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. 2022 Sep 19;163(3):179–219. doi: 10.1111/jnc.15682

TABLE 2.

Post‐translational modifications (PTM) and their main target amino acid residue. The reversal of these PTMs are not included in the table and are discussed in the main text as relevant for Nf isoforms, for example Nf dephosphorylation to reverse Nf phosphorylation

PTM Mechanism
ADP‐ribosylation Adds ADP‐ribose which is a form of glycosylation. Affected are Gglu, Asp, sSr, Arg, Cys, Lys, diphthamide, phosphoserine, Asn
Acetylation Acetylates Lys
C‐terminal Amination (adds an amine group), glycosyl phosphatidylinositol attachment, phosphorylation
Carbonylation Adds carbon monoxide
Carboxylation Adds a carboxyl group to glutamate
Citrullination Synonymous to deimination, converts Argto Cit
Farnesylation Adds a lipid group
Glutamylation Adds glutamate
Glycation Adds a sugar aldehyde or ketone, the late stage is characterised by formation of advanced glycation end products (AGEs)
Glycosylation Similar to glycation only that this is enzyme mediated
Glycylation Adds glycine
Hydroxylation Changes Pro to Hyp, also works with Lys
Isomerisation Transformation into an isomer which changes the chemical structure
Methylation Add a methyl group to Arg
N‐terminal Arginylation (adds Argi), formylation (adds a formyl group), pyroglutamate (N‐terminal Glu forms a pyroglutamate group)
Nitrosylation Adds nitric oxide
Oxidation Adds oxygen species
Phosphorylation Adds phosphorus to Ser and to a lesser degree also to Thr and Tyr
SUMOylation Adds a small ubiquitin‐related modifier (SUMO)
Sulphation Adds sulphate to Tyr
Tyrosination Adds Tyr
Ubiquitination Adds ubiquitin to Lys