PRKAA2

5'-AMP-activated protein kinase catalytic subunit alpha-2 is an enzyme that in humans is encoded by the PRKAA2 gene.[5][6]

PRKAA2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2H6D, 2LTU, 2YZA, 3AQV, 4CFE, 4CFF, 4ZHX, 5EZV
Identifiers
Aliases	PRKAA2, AMPK, AMPK2, AMPKa2, PRKAA, protein kinase AMP-activated catalytic subunit alpha 2
External IDs	OMIM: 600497 MGI: 1336173 HomoloGene: 4551 GeneCards: PRKAA2
EC number	2.7.11.27
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1p32.2 Start 56,645,314 bp[1] End 56,715,335 bp[1]
Gene location (Mouse) Chr. Chromosome 4 (mouse)[2] Band 4|4 C6 Start 105,029,874 bp[2] End 105,109,890 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • transferase activity • nucleotide binding • protein kinase activity • [acetyl-CoA carboxylase kinase activity] • AMP-activated protein kinase activity • histone serine kinase activity • chromatin binding • metal ion binding • kinase activity • protein serine/threonine kinase activity • GO:0001948 protein binding • [hydroxymethylglutaryl-CoA reductase (NADPH) kinase activity] • protein serine/threonine/tyrosine kinase activity • ATP binding Cellular component • cytoplasm • cytosol • nucleoplasm • nucleotide-activated protein kinase complex • cell nucleus • Golgi apparatus • nuclear speck • Stress granule • axon • dendrite • neuronal cell body Biological process • carnitine shuttle • steroid metabolic process • GO:0007243 intracellular signal transduction • cellular response to glucose starvation • sterol biosynthetic process • lipid biosynthetic process • regulation of transcription, DNA-templated • glucose homeostasis • positive regulation of autophagy • phosphorylation • rhythmic process • lipid metabolism • response to stress • negative regulation of apoptotic process • cholesterol metabolic process • Wnt signaling pathway • regulation of fatty acid biosynthetic process • fatty acid metabolic process • transcription, DNA-templated • cellular response to prostaglandin E stimulus • autophagy • protein phosphorylation • negative regulation of TOR signaling • positive regulation of macroautophagy • cellular response to drug • fatty acid biosynthetic process • fatty acid homeostasis • regulation of circadian rhythm • cell cycle arrest • cellular response to nutrient levels • regulation of gene expression • cholesterol biosynthetic process • response to muscle activity • positive regulation of glycolytic process • macroautophagy • signal transduction • steroid biosynthetic process • regulation of signal transduction by p53 class mediator • histone-serine phosphorylation • regulation of macroautophagy • chromatin organization • negative regulation of gene expression • cellular response to oxidative stress • regulation of stress granule assembly • regulation of microtubule cytoskeleton organization • cellular response to calcium ion • cellular response to glucose stimulus • energy homeostasis • positive regulation of cellular protein localization • negative regulation of tubulin deacetylation • positive regulation of peptidyl-lysine acetylation Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	5563	108079
Ensembl	ENSG00000162409	ENSMUSG00000028518
UniProt	P54646	Q8BRK8
RefSeq (mRNA)	NM_006252	NM_178143 NM_001356568
RefSeq (protein)	NP_006243	NP_835279 NP_001343497
Location (UCSC)	Chr 1: 56.65 – 56.72 Mb	Chr 4: 105.03 – 105.11 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

The protein encoded by this gene is a catalytic 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. Studies of the mouse counterpart suggest that this catalytic subunit may control whole-body insulin sensitivity and is necessary for maintaining myocardial energy homeostasis during ischemia.[6]

References

1. GRCh38: Ensembl release 89: ENSG00000162409 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000028518 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Aguan K, Scott J, See CG, Sarkar NH (Dec 1994). "Characterization and chromosomal localization of the human homologue of a rat AMP-activated protein kinase-encoding gene: a major regulator of lipid metabolism in mammals". Gene. 149 (2): 345–50. doi:10.1016/0378-1119(94)90174-0. PMID 7959015.
6. "Entrez Gene: PRKAA2 protein kinase, AMP-activated, alpha 2 catalytic subunit".

