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5'-AMP-activated protein kinase catalytic subunit alpha-2 (AMPK subunit alpha-2) (EC 2.7.11.1) (Acetyl-CoA carboxylase kinase) (ACACA kinase) (EC 2.7.11.27) (Hydroxymethylglutaryl-CoA reductase kinase) (HMGCR kinase) (EC 2.7.11.31)

 AAPK2_HUMAN             Reviewed;         552 AA.
P54646; Q9H1E8; Q9UD43;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
16-APR-2002, sequence version 2.
27-SEP-2017, entry version 182.
RecName: Full=5'-AMP-activated protein kinase catalytic subunit alpha-2;
Short=AMPK subunit alpha-2;
EC=2.7.11.1 {ECO:0000250|UniProtKB:Q09137};
AltName: Full=Acetyl-CoA carboxylase kinase;
Short=ACACA kinase;
EC=2.7.11.27 {ECO:0000250|UniProtKB:Q09137};
AltName: Full=Hydroxymethylglutaryl-CoA reductase kinase;
Short=HMGCR kinase;
EC=2.7.11.31 {ECO:0000250|UniProtKB:Q09137};
Name=PRKAA2; Synonyms=AMPK, AMPK2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
TISSUE=Heart;
PubMed=7959015; DOI=10.1016/0378-1119(94)90174-0;
Aguan K., Scott J., See C.G., Sarkar N.H.;
"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 149:345-350(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Skeletal muscle;
PubMed=7988703; DOI=10.1016/0014-5793(94)01247-4;
Beri R.K., Marley A.E., See C.G., Sopwith W.F., Aguan K., Carling D.,
Scott J., Carey F.;
"Molecular cloning, expression and chromosomal localisation of human
AMP-activated protein kinase.";
FEBS Lett. 356:117-121(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION.
PubMed=11554766; DOI=10.1006/bbrc.2001.5627;
Imamura K., Ogura T., Kishimoto A., Kaminishi M., Esumi H.;
"Cell cycle regulation via p53 phosphorylation by a 5'-AMP activated
protein kinase activator, 5-aminoimidazole-4-carboxamide-1-beta-D-
ribofuranoside, in a human hepatocellular carcinoma cell line.";
Biochem. Biophys. Res. Commun. 287:562-567(2001).
[6]
FUNCTION IN PHOSPHORYLATION OF EP300.
PubMed=11518699; DOI=10.1074/jbc.C100316200;
Yang W., Hong Y.H., Shen X.Q., Frankowski C., Camp H.S., Leff T.;
"Regulation of transcription by AMP-activated protein kinase:
phosphorylation of p300 blocks its interaction with nuclear
receptors.";
J. Biol. Chem. 276:38341-38344(2001).
[7]
ENZYME REGULATION.
PubMed=11602624; DOI=10.1172/JCI13505;
Zhou G., Myers R., Li Y., Chen Y., Shen X., Fenyk-Melody J., Wu M.,
Ventre J., Doebber T., Fujii N., Musi N., Hirshman M.F.,
Goodyear L.J., Moller D.E.;
"Role of AMP-activated protein kinase in mechanism of metformin
action.";
J. Clin. Invest. 108:1167-1174(2001).
[8]
FUNCTION IN PHOSPHORYLATION OF CFTR.
PubMed=12519745; DOI=10.1152/ajpcell.00227.2002;
Hallows K.R., Kobinger G.P., Wilson J.M., Witters L.A., Foskett J.K.;
"Physiological modulation of CFTR activity by AMP-activated protein
kinase in polarized T84 cells.";
Am. J. Physiol. 284:C1297-C1308(2003).
[9]
FUNCTION IN PHOSPHORYLATION OF TSC2.
PubMed=14651849; DOI=10.1016/S0092-8674(03)00929-2;
Inoki K., Zhu T., Guan K.L.;
"TSC2 mediates cellular energy response to control cell growth and
survival.";
Cell 115:577-590(2003).
[10]
PHOSPHORYLATION AT THR-172, AND ENZYME REGULATION.
