| + |
PJA2 | down-regulates quantity by destabilization 
polyubiquitination
|
PRKAR1B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271857 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21423175 |
Praja2 controls the stability of PKA regulatory subunits. Praja2 ubiquitylates RIIα/β subunits. Subunits |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKAR1B | down-regulates activity
binding
|
PRKACA |
0.851 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258753 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26687711 |
Inactive PKA exists as a holoenzyme, comprised of two regulatory (R) subunits and two catalytic subunits . In the presence of cAMP, the holoenzyme becomes active by binding two cAMP molecules cooperatively to each R subunit, resulting in a conformational change in the R subunits, thus releasing the two C subunits to phosphorylate downstream targets |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKAR1B | down-regulates activity
binding
|
PRKACB |
0.876 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258756 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26687711 |
Inactive PKA exists as a holoenzyme, comprised of two regulatory (R) subunits and two catalytic subunits . In the presence of cAMP, the holoenzyme becomes active by binding two cAMP molecules cooperatively to each R subunit, resulting in a conformational change in the R subunits, thus releasing the two C subunits to phosphorylate downstream targets |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
3',5'-cyclic AMP | down-regulates activity
chemical inhibition
|
PRKAR1B |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258760 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26687711 |
Inactive PKA exists as a holoenzyme, comprised of two regulatory (R) subunits and two catalytic subunits . In the presence of cAMP, the holoenzyme becomes active by binding two cAMP molecules cooperatively to each R subunit, resulting in a conformational change in the R subunits, thus releasing the two C subunits to phosphorylate downstream targets |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
PRKAR1B
- 
- 