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Literature summary for 2.7.11.11 extracted from

  • Manni, S.; Mauban, J.H.; Ward, C.W.; Bond, M.
    Phosphorylation of the cAMP-dependent protein kinase (PKA) regulatory subunit modulates PKA-AKAP interaction, substrate phosphorylation, and calcium signaling in cardiac cells (2008), J. Biol. Chem., 283, 24145-24154.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
3-isobutyryl-1-methylxanthine stimulates activity at 0.1 mM Rattus norvegicus
8-bromo-cAMP stimulates activity at 0.1 mM Rattus norvegicus
forskolin stimulates activity at 0.025 mM Rattus norvegicus
isoproterenol stimulates activity at 2.5 nM Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
R96D the mutation mimics phosphorylated regulatory subunit RII Rattus norvegicus
RS96A the mutation mimics unphosphorylated regulatory subunit RII Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
Rattus norvegicus 5737
-

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
cardiomyocyte
-
Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + ryanodine receptor
-
Rattus norvegicus ADP + phosphorylated ryanodine receptor
-
?
additional information autophosphorylation of the PKA type II regulatory subunit (RII) can alter its affinity for protein kinase A-anchoring proteins and the catalytic subunit of PKA, RII phosphorylation regulates PKA-dependent substrate phosphorylation and may have significant implications for modulation of cardiac function Rattus norvegicus ?
-
?

Synonyms

Synonyms Comment Organism
PKA
-
Rattus norvegicus
protein kinase A
-
Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
ATP
-
Rattus norvegicus
cAMP dependent Rattus norvegicus