The protein phosphorylation catalyzed by protein kinases (PKs) plays an essential role in almost all biological progress. The identification of PKs and kinase-specific substrates is fundamental for understanding the regulatory mechanisms of protein phosphorylation in organisms. Moreover, dynamic protein phosphorylation is also an essential regulatory mechanism in various organisms. In this capacity, it is involved in a multitude of signal transduction pathways, which drives motivation for the development of compounds modulating phosphorylation activity.
Kinase-specific phosphorylation data lay the foundation for the reconstruction of signal transduction networks. Therefore, precise annotation of phosphorylated proteins is the first step toward simulating cell signaling pathways. The vast majority of kinase-specific phosphorylation data remain to be discovered. Existing experimental methods and computational phosphorylation site (P-site) prediction tools have various applications with respect to addressing this problem.
Widely Used P-site Prediction Tools
KinasePhos 2.0
Musite
GPS2.1
Phospho.ELM
PKIS web server
Computational approaches are needed for learning the interaction determinants and for the inference of the effect of small compounds on a given kinase. CD ComputaBio provides kinase proteins at crystallography grade for computational research applications.