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Template
:
Protein primary structure
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From Wikipedia, the free encyclopedia
v
t
e
Protein primary structure
and
posttranslational modifications
General
N–O acyl shift
Peptide bond
Protein biosynthesis
Proteolysis
Racemization
N terminus
Acetylation
Carbamylation
Formylation
Glycation
Methylation
Myristoylation
(Gly)
C terminus
Amidation
Detyrosination
Glycosyl phosphatidylinositol (GPI)
O-methylation
Single specific
AAs
Serine
/
Threonine
ADP-ribosylation
Dephosphorylation
Glycosylation
O
-GlcNAc
Phosphorylation
Tyrosine
Adenylylation
ADP-ribosylation
Dephosphorylation
Detyrosination
Flavin linkage
Phosphorylation
Porphyrin ring linkage
Sulfation
Topaquinone (TPQ) formation
Cysteine
Palmitoylation
Prenylation
Aspartate
ADP-ribosylation
Succinimide formation
Glutamate
ADP-ribosylation
Carboxylation
Methylation
Polyglutamylation
Polyglycylation
Asparagine
Deamidation
Glycosylation
Glutamine
Transglutamination
Lysine
Acetylation
Acylation
Adenylylation
ADP-ribosylation
Butyrylation
Carbamylation
Deamination
Glutarylation
Glycation
Hydroxylation
Imine formation
Lactylation
Malonylation
Methylation
Methylmalonylation
O
-glycosylation
Oxidative deamination to aldehyde
Propionylation
Succinylation
Sumoylation
Ubiquitination
Arginine
ADP-ribosylation
Citrullination
Methylation
Proline
Hydroxylation
Histidine
Adenylylation
Diphthamide
formation
Tryptophan
C-mannosylation
Crosslinks between two
AAs
Cysteine
–
Cysteine
ADP-ribosylation
Disulfide bond
Methionine
–
Hydroxylysine
Sulfilimine bond
Lysine
–
Tyrosine
Lysine tyrosylquinone (LTQ) formation
Tryptophan
–
Tryptophan
Tryptophan tryptophylquinone (TTQ) formation
Crosslinks between three
AAs
Serine
–
Tyrosine
–
Glycine
p-Hydroxybenzylidene-imidazolinone (HBI) formation
(chromophore)
Histidine
–
Tyrosine
–
Glycine
4-(p-hydroxybenzylidene)-5-imidazolinone (HBI) formation
(chromophore)
Alanine
–
Serine
–
Glycine
Methylidene-imidazolone (MIO) formation
Crosslinks between four
AAs
Allysine
–
Allysine
–
Allysine
–
Lysine
Desmosine
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Protein primary structure
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