Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Serine/threonine-protein kinase PLK3 (EC 2.7.11.21) (Cytokine-inducible serine/threonine-protein kinase) (FGF-inducible kinase) (Polo-like kinase 3) (PLK-3) (Proliferation-related kinase)

 PLK3_HUMAN              Reviewed;         646 AA.
Q9H4B4; Q15767; Q5JR99; Q96CV1;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
16-AUG-2004, sequence version 2.
25-OCT-2017, entry version 163.
RecName: Full=Serine/threonine-protein kinase PLK3;
EC=2.7.11.21;
AltName: Full=Cytokine-inducible serine/threonine-protein kinase;
AltName: Full=FGF-inducible kinase;
AltName: Full=Polo-like kinase 3;
Short=PLK-3;
AltName: Full=Proliferation-related kinase;
Name=PLK3; Synonyms=CNK, FNK, PRK;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Embryo;
PubMed=11039900; DOI=10.1038/sj.onc.1203845;
Holtrich U., Wolf G., Yuan J., Bereiter-Hahn J., Karn T., Weiler M.,
Kauselmann G., Rehli M., Andreesen R., Kaufmann M., Kuhl D.,
Strebhardt K.;
"Adhesion induced expression of the serine/threonine kinase Fnk in
human macrophages.";
Oncogene 19:4832-4839(2000).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-61; PHE-68;
PHE-283; CYS-483; LEU-498 AND PRO-618.
NIEHS SNPs program;
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASN-491.
TISSUE=Brain;
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 28-646.
TISSUE=Placenta;
PubMed=8702627; DOI=10.1074/jbc.271.32.19402;
Li B., Ouyang B., Pan H., Reissmann P.T., Slamon D.J., Arceci R.,
Lu L., Dai W.;
"Prk, a cytokine-inducible human protein serine/threonine kinase whose
expression appears to be down-regulated in lung carcinomas.";
J. Biol. Chem. 271:19402-19408(1996).
[7]
INDUCTION.
PubMed=11746980; DOI=10.1002/gcc.1204;
Wiest J., Clark A.M., Dai W.;
"Intron/exon organization and polymorphisms of the PLK3/PRK gene in
human lung carcinoma cell lines.";
Genes Chromosomes Cancer 32:384-389(2001).
[8]
FUNCTION IN PHOSPHORYLATION OF TP53 AND CHEK2, AND PHOSPHORYLATION.
PubMed=12242661; DOI=10.1038/sj.onc.1205850;
Bahassi el M., Conn C.W., Myer D.L., Hennigan R.F., McGowan C.H.,
Sanchez Y., Stambrook P.J.;
"Mammalian Polo-like kinase 3 (Plk3) is a multifunctional protein
involved in stress response pathways.";
Oncogene 21:6633-6640(2002).
[9]
FUNCTION.
PubMed=9353331; DOI=10.1074/jbc.272.45.28646;
Ouyang B., Pan H., Lu L., Li J., Stambrook P., Li B., Dai W.;
"Human Prk is a conserved protein serine/threonine kinase involved in
regulating M phase functions.";
J. Biol. Chem. 272:28646-28651(1997).
[10]
FUNCTION.
PubMed=10557092; DOI=10.1038/sj.onc.1202983;
Ouyang B., Li W., Pan H., Meadows J., Hoffmann I., Dai W.;
"The physical association and phosphorylation of Cdc25C protein
phosphatase by Prk.";
Oncogene 18:6029-6036(1999).
[11]
FUNCTION, AND MUTAGENESIS OF ASP-203.
PubMed=11156373;
Conn C.W., Hennigan R.F., Dai W., Sanchez Y., Stambrook P.J.;
"Incomplete cytokinesis and induction of apoptosis by overexpression
of the mammalian polo-like kinase, Plk3.";
Cancer Res. 60:6826-6831(2000).
[12]
FUNCTION IN PHOSPHORYLATION OF TP53, AND MUTAGENESIS OF LYS-91.
PubMed=11447225; DOI=10.1074/jbc.M104157200;
Xie S., Wang Q., Wu H., Cogswell J., Lu L., Jhanwar-Uniyal M., Dai W.;
"Reactive oxygen species-induced phosphorylation of p53 on serine 20
is mediated in part by polo-like kinase-3.";
J. Biol. Chem. 276:36194-36199(2001).
[13]
FUNCTION IN PHOSPHORYLATION OF TP53.
PubMed=11551930; DOI=10.1074/jbc.M106050200;
Xie S., Wu H., Wang Q., Cogswell J.P., Husain I., Conn C.,
Stambrook P., Jhanwar-Uniyal M., Dai W.;
"Plk3 functionally links DNA damage to cell cycle arrest and apoptosis
at least in part via the p53 pathway.";
J. Biol. Chem. 276:43305-43312(2001).
[14]
FUNCTION.
PubMed=11971976; DOI=10.1128/MCB.22.10.3450-3459.2002;
Wang Q., Xie S., Chen J., Fukasawa K., Naik U., Traganos F.,
Darzynkiewicz Z., Jhanwar-Uniyal M., Dai W.;
"Cell cycle arrest and apoptosis induced by human Polo-like kinase 3
is mediated through perturbation of microtubule integrity.";
Mol. Cell. Biol. 22:3450-3459(2002).
[15]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH GOLGB1, AND
MUTAGENESIS OF LYS-91.
PubMed=14980500; DOI=10.1016/j.yexcr.2003.10.022;
Ruan Q., Wang Q., Xie S., Fang Y., Darzynkiewicz Z., Guan K.,
Jhanwar-Uniyal M., Dai W.;
"Polo-like kinase 3 is Golgi localized and involved in regulating
Golgi fragmentation during the cell cycle.";
Exp. Cell Res. 294:51-59(2004).
[16]
FUNCTION IN PHOSPHORYLATION OF CDC25C.
PubMed=14968113; DOI=10.1038/sj.onc.1207425;
Bahassi el M., Hennigan R.F., Myer D.L., Stambrook P.J.;
"Cdc25C phosphorylation on serine 191 by Plk3 promotes its nuclear
translocation.";
Oncogene 23:2658-2663(2004).
[17]
FUNCTION.
PubMed=15021912; DOI=10.1038/sj.onc.1207479;
Xie S., Wang Q., Ruan Q., Liu T., Jhanwar-Uniyal M., Guan K., Dai W.;
"MEK1-induced Golgi dynamics during cell cycle progression is partly
mediated by Polo-like kinase-3.";
Oncogene 23:3822-3829(2004).
[18]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF THR-219 AND
467-TRP-VAL-468.
PubMed=16478733; DOI=10.1074/jbc.M513156200;
Jiang N., Wang X., Jhanwar-Uniyal M., Darzynkiewicz Z., Dai W.;
"Polo box domain of Plk3 functions as a centrosome localization
signal, overexpression of which causes mitotic arrest, cytokinesis
defects, and apoptosis.";
J. Biol. Chem. 281:10577-10582(2006).
[19]
FUNCTION IN PHOSPHORYLATION OF TP53 AND CHEK2.
PubMed=16481012; DOI=10.1016/j.mrfmmm.2005.12.002;
Bahassi el M., Myer D.L., McKenney R.J., Hennigan R.F.,
Stambrook P.J.;
"Priming phosphorylation of Chk2 by polo-like kinase 3 (Plk3) mediates
its full activation by ATM and a downstream checkpoint in response to
DNA damage.";
Mutat. Res. 596:166-176(2006).
[20]
FUNCTION IN PHOSPHORYLATION OF JUN, AND MUTAGENESIS OF LYS-91.
PubMed=17804415; DOI=10.1074/jbc.M702791200;
Wang L., Dai W., Lu L.;
"Stress-induced c-Jun activation mediated by Polo-like kinase 3 in
corneal epithelial cells.";
J. Biol. Chem. 282:32121-32127(2007).
[21]
FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=17264206; DOI=10.1073/pnas.0610856104;
Zimmerman W.C., Erikson R.L.;
"Polo-like kinase 3 is required for entry into S phase.";
Proc. Natl. Acad. Sci. U.S.A. 104:1847-1852(2007).
[22]
FUNCTION IN PHOSPHORYLATION OF TOP2A.
PubMed=18062778; DOI=10.1042/BJ20071394;
Iida M., Matsuda M., Komatani H.;
"Plk3 phosphorylates topoisomerase IIalpha at Thr(1342), a site that
is not recognized by Plk1.";
Biochem. J. 411:27-32(2008).
[23]
FUNCTION IN PHOSPHORYLATION OF JUN, AND SUBCELLULAR LOCATION.
PubMed=18650425; DOI=10.1074/jbc.M801326200;
Wang L., Gao J., Dai W., Lu L.;
"Activation of Polo-like kinase 3 by hypoxic stresses.";
J. Biol. Chem. 283:25928-25935(2008).
[24]
FUNCTION IN PHOSPHORYLATION OF TP73, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF LYS-91.
