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bioRxiv · 10.1101/386268

iProteinDB: an integrative database of Drosophila post-translational modifications

Hu, Y.·Sopko, R.·Chung, V.·Studer, R. A.·Landry, S. D.·Liu, D.·Rabinow, L.·Gnad, F.·Beltrao, P.·Perrimon, N.
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Abstract

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 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 from Drosophila embryos 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 for Drosophila. At iProteinDB, scientists can view the PTM landscape for any Drosophila protein and identify predicted functional phosphosites based on a comparative analysis of data from closely-related Drosophila species. Further, iProteinDB enables comparison of PTM data from Drosophila to that of orthologous proteins from other model organisms, including human, mouse, rat, Xenopus laevis, Danio rerio, and Caenorhabditis elegans.

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Hu, Y., Sopko, R., Chung, V., Studer, R. A., Landry, S. D., Liu, D., Rabinow, L., Gnad, F., Beltrao, P., Perrimon, N.. 2018-08-07. iProteinDB: an integrative database of Drosophila post-translational modifications. https://doi.org/10.1101/386268

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