Abstract Protein phosphorylation by kinases is an important regulatory modification that controls many cellular processes. Advances in tools and approaches to study this modification have greatly expanded the catalog of known phosphorylation sites but there remain substantial gaps in our knowledge. We will apply novel kinome- centric analyses to study canonical cell signaling pathways in order to define pathway-specific signaling modules. Our goal is to develop a mass spectrometry-based phenotyping assay that can identify phosphosignatures of cell signaling.