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Serine/threonine-protein kinase PLK4 (EC 2.7.11.21) (Polo-like kinase 4) (PLK-4) (Serine/threonine-protein kinase 18) (Serine/threonine-protein kinase Sak)

 PLK4_HUMAN              Reviewed;         970 AA.
O00444; B2RAL0; B7Z837; B7Z8G7; Q8IYF0; Q96Q95; Q9UD84; Q9UDE2;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
13-NOV-2007, sequence version 3.
22-NOV-2017, entry version 166.
RecName: Full=Serine/threonine-protein kinase PLK4;
EC=2.7.11.21;
AltName: Full=Polo-like kinase 4;
Short=PLK-4;
AltName: Full=Serine/threonine-protein kinase 18;
AltName: Full=Serine/threonine-protein kinase Sak;
Name=PLK4; Synonyms=SAK, STK18;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS THR-232 AND
ASP-830.
TISSUE=Lung;
Karn T., Holtrich U., Wolf G., Hock B., Strebhardt K.,
Ruebsamen-Waigmann H.;
"Human SAK related to the PLK/polo family of cell cycle kinases shows
high mRNA expression in testis.";
Oncol. Rep. 4:505-510(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION BY TEC, AND
VARIANTS THR-232 AND ASP-830.
TISSUE=Blood;
PubMed=11489907; DOI=10.1074/jbc.M106249200;
Yamashita Y., Kajigaya S., Yoshida K., Ueno S., Ota J., Ohmine K.,
Ueda M., Miyazato A., Ohya K., Kitamura T., Ozawa K., Mano H.;
"Sak serine-threonine kinase acts as an effector of Tec tyrosine
kinase.";
J. Biol. Chem. 276:39012-39020(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND
VARIANTS THR-232 AND ASP-830.
TISSUE=Testis, and Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
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.,
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 134-196.
PubMed=8260651; DOI=10.1006/smim.1993.1041;
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.;
"Transmembrane signaling by the interleukin-2 receptor: progress and
conundrums.";
Semin. Immunol. 5:345-364(1993).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 135-196.
TISSUE=Mammary carcinoma;
PubMed=1311287; DOI=10.1002/ijc.2910500419;
Lehtola L., Partanen J., Sistonen L., Korhonen J., Warri A.,
Harkonen P., Clarke R., Alitalo K.;
"Analysis of tyrosine kinase mRNAs including four FGF receptor mRNAs
expressed in MCF-7 breast-cancer cells.";
Int. J. Cancer 50:598-603(1992).
[7]
FUNCTION.
PubMed=16326102; DOI=10.1016/j.cub.2005.11.042;
Bettencourt-Dias M., Rodrigues-Martins A., Carpenter L.,
Riparbelli M., Lehmann L., Gatt M.K., Carmo N., Balloux F.,
Callaini G., Glover D.M.;
"SAK/PLK4 is required for centriole duplication and flagella
development.";
Curr. Biol. 15:2199-2207(2005).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-154.
PubMed=16244668; DOI=10.1038/ncb1320;
Habedanck R., Stierhof Y.-D., Wilkinson C.J., Nigg E.A.;
"The Polo kinase Plk4 functions in centriole duplication.";
Nat. Cell Biol. 7:1140-1146(2005).
[9]
INDUCTION BY TP53.
PubMed=15967108; DOI=10.1593/neo.04325;
Li J., Tan M., Li L., Pamarthy D., Lawrence T.S., Sun Y.;
"SAK, a new polo-like kinase, is transcriptionally repressed by p53
and induces apoptosis upon RNAi silencing.";
Neoplasia 7:312-323(2005).
[10]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=17681131; DOI=10.1016/j.devcel.2007.07.002;
Kleylein-Sohn J., Westendorf J., Le Clech M., Habedanck R.,
Stierhof Y.-D., Nigg E.A.;
"Plk4-induced centriole biogenesis in human cells.";
Dev. Cell 13:190-202(2007).
[11]
FUNCTION, AND MUTAGENESIS OF LYS-41 AND THR-170.
PubMed=18239451; DOI=10.4161/cc.7.4.5387;
Bonni S., Ganuelas M.L., Petrinac S., Hudson J.W.;
"Human Plk4 phosphorylates Cdc25C.";
Cell Cycle 7:545-547(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
FUNCTION, AND MUTAGENESIS OF LYS-41 AND THR-170.
