+ |
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 |
+ |
FAM20C | down-regulates activity
phosphorylation
|
FGF23 |
0.627 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260925 |
Ser180 |
IPRRHTRsAEDDSER |
Homo sapiens |
|
pmid |
sentence |
24706917 |
Here we show that Fam20C directly phosphorylates FGF23 on Ser(180) | Our above results support, phosphorylation of FGF23 at Ser180 inhibits O-glycosylation and would therefore promote hormone proteolysis and thus inactivation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
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 |
+ |
FAM20C | up-regulates activity
phosphorylation
|
HRC |
0.378 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273639 |
Ser96 |
EKEDEDVsKEYGHLL |
Rattus norvegicus |
H9c2 Cell |
pmid |
sentence |
28784772 |
Here, we demonstrate that family with sequence similarity 20C (Fam20C), a recently characterized protein kinase in the secretory pathway, phosphorylates HRC on Ser96. HRC Ser96 phosphorylation was confirmed in cells and human hearts.The pSer96-HRC binds tighter to triadin than S96A-HRC, which cannot be phosphorylated. Conversely, S96A-HRC or unphosphorylated Ser96-HRC binds tighter to SERCA2a. This suggests that Ser96-HRC phosphorylation (P) regulates HRC’s interactions with the major SR Ca-cycling proteins. |
|
Publications: |
1 |
Organism: |
Rattus Norvegicus |