Aliases for PRKAR1A Gene
External Ids for PRKAR1A Gene
Previous HGNC Symbols for PRKAR1A Gene
Previous GeneCards Identifiers for PRKAR1A Gene
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. This gene encodes one of the regulatory subunits. This protein was found to be a tissue-specific extinguisher that down-regulates the expression of seven liver genes in hepatoma x fibroblast hybrids. Mutations in this gene cause Carney complex (CNC). This gene can fuse to the RET protooncogene by gene rearrangement and form the thyroid tumor-specific chimeric oncogene known as PTC2. A nonconventional nuclear localization sequence (NLS) has been found for this protein which suggests a role in DNA replication via the protein serving as a nuclear transport protein for the second subunit of the Replication Factor C (RFC40). Several alternatively spliced transcript variants encoding two different isoforms have been observed. [provided by RefSeq, Jan 2013]
GeneCards Summary for PRKAR1A Gene
PRKAR1A (Protein Kinase, CAMP-Dependent, Regulatory, Type I, Alpha) is a Protein Coding gene. Diseases associated with PRKAR1A include carney complex, type 1 and myxoma, intracardiac. Among its related pathways are Signaling by FGFR and Signaling by FGFR. GO annotations related to this gene include ubiquitin protein ligase binding and cAMP binding. An important paralog of this gene is PRKAR2B.
UniProtKB/Swiss-Prot for PRKAR1A Gene
Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells.
Protein kinase A (PKA, aka cAMP-dependent protein kinase) is involved in the regulation of lipid and glucose metabolism and is a component of the signal transduction mechanism of certain GPCRs. Protein kinase A is composed of two regulatory subunits and two catalytic subunits. There are multiple isoforms of the regulatory subunit (RIalpha- and RIbeta-, RIIalpha- and RIIbeta-). Binding of cAMP to the regulatory subunit releases the catalytic subunits, which then phosphorylate a diverse set of proteins including the transcription factor CREB, ion channels and metabolic enzymes. Protein kinase A is localized to specific sites near these substrates within cells by scaffold proteins known as A kinase anchoring proteins (AKAPs).