Accession: | |
---|---|
Functional site class: | N-glycosylation site |
Functional site description: | N-linked glycosylation is a co-translational process involving the transfer of a oligosaccharide chain to asparagine residue in the protein. |
ELMs with same func. site: | MOD_N-GLC_1 MOD_N-GLC_2 |
ELM Description: | Generic motif for N-glycosylation. It was shown that Trp, Asp, and Glu are uncommon before the Ser/Thr position (Shakin-Eshleman,1996). Efficient glycosylation usually occurs when ~60 residues or more separate the glycosylation acceptor site from the C-terminus. |
Pattern: | .(N)[^P][ST].. |
Pattern Probability: | 0.0050178 |
Present in taxon: | Eukaryota |
Interaction Domain: |
STT3 (PF02516)
Oligosaccharyl transferase STT3 subunit
(Stochiometry: 1 : 1)
PDB Structure: 2HG0
|
Abstract |
N-glycosylation is the most common modification of secretory and membrane-bound proteins in eukaryotic cells. The whole process of N-glycosylation comprises more than 100 enzymes and transport proteins. The biosynthesis of all N-linked oligosaccharides begins in the ER with a large precursor oligosaccharid. The structure of this oligosaccharide [(Glc)3(Man)9(GlcNAc)2] is the same in plants, animals, and single cell eukaryotes. This precursor is linked to a dolichol, a long-chain polyisoprenoid lipid that act as a carrier for the oligosaccharide. The oligosaccharide is then transferred by an ER enzyme from the dodichol carrier to an asparagine residue on a nascent protein. The oligosaccharide chain is then processed as the glycoprotein moves through the Golgi apparatus. In some cases this modification involves attachment of more mannose groups, in other cases a more complex type of structure is attached. |
7 GO-Terms:
156 Instances for MOD_N-GLC_1
(click table headers for sorting; Notes column: =Number of Switches, =Number of Interactions)
(click table headers for sorting; Notes column: =Number of Switches, =Number of Interactions)
Please cite:
ELM-the Eukaryotic Linear Motif resource-2024 update.
(PMID:37962385)
ELM data can be downloaded & distributed for non-commercial use according to the ELM Software License Agreement
ELM data can be downloaded & distributed for non-commercial use according to the ELM Software License Agreement