Protein kinase, AMP-activated, alpha 1

5'-AMP-activated protein kinase catalytic subunit alpha-1 is an enzyme that in humans is encoded by the PRKAA1 gene.[5][6]

PRKAA1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4RED, 4RER, 4REW, 5EZV
Identifiers
Aliases	PRKAA1, AMPK, AMPKa1, Protein kinase, AMP-activated, alpha 1, protein kinase AMP-activated catalytic subunit alpha 1
External IDs	OMIM: 602739 MGI: 2145955 HomoloGene: 49590 GeneCards: PRKAA1
EC number	2.7.11.26
Gene location (Human) Chr. Chromosome 5 (human)[1] Band n/a Start 40,759,379 bp[1] End 40,798,374 bp[1]
Gene location (Mouse) Chr. Chromosome 15 (mouse)[2] Band 15|15 A1 Start 5,143,861 bp[2] End 5,181,899 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • transferase activity • nucleotide binding • protein kinase activity • cAMP-dependent 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 • tau-protein kinase activity • protein C-terminus binding • GO:0001948 protein binding • [hydroxymethylglutaryl-CoA reductase (NADPH) kinase activity] • ATP binding • tau protein binding Cellular component • nucleotide-activated protein kinase complex • apical plasma membrane • nucleoplasm • cell nucleus • cytoplasm • cytosol • nuclear speck • intracellular • axon • dendrite • macromolecular complex • neuronal cell body Biological process • cellular response to organonitrogen compound • steroid metabolic process • cellular response to glucose starvation • sterol biosynthetic process • lipid biosynthetic process • regulation of transcription, DNA-templated • response to hypoxia • cellular response to ethanol • glucose homeostasis • positive regulation of skeletal muscle tissue development • protein heterooligomerization • rhythmic process • phosphorylation • lipid metabolism • regulation of vesicle-mediated transport • negative regulation of apoptotic process • cholesterol metabolic process • Wnt signaling pathway • response to activity • fatty acid metabolic process • transcription, DNA-templated • cellular response to prostaglandin E stimulus • autophagy • protein phosphorylation • negative regulation of TOR signaling • cold acclimation • positive regulation of gene expression • response to camptothecin • fatty acid biosynthetic process • fatty acid homeostasis • regulation of circadian rhythm • activation of MAPK activity • fatty acid oxidation • regulation of peptidyl-serine phosphorylation • cellular response to nutrient levels • positive regulation of cell proliferation • negative regulation of glucosylceramide biosynthetic process • glucose metabolic process • cell cycle arrest • positive regulation of cholesterol biosynthetic process • response to caffeine • histone-serine phosphorylation • cholesterol biosynthetic process • negative regulation of lipid catabolic process • response to gamma radiation • macroautophagy • response to UV • positive regulation of glycolytic process • response to hydrogen peroxide • cellular response to hypoxia • signal transduction • cellular response to hydrogen peroxide • steroid biosynthetic process • regulation of signal transduction by p53 class mediator • positive regulation of autophagy • CAMKK-AMPK signaling cascade • regulation of macroautophagy • chromatin organization • positive regulation of transcription from mitochondrial promoter • positive regulation of protein targeting to mitochondrion • negative regulation of gene expression • cellular response to oxidative stress • GO:0007243 intracellular signal transduction • negative regulation of insulin receptor signaling pathway • motor behavior • regulation of stress granule assembly • neuron cellular homeostasis • 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	5562	105787
Ensembl	ENSG00000132356	ENSMUSG00000050697
UniProt	Q13131	Q5EG47
RefSeq (mRNA)	NM_006251 NM_206907	NM_001013367 NM_001355640
RefSeq (protein)	NP_006242 NP_996790 NP_001341957 NP_001341958 NP_001341963 NP_001341964 NP_001341965 NP_001341966	NP_001013385 NP_001342569
Location (UCSC)	Chr 5: 40.76 – 40.8 Mb	Chr 15: 5.14 – 5.18 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

The protein encoded by this gene belongs to the serine/threonine protein kinase family. It is the catalytic subunit of the 5'-prime-AMP-activated protein kinase (AMPK). AMPK is a cellular energy sensor conserved in all eukaryotic cells. The kinase activity of AMPK is activated by the stimuli that increase the cellular AMP/ATP ratio. AMPK regulates the activities of a number of key metabolic enzymes through phosphorylation. It protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. Alternatively spliced transcript variants encoding distinct isoforms have been observed.[6]

Interactions

Protein kinase, AMP-activated, alpha 1 has been shown to interact with TSC2.[7][8]

References

1. GRCh38: Ensembl release 89: ENSG00000132356 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000050697 - 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. Stapleton D, Mitchelhill KI, Gao G, Widmer J, Michell BJ, Teh T, House CM, Fernandez CS, Cox T, Witters LA, Kemp BE (Feb 1996). "Mammalian AMP-activated protein kinase subfamily". J Biol Chem. 271 (2): 611–4. doi:10.1074/jbc.271.2.611. PMID 8557660.
6. "Entrez Gene: PRKAA1 protein kinase, AMP-activated, alpha 1 catalytic subunit".
7. Inoki, Ken; Zhu Tianqing; Guan Kun-Liang (Nov 2003). "TSC2 mediates cellular energy response to control cell growth and survival". Cell. United States. 115 (5): 577–90. doi:10.1016/S0092-8674(03)00929-2. ISSN 0092-8674. PMID 14651849.
8. Shaw, Reuben J; Bardeesy Nabeel; Manning Brendan D; Lopez Lyle; Kosmatka Monica; DePinho Ronald A; Cantley Lewis C (Jul 2004). "The LKB1 tumor suppressor negatively regulates mTOR signaling". Cancer Cell. United States. 6 (1): 91–9. doi:10.1016/j.ccr.2004.06.007. ISSN 1535-6108. PMID 15261145.

