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. The studies also suggest that this subunit may mediate the gene induction and cataleptic behavior induced by haloperidol. [provided by RefSeq, Jul 2008]

Description

Protein kinase cAMP-dependent type II regulatory subunit beta

Tissue specificity

Tissue enhanced (adipose tissue)

Subcell location

Mitochondria

Predicted location

Intracellular

Protein family

Mapped to neXtProt
Mapped to UniProt SWISS-PROT
Metabolic proteins
Predicted intracellular proteins
Protein evidence (Ezkurdia et al 2014)
Protein evidence (Kim et al 2014)

Chromosome

7 (107044705 - 107161811)

Ensembl ID

ENSG00000005249  (ver. 103.38)

Orthologs

Mouse Prkar2b: ENSMUSG00000002997

UniProt

P31323

neXtProt

NX_P31323

Human splice variants
Mouse splice variants

Protein structure