PubMed=15980064; DOI=10.1074/jbc.M503824200;
Hurley R.L., Anderson K.A., Franzone J.M., Kemp B.E., Means A.R.,
Witters L.A.;
"The Ca2+/calmodulin-dependent protein kinase kinases are AMP-
activated protein kinase kinases.";
J. Biol. Chem. 280:29060-29066(2005).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15866171; DOI=10.1016/j.molcel.2005.03.027;
Jones R.G., Plas D.R., Kubek S., Buzzai M., Mu J., Xu Y.,
Birnbaum M.J., Thompson C.B.;
"AMP-activated protein kinase induces a p53-dependent metabolic
checkpoint.";
Mol. Cell 18:283-293(2005).
[12]
FUNCTION IN PHOSPHORYLATION OF FOXO3.
PubMed=17711846; DOI=10.1074/jbc.M705325200;
Greer E.L., Oskoui P.R., Banko M.R., Maniar J.M., Gygi M.P.,
Gygi S.P., Brunet A.;
"The energy sensor AMP-activated protein kinase directly regulates the
mammalian FOXO3 transcription factor.";
J. Biol. Chem. 282:30107-30119(2007).
[13]
FUNCTION IN CELL POLARITY.
PubMed=17486097; DOI=10.1038/nature05828;
Lee J.H., Koh H., Kim M., Kim Y., Lee S.Y., Karess R.E., Lee S.H.,
Shong M., Kim J.M., Kim J., Chung J.;
"Energy-dependent regulation of cell structure by AMP-activated
protein kinase.";
Nature 447:1017-1020(2007).
[14]
FUNCTION IN PHOSPHORYLATION OF HDAC5.
PubMed=18184930; DOI=10.2337/db07-0843;
McGee S.L., van Denderen B.J., Howlett K.F., Mollica J.,
Schertzer J.D., Kemp B.E., Hargreaves M.;
"AMP-activated protein kinase regulates GLUT4 transcription by
phosphorylating histone deacetylase 5.";
Diabetes 57:860-867(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[18]
FUNCTION IN PHOSPHORYLATION OF KLC1.
PubMed=20074060; DOI=10.1042/BST0380205;
McDonald A., Fogarty S., Leclerc I., Hill E.V., Hardie D.G.,
Rutter G.A.;
"Cell-wide analysis of secretory granule dynamics in three dimensions
in living pancreatic beta-cells: evidence against a role for AMPK-
dependent phosphorylation of KLC1 at Ser517/Ser520 in glucose-
stimulated insulin granule movement.";
Biochem. Soc. Trans. 38:205-208(2010).
[19]
FUNCTION.
PubMed=20160076; DOI=10.1073/pnas.0913860107;
Alexander A., Cai S.L., Kim J., Nanez A., Sahin M., MacLean K.H.,
Inoki K., Guan K.L., Shen J., Person M.D., Kusewitt D., Mills G.B.,
Kastan M.B., Walker C.L.;
"ATM signals to TSC2 in the cytoplasm to regulate mTORC1 in response
to ROS.";
Proc. Natl. Acad. Sci. U.S.A. 107:4153-4158(2010).
[20]
PHOSPHORYLATION BY ULK1.
PubMed=21460634; DOI=10.4161/auto.7.7.15451;
Loffler A.S., Alers S., Dieterle A.M., Keppeler H., Franz-Wachtel M.,
Kundu M., Campbell D.G., Wesselborg S., Alessi D.R., Stork B.;
"Ulk1-mediated phosphorylation of AMPK constitutes a negative
regulatory feedback loop.";
Autophagy 7:696-706(2011).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[22]
FUNCTION IN PHOSPHORYLATION OF ULK1.
PubMed=21205641; DOI=10.1126/science.1196371;
Egan D.F., Shackelford D.B., Mihaylova M.M., Gelino S., Kohnz R.A.,
Mair W., Vasquez D.S., Joshi A., Gwinn D.M., Taylor R., Asara J.M.,
Fitzpatrick J., Dillin A., Viollet B., Kundu M., Hansen M., Shaw R.J.;
"Phosphorylation of ULK1 (hATG1) by AMP-activated protein kinase
connects energy sensing to mitophagy.";
Science 331:456-461(2011).
[23]
REVIEW ON FUNCTION.
PubMed=17307971; DOI=10.1161/01.RES.0000256090.42690.05;
Towler M.C., Hardie D.G.;
"AMP-activated protein kinase in metabolic control and insulin
signaling.";
Circ. Res. 100:328-341(2007).
[24]
REVIEW ON FUNCTION.
