+ |
PRKCA | up-regulates
phosphorylation
|
PDE3A |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-184448 |
Ser312 |
SKSHRRTsLPCIPRE |
Homo sapiens |
|
pmid |
sentence |
19261611 |
Phosphorylation and activation of pde3a required the activation of pkc |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-184452 |
Ser428 |
IPKRLRRsLPPGLLR |
Homo sapiens |
|
pmid |
sentence |
19261611 |
Protein kinase c-mediated phosphorylation and activation of pde3a regulate camp levels in human platelets. together, these results demonstrate that platelet activation stimulates pkc-dependent phosphorylation of pde3a on ser(312), ser(428), ser(438), ser(465), and ser(492) leading to a subsequent increase in camp hydrolysis and 14-3-3 binding. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-184456 |
Ser438 |
PGLLRRVsSTWTTTT |
Homo sapiens |
|
pmid |
sentence |
19261611 |
Protein kinase c-mediated phosphorylation and activation of pde3a regulate camp levels in human platelets. together, these results demonstrate that platelet activation stimulates pkc-dependent phosphorylation of pde3a on ser(312), ser(428), ser(438), ser(465), and ser(492) leading to a subsequent increase in camp hydrolysis and 14-3-3 binding. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-184460 |
Ser465 |
VRRDRSTsIKLQEAP |
Homo sapiens |
|
pmid |
sentence |
19261611 |
Protein kinase c-mediated phosphorylation and activation of pde3a regulate camp levels in human platelets. together, these results demonstrate that platelet activation stimulates pkc-dependent phosphorylation of pde3a on ser(312), ser(428), ser(438), ser(465), and ser(492) leading to a subsequent increase in camp hydrolysis and 14-3-3 binding. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-184464 |
Ser492 |
MTLTKSRsFTSSYAI |
Homo sapiens |
|
pmid |
sentence |
19261611 |
Protein kinase c-mediated phosphorylation and activation of pde3a regulate camp levels in human platelets. together, these results demonstrate that platelet activation stimulates pkc-dependent phosphorylation of pde3a on ser(312), ser(428), ser(438), ser(465), and ser(492) leading to a subsequent increase in camp hydrolysis and 14-3-3 binding. |
|
Publications: |
5 |
Organism: |
Homo Sapiens |
+ |
PRKACA |
phosphorylation
|
PDE3A |
0.495 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-140289 |
Ser312 |
SKSHRRTsLPCIPRE |
Homo sapiens |
|
pmid |
sentence |
16153182 |
Ser312 of pde3a was phosphorylated in an h-89-sensitive response to forskolin, indicative of phosphorylation by pka (camp-dependent protein kinase), but phosphorylation at this site did not stimulate 14-3-3 binding. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PDE3A | down-regulates activity
binding
|
ATP2A2 |
0.348 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262051 |
|
|
Homo sapiens |
|
pmid |
sentence |
25593322 |
Regulation of sarcoplasmic reticulum Ca2+ ATPase 2 (SERCA2) activity by phosphodiesterase 3A (PDE3A) in human myocardium: phosphorylation-dependent interaction of PDE3A1 with SERCA2.|PDE3A co-localized with PLB, SERCA2, and an AKAP18 variant|our studies show that PDE3-selective inhibition (but not PDE4 inhibition) potentiates the phosphorylation of PLB by endogenous PKA and stimulation of SERCA2 activity and Ca2+ uptake in SR-enriched vesicles prepared from human myocardium. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Cardiac Muscle |