PubMed=19164942; DOI=10.4161/cc.8.2.7355;
Petrinac S., Ganuelas M.L., Bonni S., Nantais J., Hudson J.W.;
"Polo-like kinase 4 phosphorylates Chk2.";
Cell Cycle 8:327-329(2009).
[15]
INDUCTION.
PubMed=19454482; DOI=10.1242/jcs.036715;
Kuriyama R., Bettencourt-Dias M., Hoffmann I., Arnold M., Sandvig L.;
"Gamma-tubulin-containing abnormal centrioles are induced by
insufficient Plk4 in human HCT116 colorectal cancer cells.";
J. Cell Sci. 122:2014-2023(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401 AND SER-817, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[17]
INTERACTION WITH CEP152.
PubMed=21059844; DOI=10.1083/jcb.201007107;
Cizmecioglu O., Arnold M., Bahtz R., Settele F., Ehret L.,
Haselmann-Weiss U., Antony C., Hoffmann I.;
"Cep152 acts as a scaffold for recruitment of Plk4 and CPAP to the
centrosome.";
J. Cell Biol. 191:731-739(2010).
[18]
INTERACTION WITH CEP152.
PubMed=20852615; DOI=10.1038/nature09445;
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.;
"Asterless is a scaffold for the onset of centriole assembly.";
Nature 467:714-718(2010).
[19]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=22020124; DOI=10.1038/emboj.2011.378;
Tang C.J., Lin S.Y., Hsu W.B., Lin Y.N., Wu C.T., Lin Y.C.,
Chang C.W., Wu K.S., Tang T.K.;
"The human microcephaly protein STIL interacts with CPAP and is
required for procentriole formation.";
EMBO J. 30:4790-4804(2011).
[20]
FUNCTION IN PHOSPHORYLATION OF FBXW5.
PubMed=21725316; DOI=10.1038/ncb2282;
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.;
"The SCF-FBXW5 E3-ubiquitin ligase is regulated by PLK4 and targets
HsSAS-6 to control centrosome duplication.";
Nat. Cell Biol. 13:1004-1009(2011).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-665, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[22]
INVOLVEMENT IN MCPHCR.
PubMed=25344692; DOI=10.1038/ng.3122;
Martin C.A., Ahmad I., Klingseisen A., Hussain M.S., Bicknell L.S.,
Leitch A., Nuernberg G., Toliat M.R., Murray J.E., Hunt D., Khan F.,
Ali Z., Tinschert S., Ding J., Keith C., Harley M.E., Heyn P.,
Mueller R., Hoffmann I., Daire V.C., Dollfus H., Dupuis L.,
Bashamboo A., McElreavey K., Kariminejad A., Mendoza-Londono R.,
Moore A.T., Saggar A., Schlechter C., Weleber R., Thiele H.,
Altmueller J., Hoehne W., Hurles M.E., Noegel A.A., Baig S.M.,
Nuernberg P., Jackson A.P.;
"Mutations in PLK4, encoding a master regulator of centriole
biogenesis, cause microcephaly, growth failure and retinopathy.";
Nat. Genet. 46:1283-1292(2014).
[23]
INTERACTION WITH CEP78, AND SUBCELLULAR LOCATION.
PubMed=27246242; DOI=10.1242/jcs.184093;
Brunk K., Zhu M., Baerenz F., Kratz A.S., Haselmann-Weiss U.,
Antony C., Hoffmann I.;
"Cep78 is a new centriolar protein involved in Plk4-induced centriole
overduplication.";
J. Cell Sci. 129:2713-2718(2016).
[24]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 2-275.
New York structural genomix research consortium (NYSGXRC);
"Crystal structure of PLK4 kinase.";
Submitted (JUN-2009) to the PDB data bank.
[25]
VARIANTS [LARGE SCALE ANALYSIS] CYS-86; HIS-146; THR-226; THR-232;
LEU-317; ASP-449; SER-519 AND ASP-830.
PubMed=17344846; DOI=10.1038/nature05610;
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., 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.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- 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. Required for the
recruitment of STIL to the centriole and for STIL-mediated
centriole amplification (PubMed:22020124).
{ECO:0000269|PubMed:16244668, ECO:0000269|PubMed:16326102,
ECO:0000269|PubMed:17681131, ECO:0000269|PubMed:18239451,
ECO:0000269|PubMed:19164942, ECO:0000269|PubMed:21725316,
ECO:0000269|PubMed:22020124}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBUNIT: Homodimer (By similarity). Interacts with CEP152 (via N-
terminus). Interacts with CEP78; this interaction may be important
for proper PLK4 localization to the centriole and PLK4-induced
overduplication of centrioles (PubMed:27246242).
