PKA 2 beta Products

Description

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.

Bioinformatics

Entrez	19088 Mouse 24679 Rat 5577 Human
Uniprot	AAH75800.1 Human KAP3_HUMAN Human NM_002736 Human NP_002727 Human P31323 Human
Product By Gene ID	5577
Alternate Names	cAMP-dependent protein kinase type II-beta regulatory chain cAMP-dependent protein kinase type II-beta regulatory subunit H_RG363E19.2 PRKAR2 protein kinase, cAMP-dependent, regulatory, type II, beta RII-BETA WUGSC:H_RG363E19.2

Research Areas for PKA 2 beta

Find related products by research area and learn more about each of the different research areas below.

Phospho-Specific
Signal Transduction