| + |
PRKCA | up-regulates activity 
phosphorylation
|
NRGN |
0.385 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248913 |
Ser36 |
AAAKIQAsFRGHMAR |
in vitro |
|
| pmid |
sentence |
| 8080473 |
Phosphorylation of RC3 by PKC alpha, beta, or gamma was stimulated by Ca2+, phospholipid, and diacylglycerol. A single site, Ser36, which is adjacent to the predicted calmodulin (CaM)-binding domain, was phosphorylated by these enzymes. Phosphorylation of RC3 by PKC or PKM, a protease-degraded PKC, was inhibited by CaM. The effect of CaM apparently targets at RC3, as phosphorylation of protamine sulfate by PKM was not inhibited by CaM. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKCG | up-regulates activity
phosphorylation
|
NRGN |
0.42 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248915 |
Ser36 |
AAAKIQAsFRGHMAR |
in vitro |
|
| pmid |
sentence |
| 8080473 |
Phosphorylation of RC3 by PKC alpha, beta, or gamma was stimulated by Ca2+, phospholipid, and diacylglycerol. A single site, Ser36, which is adjacent to the predicted calmodulin (CaM)-binding domain, was phosphorylated by these enzymes. Phosphorylation of RC3 by PKC or PKM, a protease-degraded PKC, was inhibited by CaM. The effect of CaM apparently targets at RC3, as phosphorylation of protamine sulfate by PKM was not inhibited by CaM. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKCB | up-regulates activity
phosphorylation
|
NRGN |
0.353 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248914 |
Ser36 |
AAAKIQAsFRGHMAR |
in vitro |
|
| pmid |
sentence |
| 8080473 |
Phosphorylation of RC3 by PKC alpha, beta, or gamma was stimulated by Ca2+, phospholipid, and diacylglycerol. A single site, Ser36, which is adjacent to the predicted calmodulin (CaM)-binding domain, was phosphorylated by these enzymes. Phosphorylation of RC3 by PKC or PKM, a protease-degraded PKC, was inhibited by CaM. The effect of CaM apparently targets at RC3, as phosphorylation of protamine sulfate by PKM was not inhibited by CaM. |
|
| Publications: |
1 |
Organism: |
In Vitro |
4.0
NRGN
- 
- 