PubMed=19490146; DOI=10.1111/j.1365-2443.2009.01309.x;
Sang M., Ando K., Okoshi R., Koida N., Li Y., Zhu Y., Shimozato O.,
Geng C., Shan B., Nakagawara A., Ozaki T.;
"Plk3 inhibits pro-apoptotic activity of p73 through physical
interaction and phosphorylation.";
Genes Cells 14:775-788(2009).
[25]
FUNCTION IN PHOSPHORYLATION OF VRK1, AND MUTAGENESIS OF LYS-91.
PubMed=19103756; DOI=10.1128/MCB.01341-08;
Lopez-Sanchez I., Sanz-Garcia M., Lazo P.A.;
"Plk3 interacts with and specifically phosphorylates VRK1 in Ser342, a
downstream target in a pathway that induces Golgi fragmentation.";
Mol. Cell. Biol. 29:1189-1201(2009).
[26]
FUNCTION IN PHOSPHORYLATION OF HIF1A, AND MUTAGENESIS OF LYS-91.
PubMed=20889502; DOI=10.1074/jbc.M110.160325;
Xu D., Yao Y., Lu L., Costa M., Dai W.;
"Plk3 functions as an essential component of the hypoxia regulatory
pathway by direct phosphorylation of HIF-1alpha.";
J. Biol. Chem. 285:38944-38950(2010).
[27]
FUNCTION IN PHOSPHORYLATION OF PTEN, AND MUTAGENESIS OF LYS-91.
PubMed=20940307; DOI=10.1074/jbc.M110.166462;
Xu D., Yao Y., Jiang X., Lu L., Dai W.;
"Regulation of PTEN stability and activity by Plk3.";
J. Biol. Chem. 285:39935-39942(2010).
[28]
FUNCTION, INTERACTION WITH CIB1, AND SUBCELLULAR LOCATION.
PubMed=20951827; DOI=10.1016/j.biocel.2010.10.003;
Naik M.U., Naik U.P.;
"Calcium- and integrin-binding protein 1 regulates microtubule
organization and centrosome segregation through polo like kinase 3
during cell cycle progression.";
Int. J. Biochem. Cell Biol. 43:120-129(2011).
[29]
INTERACTION WITH CIB1.
PubMed=20473878; DOI=10.1002/ijc.25388;
Naik M.U., Pham N.T., Beebe K., Dai W., Naik U.P.;
"Calcium-dependent inhibition of polo-like kinase 3 activity by CIB1
in breast cancer cells.";
Int. J. Cancer 128:587-596(2011).
[30]
FUNCTION IN PHOSPHORYLATION OF ATF2, AND SUBCELLULAR LOCATION.
PubMed=21098032; DOI=10.1074/jbc.M110.166009;
Wang L., Payton R., Dai W., Lu L.;
"Hyperosmotic stress-induced ATF-2 activation through Polo-like kinase
3 in human corneal epithelial cells.";
J. Biol. Chem. 286:1951-1958(2011).
[31]
FUNCTION IN PHOSPHORYLATION OF BCL2L1.
PubMed=21840391; DOI=10.1016/j.cellsig.2011.07.017;
Wang J., Beauchemin M., Bertrand R.;
"Bcl-xL phosphorylation at Ser49 by polo kinase 3 during cell cycle
progression and checkpoints.";
Cell. Signal. 23:2030-2038(2011).
[32]
FUNCTION IN PHOSPHORYLATION OF CDC25A.
PubMed=21376736; DOI=10.1016/j.mrfmmm.2011.02.006;
Myer D.L., Robbins S.B., Yin M., Boivin G.P., Liu Y., Greis K.D.,
Bahassi el M., Stambrook P.J.;
"Absence of polo-like kinase 3 in mice stabilizes Cdc25A after DNA
damage but is not sufficient to produce tumors.";
Mutat. Res. 714:1-10(2011).
[33]
FUNCTION, AND INTERACTION WITH CIB1.
PubMed=21264284; DOI=10.1371/journal.pone.0014513;
Kostyak J.C., Naik U.P.;
"Calcium- and integrin-binding protein 1 regulates endomitosis and its
interaction with Polo-like kinase 3 is enhanced in endomitotic Dami
cells.";
PLoS ONE 6:E14513-E14513(2011).
[34]
REVIEW ON FUNCTION.