PubMed=17712357; DOI=10.1038/nrm2249;
Hardie D.G.;
"AMP-activated/SNF1 protein kinases: conserved guardians of cellular
energy.";
Nat. Rev. Mol. Cell Biol. 8:774-785(2007).
[25]
ENZYME REGULATION BY SALICYLATE.
PubMed=22517326; DOI=10.1126/science.1215327;
Hawley S.A., Fullerton M.D., Ross F.A., Schertzer J.D., Chevtzoff C.,
Walker K.J., Peggie M.W., Zibrova D., Green K.A., Mustard K.J.,
Kemp B.E., Sakamoto K., Steinberg G.R., Hardie D.G.;
"The ancient drug salicylate directly activates AMP-activated protein
kinase.";
Science 336:918-922(2012).
[26]
DEPHOSPHORYLATION AT THR-172.
PubMed=23088624; DOI=10.1042/BJ20121201;
Chida T., Ando M., Matsuki T., Masu Y., Nagaura Y.,
Takano-Yamamoto T., Tamura S., Kobayashi T.;
"N-Myristoylation is essential for protein phosphatases PPM1A and
PPM1B to dephosphorylate their physiological substrates in cells.";
Biochem. J. 449:741-749(2013).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[28]
FUNCTION, AND SUBUNIT.
PubMed=25687571; DOI=10.1074/mcp.M114.047159;
Boutchueng-Djidjou M., Collard-Simard G., Fortier S., Hebert S.S.,
Kelly I., Landry C.R., Faure R.L.;
"The last enzyme of the de novo purine synthesis pathway 5-
aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP
cyclohydrolase (ATIC) plays a central role in insulin signaling and
the Golgi/endosomes protein network.";
Mol. Cell. Proteomics 14:1079-1092(2015).
[29]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 6-279.
PubMed=20124709; DOI=10.1107/S1744309109052543;
Littler D.R., Walker J.R., Davis T., Wybenga-Groot L.E.,
Finerty P.J. Jr., Newman E., Mackenzie F., Dhe-Paganon S.;
"A conserved mechanism of autoinhibition for the AMPK kinase domain:
ATP-binding site and catalytic loop refolding as a means of
regulation.";
Acta Crystallogr. F 66:143-151(2010).
[30]
X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 6-279 OF MUTANT THR-172 IN
COMPLEX WITH COMPOUND C, AND ENZYME REGULATION.
PubMed=21543851; DOI=10.1107/S0907444911010201;
Handa N., Takagi T., Saijo S., Kishishita S., Takaya D., Toyama M.,
Terada T., Shirouzu M., Suzuki A., Lee S., Yamauchi T.,
Okada-Iwabu M., Iwabu M., Kadowaki T., Minokoshi Y., Yokoyama S.;
"Structural basis for compound C inhibition of the human AMP-activated
protein kinase alpha2 subunit kinase domain.";
Acta Crystallogr. D 67:480-487(2011).
[31]
VARIANTS [LARGE SCALE ANALYSIS] THR-371 AND GLY-523.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[32]
VARIANTS [LARGE SCALE ANALYSIS] THR-371 AND GLN-407.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Catalytic subunit of AMP-activated protein kinase
(AMPK), an energy sensor protein kinase that plays a key role in
regulating cellular energy metabolism. In response to reduction of
intracellular ATP levels, AMPK activates energy-producing pathways
and inhibits energy-consuming processes: inhibits protein,
carbohydrate and lipid biosynthesis, as well as cell growth and
proliferation. AMPK acts via direct phosphorylation of metabolic
enzymes, and by longer-term effects via phosphorylation of
transcription regulators. Also acts as a regulator of cellular
polarity by remodeling the actin cytoskeleton; probably by
indirectly activating myosin. Regulates lipid synthesis by
phosphorylating and inactivating lipid metabolic enzymes such as
ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and
cholesterol synthesis by phosphorylating acetyl-CoA carboxylase
(ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes,
respectively. Regulates insulin-signaling and glycolysis by
phosphorylating IRS1, PFKFB2 and PFKFB3. Involved in insulin
receptor/INSR internalization (PubMed:25687571). AMPK stimulates
glucose uptake in muscle by increasing the translocation of the
glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly
by mediating phosphorylation of TBC1D4/AS160. Regulates
transcription and chromatin structure by phosphorylating
transcription regulators involved in energy metabolism such as
CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP,
EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A. Acts as a key
regulator of glucose homeostasis in liver by phosphorylating
CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the
cytoplasm. In response to stress, phosphorylates 'Ser-36' of
histone H2B (H2BS36ph), leading to promote transcription. Acts as
a key regulator of cell growth and proliferation by
phosphorylating TSC2, RPTOR and ATG1/ULK1: in response to nutrient
limitation, negatively regulates the mTORC1 complex by
phosphorylating RPTOR component of the mTORC1 complex and by
phosphorylating and activating TSC2. In response to nutrient
limitation, promotes autophagy by phosphorylating and activating
ATG1/ULK1. AMPK also acts as a regulator of circadian rhythm by
mediating phosphorylation of CRY1, leading to destabilize it. May
regulate the Wnt signaling pathway by phosphorylating CTNNB1,
leading to stabilize it. Also phosphorylates CFTR, EEF2K, KLC1,
NOS3 and SLC12A1. Plays an important role in the differential
regulation of pro-autophagy (composed of PIK3C3, BECN1, PIK3R4 and
UVRAG or ATG14) and non-autophagy (composed of PIK3C3, BECN1 and
PIK3R4) complexes, in response to glucose starvation. Can inhibit
the non-autophagy complex by phosphorylating PIK3C3 and can
activate the pro-autophagy complex by phosphorylating BECN1 (By
similarity). {ECO:0000250|UniProtKB:Q8BRK8,
ECO:0000269|PubMed:11518699, ECO:0000269|PubMed:11554766,
ECO:0000269|PubMed:12519745, ECO:0000269|PubMed:14651849,
ECO:0000269|PubMed:15866171, ECO:0000269|PubMed:17486097,
ECO:0000269|PubMed:17711846, ECO:0000269|PubMed:18184930,
ECO:0000269|PubMed:20074060, ECO:0000269|PubMed:20160076,
ECO:0000269|PubMed:21205641, ECO:0000269|PubMed:25687571,
ECO:0000269|PubMed:7959015}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000250|UniProtKB:Q09137}.
-!- CATALYTIC ACTIVITY: ATP + [acetyl-CoA carboxylase] = ADP +
[acetyl-CoA carboxylase] phosphate.
{ECO:0000250|UniProtKB:Q09137}.
-!- CATALYTIC ACTIVITY: ATP + [hydroxymethylglutaryl-CoA reductase
(NADPH)] = ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
phosphate. {ECO:0000250|UniProtKB:Q09137}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- ENZYME REGULATION: Activated by phosphorylation on Thr-172.
Binding of AMP to non-catalytic gamma subunit (PRKAG1, PRKAG2 or
PRKAG3) results in allosteric activation, inducing phosphorylation
on Thr-172. AMP-binding to gamma subunit also sustains activity by
preventing dephosphorylation of Thr-172. ADP also stimulates Thr-
172 phosphorylation, without stimulating already phosphorylated
AMPK. ATP promotes dephosphorylation of Thr-172, rendering the
enzyme inactive. Under physiological conditions AMPK mainly exists
in its inactive form in complex with ATP, which is much more
abundant than AMP. AMPK is activated by antihyperglycemic drug
metformin, a drug prescribed to patients with type 2 diabetes: in
vivo, metformin seems to mainly inhibit liver gluconeogenesis.
However, metformin can be used to activate AMPK in muscle and
other cells in culture or ex vivo (PubMed:11602624). Selectively
inhibited by compound C (6-[4-(2-Piperidin-1-yl-ethoxy)-phenyl)]-
3-pyridin-4-yl-pyyrazolo[1,5-a] pyrimidine. Activated by
resveratrol, a natural polyphenol present in red wine, and S17834,
a synthetic polyphenol. Salicylate/aspirin directly activates
kinase activity, primarily by inhibiting Thr-172
dephosphorylation. {ECO:0000269|PubMed:11602624,
ECO:0000269|PubMed:15980064, ECO:0000269|PubMed:21543851,
ECO:0000269|PubMed:22517326}.
-!- SUBUNIT: AMPK is a heterotrimer of an alpha catalytic subunit
(PRKAA1 or PRKAA2), a beta (PRKAB1 or PRKAB2) and a gamma non-
catalytic subunits (PRKAG1, PRKAG2 or PRKAG3). Interacts with
FNIP1 and FNIP2. Associates with internalized insulin
receptor/INSR complexes on Golgi/endosomal membranes; PRKAA2/AMPK2
together with ATIC and HACD3/PTPLAD1 is proposed to be part of a
signaling network regulating INSR autophosphorylation and
endocytosis (PubMed:25687571). {ECO:0000269|PubMed:21543851,
ECO:0000269|PubMed:25687571}.
