Protein function is highly regulated by the co-ordinated expression and interaction in different tissues and the correct localization within different sub-cellular compartments. A common mechanism for protein regulation are post-translational modifications (PTMs). Protein phosphorylation is the most prevalent and well-studied PTM in eukaryotes, with involvement in diseases such as cancer and Alzheimer’s. This reversible modification is regulated by two key enzymes;kinases and phosphatases. Despite their importance, the available kinase-substrate data on phosphorylation and its biological context (e.g. sub-cellular localizations and pathological association) is very limited. However, with kinase-substrate associations important pharmacological targets, better context-aware information on protein phosphorylation and kinase-substrate association is essential to define their role in cellular communication and disease. In this project, we aim to identify and extend kinase-substrate association based on different biological and pathological context by re-processing and re-using available public mass-spectrometry based proteomics data, which we will integrate with functional and physical protein association networks, tissue and sub-cellular annotations, and various sequence, structural and biophysical features. The results from this research will be made available through the interactive Scop3P web-interface, an established knowledge-base on human protein phosphorylation.