NP_005390.1
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NCBI GenBank Nucleotide #
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UniProt Primary Accession #
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UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
57.3 kDa
NCBI Official Full Name
5'-AMP-activated protein kinase subunit beta-2
NCBI Official Synonym Full Names
protein kinase, AMP-activated, beta 2 non-catalytic subunit
NCBI Protein Information
5'-AMP-activated protein kinase subunit beta-2; AMPK beta 2; AMPK beta-2 chain; AMPK subunit beta-2; 5'-AMP-activated protein kinase, beta-2 subunit; AMP-activated protein kinase beta 2 non-catalytic subunit
UniProt Protein Name
5'-AMP-activated protein kinase subunit beta-2
UniProt Synonym Gene Names
UniProt Entry Name
AAKB2_HUMAN
NCBI Summary for PRKAB2
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. It is highly expressed in skeletal muscle and thus may have tissue-specific roles. Multiple alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Jul 2013]
UniProt Comments for PRKAB2
AMPKB2: a non-catalytic subunit of AMPK, a conserved kinase of the CAMKL family. AMPK is an energy-sensing protein that plays a key role in regulating cellular energy homeostasis. Environmental stress, such as heat shock, nutrient deprivation, hypoxia and ischemia, indirectly activate AMPK by the depletion of cellular ATP and the concomitant rise of ADP and AMP levels. Allosteric activation is achieved primarily by rising ADP levels, and not solely by AMP levels as previously thought. 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. AMPK is a heterotrimer of an alpha catalytic subunit (AMPKA1 or -2), a beta (AMPKB1 or -2) and a gamma non-catalytic subunit (AMPKG1, -2 or -3). Different possible combinations of subunits give rise to 12 different holoenzymes. Beta subunits act as scaffolds on which the AMPK complex assembles, via its C-terminus that bridges alpha and gamma subunits. AMPK-beta1 or -beta2 subunits are required for assembling of AMPK heterotrimers and are important for regulating enzyme activity and cellular localization. AMPK beta1beta2 null mouse muscles reveal an essential role for AMPK in maintaining mitochondrial content and glucose uptake during exercise. Phosphorylation by ULK1 and ULK2 inhibits AMPK activity.
Protein type: Autophagy; Protein kinase, regulatory subunit
Chromosomal Location of Human Ortholog: 1q21.1
Cellular Component: nucleoplasm; cytosol; AMP-activated protein kinase complex
Molecular Function: AMP-activated protein kinase activity; identical protein binding; protein binding
Biological Process: mitochondrion organization and biogenesis; regulation of fatty acid biosynthetic process; organelle organization and biogenesis; energy reserve metabolic process; insulin receptor signaling pathway; cellular lipid metabolic process; carnitine shuttle; signal transduction; cell cycle arrest; regulation of protein kinase activity; protein amino acid phosphorylation; fatty acid biosynthetic process
Research Articles on PRKAB2
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Products associated with PRKAB2 recombinant protein
Pathways associated with PRKAB2 recombinant protein
Diseases associated with PRKAB2 recombinant protein
Organs/Tissues associated with PRKAB2 recombinant protein
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