AMP-activated protein kinase alpha-1 subunit (AMPK alpha-1 chain, PRKAA1, AMPK1)

Function: - catalytic subunit of AMP-activated protein kinase - regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase - also regulates cholesterol synthesis via phosphorylation & inactivation of hormone-sensitive lipase & hydroxymethylglutaryl-CoA reductase - appears to act as a metabolic stress-sensing protein kinase switching off biosynthetic pathways when cellular ATP levels are depleted & when 5'-AMP rises in response to fuel limitation &/or hypoxia - interacts with FNIP1 - binding of AMP results in allosteric activation, inducing phosphorylation on Thr-174 by STK11 in complex with STE20-related adapter-alpha (STRAD alpha) pseudo kinase & CAB39 - also activated by phosphorylation by CAMKK2 - triggered by a rise in intracellular Ca⁺², without detectable changes in the AMP/ATP ratio Cofactor: Mg⁺² Structure: - belongs to the protein kinase superfamily, CAMK Ser/Thr protein kinase family, SNF1 subfamily - contains 1 protein kinase domain

General

AMP-activated protein kinase-alpha subunit (AMPKa) phosphoprotein

Properties

SIZE: entity length = 550 aa MW = 63 kD MOTIF: kinase domain SITE: 18-270 MOTIF: ATP-binding site NAME: ATP-binding site SITE: 24-32 ATP-binding site NAME: ATP-binding site SITE: 47-47 aspartate residue {D141} Thr phosphorylation site {T174} Ser phosphorylation site {S175} Ser phosphorylation site {S487} Ser phosphorylation site {S499}

Database Correlations

OMIM 602739 UniProt Q13131 Pfam PF00069 Kegg hsa:5562 ENZYME 2.7.11.1

References

UniProt :accession Q13131