User:Pedrobeltrao/Notebook/Structural analysis of phosphorylation sites/data collection and stats

Data collection

Phosphorylation data for S. cerevisiae was collected from previously published phosphoproteomic datasets. Protein domain predictions were obtained from PFAM and homology models for a large fraction of the S. cerevisiae proteome were obtained from modbase. Only models with more than 30% identity to the template structure were kept. Conservation of the phosphorylation site was determined by alignment with orthologs in other species with available phosphorylation data. For the following general analysis we considered that a S. cerevisiae phosphorylation site was conserved if the ortholog had a phosphorylation site within 10 alignment positions of the S. cerevisiae phosphorylation site.

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