Editing Proteomics (section)

====Phosphorylation====
One such modification is [[phosphorylation]], which happens to many [[enzymes]] and structural proteins in the process of [[cell signaling]]. The addition of a phosphate to particular amino acids—most commonly [[serine]] and [[threonine]]<ref>{{cite journal | vauthors = Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M | title = Global, in vivo, and site-specific phosphorylation dynamics in signaling networks | journal = Cell | volume = 127 | issue = 3 | pages = 635–648 | date = November 2006 | pmid = 17081983 | doi = 10.1016/j.cell.2006.09.026 | s2cid = 7827573 | doi-access = free }}</ref> mediated by serine-threonine [[kinase]]s, or more rarely [[tyrosine]] mediated by tyrosine [[kinases]]—causes a protein to become a target for binding or interacting with a distinct set of other proteins that recognize the phosphorylated domain.{{citation needed|date=April 2023}}

Because protein phosphorylation is one of the most studied protein modifications, many "proteomic" efforts are geared to determining the set of phosphorylated proteins in a particular cell or tissue-type under particular circumstances. This alerts the scientist to the signaling pathways that may be active in that instance.