For this purpose, we have developed experimental and computational methods to identify the protein-interactions (stable and transient) formed by these signalling molecules and how these interactions are changed by disease, such as cancer, causing mutations. Additionally, we employ quantitative mass spectrometry - based proteomics on assessing the protein abundance changes, as well as phosphorylation status of the cells. Furthermore, combining the data from the different sets of ‘omics’ data (proteomics, HTS and HiSeq), allows us to generate global and systems level understanding on how disease-causing mutations mediate their effects, enabling also the development of therapeutic or diagnostic approaches.