBXW5 ability to ubiquitinate SASS6. Its central role in centriole replication suggests a possible role in tumorigenesis, centrosome aberrations being frequently observed in tumors. Also involved in deuterosome-mediated centriole amplification in multiciliated that can generate more than 100 centrioles. Also involved in trophoblast differentiation by phosphorylating HAND1, leading to disrupt the interaction between HAND1 and MDFIC and activate HAND1. Phosphorylates CDC25C and CHEK2. Ref.7 Ref.8 Ref.10 Ref.11 Ref.14 Ref.19

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

Homodimer By similarity. Interacts with CEP152 (via N-terminus). Ref.17 Ref.18

Subcellular location

Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole. Nucleusnucleolus By similarity. Cleavage furrow. Note: Component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells that can generate more than 100 centrioles. Associates with centrioles throughout the cell cycle. According to Ref.8, it is not present at cleavage furrows. Ref.8 Ref.10

Induction

Down-regulated in HCT 116 colorectal cancer cells, leading to aberrant centrioles composed of disorganized cylindrical microtubules and displaced appendages. Down-regulated by p53/TP53. Ref.9 Ref.15

Post-translational modification

Ubiquitinated; leading to its degradation by the proteasome By similarity.

Tyrosine-phosphorylated by TEC. Ref.2

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
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

centriole replication

Inferred from mutant phenotype Ref.19. Source: UniProtKB

de novo centriole assembly

Inferred from sequence or structural similarity. Source: UniProtKB

mitotic cell cycle

Traceable author statement. Source: Reactome

positive regulation of centriole replication

Inferred from mutant phenotype Ref.8Ref.10. Source: UniProtKB

protein phosphorylation

Traceable author statement PubMed 10607900. Source: ProtInc

trophoblast giant cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcentriole

Inferred from direct assay Ref.8Ref.10. Source: UniProtKB

centrosome

Inferred from direct assay PubMed 21399614. Source: UniProtKB

cleavage furrow

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Traceable author statement. Source: Reactome

deuterosome

Inferred from sequence or structural similarity. Source: UniProtKB

nucleolus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.18Ref.17Ref.19. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from direct assay Ref.19. Source: UniProtKB

protein tyrosine kinase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SFNP319472EBI-746202,EBI-476295

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O00444-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O00444-2)

The sequence of this isoform differs from the canonical sequence as follows:
     43-74: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: O00444-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-41: Missing.
Note: No experimental confirmation available.

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 Probable

Amino acid modifications

Modified residue4011Phosphoserine Ref.12 Ref.16
Modified residue8171Phosphoserine Ref.16

Natural variations

Alternative sequence1 – 4141Missing in isoform 3.
VSP_038116
Alternative sequence43 – 7432Missing in isoform 2.
VSP_038117
Natural variant861Y → C. Ref.21
Corresponds to variant rs34156294 [ dbSNP | Ensembl ].
VAR_041027
Natural variant1461R → H. Ref.21
Corresponds to variant rs35232579 [ dbSNP | Ensembl ].
VAR_041028
Natural variant2261A → T. Ref.21
Corresponds to variant rs35448573 [ dbSNP | Ensembl ].
VAR_041029
Natural variant2321S → T. Ref.1 Ref.2 Ref.3 Ref.21
Corresponds to variant rs3811740 [ dbSNP | Ensembl ].
VAR_019632
Natural variant3171P → L. Ref.21
Corresponds to variant rs35049837 [ dbSNP | Ensembl ].
VAR_041030
Natural variant4491N → D. Ref.21
Corresponds to variant rs34906574 [ dbSNP | Ensembl ].
VAR_041031
Natural variant5191W → S. Ref.21
Corresponds to variant rs56043017 [ dbSNP | Ensembl ].
VAR_041032
Natural variant8301E → D. Ref.1 Ref.2 Ref.3 Ref.21
Corresponds to variant rs17012739 [ dbSNP | Ensembl ].
VAR_041033

Experimental info

Mutagenesis411K → M: Abolishes ability to phosphorylate CDC25C and CHEK2. Ref.11 Ref.14
Mutagenesis1541D → A: Catalytically inactive mutant that causes some centrosome amplification above background levels when overexpressed. Ref.8
Mutagenesis1701T → D: Activating mutant. Ref.11 Ref.14
Sequence conflict341T → S in BAB69958. Ref.2
Sequence conflict581Q → K in CAA73575. Ref.1
Sequence conflict3331D → N in BAH13823. Ref.3
Sequence conflict3871S → R in BAB69958. Ref.2
Sequence conflict6921F → S in BAH13823. Ref.3
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
Isoform 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

Isoform 2 [UniParc].

Checksum: 3605FA717C82C2B7
Show »

FASTA938105,253
Isoform 3 [UniParc].

Checksum: ECD6808B29B9D8D9
Show »

FASTA929104,636

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] (ISOFORM 1), 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION BY TEC, VARIANTS THR-232 AND ASP-830.
Tissue: Blood.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), VARIANTS THR-232 AND ASP-830.
Tissue: Testis and Thymus.
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Testis.
[5]"Transmembrane signaling by the interleukin-2 receptor: progress and conundrums."
Mills G.B., Schmandt R., Gibson S., Leung B., Hill M., May C., Shi Y.F., Branch D.R., Radvanyi L., Truitt K.E., Imboden J.
Semin. Immunol. 5:345-364(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 134-196.
[6]"Analysis of tyrosine kinase mRNAs including four FGF receptor mRNAs expressed in MCF-7 breast-cancer cells."
Lehtola L., Partanen J., Sistonen L., Korhonen J., Warri A., Harkonen P., Clarke R., Alitalo K.
Int. J. Cancer 50:598-603(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 135-196.
Tissue: Mammary carcinoma.
[7]"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.
[8]"The Polo kinase Plk4 functions in centriole duplication."
Habedanck R., Stierhof Y.-D., Wilkinson C.J., Nigg E.A.
Nat. Cell Biol. 7:1140-1146(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-154.
[9]"SAK, a new polo-like kinase, is transcriptionally repressed by p53 and induces apoptosis upon RNAi silencing."
Li J., Tan M., Li L., Pamarthy D., Lawrence T.S., Sun Y.
Neoplasia 7:312-323(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY TP53.
[10]"Plk4-induced centriole biogenesis in human cells."
Kleylein-Sohn J., Westendorf J., Le Clech M., Habedanck R., Stierhof Y.-D., Nigg E.A.
Dev. Cell 13:190-202(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]"Human Plk4 phosphorylates Cdc25C."
Bonni S., Ganuelas M.L., Petrinac S., Hudson J.W.
Cell Cycle 7:545-547(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF LYS-41 AND THR-170.
[12]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Polo-like kinase 4 phosphorylates Chk2."
Petrinac S., Ganuelas M.L., Bonni S., Nantais J., Hudson J.W.
Cell Cycle 8:327-329(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF LYS-41 AND THR-170.
[15]"Gamma-tubulin-containing abnormal centrioles are induced by insufficient Plk4 in human HCT116 colorectal cancer cells."
Kuriyama R., Bettencourt-Dias M., Hoffmann I., Arnold M., Sandvig L.
J. Cell Sci. 122:2014-2023(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[16]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401 AND SER-817, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Cep152 acts as a scaffold for recruitment of Plk4 and CPAP to the centrosome."
Cizmecioglu O., Arnold M., Bahtz R., Settele F., Ehret L., Haselmann-Weiss U., Antony C., Hoffmann I.
J. Cell Biol. 191:731-739(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CEP152.
[18]"Asterless is a scaffold for the onset of centriole assembly."
Dzhindzhev N.S., Yu Q.D., Weiskopf K., Tzolovsky G., Cunha-Ferreira I., Riparbelli M., Rodrigues-Martins A., Bettencourt-Dias M., Callaini G., Glover D.M.
Nature 467:714-718(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CEP152.
[19]"The SCF-FBXW5 E3-ubiquitin ligase is regulated by PLK4 and targets HsSAS-6 to control centrosome duplication."
Puklowski A., Homsi Y., Keller D., May M., Chauhan S., Kossatz U., Grunwald V., Kubicka S., Pich A., Manns M.P., Hoffmann I., Gonczy P., Malek N.P.
Nat. Cell Biol. 13:1004-1009(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF FBXW5.
[20]"Crystal structure of PLK4 kinase."
New York structural genomix research consortium (NYSGXRC)
Submitted (JUN-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 2-275.
[21]"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] [Europe PMC] [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

EMBL
GenBank
DDBJ
Y13115 mRNA. Translation: CAA73575.1.
AB006972 mRNA. Translation: BAB69958.1.
AK302858 mRNA. Translation: BAH13823.1.
AK303399 mRNA. Translation: BAH13953.1.
AK314238 mRNA. Translation: BAG36907.1.
BC036023 mRNA. Translation: AAH36023.1.
CCDSCCDS3735.1. [O00444-1]
CCDS54803.1. [O00444-2]
CCDS54804.1. [O00444-3]
RefSeqNP_001177728.1. NM_001190799.1. [O00444-2]
NP_001177730.1. NM_001190801.1. [O00444-3]
NP_055079.3. NM_014264.4. [O00444-1]
UniGeneHs.172052.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3COKX-ray2.25A/B2-275[»]
4JXFX-ray2.40A4-269[»]
ProteinModelPortalO00444.
SMRO00444. Positions 4-319, 593-807, 890-964.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115956. 15 interactions.
DIPDIP-34467N.
IntActO00444. 6 interactions.
MINTMINT-1460432.
STRING9606.ENSP00000270861.

Chemistry

BindingDBO00444.
ChEMBLCHEMBL3788.
GuidetoPHARMACOLOGY2171.

PTM databases

PhosphoSiteO00444.

Proteomic databases

PaxDbO00444.
PRIDEO00444.

Protocols and materials databases

DNASU10733.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000270861; ENSP00000270861; ENSG00000142731. [O00444-1]
ENST00000513090; ENSP00000427554; ENSG00000142731. [O00444-2]
ENST00000514379; ENSP00000423582; ENSG00000142731. [O00444-3]
GeneID10733.
KEGGhsa:10733.
UCSCuc003ifo.3. human. [O00444-1]
uc011cgs.2. human. [O00444-2]

Organism-specific databases

CTD10733.
GeneCardsGC04P128802.
HGNCHGNC:11397. PLK4.
HPAHPA035026.
HPA043198.
MIM605031. gene.
neXtProtNX_O00444.
PharmGKBPA36205.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG053617.
InParanoidO00444.
KOK08863.
OMAMERCHSA.
OrthoDBEOG7NCV33.
PhylomeDBO00444.
TreeFamTF101090.

Enzyme and pathway databases

BRENDA2.7.11.21. 2681.
ReactomeREACT_115566. Cell Cycle.
SignaLinkO00444.

Gene expression databases

ArrayExpressO00444.
BgeeO00444.
CleanExHS_PLK4.
GenevestigatorO00444.

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.
PF00659. POLO_box. 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

EvolutionaryTraceO00444.
GeneWikiPLK4.
GenomeRNAi10733.
NextBio40744.
PROO00444.
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Entry information

Entry namePLK4_HUMAN
AccessionPrimary (citable) accession number: O00444
Secondary accession number(s): B2RAL0 expand/collapse secondary AC list , B7Z837, B7Z8G7, Q8IYF0, Q96Q95, Q9UD84, Q9UDE2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: November 13, 2007
Last modified: July 9, 2014
This is version 131 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

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