-!- INTERACTION:
Q9NYB9:ABI2; NbExp=3; IntAct=EBI-1383852, EBI-743598;
Q08117:AES; NbExp=3; IntAct=EBI-1383852, EBI-717810;
Q13155:AIMP2; NbExp=3; IntAct=EBI-1383852, EBI-745226;
Q92624:APPBP2; NbExp=3; IntAct=EBI-1383852, EBI-743771;
Q9NPC3:CCNB1IP1; NbExp=3; IntAct=EBI-1383852, EBI-745269;
P50570:DNM2; NbExp=4; IntAct=EBI-1383852, EBI-346547;
Q6FG41:FOS; NbExp=3; IntAct=EBI-1383852, EBI-10198738;
P08151:GLI1; NbExp=3; IntAct=EBI-1383852, EBI-308084;
Q6NT76:HMBOX1; NbExp=3; IntAct=EBI-1383852, EBI-2549423;
Q8IX15-3:HOMEZ; NbExp=3; IntAct=EBI-1383852, EBI-10172004;
Q719H9:KCTD1; NbExp=3; IntAct=EBI-1383852, EBI-9027502;
Q96L93-6:KIF16B; NbExp=4; IntAct=EBI-1383852, EBI-10988217;
Q5T7B8-2:KIF24; NbExp=3; IntAct=EBI-1383852, EBI-10213781;
Q9BVG8:KIFC3; NbExp=4; IntAct=EBI-1383852, EBI-2125614;
Q15323:KRT31; NbExp=3; IntAct=EBI-1383852, EBI-948001;
Q96JM7:L3MBTL3; NbExp=3; IntAct=EBI-1383852, EBI-2686809;
Q9UBR4-2:LHX3; NbExp=4; IntAct=EBI-1383852, EBI-12039345;
Q7Z6G3-2:NECAB2; NbExp=3; IntAct=EBI-1383852, EBI-10172876;
Q15233-2:NONO; NbExp=3; IntAct=EBI-1383852, EBI-10203843;
Q7Z3S9:NOTCH2NL; NbExp=3; IntAct=EBI-1383852, EBI-945833;
Q86Y26:NUTM1; NbExp=3; IntAct=EBI-1383852, EBI-10178410;
Q9Y478:PRKAB1; NbExp=3; IntAct=EBI-1383852, EBI-719769;
O43741:PRKAB2; NbExp=11; IntAct=EBI-1383852, EBI-1053424;
P54619:PRKAG1; NbExp=9; IntAct=EBI-1383852, EBI-1181439;
Q93062:RBPMS; NbExp=3; IntAct=EBI-1383852, EBI-740322;
Q8HWS3:RFX6; NbExp=3; IntAct=EBI-1383852, EBI-746118;
Q5JUK2:SOHLH1; NbExp=4; IntAct=EBI-1383852, EBI-12288855;
P15884:TCF4; NbExp=3; IntAct=EBI-1383852, EBI-533224;
Q15654:TRIP6; NbExp=3; IntAct=EBI-1383852, EBI-742327;
Q9Y3Q8:TSC22D4; NbExp=3; IntAct=EBI-1383852, EBI-739485;
Q8N6Y0:USHBP1; NbExp=3; IntAct=EBI-1383852, EBI-739895;
Q8N1B4:VPS52; NbExp=3; IntAct=EBI-1383852, EBI-2799833;
Q96BR9:ZBTB8A; NbExp=3; IntAct=EBI-1383852, EBI-742740;
Q8NF99:ZNF397; NbExp=3; IntAct=EBI-1383852, EBI-10213894;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000269|PubMed:15866171}. Note=In response to stress,
recruited by p53/TP53 to specific promoters.
-!- DOMAIN: The AIS (autoinhibitory sequence) region shows some
sequence similarity with the ubiquitin-associated domains and
represses kinase activity.
-!- PTM: Ubiquitinated. {ECO:0000250}.
