| + |
CAMK2A |
phosphorylation
|
PDC |
0.308 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250636 |
Ser54 |
KEILRQMsSPQSRNG |
|
|
| pmid |
sentence |
| 11331285 |
In this study, we report that Pd was rapidly phosphorylated by Ca(2+)/calmodulin-dependent kinase II, resulting in 100-fold greater inhibition of Gbetagamma binding than cAMP-dependent protein kinase phosphorylation. Furthermore, Pd phosphorylation by Ca(2+)/calmodulin-dependent kinase II at Ser-54 and Ser-73 led to binding of the phosphoserine-binding protein 14-3-3. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250637 |
Ser73 |
ERVSRKMsIQEYELI |
|
|
| pmid |
sentence |
| 11331285 |
In this study, we report that Pd was rapidly phosphorylated by Ca(2+)/calmodulin-dependent kinase II, resulting in 100-fold greater inhibition of Gbetagamma binding than cAMP-dependent protein kinase phosphorylation. Furthermore, Pd phosphorylation by Ca(2+)/calmodulin-dependent kinase II at Ser-54 and Ser-73 led to binding of the phosphoserine-binding protein 14-3-3. |
|
| Publications: |
2 |
| + |
GRK2 | down-regulates activity 
phosphorylation
|
PDC |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279411 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10884381 |
Phosphorylation of phosducin by GRK2 markedly reduces its G beta gamma binding ability|The phosphorylation of purified phosducin and PhLP by recombinant GRK2 proceeds rapidly and stoichiometrically (0.82 +/- 0.1 and 0.83 +/- 0.09 mol of P(i)/mol of protein, respectively). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
PDC
- 
- 