{ECO:0000250|UniProtKB:Q64702, ECO:0000269|PubMed:20852615,
ECO:0000269|PubMed:21059844, ECO:0000269|PubMed:27246242}.
-!- INTERACTION:
Self; NbExp=10; IntAct=EBI-746202, EBI-746202;
P36575:ARR3; NbExp=3; IntAct=EBI-746202, EBI-718116;
Q9NX04:C1orf109; NbExp=3; IntAct=EBI-746202, EBI-8643161;
O94986:CEP152; NbExp=5; IntAct=EBI-746202, EBI-311012;
O94986-3:CEP152; NbExp=16; IntAct=EBI-746202, EBI-15878364;
Q8TEP8-3:CEP192; NbExp=13; IntAct=EBI-746202, EBI-16111881;
P59910:DNAJB13; NbExp=4; IntAct=EBI-746202, EBI-11514233;
Q9H8V3:ECT2; NbExp=3; IntAct=EBI-746202, EBI-1054039;
Q14241:ELOA; NbExp=5; IntAct=EBI-746202, EBI-742350;
P31947:SFN; NbExp=2; IntAct=EBI-746202, EBI-476295;
Q96R06:SPAG5; NbExp=4; IntAct=EBI-746202, EBI-413317;
O15060:ZBTB39; NbExp=4; IntAct=EBI-746202, EBI-9995672;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome, centriole
{ECO:0000269|PubMed:22020124, ECO:0000269|PubMed:27246242}.
Nucleus, nucleolus {ECO:0000250}. 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 PubMed:16244668, it is not present at cleavage
furrows.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=O00444-1; Sequence=Displayed;
Name=2;
IsoId=O00444-2; Sequence=VSP_038117;
Note=No experimental confirmation available.;
Name=3;
IsoId=O00444-3; Sequence=VSP_038116;
Note=No experimental confirmation available.;
-!- 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. {ECO:0000269|PubMed:15967108,
ECO:0000269|PubMed:19454482}.
-!- PTM: Ubiquitinated; leading to its degradation by the proteasome.
{ECO:0000250}.
-!- PTM: Tyrosine-phosphorylated by TEC.
{ECO:0000269|PubMed:11489907}.
-!- DISEASE: Microcephaly and chorioretinopathy, autosomal recessive,
2 (MCCRP2) [MIM:616171]: A severe disorder characterized by
microcephaly, delayed psychomotor development, growth retardation
with dwarfism, and ocular abnormalities.
{ECO:0000269|PubMed:25344692}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. CDC5/Polo subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; Y13115; CAA73575.1; -; mRNA.
EMBL; AB006972; BAB69958.1; -; mRNA.
EMBL; AK302858; BAH13823.1; -; mRNA.
EMBL; AK303399; BAH13953.1; -; mRNA.
EMBL; AK314238; BAG36907.1; -; mRNA.
EMBL; BC036023; AAH36023.1; -; mRNA.
CCDS; CCDS3735.1; -. [O00444-1]
CCDS; CCDS54803.1; -. [O00444-2]
CCDS; CCDS54804.1; -. [O00444-3]
RefSeq; NP_001177728.1; NM_001190799.1. [O00444-2]
RefSeq; NP_001177730.1; NM_001190801.1. [O00444-3]
RefSeq; NP_055079.3; NM_014264.4. [O00444-1]
UniGene; Hs.172052; -.
PDB; 2N19; NMR; -; A=884-970.
PDB; 3COK; X-ray; 2.25 A; A/B=2-275.
PDB; 4JXF; X-ray; 2.40 A; A=4-269.
PDB; 4N7V; X-ray; 2.76 A; A/B=580-808.
PDB; 4N7Z; X-ray; 2.85 A; A=580-808.
PDB; 4N9J; X-ray; 2.60 A; A/B=581-808.
PDB; 4YUR; X-ray; 2.65 A; A=2-275.
PDB; 4YYP; X-ray; 2.60 A; A=884-970.
PDB; 5LHY; X-ray; 3.31 A; 1/2/3/4/5/6/7/8/9/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U=884-970.
PDB; 5LHZ; X-ray; 2.51 A; A/B/C=884-970.
PDBsum; 2N19; -.
PDBsum; 3COK; -.
PDBsum; 4JXF; -.
PDBsum; 4N7V; -.
PDBsum; 4N7Z; -.
