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PRKAR2A

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

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).

Gene Name: protein kinase, cAMP-dependent, regulatory, type II, alpha
Family/Subfamily: Protein Kinase Non Catalytic , not assigned-Protein Kinase Non Catalytic
Synonyms: PRKAR2A, PKR2, PRKAR2
Target Sequences: BT007225 AAP35889.1 P13861

Publications (1)

1
Phosphorylation of the cAMP-dependent protein kinase (PKA) regulatory subunit modulates PKA-AKAP interaction, substrate phosphorylation, and calcium signaling in cardiac cells. Manni S, Mauban JH, Ward CW, Bond M. The Journal of biological chemistry. 2008 283:24145-54. (WB) [PubMed:18550536] [PMC:PMC2527120]

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For RESEARCH USE ONLY. Intended for use by laboratory professionals. Not intended for human diagnostic or therapeutic purposes.

The data on this page has been compiled from LifeSpan internal sources, the National Center for Biotechnology Information (NCBI), and The Universal Protein Resource (UniProt).