+ |
PRKAR2B | up-regulates activity
phosphorylation
|
PRKAR2B |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250076 |
Ser114 |
NRFTRRAsVCAEAYN |
Mus musculus |
|
pmid |
sentence |
15822905 |
Ser114 (the autophosphorylation site) of human RII beta. Point mutation of the autophosphorylation site or in the nuclear location signal causes protein kinase A RII beta regulatory subunit to lose its ability to revert transformed fibroblasts. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
PRKACA | up-regulates activity
phosphorylation
|
PRKAR2B |
0.876 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-125545 |
Ser114 |
NRFTRRAsVCAEAYN |
Homo sapiens |
|
pmid |
sentence |
15187164 |
Serine 114 phosphorylation is required for both nuclear localization and down-regulation of il-2 production by riibeta. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRKAR2B | down-regulates activity
binding
|
PRKACA |
0.876 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-258754 |
|
|
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 |
+ |
PJA2 | down-regulates quantity by destabilization
polyubiquitination
|
PRKAR2B |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271858 |
|
|
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 |
+ |
PRKAR2B | down-regulates activity
binding
|
PRKACB |
0.89 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-258758 |
|
|
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
|
PRKAR2B |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-258762 |
|
|
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 |