-!- PTM: Phosphorylated at Thr-172 by STK11/LKB1 in complex with
STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Also
phosphorylated at Thr-172 by CAMKK2; triggered by a rise in
intracellular calcium ions, without detectable changes in the
AMP/ATP ratio. CAMKK1 can also phosphorylate Thr-172, but at much
lower level. Dephosphorylated by protein phosphatase 2A and 2C
(PP2A and PP2C). Phosphorylated by ULK1; leading to negatively
regulate AMPK activity and suggesting the existence of a
regulatory feedback loop between ULK1 and AMPK. Dephosphorylated
by PPM1A and PPM1B at Thr-172 (mediated by STK11/LKB1).
{ECO:0000269|PubMed:15980064, ECO:0000269|PubMed:21460634}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. SNF1 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U06454; AAA64745.1; -; mRNA.
EMBL; AL035705; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC069680; AAH69680.1; -; mRNA.
EMBL; BC069740; AAH69740.1; -; mRNA.
EMBL; BC069823; AAH69823.1; -; mRNA.
CCDS; CCDS605.1; -.
PIR; S51025; S51025.
RefSeq; NP_006243.2; NM_006252.3.
UniGene; Hs.437039; -.
PDB; 2H6D; X-ray; 1.85 A; A=6-279.
PDB; 2LTU; NMR; -; A=282-339.
PDB; 2YZA; X-ray; 3.02 A; A=6-279.
PDB; 3AQV; X-ray; 2.08 A; A=6-279.
PDB; 4CFE; X-ray; 3.02 A; A/C=1-552.
PDB; 4CFF; X-ray; 3.92 A; A/C=1-552.
PDB; 4ZHX; X-ray; 2.99 A; A/C=2-552.
PDB; 5EZV; X-ray; 2.99 A; A/C=2-347, A/C=397-552.
PDB; 5ISO; X-ray; 2.63 A; A/C=1-552.
PDBsum; 2H6D; -.
PDBsum; 2LTU; -.
PDBsum; 2YZA; -.
PDBsum; 3AQV; -.
PDBsum; 4CFE; -.
PDBsum; 4CFF; -.
PDBsum; 4ZHX; -.
PDBsum; 5EZV; -.
PDBsum; 5ISO; -.
ProteinModelPortal; P54646; -.
SMR; P54646; -.
BioGrid; 111550; 85.
CORUM; P54646; -.
DIP; DIP-39796N; -.
IntAct; P54646; 134.
MINT; MINT-2804161; -.
STRING; 9606.ENSP00000360290; -.
BindingDB; P54646; -.
ChEMBL; CHEMBL2116; -.
DrugBank; DB00945; Acetylsalicylic acid.
GuidetoPHARMACOLOGY; 1542; -.
iPTMnet; P54646; -.
PhosphoSitePlus; P54646; -.
BioMuta; PRKAA2; -.
DMDM; 20178276; -.
EPD; P54646; -.
MaxQB; P54646; -.
PaxDb; P54646; -.
PeptideAtlas; P54646; -.
PRIDE; P54646; -.
DNASU; 5563; -.
Ensembl; ENST00000371244; ENSP00000360290; ENSG00000162409.
GeneID; 5563; -.
KEGG; hsa:5563; -.
UCSC; uc001cyk.5; human.
CTD; 5563; -.
DisGeNET; 5563; -.
EuPathDB; HostDB:ENSG00000162409.10; -.
GeneCards; PRKAA2; -.
HGNC; HGNC:9377; PRKAA2.
HPA; HPA044540; -.
MIM; 600497; gene.
neXtProt; NX_P54646; -.
OpenTargets; ENSG00000162409; -.
PharmGKB; PA33745; -.
eggNOG; KOG0586; Eukaryota.
eggNOG; ENOG410XNQ0; LUCA.
GeneTree; ENSGT00790000122947; -.
HOGENOM; HOG000233016; -.
HOVERGEN; HBG050432; -.
KO; K07198; -.
OMA; RWHFGIR; -.
PhylomeDB; P54646; -.
TreeFam; TF314032; -.
BRENDA; 2.7.11.1; 2681.
Reactome; R-HSA-1445148; Translocation of GLUT4 to the plasma membrane.
Reactome; R-HSA-1632852; Macroautophagy.
Reactome; R-HSA-163680; AMPK inhibits chREBP transcriptional activation activity.
Reactome; R-HSA-200425; Import of palmitoyl-CoA into the mitochondrial matrix.
