Title : Identification of csk tyrosine phosphorylation sites and a tyrosine residue important for kinase domain structure.

Pub. Date : 1997 Mar 15

PMID : 9148770






7 Functional Relationships(s)
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1 Identification of csk tyrosine phosphorylation sites and a tyrosine residue important for kinase domain structure. Tyrosine C-terminal Src kinase Homo sapiens
2 The lack of a conserved tyrosine autophosphorylation site is a unique feature of the C-terminal Src-kinase, Csk, although this protein tyrosine kinase can be autophosphorylated on tyrosine residues in vitro and in bacteria. Tyrosine C-terminal Src kinase Homo sapiens
3 The lack of a conserved tyrosine autophosphorylation site is a unique feature of the C-terminal Src-kinase, Csk, although this protein tyrosine kinase can be autophosphorylated on tyrosine residues in vitro and in bacteria. Tyrosine C-terminal Src kinase Homo sapiens
4 Here we show that human Csk is tyrosine phosphorylated in HeLa cells treated with sodium pervanadate. Tyrosine C-terminal Src kinase Homo sapiens
5 A catalytically inactive form of Csk was also phosphorylated on Tyr-184 in vivo, suggesting that this is not a site of autophosphorylation. Tyrosine C-terminal Src kinase Homo sapiens
6 Taken together these results indicate that Csk can be phosphorylated in vivo at Tyr-184 by an as yet unknown tyrosine kinase, and that autophosphorylation of Tyr-304 occurs only at abnormally high Csk concentrations in vitro. Tyrosine C-terminal Src kinase Homo sapiens
7 Furthermore, Tyr-304 is required for the maintenance of the structure of the Csk kinase domain. Tyrosine C-terminal Src kinase Homo sapiens