PubMed=20671765; DOI=10.1038/nrd3184;
Strebhardt K.;
"Multifaceted polo-like kinases: drug targets and antitargets for
cancer therapy.";
Nat. Rev. Drug Discov. 9:643-660(2010).
-!- FUNCTION: Serine/threonine-protein kinase involved in cell cycle
regulation, response to stress and Golgi disassembly. Polo-like
kinases act by binding and phosphorylating proteins are that
already phosphorylated on a specific motif recognized by the POLO
box domains. Phosphorylates ATF2, BCL2L1, CDC25A, CDC25C, CHEK2,
HIF1A, JUN, p53/TP53, p73/TP73, PTEN, TOP2A and VRK1. Involved in
cell cycle regulation: required for entry into S phase and
cytokinesis. Phosphorylates BCL2L1, leading to regulate the G2
checkpoint and progression to cytokinesis during mitosis. Plays a
key role in response to stress: rapidly activated upon stress
stimulation, such as ionizing radiation, reactive oxygen species
(ROS), hyperosmotic stress, UV irradiation and hypoxia. Involved
in DNA damage response and G1/S transition checkpoint by
phosphorylating CDC25A, p53/TP53 and p73/TP73. Phosphorylates
p53/TP53 in response to reactive oxygen species (ROS), thereby
promoting p53/TP53-mediated apoptosis. Phosphorylates CHEK2 in
response to DNA damage, promoting the G2/M transition checkpoint.
Phosphorylates the transcription factor p73/TP73 in response to
DNA damage, leading to inhibit p73/TP73-mediated transcriptional
activation and pro-apoptotic functions. Phosphorylates HIF1A and
JUN is response to hypoxia. Phosphorylates ATF2 following
hyperosmotic stress in corneal epithelium. Also involved in Golgi
disassembly during the cell cycle: part of a MEK1/MAP2K1-dependent
pathway that induces Golgi fragmentation during mitosis by
mediating phosphorylation of VRK1. May participate in endomitotic
cell cycle, a form of mitosis in which both karyokinesis and
cytokinesis are interrupted and is a hallmark of megakaryocyte
differentiation, via its interaction with CIB1.
{ECO:0000269|PubMed:10557092, ECO:0000269|PubMed:11156373,
ECO:0000269|PubMed:11447225, ECO:0000269|PubMed:11551930,
ECO:0000269|PubMed:11971976, ECO:0000269|PubMed:12242661,
ECO:0000269|PubMed:14968113, ECO:0000269|PubMed:14980500,
ECO:0000269|PubMed:15021912, ECO:0000269|PubMed:16478733,
ECO:0000269|PubMed:16481012, ECO:0000269|PubMed:17264206,
ECO:0000269|PubMed:17804415, ECO:0000269|PubMed:18062778,
ECO:0000269|PubMed:18650425, ECO:0000269|PubMed:19103756,
ECO:0000269|PubMed:19490146, ECO:0000269|PubMed:20889502,
ECO:0000269|PubMed:20940307, ECO:0000269|PubMed:20951827,
ECO:0000269|PubMed:21098032, ECO:0000269|PubMed:21264284,
ECO:0000269|PubMed:21376736, ECO:0000269|PubMed:21840391,
ECO:0000269|PubMed:9353331}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBUNIT: Interacts (via the POLO-box domain) with CIB1; leading to
inhibit PLK3 kinase activity. Interacts with GOLGB1.
{ECO:0000269|PubMed:14980500, ECO:0000269|PubMed:20473878,
ECO:0000269|PubMed:20951827, ECO:0000269|PubMed:21264284}.
-!- INTERACTION:
P14859:POU2F1; NbExp=3; IntAct=EBI-751877, EBI-624770;
P04156:PRNP; NbExp=4; IntAct=EBI-751877, EBI-977302;
Q99986:VRK1; NbExp=12; IntAct=EBI-751877, EBI-1769146;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, nucleolus.
Golgi apparatus. Cytoplasm, cytoskeleton, microtubule organizing
center, centrosome. Note=Translocates to the nucleus upon
cisplatin treatment. Localizes to the Golgi apparatus during
interphase. According to a report, PLK3 localizes only in the
nucleolus and not in the centrosome, or in any other location in
the cytoplasm (PubMed:17264206). The discrepancies in results may
be explained by the PLK3 antibody specificity, by cell line-
specific expression or post-translational modifications.
{ECO:0000269|PubMed:17264206}.
