Editing Post-translational modification (section)

====Smaller chemical groups====
* [[acylation]], e.g. ''O''-acylation ([[esters]]), ''N''-acylation ([[amides]]), ''S''-acylation ([[thioesters]])
** [[acetylation]], the addition of an [[acetyl]] group, either at the [[N-terminus]] of the protein or at [[lysine]] residues.<ref name="pmid29405707">{{cite journal | vauthors = Ali I, Conrad RJ, Verdin E, Ott M | title = Lysine Acetylation Goes Global: From Epigenetics to Metabolism and Therapeutics | journal = Chem Rev | volume = 118 | issue = 3 | pages = 1216–1252 | date = February 2018 | pmid = 29405707 | pmc = 6609103 | doi = 10.1021/acs.chemrev.7b00181 }}</ref> The reverse is called [[deacetylation]].
** [[formylation]]
* [[alkylation]], the addition of an [[alkyl]] group, e.g. [[methyl]], [[ethyl group|ethyl]]
** [[methylation]] the addition of a [[methyl]] group, usually at [[lysine]] or [[arginine]] residues. The reverse is called [[demethylation]].
* <span id="amidation">amidation</span> at C-terminus. Formed by oxidative dissociation of a C-terminal Gly residue.<ref name="amidation">{{cite journal | vauthors = Bradbury AF, Smyth DG | title = Peptide amidation | journal = Trends in Biochemical Sciences | volume = 16 | issue = 3 | pages = 112–5 | date = March 1991 | pmid = 2057999 | doi = 10.1016/0968-0004(91)90044-v }}</ref>
* [[amide]] bond formation
** [[amino acid]] addition
*** [[arginylation]], a [[tRNA]]-mediation addition
*** [[polyglutamylation]], covalent linkage of [[glutamic acid]] residues to the N-terminus of tubulin and some other proteins.<ref name="pmid1967194">{{cite journal | vauthors = Eddé B, Rossier J, Le Caer JP, Desbruyères E, Gros F, Denoulet P | title = Posttranslational glutamylation of alpha-tubulin | journal = Science | volume = 247 | issue = 4938 | pages = 83–5 | date = January 1990 | pmid = 1967194 | doi = 10.1126/science.1967194 | bibcode = 1990Sci...247...83E }}</ref> (See [[tubulin polyglutamylase]])
*** [[polyglycylation]], covalent linkage of one to more than 40 [[glycine]] residues to the [[tubulin]] C-terminal tail
* [[butyrylation]]
* [[gamma-carboxylation]] dependent on [[Vitamin K]]<ref>{{cite journal | vauthors = Walker CS, Shetty RP, Clark K, Kazuko SG, Letsou A, Olivera BM, Bandyopadhyay PK | title = On a potential global role for vitamin K-dependent gamma-carboxylation in animal systems. Evidence for a gamma-glutamyl carboxylase in Drosophila | journal = The Journal of Biological Chemistry | volume = 276 | issue = 11 | pages = 7769–74 | date = March 2001 | pmid = 11110799 | doi = 10.1074/jbc.M009576200 | display-authors = etal | doi-access = free }}</ref>
* [[glycosylation]], the addition of a [[glycosyl]] group to either [[arginine]], [[asparagine]], [[cysteine]], [[hydroxylysine]], [[serine]], [[threonine]], [[tyrosine]], or [[tryptophan]]  resulting in a [[glycoprotein]]. Distinct from [[glycation]], which is regarded as a nonenzymatic attachment of sugars.
** [[O-GlcNAc|''O''-GlcNAc]], addition of ''N''-acetylglucosamine to serine or threonine residues in a β-glycosidic linkage
** polysialylation, addition of [[polysialic acid]] (PSA) to [[neural cell adhesion molecule]] (NCAM)
* [[malonylation]]
* [[protein hydroxylation|hydroxylation]]: addition of an oxygen atom to the side-chain of a Pro or Lys residue
* [[iodination]]: addition of an iodine atom to the aromatic ring of a tyrosine residue (e.g. in [[thyroglobulin]])
* [[ADP-ribosylation|nucleotide addition]] such as [[ADP-ribosylation]]
* [[phosphate ester]] (''O''-linked) or [[phosphoramidate]] (''N''-linked) formation
** [[phosphorylation]], the addition of a [[phosphate]] group, usually to [[serine]], [[threonine]], and [[tyrosine]] (''O''-linked), or [[histidine]] (''N''-linked)
** [[adenylylation]], the addition of an [[adenylyl]] moiety, usually to [[tyrosine]] (''O''-linked), or [[histidine]] and [[lysine]] (''N''-linked)
** uridylylation, the addition of an uridylyl-group (i.e. [[uridine monophosphate]] (UMP)), usually to tyrosine
* [[propionylation]]
* [[pyroglutamate]] formation
* [[S-glutathionylation|''S''-glutathionylation]]
* [[S-nitrosylation|''S''-nitrosylation]]
* ''S''-sulfenylation (''aka'' ''S''-sulphenylation), reversible covalent addition of one oxygen atom to the [[thiol]] group of a [[cysteine]] residue<ref name="CysOx">{{cite journal | vauthors = Chung HS, Wang SB, Venkatraman V, Murray CI, Van Eyk JE | title = Cysteine oxidative posttranslational modifications: emerging regulation in the cardiovascular system | journal = Circulation Research | volume = 112 | issue = 2 | pages = 382–92 | date = January 2013 | pmid = 23329793 | pmc = 4340704 | doi = 10.1161/CIRCRESAHA.112.268680 | display-authors = 1 }}</ref>
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* ''S''-sulfinylation, normally irreversible covalent addition of two oxygen atoms to the [[thiol]] group of a [[cysteine]] residue<ref name="CysOx" />
* ''S''-sulfonylation, normally irreversible covalent addition of three oxygen atoms to the [[thiol]] group of a [[cysteine]] residue, resulting in the formation of a [[cysteic acid]] residue<ref name="CysOx" />
* [[succinylation]] addition of a [[succinyl]] group to [[lysine]]
* [[tyrosine sulfation|sulfation]], the addition of a sulfate group to a [[tyrosine]].