Aliases for PRKAB1 Gene
External Ids for PRKAB1 Gene
The protein encoded by this gene is a regulatory subunit of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status. In response to cellular metabolic stresses, AMPK is activated, and thus phosphorylates and inactivates acetyl-CoA carboxylase (ACC) and beta-hydroxy beta-methylglutaryl-CoA reductase (HMGCR), key enzymes involved in regulating de novo biosynthesis of fatty acid and cholesterol. This subunit may be a positive regulator of AMPK activity. The myristoylation and phosphorylation of this subunit have been shown to affect the enzyme activity and cellular localization of AMPK. This subunit may also serve as an adaptor molecule mediating the association of the AMPK complex. [provided by RefSeq, Jul 2008]
GeneCards Summary for PRKAB1 Gene
PRKAB1 (Protein Kinase, AMP-Activated, Beta 1 Non-Catalytic Subunit) is a Protein Coding gene. Diseases associated with PRKAB1 include krabbe disease. Among its related pathways are Signaling by GPCR and Insulin receptor signalling cascade. GO annotations related to this gene include protein kinase binding and protein kinase activity. An important paralog of this gene is PRKAB2.
UniProtKB/Swiss-Prot for PRKAB1 Gene
Non-catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C-terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3)
AMP-activated protein kinase (AMPK) is a heterodimeric protein serine/threonine kinase that is composed of alpha- (catalytic) and beta/gamma- (regulatory) subunits. AMPK acts as a sensor of the energy status of cells and ensures survival at times of metabolic stress. AMPK phosphorylates many metabolic enzymes to stimulate catabolic pathways, such as ketogenesis, and inhibit anabolic pathways, such as protein synthesis. The long-term activation of AMPK increases the capacity of cells to produce ATP. AMPK is regulated by phosphorylation at the Thr-172 residue of the alpha-subunit by AMPKK and by phosphorylation by calmodulin-dependent protein kinase kinase-beta (CamKKbeta). In addition, the ratio of AMP:ATP mediates allosteric activation of the enzyme. AMPK is found throughout the body with high concentrations in metabolically active tissues such as the skeletal muscles and liver.