PRKAR2A

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]

Description

Protein kinase cAMP-dependent type II regulatory subunit alpha

Tissue specificity

Tissue enhanced (skeletal muscle, testis)

Predicted location

Intracellular

Protein family

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

Chromosome

3 (48744597 - 48847874)

Ensembl ID

ENSG00000114302  (ver. 103.38)

Orthologs

Mouse Prkar2a: ENSMUSG00000032601

UniProt

P13861

neXtProt

NX_P13861

Human splice variants
Mouse splice variants

Protein structure