Reactome; R-HSA-2151209; Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
Reactome; R-HSA-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
SignaLink; P54646; -.
SIGNOR; P54646; -.
ChiTaRS; PRKAA2; human.
EvolutionaryTrace; P54646; -.
GeneWiki; PRKAA2; -.
GenomeRNAi; 5563; -.
PRO; PR:P54646; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000162409; -.
CleanEx; HS_PRKAA2; -.
ExpressionAtlas; P54646; baseline and differential.
Genevisible; P54646; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0031588; C:nucleotide-activated protein kinase complex; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0050405; F:[acetyl-CoA carboxylase] kinase activity; IEA:UniProtKB-EC.
GO; GO:0047322; F:[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase activity; IEA:UniProtKB-EC.
GO; GO:0004679; F:AMP-activated protein kinase activity; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0035174; F:histone serine kinase activity; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004672; F:protein kinase activity; TAS:ProtInc.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IDA:MGI.
GO; GO:0006853; P:carnitine shuttle; TAS:Reactome.
GO; GO:0007050; P:cell cycle arrest; TAS:Reactome.
GO; GO:0035690; P:cellular response to drug; IEA:Ensembl.
GO; GO:0042149; P:cellular response to glucose starvation; ISS:UniProtKB.
GO; GO:0031669; P:cellular response to nutrient levels; ISS:UniProtKB.
GO; GO:0071380; P:cellular response to prostaglandin E stimulus; IEA:Ensembl.
GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0055089; P:fatty acid homeostasis; ISS:UniProtKB.
GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
GO; GO:0035404; P:histone-serine phosphorylation; IBA:GO_Central.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0008610; P:lipid biosynthetic process; ISS:UniProtKB.
GO; GO:0016236; P:macroautophagy; TAS:Reactome.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0032007; P:negative regulation of TOR signaling; ISS:UniProtKB.
GO; GO:0010508; P:positive regulation of autophagy; ISS:UniProtKB.
GO; GO:0045821; P:positive regulation of glycolytic process; ISS:UniProtKB.
GO; GO:0016239; P:positive regulation of macroautophagy; TAS:ParkinsonsUK-UCL.
GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
GO; GO:2000505; P:regulation of energy homeostasis; ISS:UniProtKB.
GO; GO:0042304; P:regulation of fatty acid biosynthetic process; TAS:Reactome.
GO; GO:0016241; P:regulation of macroautophagy; ISS:UniProtKB.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0014850; P:response to muscle activity; IEA:Ensembl.
GO; GO:0006950; P:response to stress; ISS:UniProtKB.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
InterPro; IPR032270; AMPK_C.
InterPro; IPR028375; KA1/Ssp2_C.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF16579; AdenylateSensor; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF103243; SSF103243; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Autophagy; Biological rhythms;
Cholesterol biosynthesis; Cholesterol metabolism; Chromatin regulator;
Complete proteome; Cytoplasm; Fatty acid biosynthesis;
Fatty acid metabolism; Kinase; Lipid biosynthesis; Lipid metabolism;
Magnesium; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Serine/threonine-protein kinase;
Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
Sterol metabolism; Transcription; Transcription regulation;
Transferase; Ubl conjugation; Wnt signaling pathway.
CHAIN 1 552 5'-AMP-activated protein kinase catalytic
subunit alpha-2.
/FTId=PRO_0000085594.
DOMAIN 16 268 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 22 30 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 291 376 AIS. {ECO:0000250}.
ACT_SITE 139 139 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 45 45 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 172 172 Phosphothreonine; by LKB1 and CaMKK2.
{ECO:0000269|PubMed:15980064}.
MOD_RES 258 258 Phosphothreonine.
{ECO:0000250|UniProtKB:Q09137}.
MOD_RES 377 377 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:23186163}.
MOD_RES 491 491 Phosphoserine.
{ECO:0000250|UniProtKB:Q09137}.
VARIANT 371 371 P -> T (in breast cancer samples;
infiltrating ductal carcinoma; somatic
mutation). {ECO:0000269|PubMed:16959974,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_035623.
VARIANT 407 407 R -> Q (in a gastric adenocarcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040355.
VARIANT 523 523 S -> G (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035624.
MUTAGEN 172 172 T->D: Phosphomimetic mutant.
CONFLICT 180 180 A -> T (in Ref. 1; AAA64745).
