| + |
PRKG1 | up-regulates activity 
phosphorylation
|
PRKAR1A |
0.235 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277383 |
Ser101 |
RRRRGAIsAEVYTEE |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 29378851 |
In this study, we further examined the potential of RIα phosphorylation to regulate physiologically relevant "desensitization" of PKAc activity. First, the serine 101 site of RIα was validated as a target of PKGIα phosphorylation both in vitro and in cells.These findings suggest that RIα phosphorylation may be a novel mechanism to circumvent the requirement of cAMP stimulus to activate type I PKA in cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK2 | up-regulates
phosphorylation
|
PRKAR1A |
0.344 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-145577 |
Ser83 |
DSREDEIsPPPPNPV |
Homo sapiens |
|
| pmid |
sentence |
| 16582606 |
In this context, we have identified rialpha as a novel substrate for the g(1)/s-cyclin-dependent kinase, cdk2/cyclin e, and found that rialpha is specifically phosphorylated at the serine residue. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK16 | up-regulates activity
phosphorylation
|
PRKAR1A |
0.272 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273018 |
Ser83 |
DSREDEIsPPPPNPV |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 25605337 |
PCTK1 regulates spindle orientation in a kinase-dependent manner. Phosphoproteomic analysis together with an RNA interference screen revealed that PCTK1 regulates spindle orientation through phosphorylation of Ser83 on KAP0, a regulatory subunit of protein kinase A (PKA) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CyclinY/CDK16 | up-regulates activity
phosphorylation
|
PRKAR1A |
0.272 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273014 |
Ser83 |
DSREDEIsPPPPNPV |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 25605337 |
PCTK1 regulates spindle orientation in a kinase-dependent manner. Phosphoproteomic analysis together with an RNA interference screen revealed that PCTK1 regulates spindle orientation through phosphorylation of Ser83 on KAP0, a regulatory subunit of protein kinase A (PKA) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CyclinE/CDK2 | up-regulates
phosphorylation
|
PRKAR1A |
0.302 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216729 |
Ser83 |
DSREDEIsPPPPNPV |
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 16582606 |
In this context, we have identified rialpha as a novel substrate for the g(1)/s-cyclin-dependent kinase, cdk2/cyclin e, and found that rialpha is specifically phosphorylated at the serine residue. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PDE4DIP | up-regulates
binding
|
PRKAR1A |
0.316 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173769 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21569246 |
Mmgl acts as a dual-specific akap by anchoring pka regulatory isoforms r1a and r2a. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
3',5'-cyclic AMP | down-regulates activity 
chemical inhibition
|
PRKAR1A |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258759 |
|
|
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 |
| + |
PRKAR1A | down-regulates activity
binding
|
PRKACB |
0.862 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258755 |
|
|
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 |
| + |
PRKAR1A | down-regulates activity
binding
|
PRKACA |
0.885 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258751 |
|
|
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 |
| + |
FOXD2 | up-regulates quantity by expression
transcriptional regulation
|
PRKAR1A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261605 |
|
|
Homo sapiens |
JURKAT Cell |
| pmid |
sentence |
| 12621056 |
Elevating the amounts of FOXD2 expression vector up to 12-fold relative to the RIα1b reporter construct demonstrated that maximal induction of the RIα1b promoter by FOXD2 was at least 5.8-fold |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PJA2 | down-regulates quantity by destabilization
polyubiquitination
|
PRKAR1A |
0.38 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271855 |
|
|
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 |
3.0
PRKAR1A
- 
- 