. "Protein phosphorylation is a key regulatory event in most cellular processes and development. Mass spectrometry-based proteomics provides a framework for the large-scale identification and characterization of phosphorylation sites. Here, we used a well-established phosphopeptide enrichment and identification strategy including the combination of strong cation exchange chromatography, immobilized metal affinity chromatography, and high-accuracy mass spectrometry instrumentation to study phosphorylation in developing Drosophila embryos. In total, 13,720 different phosphorylation sites were discovered from 2702 proteins with an estimated false-discovery rate (FDR) of 0.63% at the peptide level. Because of the large size of the data set, both novel and known phosphorylation motifs were extracted using the Motif-X algorithm, including those representative of potential ordered phosphorylation events." . . "J. Proteome Res." . "Gygi S.P." . "Zhai B." . "Beausoleil S.A." . "Villen J." . "Mintseris J." . "2008"^^ . "1675-1682" . "Phosphoproteome analysis of Drosophila melanogaster embryos." . "7" . "doi:10.1021/pr700696a" .