PRKAR2A Blocking Peptide (C-Term) Blocking Peptide

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]

PKAR2A: a regulatory subunit of cAMP-regulated protein kinase. The inactive form of the enzyme is composed of two regulatory chains and two catalytic chains. Activation by cAMP produces two active catalytic monomers and a regulatory dimer that binds four cAMP molecules. Four types of regulatory chains are found: I-alpha, I-beta, II-alpha, and II-beta. Their expression varies among tissues and is in some cases constitutive and in others inducible.

Protein type: Protein kinase, regulatory subunit

Chromosomal Location of Human Ortholog: 3p21.3-p21.2

Cellular Component: AMP-activated protein kinase complex; centrosome; cytoplasm; cytosol; focal adhesion; membrane; plasma membrane

Molecular Function: cAMP-dependent protein kinase inhibitor activity; cAMP-dependent protein kinase regulator activity; protein binding; ubiquitin protein ligase binding

Biological Process: activation of protein kinase A; blood coagulation; renal water homeostasis