Aliases for PRKAR2B Gene
External Ids for PRKAR2B Gene
Previous Symbols for PRKAR2B 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. This subunit has been shown to interact with and suppress the transcriptional activity of the cAMP responsive element binding protein 1 (CREB1) in activated T cells. Knockout studies in mice suggest that this subunit may play an important role in regulating energy balance and adiposity. The studies also suggest that this subunit may mediate the gene induction and cataleptic behavior induced by haloperidol. [provided by RefSeq, Jul 2008]
GeneCards Summary for PRKAR2B Gene
PRKAR2B (Protein Kinase, CAMP-Dependent, Regulatory, Type II, Beta) is a Protein Coding gene. Among its related pathways are Signaling by FGFR and Signaling by FGFR. GO annotations related to this gene include protein domain specific binding and cAMP-dependent protein kinase regulator activity. An important paralog of this gene is PRKAR2A.
UniProtKB/Swiss-Prot for PRKAR2B 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).