| + |
PRKG1 | down-regulates activity 
phosphorylation
|
PLCB3 |
0.522 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249077 |
Ser1105 |
LDRKRHNsISEAKMR |
Rattus norvegicus |
Smooth Muscle Cell |
| pmid |
sentence |
| 11278298 |
PKG can directly phosphorylate PLC-beta2 and PLC-beta3 in vitro with purified proteins and in vivo with metabolic labeling. Phosphorylation of PLC-beta leads to the inhibition of G-protein-activated PLC-beta3 activity by 50-70% in COS-7 cell transfection assays. By using phosphopeptide mapping and site-directed mutagenesis, we further identified two key phosphorylation sites for the regulation of PLC-beta3 by PKG (Ser(26) and Ser(1105)). Mutation at these two sites (S26A and S1105A) of PLC-beta3 completely blocked the phosphorylation of PLC-beta3 protein catalyzed by PKG. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249079 |
Ser26 |
VETLRRGsKFIKWDE |
Rattus norvegicus |
Smooth Muscle Cell |
| pmid |
sentence |
| 11278298 |
PKG can directly phosphorylate PLC-beta2 and PLC-beta3 in vitro with purified proteins and in vivo with metabolic labeling. Phosphorylation of PLC-beta leads to the inhibition of G-protein-activated PLC-beta3 activity by 50-70% in COS-7 cell transfection assays. By using phosphopeptide mapping and site-directed mutagenesis, we further identified two key phosphorylation sites for the regulation of PLC-beta3 by PKG (Ser(26) and Ser(1105)). Mutation at these two sites (S26A and S1105A) of PLC-beta3 completely blocked the phosphorylation of PLC-beta3 protein catalyzed by PKG. |
|
| Publications: |
2 |
Organism: |
Rattus Norvegicus |
| + |
PRKCA | down-regulates
phosphorylation
|
PLCB3 |
0.458 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-58859 |
Ser1105 |
LDRKRHNsISEAKMR |
Homo sapiens |
|
| pmid |
sentence |
| 9660757 |
These data establish that direct phosphorylation by pka of ser1105 in the putative g-box of plcbeta3 inhibits galphaq-stimulated plcbeta3 activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKACA | down-regulates
phosphorylation
|
PLCB3 |
0.263 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-79148 |
Ser1105 |
LDRKRHNsISEAKMR |
Homo sapiens |
|
| pmid |
sentence |
| 10893237 |
These data indicate that pkc and pka act similarly in that they inhibit galpha(q)-stimulated plcbeta(3) as a result of phosphorylation of ser(1105). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKG2 | down-regulates activity
phosphorylation
|
PLCB3 |
0.508 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249078 |
Ser1105 |
LDRKRHNsISEAKMR |
Rattus norvegicus |
|
| pmid |
sentence |
| 11278298 |
PKG can directly phosphorylate PLC-beta2 and PLC-beta3 in vitro with purified proteins and in vivo with metabolic labeling. Phosphorylation of PLC-beta leads to the inhibition of G-protein-activated PLC-beta3 activity by 50-70% in COS-7 cell transfection assays. By using phosphopeptide mapping and site-directed mutagenesis, we further identified two key phosphorylation sites for the regulation of PLC-beta3 by PKG (Ser(26) and Ser(1105)). Mutation at these two sites (S26A and S1105A) of PLC-beta3 completely blocked the phosphorylation of PLC-beta3 protein catalyzed by PKG. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249080 |
Ser26 |
VETLRRGsKFIKWDE |
Rattus norvegicus |
Smooth Muscle Cell |
| pmid |
sentence |
| 11278298 |
PKG can directly phosphorylate PLC-beta2 and PLC-beta3 in vitro with purified proteins and in vivo with metabolic labeling. Phosphorylation of PLC-beta leads to the inhibition of G-protein-activated PLC-beta3 activity by 50-70% in COS-7 cell transfection assays. By using phosphopeptide mapping and site-directed mutagenesis, we further identified two key phosphorylation sites for the regulation of PLC-beta3 by PKG (Ser(26) and Ser(1105)). Mutation at these two sites (S26A and S1105A) of PLC-beta3 completely blocked the phosphorylation of PLC-beta3 protein catalyzed by PKG. |
|
| Publications: |
2 |
Organism: |
Rattus Norvegicus |
| + |
CAMK2B |
phosphorylation
|
PLCB3 |
0.509 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250689 |
Ser537 |
PSLEPQKsLGDEGLN |
|
|
| pmid |
sentence |
| 11325525 |
CaMK II phosphorylated PLCbeta3 but not PLCbeta1 in vitro. Phosphorylation occurred exclusively on 537Ser in the X-Y linker region of PLCbeta3. 537Ser was also phosphorylated in the basal state in cells and phosphorylation was enhanced by ionomycin treatment |
|
| Publications: |
1 |
| + |
CAMK2G |
phosphorylation
|
PLCB3 |
0.386 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250702 |
Ser537 |
PSLEPQKsLGDEGLN |
|
|
| pmid |
sentence |
| 11325525 |
CaMK II phosphorylated PLCbeta3 but not PLCbeta1 in vitro. Phosphorylation occurred exclusively on 537Ser in the X-Y linker region of PLCbeta3. 537Ser was also phosphorylated in the basal state in cells and phosphorylation was enhanced by ionomycin treatment |
|
| Publications: |
1 |
| + |
PLCB3 | up-regulates quantity 
|
superoxide |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255014 |
|
|
|
|
| pmid |
sentence |
| 23994464 |
The PI3Kγ pathway (but not PLCβ2/3) is required for chemotaxis of the cells while both pathways are required for GPCR-induced superoxide release |
|
| Publications: |
1 |
| + |
PLCB3 | up-regulates quantity 
chemical modification
|
1D-myo-inositol 1,4,5-trisphosphate(6-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255018 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23994464 |
The first phase of this signal is likely mediated by phospholipase Cβ (PLCβ) enzymes leading to the generation of IP3 and concomitant release of Ca2+ from intracellular stores |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GNB/GNG | up-regulates
|
PLCB3 |
0.367 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255016 |
|
|
|
|
| pmid |
sentence |
| 23994464 |
However, it was later shown that other PLCβ isoforms (particularly PLCβ2 and PLCβ3) can also be directly activated by Gβγ subunits |
|
| Publications: |
1 |
3.0
PLCB3
- 
- 