Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
The subcellular localization of acetyl-CoA carboxylase 2.
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ACC2 is targeted to the mitochondria by its unique hydrophobic N-terminal sequence and colocalizes with carnitine palmitoyltransferase 1, consistent with regulation of mitochondrial fatty-acid oxidation via malonyl-CoA inhibition of CPT1.
"ACC2 was associated with the mitochondria"
TRB3 links the E3 ubiquitin ligase COP1 to lipid metabolism.
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TRB3 promotes ubiquitination and degradation of ACC via COP1 during fasting, linking ACC turnover to lipid metabolism.
"stimulates lipolysis by triggering the degradation of ACC"
Expression, purification, and characterization of human and rat acetyl coenzyme A carboxylase (ACC) isozymes.
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Recombinant human ACC2 was purified with high specific activity and proper biotinylation, confirming its acetyl-CoA carboxylase activity.
"The resultant human ACC2, human ACC1, and rat ACC2 possess high"
Characterization of recombinant human acetyl-CoA carboxylase-2 steady-state kinetics.
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Steady-state kinetic analysis of purified recombinant human ACC2 directly measured malonyl-CoA formation, confirming acetyl-CoA carboxylase activity; citrate activates the enzyme.
"LC/MS/MS assay to directly measure malonyl-CoA formation"
Molecular mechanism for the regulation of human ACC2 through phosphorylation by AMPK.
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Crystal structures of the human ACC2 biotin carboxylase domain show that AMPK phosphorylation of Ser222 disrupts polymerization (the active oligomer), inactivating the enzyme; soraphen A binds the same site.
"disrupting polymerization and providing the molecular mechanism of inactivation by AMPK"
The N-terminal domain of human holocarboxylase synthetase facilitates biotinylation via direct interaction with the substrate protein.
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The N-terminal domain of human holocarboxylase synthetase (HLCS) directly interacts with biotin-acceptor substrate proteins to facilitate biotinylation; ACC2 is such a substrate.
"The domain interacts not only with biotin acceptor protein, but also with the catalytic domain of hHCS"
Induced polymerization of mammalian acetyl-CoA carboxylase by MIG12 provides a tertiary level of regulation of fatty acid synthesis.
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MIG12/MID1IP1 binds ACC and lowers the citrate threshold for polymerization into the physiological range, inducing ACC filament formation and increasing activity more than 50-fold.
"binds to ACC and lowers the threshold for citrate activation"
Crystal structure of Spot 14, a modulator of fatty acid synthesis.
Acetyl-CoA carboxylase inhibition by ND-630 reduces hepatic steatosis, improves insulin sensitivity, and modulates dyslipidemia in rats.
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The allosteric inhibitor ND-630 prevents ACC dimerization and inhibits the enzymatic activity of both ACC1 and ACC2, reducing fatty-acid synthesis and stimulating fatty-acid oxidation; ACC is a validated metabolic drug target.
"inhibit the enzymatic activity of both ACC isozymes"
Expression of Acetyl CoA Carboxylase 2 (ACACB, ACC2)
pAMPK inactivates ACACB, inhibiting malonyl-CoA synthesis
An unknown protease degrades ACACB
Btn-ACACB:2Mn2+ polymer carboxylates Ac-CoA to form Mal-CoA
Transcriptional activation of ACACB by ChREBP:MLX