Gene Ontology annotation through association of InterPro records with GO terms.
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity.
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Automated transfer of experimentally-verified manual GO annotation data to mouse-rat orthologs.
Automatic assignment of GO terms using logical inference, based on on inter-ontology links.
Automatic Gene Ontology annotation based on Rhea mapping.
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods.
Characterization of AMP-activated protein kinase gamma-subunit isoforms and their role in AMP binding.
Phosphorylation and activation of heart PFK-2 by AMPK has a role in the stimulation of glycolysis during ischaemia.
Mechanism for fatty acid "sparing" effect on glucose-induced transcription: regulation of carbohydrate-responsive element-binding protein by AMP-activated protein kinase.
Coordinate regulation of malonyl-CoA decarboxylase, sn-glycerol-3-phosphate acyltransferase, and acetyl-CoA carboxylase by AMP-activated protein kinase in rat tissues in response to exercise.
Complexes between the LKB1 tumor suppressor, STRAD alpha/beta and MO25 alpha/beta are upstream kinases in the AMP-activated protein kinase cascade.
AMP-activated protein kinase beta subunit tethers alpha and gamma subunits via its C-terminal sequence (186-270).
Activation of AMPK alpha- and gamma-isoform complexes in the intact ischemic rat heart.
Adrenaline is a critical mediator of acute exercise-induced AMP-activated protein kinase activation in adipocytes.
Caffeine acutely activates 5'adenosine monophosphate-activated protein kinase and increases insulin-independent glucose transport in rat skeletal muscles.
Polarized activities of AMPK and BRSK in primary hippocampal neurons.
The alpha1 and alpha2 isoforms of the AMP-activated protein kinase have similar activities in rat liver but exhibit differences in substrate specificity in vitro.
Regulation of HMG-CoA reductase: identification of the site phosphorylated by the AMP-activated protein kinase in vitro and in intact rat liver.
Deep research synthesis for PRKAA2 functions and regulation
Research notes on PRKAA2 with literature citations
Falcon (Edison Scientific) deep research report for rat Prkaa2 (AMPKα2)
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Prkaa2 encodes the catalytic alpha-2 subunit of the heterotrimeric
AMPK serine/threonine kinase; the alpha subunit carries the catalytic
kinase activity.
"AMPK is a **heterotrimeric serine/threonine kinase** consisting of a **catalytic α** subunit plus **regulatory β and γ** subunits."
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The alpha subunit provides the catalytic kinase activity and is
activated by phosphorylation at Thr172 in the activation loop.
"The α subunit provides the **catalytic kinase activity** and is activated primarily by phosphorylation at a conserved threonine within the activation loop (**Thr172 for α2**), which is a core mechanistic definition of “AMPK activation.”"
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Prkaa2 is a protein serine/threonine kinase (EC 2.7.11.1).
"Prkaa2 encodes a **protein kinase** (EC 2.7.11.1; Ser/Thr kinase)."
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AMP binding (via the gamma subunit) allosterically activates AMPK and
protects it from dephosphorylation, coupling ATP depletion to kinase
activation — the basis of AMP-activated protein kinase activity.
"AMP binding to AMPK (via γ subunit CBS motifs) promotes AMPK activation through allosteric effects and protection from dephosphorylation, coupling ATP depletion to kinase activation."
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Upstream kinases phosphorylate AMPKα2 at Thr172, with LKB1 as a primary
kinase and CaMKKβ/CAMKK2 as a calcium-responsive route.
"upstream kinases phosphorylate AMPKα2 at **Thr172**, with **LKB1** frequently highlighted as a primary kinase"
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AMPKα2 integrates energy stress to inhibit anabolic metabolism and
promote catabolism and autophagy — its core energy-homeostasis role.
"Functionally, AMPKα2 integrates energy stress to inhibit anabolic metabolism and promote catabolism and autophagy"
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AMPK phosphorylates metabolic targets including ACC, HMGCR, and
autophagy regulators such as ULK1.
"AMPKα2 phosphorylates metabolic targets including ACC/ACAC (canonical readout; ACC Ser79 commonly used), HMGCR, and autophagy regulators such as ULK1"
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AMPK inhibits mTORC1 via phosphorylation of TSC2 and Raptor.
"AMPK inhibits mTORC1 via phosphorylation of TSC2 and Raptor"
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AMPKα2 has a nuclear localization signal and can shuttle to the nucleus,
whereas α1 is primarily cytosolic.
"AMPKα2 contains a nuclear localization signal and can shuttle to the nucleus"
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A 2024 primary study identifies an AMPKα2-specific role in skeletal
muscle ketone utilization via binding and stabilization of SCOT.
"These results place AMPKα2 as an important regulator of **skeletal muscle ketone utilization**"
RGD ISO annotations to rat from other mammalian species.
Control of glycogen synthase through ADIPOR1-AMPK pathway in renal distal tubules of normal and diabetic rats.
Phosphorylation of rChREBP(Ser 568) by rAMPK
rLkb-1 (Stk-11) activates AMPK by phosphorylation