Scop3P: the bridge between human phosphosites, protein structure and proteomics data

Post-translational modifications (PTMs) of proteins play an important role in various cellular processes. One of the key PTM is phosphorylation, which has already been studied extensively [1,2]. With the advancements in high-throughput mass spectrometry (MS/MS) techniques, the amount of publicly available data on phosphorylation has increased dramatically over time. However, available resources on phosphorylation usually contain only sequence and phosphosite information, generally omitting structural information. Yet such structural information is particularly relevant in a crucial task: to differentiate between functional and non-functional phosphosites. We therefore developed Scop3P: a database of public proteomics data-derived human phosphosites that are annotated with detailed, residue-level structural annotation based on state-of-the-art prediction tools. Moreover, these phosphosites are also directly mapped onto 3D protein structures when available in PDB.