-!- TISSUE SPECIFICITY: Transcripts are highly detected in placenta,
lung, followed by skeletal muscle, heart, pancreas, ovaries and
kidney and weakly detected in liver and brain. May have a short
half-live. In cells of hematopoietic origin, strongly and
exclusively detected in terminally differentiated macrophages.
Transcript expression appears to be down-regulated in primary lung
tumor.
-!- DEVELOPMENTAL STAGE: Expression is cell cycle regulated with a
peak in G1 phase. {ECO:0000269|PubMed:17264206}.
-!- INDUCTION: Cytokine and cellular adhesion trigger induction. Down-
regulated in a majority of lung carcinoma samples.
{ECO:0000269|PubMed:11746980}.
-!- DOMAIN: The POLO box domains act as phosphopeptide-binding module
that recognize and bind serine-[phosphothreonine/phosphoserine]-
(proline/X) motifs. PLK3 recognizes and binds docking proteins
that are already phosphorylated on these motifs, and then
phosphorylates them (By similarity). The POLO box domains mediates
localization to the centrosome. {ECO:0000250}.
-!- PTM: Phosphorylated in an ATM-dependent manner following DNA
damage. Phosphorylated as cells enter mitosis and dephosphorylated
as cells exit mitosis. {ECO:0000269|PubMed:12242661}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. CDC5/Polo subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-!- SEQUENCE CAUTION:
Sequence=AAC50637.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/plk3/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AJ293866; CAC10659.1; -; mRNA.
EMBL; AY764184; AAU88146.1; -; Genomic_DNA.
EMBL; AL592166; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471059; EAX07021.1; -; Genomic_DNA.
EMBL; BC013899; AAH13899.1; -; mRNA.
EMBL; U56998; AAC50637.1; ALT_INIT; mRNA.
CCDS; CCDS515.1; -.
RefSeq; NP_004064.2; NM_004073.3.
UniGene; Hs.632415; -.
PDB; 4B6L; X-ray; 1.90 A; A=52-332.
PDBsum; 4B6L; -.
ProteinModelPortal; Q9H4B4; -.
SMR; Q9H4B4; -.
BioGrid; 107663; 13.
IntAct; Q9H4B4; 8.
MINT; MINT-110679; -.
STRING; 9606.ENSP00000361275; -.
BindingDB; Q9H4B4; -.
ChEMBL; CHEMBL4897; -.
GuidetoPHARMACOLOGY; 2170; -.
iPTMnet; Q9H4B4; -.
PhosphoSitePlus; Q9H4B4; -.
BioMuta; PLK3; -.
DMDM; 51338822; -.
MaxQB; Q9H4B4; -.
PaxDb; Q9H4B4; -.
PeptideAtlas; Q9H4B4; -.
PRIDE; Q9H4B4; -.
DNASU; 1263; -.
Ensembl; ENST00000372201; ENSP00000361275; ENSG00000173846.
GeneID; 1263; -.
KEGG; hsa:1263; -.
UCSC; uc001cmn.4; human.
CTD; 1263; -.
DisGeNET; 1263; -.
EuPathDB; HostDB:ENSG00000173846.12; -.
GeneCards; PLK3; -.
H-InvDB; HIX0199969; -.
HGNC; HGNC:2154; PLK3.
HPA; HPA060318; -.
MIM; 602913; gene.
neXtProt; NX_Q9H4B4; -.
OpenTargets; ENSG00000173846; -.
PharmGKB; PA26664; -.
eggNOG; KOG0575; Eukaryota.
eggNOG; ENOG410XQBP; LUCA.
GeneTree; ENSGT00530000062954; -.
HOGENOM; HOG000248546; -.
HOVERGEN; HBG001843; -.
InParanoid; Q9H4B4; -.
KO; K08862; -.
OMA; LCALRNC; -.
OrthoDB; EOG091G0D89; -.
PhylomeDB; Q9H4B4; -.
TreeFam; TF101089; -.
BRENDA; 2.7.11.21; 2681.
Reactome; R-HSA-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
SignaLink; Q9H4B4; -.
SIGNOR; Q9H4B4; -.
ChiTaRS; PLK3; human.
GeneWiki; PLK3; -.
GenomeRNAi; 1263; -.
PRO; PR:Q9H4B4; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000173846; -.
CleanEx; HS_PLK3; -.
Genevisible; Q9H4B4; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0005795; C:Golgi stack; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0002039; F:p53 binding; IDA:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; TAS:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0031122; P:cytoplasmic microtubule organization; IMP:UniProtKB.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
GO; GO:0007113; P:endomitotic cell cycle; TAS:UniProtKB.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:UniProtKB.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:UniProtKB.
