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pubmed-article:2506075pubmed:abstractTextIn two-dimensional tryptic phosphopeptide mapping, the beta-subunit of the insulin receptor phosphorylated by 12-O-tetradecanoylphorbol-13-acetate in rat hepatoma cells (H-35) was separated into one phosphothreonine-containing peptide and several phosphoserine-containing peptides. The synthetic peptide coding residues 1327-1343 in the C-terminal region of the rat insulin receptor was phosphorylated at the threonine residue by protein kinase C in a phosphatidylserine and oleoylacetylglycerol dependent manner. Tryptic digest of this phosphopeptide migrated to the same position as the phosphothreonine containing peptide obtained from the beta-subunit in two-dimensional phosphopeptide mapping. These data suggested that Thr 1336 of the insulin receptor is the site of phosphorylation by protein kinase C in intact cells.lld:pubmed
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pubmed-article:2506075pubmed:articleTitleIdentification of a phosphorylation site of the rat insulin receptor catalyzed by protein kinase C in an intact cell.lld:pubmed
pubmed-article:2506075pubmed:affiliationInstitute for Diabetes Care and Research, Asahi Life Foundation, Tokyo, Japan.lld:pubmed
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