{ECO:0000305}.
CONFLICT 271 271 D -> G (in Ref. 1; AAA64745).
{ECO:0000305}.
CONFLICT 403 404 HL -> RQ (in Ref. 1; AAA64745).
{ECO:0000305}.
STRAND 16 24 {ECO:0000244|PDB:2H6D}.
STRAND 26 35 {ECO:0000244|PDB:2H6D}.
TURN 36 38 {ECO:0000244|PDB:2H6D}.
STRAND 41 48 {ECO:0000244|PDB:2H6D}.
HELIX 49 54 {ECO:0000244|PDB:2H6D}.
HELIX 58 69 {ECO:0000244|PDB:2H6D}.
STRAND 79 84 {ECO:0000244|PDB:2H6D}.
STRAND 86 94 {ECO:0000244|PDB:2H6D}.
HELIX 101 108 {ECO:0000244|PDB:2H6D}.
HELIX 113 133 {ECO:0000244|PDB:2H6D}.
HELIX 142 144 {ECO:0000244|PDB:2H6D}.
STRAND 145 147 {ECO:0000244|PDB:2H6D}.
STRAND 153 155 {ECO:0000244|PDB:2H6D}.
HELIX 160 162 {ECO:0000244|PDB:2H6D}.
TURN 177 179 {ECO:0000244|PDB:4ZHX}.
HELIX 183 185 {ECO:0000244|PDB:2H6D}.
HELIX 192 209 {ECO:0000244|PDB:2H6D}.
HELIX 219 228 {ECO:0000244|PDB:2H6D}.
HELIX 239 248 {ECO:0000244|PDB:2H6D}.
HELIX 253 255 {ECO:0000244|PDB:2H6D}.
HELIX 259 264 {ECO:0000244|PDB:2H6D}.
HELIX 266 269 {ECO:0000244|PDB:2H6D}.
HELIX 274 276 {ECO:0000244|PDB:2H6D}.
HELIX 283 286 {ECO:0000244|PDB:4ZHX}.
TURN 291 295 {ECO:0000244|PDB:4ZHX}.
HELIX 304 311 {ECO:0000244|PDB:4ZHX}.
HELIX 323 336 {ECO:0000244|PDB:4ZHX}.
HELIX 338 341 {ECO:0000244|PDB:4ZHX}.
STRAND 403 408 {ECO:0000244|PDB:4ZHX}.
HELIX 412 425 {ECO:0000244|PDB:4ZHX}.
STRAND 429 443 {ECO:0000244|PDB:4ZHX}.
TURN 445 447 {ECO:0000244|PDB:4ZHX}.
STRAND 450 460 {ECO:0000244|PDB:4ZHX}.
TURN 461 463 {ECO:0000244|PDB:4ZHX}.
STRAND 464 471 {ECO:0000244|PDB:4ZHX}.
HELIX 535 549 {ECO:0000244|PDB:4ZHX}.
SEQUENCE 552 AA; 62320 MW; C46AAFC1D5104975 CRC64;
MAEKQKHDGR VKIGHYVLGD TLGVGTFGKV KIGEHQLTGH KVAVKILNRQ KIRSLDVVGK
IKREIQNLKL FRHPHIIKLY QVISTPTDFF MVMEYVSGGE LFDYICKHGR VEEMEARRLF
QQILSAVDYC HRHMVVHRDL KPENVLLDAH MNAKIADFGL SNMMSDGEFL RTSCGSPNYA
APEVISGRLY AGPEVDIWSC GVILYALLCG TLPFDDEHVP TLFKKIRGGV FYIPEYLNRS
VATLLMHMLQ VDPLKRATIK DIREHEWFKQ DLPSYLFPED PSYDANVIDD EAVKEVCEKF
ECTESEVMNS LYSGDPQDQL AVAYHLIIDN RRIMNQASEF YLASSPPSGS FMDDSAMHIP
PGLKPHPERM PPLIADSPKA RCPLDALNTT KPKSLAVKKA KWHLGIRSQS KPYDIMAEVY
RAMKQLDFEW KVVNAYHLRV RRKNPVTGNY VKMSLQLYLV DNRSYLLDFK SIDDEVVEQR
SGSSTPQRSC SAAGLHRPRS SFDSTTAESH SLSGSLTGSL TGSTLSSVSP RLGSHTMDFF
EMCASLITTL AR


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