PRKAR2B

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.

Protein kinase cAMP-dependent type II regulatory subunit beta

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.

Fatty acid metabolic processIEA:Ensembl
Intracellular signal transductionManual Assertion Based On ExperimentTAS:ProtInc
LearningIEA:Ensembl
Modulation of chemical synaptic transmissionIEA:Ensembl
Negative regulation of cAMP-dependent protein kinase activityManual Assertion Based On ExperimentIDA:BHF-UCL
Response to antipsychotic drugIEA:Ensembl
Response to clozapineIEA:Ensembl

Cytoplasm
Cell membrane
Colocalizes with PJA2 in the cytoplasm and at the cell membrane.

Phosphorylated by the activated catalytic chain.