Dual specificity protein kinase CLK3 is an enzyme that in humans is encoded by the CLK3gene.[1][2]
The CLK3 gene encodes a serine/threonine type proteinkinase with a non-conserved N-terminaldomain. A long and short isoform (phclk3 and pclk3/152) result from alternative splicing and coexist in different tissues. Isoform phclk3/152 lacks the kinase domain.[3]
References
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↑Talmadge CB, Finkernagel S, Sumegi J, Sciorra L, Rabinow L (Dec 1998). "Chromosomal mapping of three human LAMMER protein-kinase-encoding genes". Hum Genet. 103 (4): 523–4. doi:10.1007/s004390050861. PMID9856501.
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Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID9373149.
Duncan PI, Stojdl DF, Marius RM, et al. (1998). "The Clk2 and Clk3 dual-specificity protein kinases regulate the intranuclear distribution of SR proteins and influence pre-mRNA splicing". Exp. Cell Res. 241 (2): 300–8. doi:10.1006/excr.1998.4083. PMID9637771.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID14702039.
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Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID16189514.
Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID17081983.
Wissing J, Jänsch L, Nimtz M, et al. (2007). "Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry". Mol. Cell. Proteomics. 6 (3): 537–47. doi:10.1074/mcp.T600062-MCP200. PMID17192257.
