Aliases for PRKAR2A Gene
External Ids for PRKAR2A Gene
Previous Symbols for PRKAR2A Gene
cAMP is a signaling molecule important for a variety of cellular functions. cAMP exerts its effects by activating the cAMP-dependent protein kinase, which transduces the signal through phosphorylation of different target proteins. The inactive kinase holoenzyme is a tetramer composed of two regulatory and two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. Four different regulatory subunits and three catalytic subunits have been identified in humans. The protein encoded by this gene is one of the regulatory subunits. This subunit can be phosphorylated by the activated catalytic subunit. It may interact with various A-kinase anchoring proteins and determine the subcellular localization of cAMP-dependent protein kinase. This subunit has been shown to regulate protein transport from endosomes to the Golgi apparatus and further to the endoplasmic reticulum (ER). [provided by RefSeq, Jul 2008]
GeneCards Summary for PRKAR2A Gene
PRKAR2A (Protein Kinase, CAMP-Dependent, Regulatory, Type II, Alpha) is a Protein Coding gene. Among its related pathways are Signaling by FGFR and Signaling by FGFR. GO annotations related to this gene include ubiquitin protein ligase binding and cAMP binding. An important paralog of this gene is PRKAR2B.
UniProtKB/Swiss-Prot for PRKAR2A Gene
Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase
Protein kinase A (PKA, aka cAMP-dependent protein kinase) is involved in the regulation of lipid and glucose metabolism and is a component of the signal transduction mechanism of certain GPCRs. Protein kinase A is composed of two regulatory subunits and two catalytic subunits. There are multiple isoforms of the regulatory subunit (RIalpha- and RIbeta-, RIIalpha- and RIIbeta-). Binding of cAMP to the regulatory subunit releases the catalytic subunits, which then phosphorylate a diverse set of proteins including the transcription factor CREB, ion channels and metabolic enzymes. Protein kinase A is localized to specific sites near these substrates within cells by scaffold proteins known as A kinase anchoring proteins (AKAPs).