+ |
ULK1 | up-regulates quantity by stabilization
phosphorylation
|
SEC23B |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265285 |
Ser186 |
SCEGISKsYVFRGTK |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
30596474 |
Here, we show that the F-box protein FBXW5 targets SEC23B, a component of COPII, for proteasomal degradation and that this event limits the autophagic flux in the presence of nutrients. In response to starvation, ULK1 phosphorylates SEC23B on Serine 186, preventing the interaction of SEC23B with FBXW5 and, therefore, inhibiting SEC23B degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SEC23B |
binding
|
UBA52 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265305 |
|
|
|
|
pmid |
sentence |
30605680 |
We validate the genotype-specific differential SEC23B–UBA52 (ribosomal protein RPL40) interaction. |
|
Publications: |
1 |
+ |
SEC23B | form complex
binding
|
COPII vesicle |
0.696 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265288 |
|
|
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
|
SEC23B |
0.685 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265298 |
|
|
|
|
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
|
SEC23B |
0.354 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265306 |
|
|
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 |
+ |
FBXW5 | down-regulates quantity by destabilization
ubiquitination
|
SEC23B |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265286 |
|
|
Homo sapiens |
|
pmid |
sentence |
30596474 |
SCFFBXW5 interacts with SEC23B and targets it for ubiquitylation and proteasome-mediated degradation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |