Protein kinase, AMP-activated, alpha 1

PRKAA1

Available structures

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

MGI: 2145955 HomoloGene: 49590 GeneCards: PRKAA1

EC number

2.7.11.26

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 • kinase binding • tau-protein kinase activity • protein C-terminus binding • protein binding • [hydroxymethylglutaryl-CoA reductase (NADPH) kinase activity] • ATP binding
Cellular component	• cytoplasm • cytosol • intracellular • protein complex • nucleotide-activated protein kinase complex • apical plasma membrane • nucleus • nucleoplasm
Biological process	• cellular response to organonitrogen compound • steroid metabolic process • intracellular signal transduction • 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 autophagy • positive regulation of skeletal muscle tissue development • protein heterooligomerization • rhythmic process • phosphorylation • lipid metabolic process • regulation of vesicle-mediated transport • negative regulation of apoptotic process • cholesterol metabolic process • Wnt signaling pathway • response to activity • negative regulation of glucose import in response to insulin stimulus • 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 energy homeostasis • covalent chromatin modification • regulation of signal transduction by p53 class mediator
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


5562


105787

Ensembl


ENSG00000132356


ENSMUSG00000050697

UniProt


Q13131


Q5EG47

RefSeq (mRNA)


NM_006251 NM_206907


NM_001013367

RefSeq (protein)


NP_006242.5 NP_996790.3


NP_001013385.3

Location (UCSC)

Chr 5: 40.76 – 40.8 Mb

Chr 15: 5.14 – 5.18 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

5'-AMP-activated protein kinase catalytic subunit alpha-1 is an enzyme that in humans is encoded by the PRKAA1 gene.^[3]^[4]

The protein encoded by this gene belongs to the ser/thr 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.^[4]

Interactions

Protein kinase, AMP-activated, alpha 1 has been shown to interact with TSC2.^[5]^[6]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ 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.
1 2 "Entrez Gene: PRKAA1 protein kinase, AMP-activated, alpha 1 catalytic subunit".
↑ 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.
↑ 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.

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. 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.

PDB gallery

2h6d: Protein Kinase Domain of the Human 5'-AMP-activated protein kinase catalytic subunit alpha-2 (AMPK alpha-2 chain)

Kinases: Serine/threonine-specific protein kinases (EC 2.7.11-12)

Serine/threonine-specific protein kinases (EC 2.7.11.1-EC 2.7.11.20)

Non-specific serine/threonine protein kinases (EC 2.7.11.1)	LATS1 LATS2 MAST1 MAST2 STK38 STK38L CIT ROCK1 SGK SGK2 SGK3 Protein kinase B AKT1 AKT2 AKT3 Ataxia telangiectasia mutated Mammalian target of rapamycin EIF-2 kinases PKR HRI EIF2AK3 EIF2AK4 Wee1 WEE1

Pyruvate dehydrogenase kinase (EC 2.7.11.2)	PDK1 PDK2 PDK3

Dephospho-(reductase kinase) kinase (EC 2.7.11.3)	AMP-activated protein kinase α PRKAA1 PRKAA2 β PRKAB1 PRKAB2 γ PRKAG1 PRKAG2 PRKAG3

3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)	BCKDK BCKDHA BCKDHB

(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)	IDH2 IDH3A IDH3B IDH3G

(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)	STK4

Myosin-heavy-chain kinase (EC 2.7.11.7)	Aurora kinase Aurora A kinase Aurora B kinase

Fas-activated serine/threonine kinase (EC 2.7.11.8)	FASTK STK10

Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)	-

IκB kinase (EC 2.7.11.10)	CHUK IKK2 TBK1 IKBKE IKBKG IKBKAP

cAMP-dependent protein kinase (EC 2.7.11.11)	Protein kinase A PRKACG PRKACB PRKACA PRKY

cGMP-dependent protein kinase (EC 2.7.11.12)	Protein kinase G PRKG1

Protein kinase C (EC 2.7.11.13)	Protein kinase C Protein kinase Cζ PKC alpha PRKCB1 PRKCD PRKCE PRKCH PRKCG PRKCI PRKCQ Protein kinase N1 PKN2 PKN3

Rhodopsin kinase (EC 2.7.11.14)	Rhodopsin kinase

Beta adrenergic receptor kinase (EC 2.7.11.15)	Beta adrenergic receptor kinase Beta adrenergic receptor kinase-2

G-protein coupled receptor kinases (EC 2.7.11.16)	GRK4 GRK5 GRK6

Ca2+/calmodulin-dependent (EC 2.7.11.17)	BRSK2 CAMK1 CAMK2A CAMK2B CAMK2D CAMK2G CAMK4 MLCK CASK CHEK1 CHEK2 DAPK1 DAPK2 DAPK3 STK11 MAPKAPK2 MAPKAPK3 MAPKAPK5 MARK1 MARK2 MARK3 MARK4 MELK MKNK1 MKNK2 NUAK1 NUAK2 OBSCN PASK PHKG1 PHKG2 PIM1 PIM2 PKD1 PRKD2 PRKD3 PSKH1 SNF1LK2 KIAA0999 STK40 SNF1LK SNRK SPEG TSSK2 Kalirin TRIB1 TRIB2 TRIB3 TRIO Titin DCLK1

Myosin light-chain kinase (EC 2.7.11.18)	MYLK MYLK2 MYLK3 MYLK4

Phosphorylase kinase (EC 2.7.11.19)	PHKA1 PHKA2 PHKB PHKG1 PHKG2

Elongation factor 2 kinase (EC 2.7.11.20)	EEF2K STK19

Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4

Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)

Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4

Cyclin-dependent kinase (EC 2.7.11.22)	CDK1 CDK2 CDKL2 CDK3 CDK4 CDK5 CDKL5 CDK6 CDK7 CDK8 CDK9 CDK10 CDK12 CDC2L5 PCTK1 PCTK2 PCTK3 PFTK1 CDC2L1

(RNA-polymerase)-subunit kinase (EC 2.7.11.23)	RPS6KA5 RPS6KA4 P70S6 kinase P70-S6 Kinase 1 RPS6KB2 RPS6KA2 RPS6KA3 RPS6KA1 RPS6KC1

Mitogen-activated protein kinase (EC 2.7.11.24)	Extracellular signal-regulated MAPK1 MAPK3 MAPK4 MAPK6 MAPK7 MAPK12 MAPK15 C-Jun N-terminal MAPK8 MAPK9 MAPK10 P38 mitogen-activated protein MAPK11 MAPK13 MAPK14

MAP3K (EC 2.7.11.25)	MAP kinase kinase kinases MAP3K1 MAP3K2 MAP3K3 MAP3K4 MAP3K5 MAP3K6 MAP3K7 MAP3K8 RAFs ARAF BRAF KSR1 KSR2 MLKs MAP3K12 MAP3K13 MAP3K9 MAP3K10 MAP3K11 MAP3K7 ZAK CDC7 MAP3K14

Tau-protein kinase (EC 2.7.11.26)	TPK1 TTK GSK-3

(acetyl-CoA carboxylase) kinase (EC 2.7.11.27)	-

Tropomyosin kinase (EC 2.7.11.28)	-

Low-density-lipoprotein receptor kinase (EC 2.7.11.29)	-

Receptor protein serine/threonine kinase (EC 2.7.11.30)	Bone morphogenetic protein receptors BMPR1 BMPR1A BMPR1B BMPR2 ACVR1 ACVR1B ACVR1C ACVR2A ACVR2B ACVRL1 Anti-Müllerian hormone receptor

Dual-specificity kinases (EC 2.7.12)

MAP2K	MAP2K1 MAP2K2 MAP2K3 MAP2K4 MAP2K5 MAP2K6 MAP2K7

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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Protein kinase, AMP-activated, alpha 1

Interactions

References

Further reading