+ |
FAM20C | up-regulates activity
phosphorylation
|
P4HB |
0.36 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275574 |
Ser357 |
KIKPHLMsQELPEDW |
|
|
pmid |
sentence |
32149426 |
The secretory pathway kinase Fam20C phosphorylates Ser357 of PDI and responds rapidly to various ER stressors. Phosphorylation of Ser357 induces an open conformation of PDI and turns it from a "foldase" into a "holdase", which is critical for preventing protein misfolding in the ER. Phosphorylated PDI also binds to the lumenal domain of IRE1α, a major UPR signal transducer, and attenuates excessive IRE1α activity. |
|
Publications: |
1 |
+ |
P4HB | up-regulates quantity by stabilization
binding
|
Collagen |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269731 |
|
|
Homo sapiens |
|
pmid |
sentence |
9545296 |
We also show that PDI associates independently with the C-propeptide of monomeric procollagen chains prior to trimer formation, indicating a role for this protein in coordinating the assembly of heterotrimeric molecules. This demonstrates that PDI has multiple functions in the folding of the same protein, that is, as a catalyst for disulfide bond formation, as a subunit of P4-H during proline hydroxylation, and independently as a molecular chaperone during chain assembly. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
P4HB | down-regulates activity
binding
|
ERN1 |
0.44 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275573 |
|
|
|
|
pmid |
sentence |
32149426 |
The secretory pathway kinase Fam20C phosphorylates Ser357 of PDI and responds rapidly to various ER stressors. Phosphorylation of Ser357 induces an open conformation of PDI and turns it from a "foldase" into a "holdase", which is critical for preventing protein misfolding in the ER. Phosphorylated PDI also binds to the lumenal domain of IRE1α, a major UPR signal transducer, and attenuates excessive IRE1α activity. |
|
Publications: |
1 |