CSK is a cytoplasmic tyrosine kinase that has been shown to downregulate the tyrosine kinase activity of the c-src through tyrosine phosphorylation of the c-src carboxy terminus. A yeast 2-hybrid system has been used to identify proteins associated with CSK. The Src homology-3 (SH3) domain of CSK associates with a proline-rich region of PEP, a protein-tyrosine phosphatase expressed in hemopoietic cells. This association is highly specific and it is speculated that PEP may be an effector and/or regulator of CSK in T cells and other hemopoietic cells.
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p50csk is a tyrosine protein kinase (TPK) that represses the activity of Src family TPKs. We previously showed that Csk is a potent negative regulator of antigen receptor signaling in T lymphocytes and that its Src homology (SH) 3 and
We have isolated a cDNA encoding a novel tyrosine kinase family member, named cyl (consensus tyrosine-lacking kinase), from the K562 human leukemia cell line. The deduced cyl protein lacks signal and transmembrane sequences but contains features of known cytoplasmic tyrosine
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