+ |
FAM20C | up-regulates activity
phosphorylation
|
ERO1A |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277395 |
Ser145 |
GAVDESLsEETQKAV |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
29858230 |
We further show that ER oxidoreductin 1α (Ero1α), the pivotal sulfhydryl oxidase that catalyzes disulfide formation in the ER, is phosphorylated by Fam20C in the Golgi apparatus and retrograde-transported to the ER mediated by ERp44. The phosphorylation of Ser145 greatly enhances Ero1α oxidase activity and is critical for maintaining ER redox homeostasis and promoting oxidative protein folding. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Cullin 1-RBX1-Skp1 | down-regulates quantity by destabilization
polyubiquitination
|
ERO1A |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272332 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
27855403 |
Ero1L is a ubiquitination substrate of FBXO6. FBXO6 mediates the degradation of Ero1L through a ubiquitylation-dependent pathway. Overexpression of FBXO6 increased the polyubiquitination and decreased the stability of Ero1L, whereas inhibition of FBXO6 prolonged the half-life of Ero1L. FBXO6 is the substrate recognition component of a Skp1-Cullin1-F-box protein (SCF) ubiquitin E3 ligase complex |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ERO1A | up-regulates quantity by stabilization
binding
|
ERP44 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261049 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
11847130 |
Here, we report the functional characterization of a novel UPR-induced ER resident protein (ERp44) that forms mixed disulfides with both hEROs, as well as with partially unfolded Ig subunits. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
FBXO6 | down-regulates quantity by destabilization
binding
|
ERO1A |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272326 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
27855403 |
Ero1L is a ubiquitination substrate of FBXO6. FBXO6 mediates the degradation of Ero1L through a ubiquitylation-dependent pathway. Overexpression of FBXO6 increased the polyubiquitination and decreased the stability of Ero1L, whereas inhibition of FBXO6 prolonged the half-life of Ero1L. FBXO6 is the substrate recognition component of a Skp1-Cullin1-F-box protein (SCF) ubiquitin E3 ligase complex |
|
Publications: |
1 |
Organism: |
Homo Sapiens |