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2160-1836 9 1 2019 01 09 G3 (Bethesda, Md.) G3 (Bethesda) iProteinDB: An Integrative Database of Drosophila Post-translational Modifications. 1-11 10.1534/g3.118.200637 Post-translational modification (PTM) serves as a regulatory mechanism for protein function, influencing their stability, 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, most commonly serine, threonine and tyrosine in metazoans. As proteins are often phosphorylated at multiple sites, identifying those sites that are important for function is a challenging problem. Considering that any given phosphorylation site might be non-functional, prioritizing evolutionarily conserved phosphosites provides a general strategy to identify the putative functional sites. 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 tropicalis, Danio rerio, and Caenorhabditis elegans. Copyright © 2019 Hu et al. Hu Yanhui Y 0000-0003-1494-1402 Department of Genetics, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115. Drosophila RNAi Screening Center, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115. Sopko Richelle R Department of Genetics, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115. Chung Verena V Department of Genetics, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115. Drosophila RNAi Screening Center, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115. Foos Marianna M Department of Genetics, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115. Studer Romain A RA European Molecular Biology Laboratory (EMBL), European Bioinformatics Institute, Wellcome Genome Campus, Hinxton, Cambridge CB10 1SD, UK. Landry Sean D SD Department of Bioinformatics, Cell Signaling Technology Inc., 3 Trask Lane, Danvers, MA 01923. Liu Daniel D Drosophila RNAi Screening Center, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115. Rabinow Leonard L Department of Genetics, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115. Gnad Florian F Department of Bioinformatics, Cell Signaling Technology Inc., 3 Trask Lane, Danvers, MA 01923. Beltrao Pedro P European Molecular Biology Laboratory (EMBL), European Bioinformatics Institute, Wellcome Genome Campus, Hinxton, Cambridge CB10 1SD, UK. Perrimon Norbert N 0000-0001-7542-472X Department of Genetics, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115 perrimon@receptor.med.harvard.edu. Drosophila RNAi Screening Center, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115. Howard Hughes Medical Institute, 77 Avenue Louis Pasteur, Boston, MA 02115. eng figshare 10.25387/g3.6986945 R01 DK088718 DK NIDDK NIH HHS United States R01 GM067761 GM NIGMS NIH HHS United States P01 CA120964 CA NCI NIH HHS United States R01 GM084947 GM NIGMS NIH HHS United States R01 GM067761 GM NIGMS NIH HHS United States Journal Article Research Support, Non-U.S. Gov't Research Support, N.I.H., Extramural 2019 01 09
United States G3 (Bethesda) 101566598 2160-1836 Drosophila phosphoproteomics post-translational modification
2018 11 7 6 0 2018 11 7 6 0 2018 11 7 6 0 epublish 30397019 g3.118.200637 10.1534/g3.118.200637 PMC6325894