+ |
SEC23A | form complex
binding
|
COPII vesicle |
0.788 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265289 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
30605680 |
The Core Components of COPII Vesicles from HeLa Cells|Membrane-bound Sar1 then recruits the inner COPII coat subcomplex, the Sec23/24 heterodimer. Subsequently, together with cargo proteins recruited by the Sec24 subunit, Sar1 and Sec23/24 assemble into so-called pre-budding complexes. Finally, outer coat subcomplexes, comprising heterotetrameric Sec13/31 complexes, are recruited onto pre-budding complexes to complete the two-layered COPII coat |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SAR1A | up-regulates quantity
binding
|
SEC23A |
0.817 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265299 |
|
|
|
|
pmid |
sentence |
30605680 |
Biogenesis of COPII vesicles is initiated by the activation of the small guanosine triphosphate (GTP)-binding protein secretion-associated Ras-related protein 1 (Sar1) at specialized subdomains of the ER, called ER exit sites (ERES) or transitional ER (tER). Membrane-bound Sar1 then recruits the inner COPII coat subcomplex, the Sec23/24 heterodimer. |
|
Publications: |
1 |
+ |
SEC23IP | up-regulates activity
binding
|
SEC23A |
0.554 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265307 |
|
|
Mus musculus |
Brain |
pmid |
sentence |
10400679 |
The results showed that the N-terminal region of p125 is important for the interaction with Sec23p. We confirmed the interaction between the two proteins by a yeast two-hybrid assay. Overexpression of p125, like that of mammalian Sec23p, caused disorganization of the endoplasmic reticulum-Golgi intermediate compartment and Golgi apparatus, suggesting its role in the early secretory pathway. |
|
Publications: |
1 |
Organism: |
Mus Musculus |