+ |
RPN1 | up-regulates
binding
|
OPRM1 |
0.255 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-184651 |
|
|
Homo sapiens |
|
pmid |
sentence |
19289571 |
Ribophorin i (rpni), a component of the oligosaccharide transferase complex, could directly interact with mor. Rpni can be shown to participate in mor export by the intracellular retention of the receptor after small interfering rna knockdown of endogenous rpni. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RPN1 | form complex
binding
|
OST-B complex |
0.785 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272072 |
|
|
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 |
+ |
ASB11 | down-regulates quantity by destabilization
polyubiquitination
|
RPN1 |
0.365 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272057 |
|
|
Homo sapiens |
U2-OS Cell |
pmid |
sentence |
24337577 |
We also demonstrated that ASB11 is a novel endoplasmic reticulum-associated ubiquitin ligase with the ability to interact and promote the ubiquitination of Ribophorin 1, an integral protein of the oligosaccharyltransferase (OST) glycosylation complex. Moreover, expression of ASB11 can increase Ribophorin 1 protein turnover in vivo. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RPN1 | form complex
binding
|
OST-A complex |
0.796 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272063 |
|
|
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 |