5'-AMP-activated protein kinase subunit beta-2

Function

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).

Classification

Family (Pfam)

PF16561 AMPK1_CBM, PF04739 AMPKBI

InterPro

AMPK1_CBM, ASC_dom, ASC_dom_sf, CRP1_MDG1_kinase, Ig-like_fold, Ig_E-set

Functional cluster

Mixed Regulatory & Membrane Proteins

Experimental structures · PDB · 17

• 2F15 X-ray 2.00A
• 2V8Q X-ray 2.10A
• 2V92 X-ray 2.40A
• 2V9J X-ray 2.53A
• 2Y8L X-ray 2.50A
• 2Y8Q X-ray 2.80A
• 2YA3 X-ray 2.51A
• 4CFH X-ray 3.24A
• 4EAI X-ray 2.28A
• 4EAJ X-ray 2.61A
• 4RER X-ray 4.05A
• 4REW X-ray 4.58A
• … and 5 more

A predicted model is available from AlphaFold.

Gene Ontology · 11

• GO:0005737 cytoplasm
• GO:0005829 cytosol
• GO:0005788 endoplasmic reticulum lumen
• GO:0005654 nucleoplasm
• GO:0031588 nucleotide-activated protein kinase complex
• GO:0005634 nucleus
• GO:0019901 protein kinase binding
• GO:0031669 cellular response to nutrient levels
• GO:0006633 fatty acid biosynthetic process
• GO:0120162 positive regulation of cold-induced thermogenesis
• GO:0007165 signal transduction

Drugs targeting this protein · 1

• ACADESINE activator

Related proteins · sequence + function similarity

• 5'-AMP-activated protein kinase subunit beta-2 1.00
• 5'-AMP-activated protein kinase subunit beta-2 1.00
• 5'-AMP-activated protein kinase subunit beta-1 0.92
• 5'-AMP-activated protein kinase subunit beta-1 0.91
• 5'-AMP-activated protein kinase subunit beta-1 0.91
• 5'-AMP-activated protein kinase subunit beta-1 0.89
• 5'-AMP-activated protein kinase subunit beta-1 0.88
• Dystrobrevin alpha 0.73
• SIN3-HDAC complex-associated factor 0.72
• SIN3-HDAC complex-associated factor 0.72
• SIN3-HDAC complex-associated factor 0.72
• Dystrobrevin alpha 0.72

Co-cited proteins · studied together in the literature

• 5'-AMP-activated protein kinase subunit gamma-1 3 shared papers
• 5'-AMP-activated protein kinase catalytic subunit alpha-1 3 shared papers
• 5'-AMP-activated protein kinase subunit beta-1 3 shared papers
• 5'-AMP-activated protein kinase subunit gamma-2 3 shared papers
• 5'-AMP-activated protein kinase subunit gamma-3 3 shared papers
• 5'-AMP-activated protein kinase subunit gamma-1 3 shared papers
• 5'-AMP-activated protein kinase catalytic subunit alpha-2 3 shared papers
• 5'-AMP-activated protein kinase catalytic subunit alpha-1 3 shared papers
• 5'-AMP-activated protein kinase subunit beta-2 1 shared papers
• 5'-AMP-activated protein kinase subunit beta-2 1 shared papers
• 5'-AMP-activated protein kinase subunit gamma-1 1 shared papers
• 5'-AMP-activated protein kinase subunit gamma-2 1 shared papers

Literature · 21 cited papers

• An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J. Proteomics · 2014
• Toward a comprehensive characterization of a human cancer cell phosphoproteome. J. Proteome Res. · 2013
• Ulk1-mediated phosphorylation of AMPK constitutes a negative regulatory feedback loop. Autophagy · 2011
• System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. Sci. Signal. · 2011
• Structure of mammalian AMPK and its regulation by ADP. Nature · 2011
• Initial characterization of the human central proteome. BMC Syst. Biol. · 2011
• Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci. Signal. · 2010
• Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci. Signal. · 2009
• Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal. Chem. · 2009
• Large-scale proteomics analysis of the human kinome. Mol. Cell. Proteomics · 2009
• Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol. Cell · 2008
• A quantitative atlas of mitotic phosphorylation. Proc. Natl. Acad. Sci. U.S.A. · 2008
• … and 9 more in the literature graph