GO; GO:0090166; P:Golgi disassembly; IDA:UniProtKB.
GO; GO:0007093; P:mitotic cell cycle checkpoint; TAS:UniProtKB.
GO; GO:0044819; P:mitotic G1/S transition checkpoint; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:1904716; P:positive regulation of chaperone-mediated autophagy; IDA:ParkinsonsUK-UCL.
GO; GO:0090316; P:positive regulation of intracellular protein transport; IMP:UniProtKB.
GO; GO:2000777; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process involved in cellular response to hypoxia; IDA:UniProtKB.
GO; GO:0043491; P:protein kinase B signaling; ISS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
GO; GO:0051302; P:regulation of cell division; IDA:UniProtKB.
GO; GO:0032465; P:regulation of cytokinesis; IMP:UniProtKB.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0006970; P:response to osmotic stress; IDA:UniProtKB.
GO; GO:0009314; P:response to radiation; IDA:UniProtKB.
GO; GO:0000302; P:response to reactive oxygen species; IDA:UniProtKB.
CDD; cd13118; POLO_box_1; 1.
CDD; cd13117; POLO_box_2; 1.
Gene3D; 3.30.1120.30; -; 2.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR033701; POLO_box_1.
InterPro; IPR033695; POLO_box_2.
InterPro; IPR000959; POLO_box_dom.
InterPro; IPR036947; POLO_box_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR020658; Ser/Thr_kinase_Plk3.
PANTHER; PTHR24345:SF42; PTHR24345:SF42; 1.
Pfam; PF00069; Pkinase; 1.
Pfam; PF00659; POLO_box; 2.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50078; POLO_BOX; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Apoptosis; ATP-binding; Cell cycle; Complete proteome;
Cytoplasm; Cytoskeleton; DNA damage; Golgi apparatus; Kinase;
Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Serine/threonine-protein kinase;
Transferase.
CHAIN 1 646 Serine/threonine-protein kinase PLK3.
/FTId=PRO_0000086564.
DOMAIN 62 314 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 470 537 POLO box 1. {ECO:0000255|PROSITE-
ProRule:PRU00154}.
DOMAIN 567 637 POLO box 2. {ECO:0000255|PROSITE-
ProRule:PRU00154}.
NP_BIND 68 76 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 185 185 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 91 91 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
VARIANT 61 61 T -> S (in dbSNP:rs17884581).
{ECO:0000269|Ref.2}.
/FTId=VAR_021091.
VARIANT 68 68 L -> F (in dbSNP:rs17884316).
{ECO:0000269|Ref.2}.
/FTId=VAR_021092.
VARIANT 283 283 L -> F (in dbSNP:rs17880471).
{ECO:0000269|Ref.2}.
/FTId=VAR_021093.
VARIANT 483 483 R -> C (in dbSNP:rs17884653).
{ECO:0000269|Ref.2}.
/FTId=VAR_021094.
VARIANT 491 491 D -> N (in dbSNP:rs17855444).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_062384.
VARIANT 498 498 S -> L (in dbSNP:rs17880829).
{ECO:0000269|Ref.2}.
/FTId=VAR_021095.
VARIANT 618 618 S -> P (in dbSNP:rs17881786).
{ECO:0000269|Ref.2}.
/FTId=VAR_021096.
MUTAGEN 91 91 K->R: Kinase defective mutant, abolishes
activity. {ECO:0000269|PubMed:11447225,
ECO:0000269|PubMed:14980500,
ECO:0000269|PubMed:17804415,
ECO:0000269|PubMed:19103756,
ECO:0000269|PubMed:19490146,
ECO:0000269|PubMed:20889502,
ECO:0000269|PubMed:20940307}.
MUTAGEN 203 203 D->A: Kinase defective mutant, abolishes
activity. {ECO:0000269|PubMed:11156373}.
MUTAGEN 219 219 T->E: Kinase-defective mutant.
{ECO:0000269|PubMed:16478733}.
MUTAGEN 467 468 WV->FA: Abolishes localization to the
centrosome and ability to induce the G2/M
arrest. {ECO:0000269|PubMed:16478733}.
CONFLICT 16 16 A -> T (in Ref. 1; CAC10659).
{ECO:0000305}.
CONFLICT 20 20 P -> T (in Ref. 1; CAC10659).
{ECO:0000305}.
CONFLICT 99 99 A -> V (in Ref. 1; CAC10659).