PDBsum; 4N9J; -.
PDBsum; 4YUR; -.
PDBsum; 4YYP; -.
PDBsum; 5LHY; -.
PDBsum; 5LHZ; -.
ProteinModelPortal; O00444; -.
SMR; O00444; -.
BioGrid; 115956; 52.
DIP; DIP-34467N; -.
IntAct; O00444; 33.
MINT; MINT-1460432; -.
STRING; 9606.ENSP00000270861; -.
BindingDB; O00444; -.
ChEMBL; CHEMBL3788; -.
GuidetoPHARMACOLOGY; 2171; -.
iPTMnet; O00444; -.
PhosphoSitePlus; O00444; -.
BioMuta; PLK4; -.
MaxQB; O00444; -.
PaxDb; O00444; -.
PeptideAtlas; O00444; -.
PRIDE; O00444; -.
DNASU; 10733; -.
Ensembl; ENST00000270861; ENSP00000270861; ENSG00000142731. [O00444-1]
Ensembl; ENST00000513090; ENSP00000427554; ENSG00000142731. [O00444-2]
Ensembl; ENST00000514379; ENSP00000423582; ENSG00000142731. [O00444-3]
GeneID; 10733; -.
KEGG; hsa:10733; -.
UCSC; uc003ifo.4; human. [O00444-1]
CTD; 10733; -.
DisGeNET; 10733; -.
EuPathDB; HostDB:ENSG00000142731.10; -.
GeneCards; PLK4; -.
HGNC; HGNC:11397; PLK4.
HPA; HPA017327; -.
HPA; HPA035026; -.
MalaCards; PLK4; -.
MIM; 605031; gene.
MIM; 616171; phenotype.
neXtProt; NX_O00444; -.
OpenTargets; ENSG00000142731; -.
PharmGKB; PA36205; -.
eggNOG; KOG0575; Eukaryota.
eggNOG; ENOG410XQBP; LUCA.
GeneTree; ENSGT00870000136439; -.
HOVERGEN; HBG053617; -.
InParanoid; O00444; -.
KO; K08863; -.
OMA; GADFEVW; -.
OrthoDB; EOG091G05NQ; -.
PhylomeDB; O00444; -.
TreeFam; TF101090; -.
BRENDA; 2.7.11.21; 2681.
Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
Reactome; R-HSA-8854518; AURKA Activation by TPX2.
SignaLink; O00444; -.
SIGNOR; O00444; -.
EvolutionaryTrace; O00444; -.
GeneWiki; PLK4; -.
GenomeRNAi; 10733; -.
PRO; PR:O00444; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000142731; -.
CleanEx; HS_PLK4; -.
ExpressionAtlas; O00444; baseline and differential.
Genevisible; O00444; HS.
GO; GO:0005814; C:centriole; IDA:UniProtKB.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0098536; C:deuterosome; ISS:UniProtKB.
GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
GO; GO:0001741; C:XY body; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0007099; P:centriole replication; IMP:UniProtKB.
GO; GO:0097711; P:ciliary basal body-plasma membrane docking; TAS:Reactome.
GO; GO:0098535; P:de novo centriole assembly involved in multi-ciliated epithelial cell differentiation; ISS:UniProtKB.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0046601; P:positive regulation of centriole replication; IDA:MGI.
GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0060707; P:trophoblast giant cell differentiation; ISS:UniProtKB.
CDD; cd13114; POLO_box_Plk4_1; 1.
CDD; cd13115; POLO_box_Plk4_2; 1.
CDD; cd13116; POLO_box_Plk4_3; 1.
Gene3D; 3.30.1120.30; -; 1.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR033700; Plk4.
InterPro; IPR000959; POLO_box_dom.
InterPro; IPR036947; POLO_box_dom_sf.
InterPro; IPR033699; POLO_box_Plk4_1.
InterPro; IPR033698; POLO_box_Plk4_2.
InterPro; IPR033696; POLO_box_Plk4_C.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008266; Tyr_kinase_AS.
PANTHER; PTHR24345:SF50; PTHR24345:SF50; 1.
Pfam; PF00069; Pkinase; 1.
Pfam; PF00659; POLO_box; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50078; POLO_BOX; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Complete proteome;
Cytoplasm; Cytoskeleton; Dwarfism; Kinase; Nucleotide-binding;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
Serine/threonine-protein kinase; Transferase; Ubl conjugation.
CHAIN 1 970 Serine/threonine-protein kinase PLK4.
/FTId=PRO_0000086567.
