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Mammalian PNK catalyzes the phosphorylation of DNA at 5'-hydroxyl termini and can dephosphorylate its 3'-phosphate termini. It plays an important function in DNA repair following ionizing radiation or oxidative damage. PNK has been reported to participate in the repair of DNA-double strand breaks via PARP-1-dependent nonhomologous end-joining.

The protein encoded by this gene catalyzes the formation of inositol 1,4,5-trisphosphate and diacylglycerol from phosphatidylinositol 4,5-bisphosphate. This reaction uses calcium as a cofactor and plays an important role in the intracellular transduction of receptor-mediated tyrosine kinase activators. For example, when activated by SRC, the encoded protein causes the Ras guanine nucleotide exchange factor RasGRP1 to translocate to the Golgi, where it activates Ras. Also, this protein has bee

The protein encoded by this gene catalyzes the formation of inositol 1,4,5-trisphosphate and diacylglycerol from phosphatidylinositol 4,5-bisphosphate. This reaction uses calcium as a cofactor and plays an important role in the intracellular transduction of receptor-mediated tyrosine kinase activators. For example, when activated by SRC, the encoded protein causes the Ras guanine nucleotide exchange factor RasGRP1 to translocate to the Golgi, where it activates Ras. Also, this protein has bee

Protein-kinase-C-related kinases (PRKs) are part of the lipid-regulated protein kinases (PKC) which also include liver PAK & PKN. Human PRK1 and PRK2 share structurally similar catalytic domains, but less similar N-terminal regulatory regions suggesting different regulatory domain functions. PRK1 and PRK2, as well as a third member of this family, PRK3, show distinct patterns of expression in adult tissues. Additionally, the serine-threonine kinase PRK2 can be specifically cleaved by casp