Further reading

• Munday MR, Campbell DG, Carling D, Hardie DG (1988). "Identification by amino acid sequencing of three major regulatory phosphorylation sites on rat acetyl-CoA carboxylase". Eur. J. Biochem. 175 (2): 331–8. doi:10.1111/j.1432-1033.1988.tb14201.x. PMID 2900138.
• Woods A, Cheung PC, Smith FC, et al. (1996). "Characterization of AMP-activated protein kinase beta and gamma subunits. Assembly of the heterotrimeric complex in vitro". J. Biol. Chem. 271 (17): 10282–90. doi:10.1074/jbc.271.48.30517. PMID 8626596.
• Hawley SA, Davison M, Woods A, et al. (1996). "Characterization of the AMP-activated protein kinase kinase from rat liver and identification of threonine 172 as the major site at which it phosphorylates AMP-activated protein kinase". J. Biol. Chem. 271 (44): 27879–87. doi:10.1074/jbc.271.44.27879. PMID 8910387.
• Stapleton D, Woollatt E, Mitchelhill KI, et al. (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.
• Velasco G, Gómez del Pulgar T, Carling D, Guzmán M (1998). "Evidence that the AMP-activated protein kinase stimulates rat liver carnitine palmitoyltransferase I by phosphorylating cytoskeletal components". FEBS Lett. 439 (3): 317–20. doi:10.1016/S0014-5793(98)01400-8. PMID 9845345.
• Crute BE, Seefeld K, Gamble J, et al. (1999). "Functional domains of the alpha1 catalytic subunit of the AMP-activated protein kinase". J. Biol. Chem. 273 (52): 35347–54. doi:10.1074/jbc.273.52.35347. PMID 9857077.
• da Silva Xavier G, Leclerc I, Salt IP, et al. (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.
• Hallows KR, Raghuram V, Kemp BE, et al. (2000). "Inhibition of cystic fibrosis transmembrane conductance regulator by novel interaction with the metabolic sensor AMP-activated protein kinase". J. Clin. Invest. 105 (12): 1711–21. doi:10.1172/JCI9622. PMC 378514. PMID 10862786.
• Zhang QH, Ye M, Wu XY, et al. (2001). "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells". Genome Res. 10 (10): 1546–60. doi:10.1101/gr.140200. PMC 310934. PMID 11042152.
• Chen ZP, McConell GK, Michell BJ, et al. (2000). "AMPK signaling in contracting human skeletal muscle: acetyl-CoA carboxylase and NO synthase phosphorylation". Am. J. Physiol. Endocrinol. Metab. 279 (5): E1202–6. PMID 11052978.
• Blázquez C, Geelen MJ, Velasco G, Guzmán M (2001). "The AMP-activated protein kinase prevents ceramide synthesis de novo and apoptosis in astrocytes". FEBS Lett. 489 (2–3): 149–53. doi:10.1016/S0014-5793(01)02089-0. PMID 11165240.
• Diggle TA, Subkhankulova T, Lilley KS, et al. (2001). "Phosphorylation of elongation factor-2 kinase on serine 499 by cAMP-dependent protein kinase induces Ca2+/calmodulin-independent activity". Biochem. J. 353 (Pt 3): 621–6. doi:10.1042/0264-6021:3530621. PMC 1221608. PMID 11171059.
• Wang X, Li W, Williams M, et al. (2001). "Regulation of elongation factor 2 kinase by p90(RSK1) and p70 S6 kinase". EMBO J. 20 (16): 4370–9. doi:10.1093/emboj/20.16.4370. PMC 125559. PMID 11500364.
• Xi X, Han J, Zhang JZ (2001). "Stimulation of glucose transport by AMP-activated protein kinase via activation of p38 mitogen-activated protein kinase". J. Biol. Chem. 276 (44): 41029–34. doi:10.1074/jbc.M102824200. PMID 11546797.
• Fryer LG, Foufelle F, Barnes K, et al. (2002). "Characterization of the role of the AMP-activated protein kinase in the stimulation of glucose transport in skeletal muscle cells". Biochem. J. 363 (Pt 1): 167–74. doi:10.1042/0264-6021:3630167. PMC 1222463. PMID 11903059.
• Yang CS, Weiner H (2002). "Yeast two-hybrid screening identifies binding partners of human Tom34 that have ATPase activity and form a complex with Tom34 in the cytosol". Arch. Biochem. Biophys. 400 (1): 105–10. doi:10.1006/abbi.2002.2778. PMID 11913976.
• Bolster DR, Crozier SJ, Kimball SR, Jefferson LS (2002). "AMP-activated protein kinase suppresses protein synthesis in rat skeletal muscle through down-regulated mammalian target of rapamycin (mTOR) signaling". J. Biol. Chem. 277 (27): 23977–80. doi:10.1074/jbc.C200171200. PMID 11997383.
• Esumi H, Izuishi K, Kato K, et al. (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.
• Horman S, Browne G, Krause U, et al. (2003). "Activation of AMP-activated protein kinase leads to the phosphorylation of elongation factor 2 and an inhibition of protein synthesis". Curr. Biol. 12 (16): 1419–23. doi:10.1016/S0960-9822(02)01077-1. PMID 12194824.

External links

• PDBe-KB provides an overview of all the structure information available in the PDB for Human 5'-AMP-activated protein kinase catalytic subunit alpha-1 (PRKAA1)