DOMAIN 12 265 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 892 956 POLO box. {ECO:0000255|PROSITE-
ProRule:PRU00154}.
NP_BIND 18 26 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 136 136 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 41 41 ATP. {ECO:0000305}.
MOD_RES 401 401 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195}.
MOD_RES 665 665 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 817 817 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
VAR_SEQ 1 41 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_038116.
VAR_SEQ 43 74 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_038117.
VARIANT 86 86 Y -> C (in dbSNP:rs34156294).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041027.
VARIANT 146 146 R -> H (in dbSNP:rs35232579).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041028.
VARIANT 226 226 A -> T (in dbSNP:rs35448573).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041029.
VARIANT 232 232 S -> T (in dbSNP:rs3811740).
{ECO:0000269|PubMed:11489907,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:17344846,
ECO:0000269|Ref.1}.
/FTId=VAR_019632.
VARIANT 317 317 P -> L (in dbSNP:rs35049837).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041030.
VARIANT 449 449 N -> D (in dbSNP:rs34906574).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041031.
VARIANT 519 519 W -> S (in dbSNP:rs56043017).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041032.
VARIANT 830 830 E -> D (in dbSNP:rs17012739).
{ECO:0000269|PubMed:11489907,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:17344846,
ECO:0000269|Ref.1}.
/FTId=VAR_041033.
MUTAGEN 41 41 K->M: Abolishes ability to phosphorylate
CDC25C and CHEK2.
{ECO:0000269|PubMed:18239451,
ECO:0000269|PubMed:19164942}.
MUTAGEN 154 154 D->A: Catalytically inactive mutant that
causes some centrosome amplification
above background levels when
overexpressed.
{ECO:0000269|PubMed:16244668}.
MUTAGEN 170 170 T->D: Activating mutant.
{ECO:0000269|PubMed:18239451,
ECO:0000269|PubMed:19164942}.
CONFLICT 34 34 T -> S (in Ref. 2; BAB69958).
{ECO:0000305}.
CONFLICT 58 58 Q -> K (in Ref. 1; CAA73575).
{ECO:0000305}.
CONFLICT 333 333 D -> N (in Ref. 3; BAH13823).
{ECO:0000305}.
CONFLICT 387 387 S -> R (in Ref. 2; BAB69958).
{ECO:0000305}.
CONFLICT 692 692 F -> S (in Ref. 3; BAH13823).
{ECO:0000305}.
CONFLICT 696 696 V -> L (in Ref. 2; BAB69958).
{ECO:0000305}.
CONFLICT 768 768 Y -> F (in Ref. 1; CAA73575).
{ECO:0000305}.
CONFLICT 842 842 A -> D (in Ref. 2; BAB69958).
{ECO:0000305}.
HELIX 2 5 {ECO:0000244|PDB:3COK}.
HELIX 9 11 {ECO:0000244|PDB:3COK}.
STRAND 12 20 {ECO:0000244|PDB:3COK}.
STRAND 22 31 {ECO:0000244|PDB:3COK}.
TURN 32 34 {ECO:0000244|PDB:3COK}.
STRAND 37 44 {ECO:0000244|PDB:3COK}.
HELIX 45 50 {ECO:0000244|PDB:3COK}.
HELIX 54 64 {ECO:0000244|PDB:3COK}.
STRAND 75 80 {ECO:0000244|PDB:3COK}.
STRAND 82 90 {ECO:0000244|PDB:3COK}.
HELIX 97 102 {ECO:0000244|PDB:3COK}.
STRAND 104 106 {ECO:0000244|PDB:4JXF}.
HELIX 110 129 {ECO:0000244|PDB:3COK}.
HELIX 139 141 {ECO:0000244|PDB:3COK}.
STRAND 142 144 {ECO:0000244|PDB:3COK}.
STRAND 150 152 {ECO:0000244|PDB:3COK}.
TURN 158 161 {ECO:0000244|PDB:4JXF}.
HELIX 193 206 {ECO:0000244|PDB:3COK}.
HELIX 217 225 {ECO:0000244|PDB:4JXF}.
HELIX 236 245 {ECO:0000244|PDB:3COK}.
HELIX 250 252 {ECO:0000244|PDB:3COK}.
HELIX 256 259 {ECO:0000244|PDB:3COK}.
TURN 263 265 {ECO:0000244|PDB:3COK}.
HELIX 587 590 {ECO:0000244|PDB:4N9J}.
STRAND 602 605 {ECO:0000244|PDB:4N9J}.
