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CSK is a tyrosine kinase that has been shown to downregulate the activity of SRC oncoprotein through phosphorylation of its carboxy terminus. Since cell transformation by SRC is caused by various mechanisms that interfere with this phosphorylation, the CSK gene might function as an antioncogene. CSK plays an important role in the regulation of cell growth, differentiation, migration, and immune responses. CSK phosphorylates tyrosine residues located in the C-terminal tails of Src-family kinases including LCK, SRC, HCK, FYN, LYN, CSK, and YES1. CSK is expressed ubiquitously as a protein of approximately 50 KDa in cytosol, but a fraction distributes to lipid rafts due to interaction with the lipid raft-associated protein PAG (Csk-binding protein).
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