{ECO:0000305}.
CONFLICT 353 353 G -> V (in Ref. 1; CAC10659).
{ECO:0000305}.
CONFLICT 419 419 D -> H (in Ref. 1; CAC10659).
{ECO:0000305}.
CONFLICT 464 470 VSKWVDY -> FSEWVGF (in Ref. 1; CAC10659).
{ECO:0000305}.
CONFLICT 522 522 P -> R (in Ref. 1; CAC10659).
{ECO:0000305}.
STRAND 62 69 {ECO:0000244|PDB:4B6L}.
STRAND 75 81 {ECO:0000244|PDB:4B6L}.
TURN 82 84 {ECO:0000244|PDB:4B6L}.
STRAND 87 94 {ECO:0000244|PDB:4B6L}.
HELIX 95 98 {ECO:0000244|PDB:4B6L}.
HELIX 101 114 {ECO:0000244|PDB:4B6L}.
STRAND 125 130 {ECO:0000244|PDB:4B6L}.
STRAND 132 139 {ECO:0000244|PDB:4B6L}.
HELIX 147 154 {ECO:0000244|PDB:4B6L}.
HELIX 159 178 {ECO:0000244|PDB:4B6L}.
HELIX 188 190 {ECO:0000244|PDB:4B6L}.
STRAND 191 193 {ECO:0000244|PDB:4B6L}.
STRAND 199 201 {ECO:0000244|PDB:4B6L}.
TURN 213 215 {ECO:0000244|PDB:4B6L}.
TURN 224 226 {ECO:0000244|PDB:4B6L}.
HELIX 229 232 {ECO:0000244|PDB:4B6L}.
HELIX 239 255 {ECO:0000244|PDB:4B6L}.
HELIX 265 273 {ECO:0000244|PDB:4B6L}.
HELIX 285 294 {ECO:0000244|PDB:4B6L}.
HELIX 299 301 {ECO:0000244|PDB:4B6L}.
HELIX 305 309 {ECO:0000244|PDB:4B6L}.
HELIX 312 315 {ECO:0000244|PDB:4B6L}.
HELIX 325 328 {ECO:0000244|PDB:4B6L}.
SEQUENCE 646 AA; 71629 MW; 324CA3E9DE482514 CRC64;
MEPAAGFLSP RPFQRAAAAP APPAGPGPPP SALRGPELEM LAGLPTSDPG RLITDPRSGR
TYLKGRLLGK GGFARCYEAT DTETGSAYAV KVIPQSRVAK PHQREKILNE IELHRDLQHR
HIVRFSHHFE DADNIYIFLE LCSRKSLAHI WKARHTLLEP EVRYYLRQIL SGLKYLHQRG
ILHRDLKLGN FFITENMELK VGDFGLAARL EPPEQRKKTI CGTPNYVAPE VLLRQGHGPE
ADVWSLGCVM YTLLCGSPPF ETADLKETYR CIKQVHYTLP ASLSLPARQL LAAILRASPR
DRPSIDQILR HDFFTKGYTP DRLPISSCVT VPDLTPPNPA RSLFAKVTKS LFGRKKKSKN
HAQERDEVSG LVSGLMRTSV GHQDARPEAP AASGPAPVSL VETAPEDSSP RGTLASSGDG
FEEGLTVATV VESALCALRN CIAFMPPAEQ NPAPLAQPEP LVWVSKWVDY SNKFGFGYQL
SSRRVAVLFN DGTHMALSAN RKTVHYNPTS TKHFSFSVGA VPRALQPQLG ILRYFASYME
QHLMKGGDLP SVEEVEVPAP PLLLQWVKTD QALLMLFSDG TVQVNFYGDH TKLILSGWEP
LLVTFVARNR SACTYLASHL RQLGCSPDLR QRLRYALRLL RDRSPA


Related products :

Catalog number Product name Quantity
EIAAB31531 CNK,Cytokine-inducible serine_threonine-protein kinase,FGF-inducible kinase,FNK,Homo sapiens,Human,PLK3,PLK-3,Polo-like kinase 3,PRK,Proliferation-related kinase,Serine_threonine-protein kinase PLK3
EIAAB31334 Bos taurus,Bovine,PKN,PKN1,PRK1,PRKCL1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein kinase PKN-alpha,Protein-kinase C-related kinase 1,Serine_threonine-protein kinase N1,Serine-threonine
EIAAB31533 Cnk,Cytokine-inducible serine_threonine-protein kinase,FGF-inducible kinase,Fnk,Mouse,Mus musculus,Plk3,PLK-3,Polo-like kinase 3,Serine_threonine-protein kinase PLK3
EIAAB31532 Cnk,Cytokine-inducible serine_threonine-protein kinase,FGF-inducible kinase,Fnk,Plk3,PLK-3,Polo-like kinase 3,Rat,Rattus norvegicus,Serine_threonine-protein kinase PLK3
EIAAB31332 Mouse,Mus musculus,Pkn,Pkn1,Prk1,Prkcl1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein-kinase C-related kinase 1,Serine_threonine-protein kinase N1,Serine-threonine protein kinase N
