PLK3

From Wikipedia, the free encyclopedia

Polo-like kinase 3 (Drosophila)

Identifiers

PLK3; CNK; FNK; PRK

External IDs

OMIM: 602913 MGI: 109604 HomoloGene: 20865

Gene ontology
Molecular Function:	• nucleotide binding • protein serine/threonine kinase activity • protein binding • ATP binding • transferase activity
Biological Process:	• regulation of progression through cell cycle • protein amino acid phosphorylation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_004073 (mRNA)
NP_004064 (protein)

NM_013807 (mRNA)
NP_038835 (protein)

Location

Chr 1: 45.04 - 45.05 Mb

Chr 4: 116.63 - 116.63 Mb

Pubmed search

[1]

[2]

Polo-like kinase 3 (Drosophila), also known as PLK3, is a human gene.^[1]

Cytokine-inducible kinase is a putative serine/threonine kinase. CNK contains both a catalytic domain and a putative regulatory domain. It may play a role in regulation of cell cycle progression and tumorigenesis.^[1]

[edit] References

^ ^a ^b Entrez Gene: PLK3 polo-like kinase 3 (Drosophila).

[edit] Further reading

Li B, Ouyang B, Pan H, et al. (1996). "Prk, a cytokine-inducible human protein serine/threonine kinase whose expression appears to be down-regulated in lung carcinomas.". J. Biol. Chem. 271 (32): 19402–8. PMID 8702627.
Peng CY, Graves PR, Thoma RS, et al. (1997). "Mitotic and G2 checkpoint control: regulation of 14-3-3 protein binding by phosphorylation of Cdc25C on serine-216.". Science 277 (5331): 1501–5. PMID 9278512.
Ouyang B, Pan H, Lu L, et al. (1997). "Human Prk is a conserved protein serine/threonine kinase involved in regulating M phase functions.". J. Biol. Chem. 272 (45): 28646–51. PMID 9353331.
Kauselmann G, Weiler M, Wulff P, et al. (1999). "The polo-like protein kinases Fnk and Snk associate with a Ca(2+)- and integrin-binding protein and are regulated dynamically with synaptic plasticity.". EMBO J. 18 (20): 5528–39. doi:10.1093/emboj/18.20.5528. PMID 10523297.
Ouyang B, Li W, Pan H, et al. (1999). "The physical association and phosphorylation of Cdc25C protein phosphatase by Prk.". Oncogene 18 (44): 6029–36. doi:10.1038/sj.onc.1202983. PMID 10557092.
Shieh SY, Ahn J, Tamai K, et al. (2000). "The human homologs of checkpoint kinases Chk1 and Cds1 (Chk2) phosphorylate p53 at multiple DNA damage-inducible sites.". Genes Dev. 14 (3): 289–300. PMID 10673501.
Dai W, Li Y, Ouyang B, et al. (2000). "PRK, a cell cycle gene localized to 8p21, is downregulated in head and neck cancer.". Genes Chromosomes Cancer 27 (3): 332–6. PMID 10679924.
Matsuoka S, Rotman G, Ogawa A, et al. (2000). "Ataxia telangiectasia-mutated phosphorylates Chk2 in vivo and in vitro.". Proc. Natl. Acad. Sci. U.S.A. 97 (19): 10389–94. doi:10.1073/pnas.190030497. PMID 10973490.
Holtrich U, Wolf G, Yuan J, et al. (2000). "Adhesion induced expression of the serine/threonine kinase Fnk in human macrophages.". Oncogene 19 (42): 4832–9. doi:10.1038/sj.onc.1203845. PMID 11039900.
Bulavin DV, Higashimoto Y, Popoff IJ, et al. (2001). "Initiation of a G2/M checkpoint after ultraviolet radiation requires p38 kinase.". Nature 411 (6833): 102–7. doi:10.1038/35075107. PMID 11333986.
Xie S, Wu H, Wang Q, et al. (2001). "Plk3 functionally links DNA damage to cell cycle arrest and apoptosis at least in part via the p53 pathway.". J. Biol. Chem. 276 (46): 43305–12. doi:10.1074/jbc.M106050200. PMID 11551930.
Latonen L, Taya Y, Laiho M (2001). "UV-radiation induces dose-dependent regulation of p53 response and modulates p53-HDM2 interaction in human fibroblasts.". Oncogene 20 (46): 6784–93. doi:10.1038/sj.onc.1204883. PMID 11709713.
Ahn JY, Li X, Davis HL, Canman CE (2002). "Phosphorylation of threonine 68 promotes oligomerization and autophosphorylation of the Chk2 protein kinase via the forkhead-associated domain.". J. Biol. Chem. 277 (22): 19389–95. doi:10.1074/jbc.M200822200. PMID 11901158.
Sumara I, Vorlaufer E, Stukenberg PT, et al. (2002). "The dissociation of cohesin from chromosomes in prophase is regulated by Polo-like kinase.". Mol. Cell 9 (3): 515–25. PMID 11931760.
Wang Q, Xie S, Chen J, et al. (2002). "Cell cycle arrest and apoptosis induced by human Polo-like kinase 3 is mediated through perturbation of microtubule integrity.". Mol. Cell. Biol. 22 (10): 3450–9. PMID 11971976.
Bahassi el M, Conn CW, Myer DL, et al. (2002). "Mammalian Polo-like kinase 3 (Plk3) is a multifunctional protein involved in stress response pathways.". Oncogene 21 (43): 6633–40. doi:10.1038/sj.onc.1205850. PMID 12242661.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Tsvetkov L, Xu X, Li J, Stern DF (2003). "Polo-like kinase 1 and Chk2 interact and co-localize to centrosomes and the midbody.". J. Biol. Chem. 278 (10): 8468–75. doi:10.1074/jbc.M211202200. PMID 12493754.
Xie S, Wu H, Wang Q, et al. (2003). "Genotoxic stress-induced activation of Plk3 is partly mediated by Chk2.". Cell Cycle 1 (6): 424–9. PMID 12548019.
Bahassi el M, Hennigan RF, Myer DL, Stambrook PJ (2004). "Cdc25C phosphorylation on serine 191 by Plk3 promotes its nuclear translocation.". Oncogene 23 (15): 2658–63. doi:10.1038/sj.onc.1207425. PMID 14968113.