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Background:Serine phosphorylation is one of the most prevalent and reversible post-translational modifications in eukaryotic proteins. Catalyzed by kinases and reversed by phosphatases, this modification covalently attaches a phosphate group to the hydroxyl group of serine residues. It alters protein charge, conformation and intermolecular interactions, acting as a core molecular switch to regulate cell cycle, signal transduction, proliferation, differentiation, metabolism and immune response. Dysregulated serine phosphorylation is implicated in inflammation, cancer and multiple human diseases.
