Pub. Date : 1997 Mar 15
PMID : 9148770
7 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
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 |