| + |
PKA | up-regulates activity
phosphorylation
|
SEC14L2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273788 |
Ser289 |
VQISRGSsHQVEYEI |
in vitro |
|
| pmid |
sentence |
| 15680919 |
Thus, phosphorylation of SPF at Ser-289 appears necessary for maximal stimulation of squalene monooxygenase activity in vitro and absolutely required for the stimulation of cholesterol synthesis in cell culture. the 2.3-fold activation of SPF by PKA was reduced by 60% in the S289A mutant, indicating that phosphorylation of this site contributes to the activation of SPF. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276028 |
Ser289 |
VQISRGSsHQVEYEI |
in vitro |
|
| pmid |
sentence |
| 15680919 |
These results suggest that phosphorylation of SPF by PKA is a dynamic process and that, in the absence of PKA activity, SPF is rapidly inactivated.Thus, phosphorylation of SPF at Ser-289 appears necessary for maximal stimulation of squalene monooxygenase activity in vitro and absolutely required for the stimulation of cholesterol synthesis in cell culture. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PRKACA | up-regulates activity
phosphorylation
|
SEC14L2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276027 |
Ser289 |
VQISRGSsHQVEYEI |
in vitro |
|
| pmid |
sentence |
| 15680919 |
These results suggest that phosphorylation of SPF by PKA is a dynamic process and that, in the absence of PKA activity, SPF is rapidly inactivated.Thus, phosphorylation of SPF at Ser-289 appears necessary for maximal stimulation of squalene monooxygenase activity in vitro and absolutely required for the stimulation of cholesterol synthesis in cell culture. |
|
| Publications: |
1 |
Organism: |
In Vitro |