Post-translational modification (PTM) refers to the covalent and generally enzymatic modification of proteins during or after protein biosynthesis. PTMs play a key role in many cellular processes. Living cells are constantly exposed to stimuli from their environment and thus have to adapt to rapidly changing conditions. Owing to the mostly static nature of the genome, a highly dynamic and well-regulated system is required to maintain cellular homeostasis. Compared with gene expression and translational control, which are relatively slow (within minutes to hours), PTMs of proteins stand for the major level of regulation, from very fast and reversible processes such as phosphorylation (seconds) to slower and irreversible ones such as certain forms of glycosylation. Now, bioinformaticians at Creative Proteomics are glad to tell you we are open to help you with Proteomic Analysis of PTMs Service!
Through PTM of a protein, a multitude of different protein species can be generated, compensating for the incongruity between the relatively low number of encoded genes and the high number of variable regulators required in complex organisms. Currently, more than 450 PTMs are listed in the Uniprot database - with phosphorylation, lysine acetylation, ubiquitination, and proteolytic processing being the most prominent ones. In contrast to gene expression, which merely controls the abundance of proteins, PTMs usually affect their three-dimensional structures, revealing or concealing active sites and interfaces for protein–protein interaction and thus modulating, e.g. subcellular localization, stability, and activity. They act as molecular switches and may initiate and inhibit the interaction of proteins with DNA, cofactors, lipids, as well as other proteins.
Post-translational modifications are involved in the following cellular events:
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