PKN2

From Wikipedia, the free encyclopedia


Protein kinase N2
Identifiers
Symbol(s) PKN2; PAK2; MGC150606; MGC71074; PRK2; PRKCL2; PRO2042; Pak-2
External IDs OMIM: 602549 MGI109211 HomoloGene2054
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 5586 109333
Ensembl ENSG00000065243 ENSMUSG00000004591
Uniprot Q16513 Q3TBR3
Refseq NM_006256 (mRNA)
NP_006247 (protein)
NM_178654 (mRNA)
NP_848769 (protein)
Location Chr 1: 88.92 - 89.07 Mb Chr 3: 142.73 - 142.82 Mb
Pubmed search [1] [2]

Protein kinase N2, also known as PKN2, is a human gene.[1]


[edit] References

[edit] Further reading

  • Palmer RH, Ridden J, Parker PJ (1995). "Cloning and expression patterns of two members of a novel protein-kinase-C-related kinase family.". Eur. J. Biochem. 227 (1-2): 344–51. PMID 7851406. 
  • Palmer RH, Ridden J, Parker PJ (1995). "Identification of multiple, novel, protein kinase C-related gene products.". FEBS Lett. 356 (1): 5–8. PMID 7988719. 
  • Quilliam LA, Lambert QT, Mickelson-Young LA, et al. (1997). "Isolation of a NCK-associated kinase, PRK2, an SH3-binding protein and potential effector of Rho protein signaling.". J. Biol. Chem. 271 (46): 28772–6. PMID 8910519. 
  • Yu W, Liu J, Morrice NA, Wettenhall RE (1997). "Isolation and characterization of a structural homologue of human PRK2 from rat liver. Distinguishing substrate and lipid activator specificities.". J. Biol. Chem. 272 (15): 10030–4. PMID 9092545. 
  • Vincent S, Settleman J (1997). "The PRK2 kinase is a potential effector target of both Rho and Rac GTPases and regulates actin cytoskeletal organization.". Mol. Cell. Biol. 17 (4): 2247–56. PMID 9121475. 
  • Cryns VL, Byun Y, Rana A, et al. (1997). "Specific proteolysis of the kinase protein kinase C-related kinase 2 by caspase-3 during apoptosis. Identification by a novel, small pool expression cloning strategy.". J. Biol. Chem. 272 (47): 29449–53. PMID 9368003. 
  • Braverman LE, Quilliam LA (1999). "Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-containing adapter protein having similar binding and biological properties to Nck.". J. Biol. Chem. 274 (9): 5542–9. PMID 10026169. 
  • Flynn P, Mellor H, Casamassima A, Parker PJ (2000). "Rho GTPase control of protein kinase C-related protein kinase activation by 3-phosphoinositide-dependent protein kinase.". J. Biol. Chem. 275 (15): 11064–70. PMID 10753910. 
  • Sun W, Vincent S, Settleman J, Johnson GL (2000). "MEK kinase 2 binds and activates protein kinase C-related kinase 2. Bifurcation of kinase regulatory pathways at the level of an MAPK kinase kinase.". J. Biol. Chem. 275 (32): 24421–8. doi:10.1074/jbc.M003148200. PMID 10818102. 
  • Koh H, Lee KH, Kim D, et al. (2000). "Inhibition of Akt and its anti-apoptotic activities by tumor necrosis factor-induced protein kinase C-related kinase 2 (PRK2) cleavage.". J. Biol. Chem. 275 (44): 34451–8. doi:10.1074/jbc.M001753200. PMID 10926925. 
  • Gross C, Heumann R, Erdmann KS (2001). "The protein kinase C-related kinase PRK2 interacts with the protein tyrosine phosphatase PTP-BL via a novel PDZ domain binding motif.". FEBS Lett. 496 (2-3): 101–4. PMID 11356191. 
  • Hodgkinson CP, Sale GJ (2002). "Regulation of both PDK1 and the phosphorylation of PKC-zeta and -delta by a C-terminal PRK2 fragment.". Biochemistry 41 (2): 561–9. PMID 11781095. 
  • 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. 
  • McDonald C, Vacratsis PO, Bliska JB, Dixon JE (2003). "The yersinia virulence factor YopM forms a novel protein complex with two cellular kinases.". J. Biol. Chem. 278 (20): 18514–23. doi:10.1074/jbc.M301226200. PMID 12626518. 
  • Anderson NL, Polanski M, Pieper R, et al. (2004). "The human plasma proteome: a nonredundant list developed by combination of four separate sources.". Mol. Cell Proteomics 3 (4): 311–26. doi:10.1074/mcp.M300127-MCP200. PMID 14718574. 
  • Beausoleil SA, Jedrychowski M, Schwartz D, et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins.". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMID 15302935. 
  • Yarrow JC, Totsukawa G, Charras GT, Mitchison TJ (2005). "Screening for cell migration inhibitors via automated microscopy reveals a Rho-kinase inhibitor.". Chem. Biol. 12 (3): 385–95. doi:10.1016/j.chembiol.2005.01.015. PMID 15797222. 
  • DeGiorgis JA, Jaffe H, Moreira JE, et al. (2005). "Phosphoproteomic analysis of synaptosomes from human cerebral cortex.". J. Proteome Res. 4 (2): 306–15. doi:10.1021/pr0498436. PMID 15822905. 
  • Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMID 16344560. 
  • Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1.". Nature 441 (7091): 315–21. doi:10.1038/nature04727. PMID 16710414.