Biology:PKN2

Short description: Protein-coding gene in the species Homo sapiens

Generic protein structure example

Serine/threonine-protein kinase N2 is an enzyme that in humans and Strongylocentrotus purpuratus is encoded by the PKN2 gene.

Interactions

PKN2 has been shown to interact with:

• AKT1,
• NCK1,
• PTPN13,
• Phosphoinositide-dependent kinase-1, and
• RHOA.

Further reading

• "Isolation of a NCK-associated kinase, PRK2, an SH3-binding protein and potential effector of Rho protein signaling". J. Biol. Chem. 271 (46): 28772–28776. 1997. doi:10.1074/jbc.271.46.28772. PMID 8910519. 
• "Isolation and characterization of a structural homologue of human PRK2 from rat liver. Distinguishing substrate and lipid activator specificities". J. Biol. Chem. 272 (15): 10030–10034. 1997. doi:10.1074/jbc.272.15.10030. PMID 9092545. 
• "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. 1997. doi:10.1128/MCB.17.4.2247. PMID 9121475. 
• "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): 29449–29453. 1997. doi:10.1074/jbc.272.47.29449. PMID 9368003. 
• "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): 5542–5549. 1999. doi:10.1074/jbc.274.9.5542. PMID 10026169. 
• "Rho GTPase control of protein kinase C-related protein kinase activation by 3-phosphoinositide-dependent protein kinase". J. Biol. Chem. 275 (15): 11064–11070. 2000. doi:10.1074/jbc.275.15.11064. PMID 10753910. 
• "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): 24421–24428. 2000. doi:10.1074/jbc.M003148200. PMID 10818102. 
• "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): 34451–34458. 2000. doi:10.1074/jbc.M001753200. PMID 10926925. 
• "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): 101–104. 2001. doi:10.1016/S0014-5793(01)02401-2. PMID 11356191. 
• "Regulation of both PDK1 and the phosphorylation of PKC-zeta and -delta by a C-terminal PRK2 fragment". Biochemistry 41 (2): 561–569. 2002. doi:10.1021/bi010719z. PMID 11781095. 
• "The yersinia virulence factor YopM forms a novel protein complex with two cellular kinases". J. Biol. Chem. 278 (20): 18514–18523. 2003. doi:10.1074/jbc.M301226200. PMID 12626518. 
• "The human plasma proteome: a nonredundant list developed by combination of four separate sources". Mol. Cell. Proteomics 3 (4): 311–326. 2004. doi:10.1074/mcp.M300127-MCP200. PMID 14718574. 
• "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–12135. 2004. doi:10.1073/pnas.0404720101. PMID 15302935. Bibcode: 2004PNAS..10112130B. 
• "Screening for cell migration inhibitors via automated microscopy reveals a Rho-kinase inhibitor". Chem. Biol. 12 (3): 385–395. 2005. doi:10.1016/j.chembiol.2005.01.015. PMID 15797222. 
• "Phosphoproteomic analysis of synaptosomes from human cerebral cortex". J. Proteome Res. 4 (2): 306–315. 2005. doi:10.1021/pr0498436. PMID 15822905. 
• "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. 2006. doi:10.1101/gr.4039406. PMID 16344560.