Protein kinase A (PKA, cAMP-dependent protein kinase) is a key element of a ubiquitous signaling pathway important in the cell cycle, cellular communication, memory formation and behavior. PKA is composed of two catalytic (PKAc; Protein Kinase A catalytic subunit) and two regulatory subunits (PKAr). Upon binding cAMP, the complex dissociates to PKAr dimer and two activated PKAc ser/thr protein kinase catalytic monomers. The released PKAc can translocate into the nucleus and exert a regulatory role in the activation of multiple nuclear hormone receptors. However, PKAc-mediated activation of tonicity-dependent gene expression is cAMP independent. Humans express three types of PKAc subunit - PKAc alpha is present in most human tissues, PKAc beta and gamma are tissue-specific, the later is found in testes.
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Protein Aliases: C(s); C-alpha-2; C-alpha-S; cAMP-dependent protein kinase catalytic subunit alpha; cAMP-dependent protein kinase catalytic subunit alpha, isoform 1; cAMP-dependent protein kinase catalytic subunit C alpha; MGC102831; MGC48865; PKA; PKA C-alpha; pkac; protein kinase A; protein kinase A catalytic subunit; protein kinase, cAMP-dependent, alpha catalytic subunit; protein kinase, cAMP-dependent, catalytic, alpha; sperm cAMP-dependent protein kinase catalytic subunit
Gene Aliases: Cs-PKA; PKACA; PKCA1; PKCD; PPNAD4; PRKACA
Molecular Function: non-receptor serine/threonine protein kinase