Molecular Characterization of a cDNA Encoding Functional Human CLK4 Kinase and Localization to Chromosome 4q35 |
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| Authors: | J rg Schultz, Tania Jones, Peer Bork, Denise Sheer, Stephanie Blencke, Silvia Steyrer, Ursula Wellbrock, Dorian Bevec, Axel Ullrich,Christian Wallasch |
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| Affiliation: | c Axxima Pharmaceuticals AG, Am Klopferspitz 19, D-82152, Martinsried, Germany;a EMBL, Meyerhofstrasse 1, D-69012, Heidelberg, Germany;b Imperial Cancer Research Fund, Lincoln's Inn Fields, London, WC2A 3PX, United Kingdom;d Max-Planck-Institut für Biochemie, Am Klopferspitz 18A, D-82152, Martinsried, Germany |
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| Abstract: | Phosphorylated serine- and arginine-rich (SR) proteins play an important role in the formation of spliceosomes, possibly controlling the regulation of alternative splicing. Enzymes that phosphorylate the SR proteins belong to the family of CDC2/CDC28-like kinases (CLK). Employing nucleotide sequence comparison of human expressed sequence tag sequences to the murine counterpart, we identified, cloned, and recombinantly expressed the human orthologue to the murine CLK4 cDNA. When fused to glutathione S-transferase, the catalytically active human CLK4 is able to autophosphorylate and to phosphorylate myelin basic protein, but not histone H2B as a substrate. Inspection of mRNA accumulation demonstrated gene expression in all human tissues, with the most prominent abundance in liver, kidney, brain, and heart. Using fluorescence in situ hybridization, the human CLK4 cDNA was localized to band q35 on chromosome 4. |
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