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http://purl.uniprot.org/citations/10066823http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10066823http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10066823http://www.w3.org/2000/01/rdf-schema#comment"The hematopoietic lineage cell-specific protein HS1 was shown to undergo a process of sequential phosphorylation both in vitro and in vivo, which is synergistically mediated by Syk and Src family protein-tyrosine kinases and essential for B cell antigen receptor-mediated apoptosis. We have now identified tyrosine 222 as the HS1 residue phosphorylated by the Src family protein kinases c-Fgr and Lyn, and we show that a truncated form of HS1 (HS1-208-401) lacking the N-terminal putative DNA binding region and the C-terminal Src homology 3 (SH3) domain is still able to undergo all the steps of sequential phosphorylation as efficiently as full-length HS1. We also show that a stable association of phospho-HS1 with c-Fgr through its SH2 domain requires previous autophosphorylation of the kinase and is prevented by subsequent phosphorylation of Tyr-222. Kinetic studies with HS1 and its truncated forms previously phosphorylated by Syk and with a peptide substrate reproducing the sequence around tyrosine 222 support the view that efficient phosphorylation of HS1 by Src family protein kinases entirely relies on TyrP-SH2 domain interaction with negligible, if any, contribution of local specificity determinants. Our data indicate that the proline-rich region of HS1 bordered by tyrosyl residues affected by Syk and Src family kinases represents a functional domain designed to undergo a process of sequential phosphorylation."xsd:string
http://purl.uniprot.org/citations/10066823http://purl.org/dc/terms/identifier"doi:10.1074/jbc.274.11.7557"xsd:string
http://purl.uniprot.org/citations/10066823http://purl.org/dc/terms/identifier"doi:10.1074/jbc.274.11.7557"xsd:string
http://purl.uniprot.org/citations/10066823http://purl.uniprot.org/core/author"Quadroni M."xsd:string
http://purl.uniprot.org/citations/10066823http://purl.uniprot.org/core/author"Quadroni M."xsd:string
http://purl.uniprot.org/citations/10066823http://purl.uniprot.org/core/author"James P."xsd:string
http://purl.uniprot.org/citations/10066823http://purl.uniprot.org/core/author"James P."xsd:string
http://purl.uniprot.org/citations/10066823http://purl.uniprot.org/core/author"Pinna L.A."xsd:string
http://purl.uniprot.org/citations/10066823http://purl.uniprot.org/core/author"Pinna L.A."xsd:string
http://purl.uniprot.org/citations/10066823http://purl.uniprot.org/core/author"Donella-Deana A."xsd:string
http://purl.uniprot.org/citations/10066823http://purl.uniprot.org/core/author"Donella-Deana A."xsd:string
http://purl.uniprot.org/citations/10066823http://purl.uniprot.org/core/author"Marin O."xsd:string
http://purl.uniprot.org/citations/10066823http://purl.uniprot.org/core/author"Marin O."xsd:string
http://purl.uniprot.org/citations/10066823http://purl.uniprot.org/core/author"Brunati A.M."xsd:string
http://purl.uniprot.org/citations/10066823http://purl.uniprot.org/core/author"Brunati A.M."xsd:string
http://purl.uniprot.org/citations/10066823http://purl.uniprot.org/core/author"Contri A."xsd:string
http://purl.uniprot.org/citations/10066823http://purl.uniprot.org/core/author"Contri A."xsd:string
http://purl.uniprot.org/citations/10066823http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10066823http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10066823http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/10066823http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/10066823http://purl.uniprot.org/core/pages"7557-7564"xsd:string
http://purl.uniprot.org/citations/10066823http://purl.uniprot.org/core/pages"7557-7564"xsd:string