Quantitative proteome and phosphoproteome datasets of DNA replication and mitosis in Saccharomyces cerevisiae.

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Cell cycle progression is dictated by a complex network of kinases and phosphatases. These enzymes act on their substrates in a highly specific temporal manner ensuring that the process of cell division is unidirectional and irreversible. Key events of the cell cycle, such as duplication of genetic material and its redistribution to daughter cells, occur in S-phase and mitosis, respectively. Deciphering the dynamics of phosphorylation/dephosphorylation events during these cell cycle phases is important. Here, we showcase a quantitative proteomic and phosphoproteomic mass spectrometry dataset that profiles both early and late phosphorylation events and associated proteome alterations that occur during S-phase and mitotic arrest in the model organism S. cerevisiae. This dataset is of broad interest as the molecular mechanisms governing cell cycle progression are conserved throughout evolution. 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TMT labeling e", "L or ∼2µg) of each sample and analyzed it by mass spectrometry to confirm that the protein digestion was su", "and 5% acetonitrile prior to acquisition of LC-MS/MS data. 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