iProteinDB: an integrative database ofDrosophilapost-translational modifications [article]

Yanhui Hu, Richelle Sopko, Verena Chung, Romain A Studer, Sean D Landry, Daniel Liu, Leonard Rabinow, Florian Gnad, Pedro Beltrao, Norbert Perrimon
2018 bioRxiv   pre-print
Post-translational modification (PTM) serves as a regulatory mechanism for protein function, influencing stability, protein interactions, activity and localization, and is critical in many signaling pathways. The best characterized PTM is phosphorylation, whereby a phosphate is added to an acceptor residue, commonly serine, threonine and tyrosine. As proteins are often phosphorylated at multiple sites, identifying those sites that are important for function is a challenging problem. Considering
more » ... that many phosphorylation sites may be non-functional, prioritizing evolutionarily conserved phosphosites provides a general strategy to identify the putative functional sites with regards to regulation and function. To facilitate the identification of conserved phosphosites, we generated a large-scale phosphoproteomics dataset fromDrosophilaembryos collected from six closely-related species. We built iProteinDB (https://www.flyrnai.org/tools/iproteindb/), a resource integrating these data with other high-throughput PTM datasets, including vertebrates, and manually curated information forDrosophila. At iProteinDB, scientists can view the PTM landscape for anyDrosophilaprotein and identify predicted functional phosphosites based on a comparative analysis of data from closely-relatedDrosophilaspecies. Further, iProteinDB enables comparison of PTM data fromDrosophilato that of orthologous proteins from other model organisms, including human, mouse, rat,Xenopus laevis,Danio rerio, andCaenorhabditis elegans.
doi:10.1101/386268 fatcat:naoynqbaazd57iudu2jxylh6ma