GWB-CEE83D Serine threonine-protein kinase SNF1-like kinase 2 (SNF1LK2) Salt-inducible protein kinase 2 (SIK2) Rabbit anti-Human Polyclonal
GWB-5BE1E2 Serine threonine-protein kinase SNF1-like kinase 2 (SNF1LK2) Salt-inducible protein kinase 2 (SIK2) Mouse anti-Human Monoclonal
H0304 Serine threonine-protein kinase PLK3 (PLK3), Human, ELISA Kit 96T
H0305 Serine threonine-protein kinase PLK3 (PLK3), Mouse, ELISA Kit 96T
H0306 Serine threonine-protein kinase PLK3 (PLK3), Rat, ELISA Kit 96T
PLK3_RAT ELISA Kit FOR Serine per threonine-protein kinase PLK3; organism: Rat; gene name: Plk3 96T
PLK3_MOUSE ELISA Kit FOR Serine per threonine-protein kinase PLK3; organism: Mouse; gene name: Plk3 96T
EIAAB24784 GCK family kinase MiNK,Map4k6,MAPK_ERK kinase kinase kinase 6,MEK kinase kinase 6,MEKKK 6,Mink,Mink1,Misshapen_NIK-related kinase,Misshapen-like kinase 1,Mitogen-activated protein kinase kinase kinase
EIAAB24783 GCK family kinase MiNK,Map4k6,MAPK_ERK kinase kinase kinase 6,MEK kinase kinase 6,MEKKK 6,Mink,Mink1,Misshapen_NIK-related kinase,Misshapen-like kinase 1,Mitogen-activated protein kinase kinase kinase
PLK3_RAT Rat ELISA Kit FOR Serine per threonine-protein kinase PLK3 96T
MKNK1_RAT Rat ELISA Kit FOR MAP kinase-interacting serine per threonine-protein kinase 1 96T
31-031 Cdk7 is the catalytic subunit of the CDK-activating kinase (CAK) complex, a serine-threonine kinase. CAK activates the cyclin-associated kinases CDC2_CDK1, CDK2, CDK4 and CDK6 by threonine phosphoryla 0.1 mg
MKNK1_MOUSE ELISA Kit FOR MAP kinase-interacting serine per threonine-protein kinase 1; organism: Mouse; gene name: Mknk1 96T
MKNK2_MOUSE ELISA Kit FOR MAP kinase-interacting serine per threonine-protein kinase 2; organism: Mouse; gene name: Mknk2 96T
EIAAB25239 C-JUN N-terminal kinase kinase 1,Dual specificity mitogen-activated protein kinase kinase 4,JNK kinase 1,JNK-activating kinase 1,JNKK 1,Jnkk1,MAP kinase kinase 4,Map2k4,MAPK_ERK kinase 4,MAPKK 4,MEK 4
EIAAB25244 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,JNK kinase 2,JNK-activating kinase 2,JNKK 2,MAP kinase kinase 7,Map2k7,MAPK_ERK kinase 7,MAPKK 7,MEK 7,Mkk7,
EIAAB25245 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,JNK kinase 2,JNK-activating kinase 2,JNKK 2,MAP kinase kinase 7,Map2k7,MAPK_ERK kinase 7,MAPKK 7,MEK 7,Rat,R
EIAAB31528 Homo sapiens,Human,PLK2,PLK-2,Polo-like kinase 2,Serine_threonine-protein kinase PLK2,Serine_threonine-protein kinase SNK,Serum-inducible kinase,SNK
SNRK_RAT Rat ELISA Kit FOR SNF-related serine per threonine-protein kinase 96T
EIAAB31530 Plk2,PLK-2,Polo-like kinase 2,Rat,Rattus norvegicus,Serine_threonine-protein kinase PLK2,Serine_threonine-protein kinase SNK,Serum-inducible kinase,Snk


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur