| + |
PRKACB | down-regulates activity 
phosphorylation
|
TENT2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259403 |
Ser116 |
LSGERRYsMPPLFHT |
Homo sapiens |
|
| pmid |
sentence |
| 31057087 |
We found that Gld2 activity is regulated by site-specific phosphorylation in its disordered N-terminal domain. We identified two phosphorylation sites (S62, S110) where phosphomimetic substitutions increased Gld2 activity and one site (S116) that markedly reduced activity. Using mass spectrometry, we confirmed that HEK 293 cells readily phosphorylate the N-terminus of Gld2. We identified protein kinase A (PKA) and protein kinase B (Akt1) as the kinases that site-specifically phosphorylate Gld2 at S116, abolishing Gld2-mediated nucleotide addition. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKACB | down-regulates
phosphorylation
|
BAD |
0.403 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-81141 |
Ser118 |
GRELRRMsDEFVDSF |
Homo sapiens |
|
| pmid |
sentence |
| 10949026 |
Ser-155 is the major phosphoacceptor site for pka on bad, but that pka also phosphorylates ser-112 and ser-136. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-81145 |
Ser75 |
EIRSRHSsYPAGTED |
Homo sapiens |
|
| pmid |
sentence |
| 10949026 |
Ser-155 is the major phosphoacceptor site for pka on bad, but that pka also phosphorylates ser-112 and ser-136. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-81149 |
Ser99 |
PFRGRSRsAPPNLWA |
Homo sapiens |
|
| pmid |
sentence |
| 10949026 |
Ser-155 is the major phosphoacceptor site for pka on bad, but that pka also phosphorylates ser-112 and ser-136. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PRKACB | up-regulates activity 
phosphorylation
|
GPKOW |
0.311 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266311 |
Ser27 |
SFGFTRTsARRRLAD |
in vitro |
|
| pmid |
sentence |
| 21880142 |
Using yeast two-hybrid screening with the PKA Cβ2 subunit as bait we identified GPKOW, also known as MOS2 homolog or T54 protein, as an interaction partner for Cβ2. PKA phosphorylates GPKOW at S27 and T316 in vitro. GPKOWs ability to bind RNA is sensitive to mutations of its PKA phosphorylation sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266299 |
Ser27 |
SFGFTRTsARRRLAD |
|
|
| pmid |
sentence |
| 21880142 |
Using yeast two-hybrid screening with the PKA Cβ2 subunit as bait we identified GPKOW, also known as MOS2 homolog or T54 protein, as an interaction partner for Cβ2. PKA phosphorylates GPKOW at S27 and T316 in vitro. GPKOWs ability to bind RNA is sensitive to mutations of its PKA phosphorylation sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266298 |
Thr316 |
GTASSRKtLWNQELY |
|
|
| pmid |
sentence |
| 21880142 |
Using yeast two-hybrid screening with the PKA Cβ2 subunit as bait we identified GPKOW, also known as MOS2 homolog or T54 protein, as an interaction partner for Cβ2.PKA phosphorylates GPKOW at S27 and T316 in vitro. GPKOWs ability to bind RNA is sensitive to mutations of its PKA phosphorylation sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266310 |
Thr316 |
GTASSRKtLWNQELY |
in vitro |
|
| pmid |
sentence |
| 21880142 |
Using yeast two-hybrid screening with the PKA Cβ2 subunit as bait we identified GPKOW, also known as MOS2 homolog or T54 protein, as an interaction partner for Cβ2.PKA phosphorylates GPKOW at S27 and T316 in vitro. GPKOWs ability to bind RNA is sensitive to mutations of its PKA phosphorylation sites. |
|
| Publications: |
4 |
Organism: |
In Vitro, |
| + |
PRKACB | up-regulates
phosphorylation
|
MYBPC3 |
0.276 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163768 |
Ser275 |
LSAFRRTsLAGGGRR |
Homo sapiens |
|
| pmid |
sentence |
| 20151718 |
Phosphorylation of cmybp-c by pka speeds actomyosin interactions and contributes to increased cardiac contractility following _-adrenergic stimulation.7, 8 phosphorylation by pka is essential for proper cardiac function /for the human isoform, three pka sites were previously identified (ser275, ser284, and ser304) /our results indicate that pka phosphorylates up to four sites in both the murine and human m-domains including a novel site not previously described for either protein (ser307 for mouse and ser311 for human). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163772 |
Ser284 |
AGGGRRIsDSHEDTG |
Homo sapiens |
|
| pmid |
sentence |
| 20151718 |
Phosphorylation of cmybp-c by pka speeds actomyosin interactions and contributes to increased cardiac contractility following _-adrenergic stimulation.7, 8 phosphorylation by pka is essential for proper cardiac function /for the human isoform, three pka sites were previously identified (ser275, ser284, and ser304) /our results indicate that pka phosphorylates up to four sites in both the murine and human m-domains including a novel site not previously described for either protein (ser307 for mouse and ser311 for human). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163776 |
Ser304 |
SLLKKRDsFRTPRDS |
Homo sapiens |
|
| pmid |
sentence |
| 20151718 |
Phosphorylation of cmybp-c by pka speeds actomyosin interactions and contributes to increased cardiac contractility following _-adrenergic stimulation.7, 8 phosphorylation by pka is essential for proper cardiac function /for the human isoform, three pka sites were previously identified (ser275, ser284, and ser304) /our results indicate that pka phosphorylates up to four sites in both the murine and human m-domains including a novel site not previously described for either protein (ser307 for mouse and ser311 for human). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163780 |
Ser311 |
SFRTPRDsKLEAPAE |
Homo sapiens |
|
| pmid |
sentence |
| 20151718 |
Phosphorylation of cmybp-c by pka speeds actomyosin interactions and contributes to increased cardiac contractility following _-adrenergic stimulation./Phosphorylation by pka is essential for proper cardiac function /for the human isoform, three pka sites were previously identified (ser275, ser284, and ser304) /our results indicate that pka phosphorylates up to four sites in both the murine and human m-domains including a novel site not previously described for either protein (ser307 for mouse and ser311 for human). |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle |
| + |
PRKACB | up-regulates
phosphorylation
|
NGFR |
0.609 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-99755 |
Ser303 |
PEGEKLHsDSGISVD |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 12682012 |
Pka phosphorylates the p75 receptor and regulates its localization to lipid rafts. activation of camp?PKA Is required for translocation of p75ntr to lipid rafts, and for biochemical and biological activities of p75ntr, such as inactivation of rho and the neurite outgrowth. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKACB | down-regulates activity
phosphorylation
|
PHKA1 |
0.307 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267413 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10487978 |
Phosphorylation of the alpha and beta subunits by the 3',5'-cyclic adenosine monophosphate (cAMP)-dependent protein kinase (PKA) also relieves inhibition of the gamma subunit and thereby activates the enzyme. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKACB | down-regulates activity
phosphorylation
|
PHKA2 |
0.307 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267412 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10487978 |
Phosphorylation of the alpha and beta subunits by the 3',5'-cyclic adenosine monophosphate (cAMP)-dependent protein kinase (PKA) also relieves inhibition of the gamma subunit and thereby activates the enzyme. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKAR1A | down-regulates activity
binding
|
PRKACB |
0.858 |
| 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 |
| + |
Ruboxistaurin | down-regulates activity
chemical inhibition
|
PRKACB |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258275 |
|
|
in vitro |
|
| pmid |
sentence |
| 22037378 |
Our data set represents the most detailed comprehensive assessment of the reactivity of known and clinical kinase inhibitors across the kinome published to date. | The data also show that for at least 15 of the 27 kinases that are the primary, intended targets for the compounds tested and that are represented in the assay panel, selective inhibitors, as assessed by both absolute selectivity across the kinome and selectivity relative to the primary target, are among the 72 tested here. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
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-(1-methyl-3-indolyl)-4-[1-[1-(2-pyridinylmethyl)-4-piperidinyl]-3-indolyl]pyrrole-2,5-dione | down-regulates activity
chemical inhibition
|
PRKACB |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258211 |
|
|
in vitro |
|
| pmid |
sentence |
| 22037378 |
Our data set represents the most detailed comprehensive assessment of the reactivity of known and clinical kinase inhibitors across the kinome published to date. | The data also show that for at least 15 of the 27 kinases that are the primary, intended targets for the compounds tested and that are represented in the assay panel, selective inhibitors, as assessed by both absolute selectivity across the kinome and selectivity relative to the primary target, are among the 72 tested here. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
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 |
| + |
PRKAR2A | down-regulates activity
binding
|
PRKACB |
0.891 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258757 |
|
|
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
PRKACB
- 
- 