Further reading

• Hardie DG, MacKintosh RW (1995). "AMP-activated protein kinase--an archetypal protein kinase cascade?". BioEssays. 14 (10): 699–704. doi:10.1002/bies.950141011. PMID 1365882. S2CID 37111181.
• Hardie DG (1992). "Regulation of fatty acid and cholesterol metabolism by the AMP-activated protein kinase". Biochim. Biophys. Acta. 1123 (3): 231–8. doi:10.1016/0005-2760(92)90001-c. PMID 1536860.
• Carling D (2004). "The AMP-activated protein kinase cascade--a unifying system for energy control". Trends Biochem. Sci. 29 (1): 18–24. doi:10.1016/j.tibs.2003.11.005. PMID 14729328.
• Beri RK, Marley AE, See CG, Sopwith WF, Aguan K, Carling D, Scott J, Carey F (1995). "Molecular cloning, expression and chromosomal localisation of human AMP-activated protein kinase". FEBS Lett. 356 (1): 117–21. doi:10.1016/0014-5793(94)01247-4. PMID 7988703.
• Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
• Vavvas D, Apazidis A, Saha AK, Gamble J, Patel A, Kemp BE, Witters LA, Ruderman NB (1997). "Contraction-induced changes in acetyl-CoA carboxylase and 5'-AMP-activated kinase in skeletal muscle". J. Biol. Chem. 272 (20): 13255–61. doi:10.1074/jbc.272.20.13255. PMID 9148944.
• Stapleton D, Woollatt E, Mitchelhill KI, Nicholl JK, Fernandez CS, Michell BJ, Witters LA, Power DA, Sutherland GR, Kemp BE (1997). "AMP-activated protein kinase isoenzyme family: subunit structure and chromosomal location". FEBS Lett. 409 (3): 452–6. doi:10.1016/S0014-5793(97)00569-3. PMID 9224708. S2CID 39329574.
• Stein SC, Woods A, Jones NA, Davison MD, Carling D (2000). "The regulation of AMP-activated protein kinase by phosphorylation". Biochem. J. 345 (3): 437–43. doi:10.1042/0264-6021:3450437. PMC 1220775. PMID 10642499.
• da Silva Xavier G, Leclerc I, Salt IP, Doiron B, Hardie DG, Kahn A, Rutter GA (2000). "Role of AMP-activated protein kinase in the regulation by glucose of islet beta cell gene expression". Proc. Natl. Acad. Sci. U.S.A. 97 (8): 4023–8. Bibcode:2000PNAS...97.4023D. doi:10.1073/pnas.97.8.4023. PMC 18135. PMID 10760274.
• Mu J, Brozinick JT, Valladares O, Bucan M, Birnbaum MJ (2001). "A role for AMP-activated protein kinase in contraction- and hypoxia-regulated glucose transport in skeletal muscle". Mol. Cell. 7 (5): 1085–94. doi:10.1016/S1097-2765(01)00251-9. PMID 11389854.
• Minokoshi Y, Kim YB, Peroni OD, Fryer LG, Müller C, Carling D, Kahn BB (2002). "Leptin stimulates fatty-acid oxidation by activating AMP-activated protein kinase". Nature. 415 (6869): 339–43. Bibcode:2002Natur.415..339M. doi:10.1038/415339a. PMID 11797013. S2CID 4409274.
• Dubbelhuis PF, Meijer AJ (2002). "Hepatic amino acid-dependent signaling is under the control of AMP-dependent protein kinase". FEBS Lett. 521 (1–3): 39–42. doi:10.1016/S0014-5793(02)02815-6. PMID 12067722. S2CID 32171292.
• Esumi H, Izuishi K, Kato K, Hashimoto K, Kurashima Y, Kishimoto A, Ogura T, Ozawa T (2002). "Hypoxia and nitric oxide treatment confer tolerance to glucose starvation in a 5'-AMP-activated protein kinase-dependent manner". J. Biol. Chem. 277 (36): 32791–8. doi:10.1074/jbc.M112270200. PMID 12091379.
• Nielsen JN, Mustard KJ, Graham DA, Yu H, MacDonald CS, Pilegaard H, Goodyear LJ, Hardie DG, Richter EA, Wojtaszewski JF (2003). "5'-AMP-activated protein kinase activity and subunit expression in exercise-trained human skeletal muscle". J. Appl. Physiol. 94 (2): 631–41. doi:10.1152/japplphysiol.00642.2002. PMID 12391032.
• Wojtaszewski JF, Mourtzakis M, Hillig T, Saltin B, Pilegaard H (2002). "Dissociation of AMPK activity and ACCbeta phosphorylation in human muscle during prolonged exercise". Biochem. Biophys. Res. Commun. 298 (3): 309–16. doi:10.1016/S0006-291X(02)02465-8. PMID 12413941.
• Hallows KR, McCane JE, Kemp BE, Witters LA, Foskett JK (2003). "Regulation of channel gating by AMP-activated protein kinase modulates cystic fibrosis transmembrane conductance regulator activity in lung submucosal cells". J. Biol. Chem. 278 (2): 998–1004. doi:10.1074/jbc.M210621200. PMID 12427743.
• Zong H, Ren JM, Young LH, Pypaert M, Mu J, Birnbaum MJ, Shulman GI (2003). "AMP kinase is required for mitochondrial biogenesis in skeletal muscle in response to chronic energy deprivation". Proc. Natl. Acad. Sci. U.S.A. 99 (25): 15983–7. doi:10.1073/pnas.252625599. PMC 138551. PMID 12444247.