PRKAR2A Back

protein kinase, cAMP-dependent, regulatory, type II, alpha

External References:      Wikipedia GeneCards HUGO COSMIC Google Scholar

NCBI Description of 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).

Community Annotation of PRKAR2A Add / Edit PRKAR2A: Annotations

No community annotations yet for PRKAR2A.
Sort mutations by: Tumor type  Mutation type  Position  
Straightedge cursor Expand

Figure notes


• "Mouse over" a mutation to see details.
• Missense green saturation indicates evolutionary conservation of the mutated positions.
• Red hashes in protein strip are splice sites.
• Blue-white-red bars are log2 copy ratio distributions (–1 to +1) from Zack et al. (2013).


Legend

PRKAR2A is highly significantly mutated in
(none)
PRKAR2A is significantly mutated in
(none)
PRKAR2A is near significance in
(none)

Click on a tumor type to see its full list of significant genes.

Data details


Mutation list for PRKAR2A