[HTML][HTML] Systematic analysis of protein phosphorylation networks from phosphoproteomic data
In eukaryotes, hundreds of protein kinases (PKs) specifically and precisely modify
thousands of substrates at specific amino acid residues to faithfully orchestrate numerous
biological processes, and reversibly determine the cellular dynamics and plasticity. Although
over 100,000 phosphorylation sites (p-sites) have been experimentally identified from
phosphoproteomic studies, the regulatory PKs for most of these sites still remain to be
characterized. Here, we present a novel software package of iGPS for the prediction of in …
thousands of substrates at specific amino acid residues to faithfully orchestrate numerous
biological processes, and reversibly determine the cellular dynamics and plasticity. Although
over 100,000 phosphorylation sites (p-sites) have been experimentally identified from
phosphoproteomic studies, the regulatory PKs for most of these sites still remain to be
characterized. Here, we present a novel software package of iGPS for the prediction of in …
