| + |
dolichyl beta-D-mannosyl phosphate | up-regulates 
|
Protein_glycosylation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262568 |
|
|
|
|
| pmid |
sentence |
| 21384228 |
Dolichol has a well defined role as a lipid carrier for the glycan precursor in the early stages of N‐linked protein glycosylation, which is assembled in the endoplasmic reticulum of all eukaryotic cells. |
|
| Publications: |
1 |
| + |
OST-B complex | up-regulates 
|
Protein_glycosylation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272056 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31831667 |
Oligosaccharyltransferase (OST) catalyzes the transfer of a high-mannose glycan onto secretory proteins in the endoplasmic reticulum. Mammals express two distinct OST complexes that act in a cotranslational (OST-A) or posttranslocational (OST-B) manner. Here, we present high-resolution cryo-electron microscopy structures of human OST-A and OST-B. Although they have similar overall architectures, structural differences in the catalytic subunits STT3A and STT3B facilitate contacts to distinct OST subunits, DC2 in OST-A and MAGT1 in OST-B. In OST-A, interactions with TMEM258 and STT3A allow ribophorin-I to form a four-helix bundle that can bind to a translating ribosome, whereas the equivalent region is disordered in OST-B. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
OST-A complex | up-regulates
|
Protein_glycosylation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272055 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31831667 |
Oligosaccharyltransferase (OST) catalyzes the transfer of a high-mannose glycan onto secretory proteins in the endoplasmic reticulum. Mammals express two distinct OST complexes that act in a cotranslational (OST-A) or posttranslocational (OST-B) manner. Here, we present high-resolution cryo-electron microscopy structures of human OST-A and OST-B. Although they have similar overall architectures, structural differences in the catalytic subunits STT3A and STT3B facilitate contacts to distinct OST subunits, DC2 in OST-A and MAGT1 in OST-B. In OST-A, interactions with TMEM258 and STT3A allow ribophorin-I to form a four-helix bundle that can bind to a translating ribosome, whereas the equivalent region is disordered in OST-B. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GFPT1 | up-regulates
|
Protein_glycosylation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267820 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21310273 |
GFPT1 is the key enzyme of the hexosamine pathway yielding the amino sugar UDP-N-acetylglucosamine, an essential substrate for protein glycosylation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
Protein_glycosylation