STRAND 607 613 {ECO:0000244|PDB:4N9J}.
STRAND 619 627 {ECO:0000244|PDB:4N9J}.
STRAND 630 639 {ECO:0000244|PDB:4N9J}.
STRAND 645 649 {ECO:0000244|PDB:4N9J}.
HELIX 651 654 {ECO:0000244|PDB:4N9J}.
STRAND 671 674 {ECO:0000244|PDB:4N9J}.
HELIX 675 677 {ECO:0000244|PDB:4N9J}.
HELIX 680 682 {ECO:0000244|PDB:4N9J}.
HELIX 683 698 {ECO:0000244|PDB:4N9J}.
STRAND 700 706 {ECO:0000244|PDB:4N9J}.
STRAND 708 716 {ECO:0000244|PDB:4N9J}.
STRAND 723 727 {ECO:0000244|PDB:4N9J}.
STRAND 732 735 {ECO:0000244|PDB:4N9J}.
STRAND 740 743 {ECO:0000244|PDB:4N9J}.
STRAND 749 752 {ECO:0000244|PDB:4N9J}.
HELIX 755 759 {ECO:0000244|PDB:4N9J}.
HELIX 765 793 {ECO:0000244|PDB:4N9J}.
STRAND 800 804 {ECO:0000244|PDB:4N9J}.
STRAND 887 893 {ECO:0000244|PDB:5LHZ}.
TURN 894 896 {ECO:0000244|PDB:5LHZ}.
STRAND 897 902 {ECO:0000244|PDB:5LHZ}.
STRAND 905 911 {ECO:0000244|PDB:5LHZ}.
STRAND 916 922 {ECO:0000244|PDB:5LHZ}.
STRAND 924 929 {ECO:0000244|PDB:5LHZ}.
TURN 931 933 {ECO:0000244|PDB:2N19}.
STRAND 935 939 {ECO:0000244|PDB:5LHZ}.
HELIX 946 961 {ECO:0000244|PDB:5LHZ}.
SEQUENCE 970 AA; 108972 MW; 4D56F5FD983211A6 CRC64;
MATCIGEKIE DFKVGNLLGK GSFAGVYRAE SIHTGLEVAI KMIDKKAMYK AGMVQRVQNE
VKIHCQLKHP SILELYNYFE DSNYVYLVLE MCHNGEMNRY LKNRVKPFSE NEARHFMHQI
ITGMLYLHSH GILHRDLTLS NLLLTRNMNI KIADFGLATQ LKMPHEKHYT LCGTPNYISP
EIATRSAHGL ESDVWSLGCM FYTLLIGRPP FDTDTVKNTL NKVVLADYEM PSFLSIEAKD
LIHQLLRRNP ADRLSLSSVL DHPFMSRNSS TKSKDLGTVE DSIDSGHATI STAITASSST
SISGSLFDKR RLLIGQPLPN KMTVFPKNKS STDFSSSGDG NSFYTQWGNQ ETSNSGRGRV
IQDAEERPHS RYLRRAYSSD RSGTSNSQSQ AKTYTMERCH SAEMLSVSKR SGGGENEERY
SPTDNNANIF NFFKEKTSSS SGSFERPDNN QALSNHLCPG KTPFPFADPT PQTETVQQWF
GNLQINAHLR KTTEYDSISP NRDFQGHPDL QKDTSKNAWT DTKVKKNSDA SDNAHSVKQQ
NTMKYMTALH SKPEIIQQEC VFGSDPLSEQ SKTRGMEPPW GYQNRTLRSI TSPLVAHRLK
PIRQKTKKAV VSILDSEEVC VELVKEYASQ EYVKEVLQIS SDGNTITIYY PNGGRGFPLA
DRPPSPTDNI SRYSFDNLPE KYWRKYQYAS RFVQLVRSKS PKITYFTRYA KCILMENSPG
ADFEVWFYDG VKIHKTEDFI QVIEKTGKSY TLKSESEVNS LKEEIKMYMD HANEGHRICL
ALESIISEEE RKTRSAPFFP IIIGRKPGST SSPKALSPPP SVDSNYPTRE RASFNRMVMH
SAASPTQAPI LNPSMVTNEG LGLTTTASGT DISSNSLKDC LPKSAQLLKS VFVKNVGWAT
QLTSGAVWVQ FNDGSQLVVQ AGVSSISYTS PNGQTTRYGE NEKLPDYIKQ KLQCLSSILL
MFSNPTPNFH


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