Structural characterizations of phosphorylatable residues in transmembrane proteins from .

Phosphorylation is a common post-translational modification that plays important roles in a wide range of biochemical and cellular processes. Many enzymes and receptors can be switched "on" or "off" by conformational changes induced by phosphorylation. The phosphorylation process is mediated by a family of enzymes called kinase. Currently, more than 1,000 different kinases have been identified in proteome. Kinases interact with each other and with many regulatory proteins forming phosphorylation networks. These phosphorylation networks modulate the signaling processes and control the functions of cells. Normally, kinases phosphorylate serines, threonines, and tyrosines. However, in many proteins, not all of these 3 types of amino acids can be phosphorylated. Therefore, identifying the phosphorylation sites and the possible phosphorylation events is very important in decoding the processes of regulation and the function of phosphorylation networks. In this study, we applied computational and bioinformatics tools to characterize the association between phosphorylation events and structural properties of corresponding proteins by analyzing more than 50 trans-membrane proteins from A. In addition to the previously established conclusion that phosphorylation sites are closely associated with intrinsic disorder, we found that the phosphorylation process may also be affected by solvent accessibility of phosphorylation sites and further promoted by neighboring modification events.