| + |
SEC62 | up-regulates
|
Protein_translocation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265280 |
|
|
|
|
| pmid |
sentence |
| 22375059 |
Silencing the SEC62 gene inhibits post-translational transport of small presecretory proteins into the human ER |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265281 |
|
|
|
|
| pmid |
sentence |
| 22375059 |
We demonstrated, with a similar knockdown approach, a precursor-specific involvement of mammalian Sec63 in the initial phase of co-translational protein transport into the ER. |
|
| Publications: |
2 |
| + |
LMAN1-MCFD2 cargo receptor complex | up-regulates
|
Protein_translocation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281503 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32356523 |
The transmembrane intracellular lectin ER-Golgi intermediate compartment protein 53 (ERGIC-53) and the soluble EF-hand multiple coagulation factor deficiency protein 2 (MCFD2) form a complex that functions as a cargo receptor, trafficking various glycoproteins between the endoplasmic reticulum (ER) and the Golgi apparatus. It has been demonstrated that the carbohydrate-recognition domain (CRD) of ERGIC-53 (ERGIC-53CRD) interacts with N-linked glycans on cargo glycoproteins, whereas MCFD2 recognizes polypeptide segments of cargo glycoproteins. Crystal structures of ERGIC-53CRD complexed with MCFD2 and mannosyl oligosaccharides have revealed protein-protein and protein-sugar binding modes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |