CLK/STY is a member of the CDC2-like (or LAMMER) family of dual specificity protein kinases. The phosphorylated serine/arginine-rich (SR) proteins involves in the pre-mRNA processing and releasing through nucleus into nucleoplasm. CLK/STY, which could phosphorylates the specific SR proteins, such as ASF/SF2, may directly regulates the activity and compartmentalization of SR splicing factors.
forma física
Supplied in 50 mM Tris-HCl, pH 7.5, with 150 mM NaCl, 0.2 5mM DTT, 0.1 mM EGTA, 0.1 mM EDTA, 0.1 mM PMSF, and 25% glycerol.
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PRECISIO is a registered trademark of Merck KGaA, Darmstadt, Germany
The Journal of biological chemistry, 271(40), 24569-24575 (1996-10-04)
Serine/arginine-rich (SR) proteins are essential for pre-mRNA splicing, and modify the choice of splice site during alternative splicing in a process apparently regulated by protein phosphorylation. Two protein kinases have been cloned that can phosphorylate SR proteins in vitro: SRPK1
Molecular and cellular biology, 23(12), 4139-4149 (2003-05-30)
SR proteins constitute a family of splicing factors that play key roles in both constitutive and regulated splicing in metazoan organisms. The proteins are extensively phosphorylated, and kinases capable of phosphorylating them have been identified. However, little is known about
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