Covalent modification of proteins following translation, including glycosylation, phosphorylation, sulfation, acetylation, and ribosylation.

Proteins in cells can be extensively modified, typical changes being N- or C-terminal cleavages, glycosylation, phosphorylation, sulphation, etc.; as a consequence there are many more proteins in the proteome than there are genes in the genome

Alterations made to a protein after its synthesis at the ribosome. These modifications, such as the addition of carbohydrate or fatty acid chains, may be critical to the function of the protein.

An enzyme-catalysed alteration to a protein made after its translation from mRNA (such as phosphorylation, glycosylation, methylation).

The modification of a newly formed protein; may involve the deletion of amino acids, chemical modification of certain amino acids, or addition of small molecules (e.g., phosphate groups or sugars) to certain amino acids.

An enzyme-catalysed alteration to a protein made after its translation from mRNA (e.g., glycosylation, phosphorylation, myristoylation, methylation).

The enzymatic processing of a polypeptide chain after translation from messenger RNA and after peptide bond formation has occurred.

Modification of a protein after it has been synthesised by enzymatic action (Integrated Pest Management Resource Centre, no date [online]). Examples of post-translational modifications include glycosylation, acylation, proteolysis and phosphorylation.