オーラルセッション
- 第1日 5月11日（月） 16:10～16:30 A会場（特別会議場)
-
1A-O1-1610 PDF
リン酸化プロテオミクスを用いたヒトキノーム解析
Large-scale phosphoproteomics based on LC/MS/MS enables us to overview protein phosphorylation events occurring in cells. However, it is still challenging to clarify physiological roles of individual kinase in cellular signal transduction from the phosphoproteome data due to insufficient information about kinase-substrate relationships. In this study, we developed a method for identification of in vitro substrates for more than 400 recombinant human kinases by using in vitro kinase assay combined with quantitative phosphoproteomics approaches. Based on the in vitro profiling data, we performed hierarchical cluster analysis to classify the kinases and extract amino acid residues governing S/T/Y phosphorylation preference from the kinase activation loop.