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Term:
protein N-linked glycosylation via asparagine (GO:0018279)
Annotations: Rat: (16) Mouse: (16) Human: (30) Chinchilla: (29) Bonobo: (30) Dog: (16) Squirrel: (0) Pig: (16)
Parent Terms Term With Siblings Child Terms
(3-aminopropyl)(L-aspartyl-1-amino)phosphoryl-5'-adenosine biosynthetic process from asparagine 
C-terminal peptidyl-asparagine amidation 
dolichol-linked oligosaccharide biosynthetic process +   
GPI anchor biosynthetic process via N-asparaginyl-glycosylphosphatidylinositolethanolamine 
isopeptide cross-linking via N-(L-isoaspartyl)-glycine 
isopeptide cross-linking via N-(L-isoaspartyl)-L-cysteine 
N-terminal protein amino acid N-linked glycosylation 
peptide cross-linking via L-asparagine 5-imidazolinone glycine 
peptide cross-linking via N6-(L-isoaspartyl)-L-lysine +  
peptidyl-asparagine ADP-ribosylation 
peptidyl-asparagine hydroxylation +   
peptidyl-asparagine methylation 
peptidyl-asparagine racemization 
peptidyl-L-beta-methylthioasparagine biosynthetic process from peptidyl-asparagine 
peptidyl-N4-hydroxymethyl-L-asparagine biosynthetic process from peptidyl-asparagine 
protein N-linked glycosylation via arginine  
protein N-linked glycosylation via asparagine +   
The glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine and N4 glucosyl asparagine also occur. This modification typically occurs in extracellular peptides with an N-X-(ST) motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification.
protein N-linked glycosylation via tryptophan 

Synonyms
Exact Synonyms: protein amino acid N-linked glycosylation via asparagine
Definition Sources: GOC:jsg, RESID:AA0151, RESID:AA0420, RESID:AA0421

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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.