@article {1159605,
	title = {iProteinDB: An Integrative Database of Post-translational Modifications},
	journal = {G3 (Bethesda)},
	volume = {9},
	year = {2019},
	month = {2019 01 09},
	pages = {1-11},
	abstract = {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 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 At iProteinDB, scientists can view the PTM landscape for any protein and identify predicted functional phosphosites based on a comparative analysis of data from closely-related species. Further, iProteinDB enables comparison of PTM data from to that of orthologous proteins from other model organisms, including human, mouse, rat, , , and .},
	issn = {2160-1836},
	doi = {10.1534/g3.118.200637},
	author = {Hu, Yanhui and Sopko, Richelle and Chung, Verena and Foos, Marianna and Studer, Romain A and Landry, Sean D and Liu, Daniel and Rabinow, Leonard and Gnad, Florian and Beltrao, Pedro and Perrimon, Norbert}
}
