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5'-AMP-activated protein kinase catalytic subunit alpha-1 (AMPK subunit alpha-1) (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) (Tau-protein kinase PRKAA1) (EC 2.7.11.26)

 AAPK1_RAT               Reviewed;         559 AA.
P54645;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
28-JUL-2009, sequence version 2.
22-NOV-2017, entry version 172.
RecName: Full=5'-AMP-activated protein kinase catalytic subunit alpha-1;
Short=AMPK subunit alpha-1;
EC=2.7.11.1 {ECO:0000269|PubMed:2369897, ECO:0000269|PubMed:9029219};
AltName: Full=Acetyl-CoA carboxylase kinase;
Short=ACACA kinase;
EC=2.7.11.27 {ECO:0000269|PubMed:9029219};
AltName: Full=Hydroxymethylglutaryl-CoA reductase kinase;
Short=HMGCR kinase;
EC=2.7.11.31 {ECO:0000269|PubMed:2369897};
AltName: Full=Tau-protein kinase PRKAA1;
EC=2.7.11.26 {ECO:0000305|PubMed:21204788};
Name=Prkaa1; Synonyms=Ampk1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 10-559, AND PROTEIN SEQUENCE OF 24-40;
90-115; 129-140; 150-160; 166-182; 236-257; 272-276; 286-305; 326-341;
350-367; 375-384; 409-426; 437-446; 458-475 AND 507-517.
STRAIN=Sprague-Dawley; TISSUE=Hypothalamus, and Liver;
PubMed=8557660; DOI=10.1074/jbc.271.2.611;
Stapleton D., Mitchelhill K.I., Gao G., Widmer J., Michell B.J.,
Teh T., House C.M., Fernandez C.S., Cox T., Witters L.A., Kemp B.E.;
"Mammalian AMP-activated protein kinase subfamily.";
J. Biol. Chem. 271:611-614(1996).
[3]
CATALYTIC ACTIVITY, AND FUNCTION IN PHOSPHORYLATION OF HMGCR.
PubMed=2369897;
Clarke P.R., Hardie D.G.;
"Regulation of HMG-CoA reductase: identification of the site
phosphorylated by the AMP-activated protein kinase in vitro and in
intact rat liver.";
EMBO J. 9:2439-2446(1990).
[4]
IDENTIFICATION IN THE AMPK COMPLEX.
STRAIN=Sprague-Dawley; TISSUE=Hypothalamus, and Liver;
PubMed=7961907;
Stapleton D., Gao G., Michell B.J., Widmer J., Mitchelhill K.I.,
Teh T., House C.M., Witters L.A., Kemp B.E.;
"Mammalian 5'-AMP-activated protein kinase non-catalytic subunits are
homologs of proteins that interact with yeast Snf1 protein kinase.";
J. Biol. Chem. 269:29343-29346(1994).
[5]
PHOSPHORYLATION AT THR-183, AND ENZYME REGULATION.
PubMed=8910387; DOI=10.1074/jbc.271.44.27879;
Hawley S.A., Davison M., Woods A., Davies S.P., Beri R.K., Carling D.,
Hardie D.G.;
"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. 271:27879-27887(1996).
[6]
CATALYTIC ACTIVITY, AND FUNCTION IN PHOSPHORYLATION OF ACACA AND
ACACB.
PubMed=9029219;
Winder W.W., Wilson H.A., Hardie D.G., Rasmussen B.B., Hutber C.A.,
Call G.B., Clayton R.D., Conley L.M., Yoon S., Zhou B.;
"Phosphorylation of rat muscle acetyl-CoA carboxylase by AMP-activated
protein kinase and protein kinase A.";
J. Appl. Physiol. 82:219-225(1997).
[7]
FUNCTION IN PHOSPHORYLATION OF NOS3.
PubMed=10025949; DOI=10.1016/S0014-5793(98)01705-0;
Chen Z.P., Mitchelhill K.I., Michell B.J., Stapleton D.,
Rodriguez-Crespo I., Witters L.A., Power D.A.,
Ortiz de Montellano P.R., Kemp B.E.;
"AMP-activated protein kinase phosphorylation of endothelial NO
synthase.";
FEBS Lett. 443:285-289(1999).
[8]
FUNCTION IN PHOSPHORYLATION OF PFKFB2.
PubMed=11069105; DOI=10.1016/S0960-9822(00)00742-9;
Marsin A.S., Bertrand L., Rider M.H., Deprez J., Beauloye C.,
Vincent M.F., Van den Berghe G., Carling D., Hue L.;
"Phosphorylation and activation of heart PFK-2 by AMPK has a role in
the stimulation of glycolysis during ischaemia.";
Curr. Biol. 10:1247-1255(2000).
[9]
FUNCTION IN PHOSPHORYLATION OF IRS1.
PubMed=11598104; DOI=10.1074/jbc.C100483200;
Jakobsen S.N., Hardie D.G., Morrice N., Tornqvist H.E.;
"5'-AMP-activated protein kinase phosphorylates IRS-1 on Ser-789 in
mouse C2C12 myotubes in response to 5-aminoimidazole-4-carboxamide
riboside.";
J. Biol. Chem. 276:46912-46916(2001).
[10]
FUNCTION IN PHOSPHORYLATION OF MLXIPL.
PubMed=11724780; DOI=10.1074/jbc.M107895200;
Kawaguchi T., Osatomi K., Yamashita H., Kabashima T., Uyeda K.;
"Mechanism for fatty acid 'sparing' effect on glucose-induced
transcription: regulation of carbohydrate-responsive element-binding
protein by AMP-activated protein kinase.";
J. Biol. Chem. 277:3829-3835(2002).
[11]
FUNCTION IN PHOSPHORYLATION OF PFKFB3.
PubMed=12065600; DOI=10.1074/jbc.M205213200;
Marsin A.S., Bouzin C., Bertrand L., Hue L.;
"The stimulation of glycolysis by hypoxia in activated monocytes is
mediated by AMP-activated protein kinase and inducible 6-
phosphofructo-2-kinase.";
J. Biol. Chem. 277:30778-30783(2002).
[12]
PHOSPHORYLATION AT THR-183, AND ENZYME REGULATION.
PubMed=14614828; DOI=10.1016/j.cub.2003.10.031;
Woods A., Johnstone S.R., Dickerson K., Leiper F.C., Fryer L.G.,
Neumann D., Schlattner U., Wallimann T., Carlson M., Carling D.;
"LKB1 is the upstream kinase in the AMP-activated protein kinase
cascade.";
Curr. Biol. 13:2004-2008(2003).
[13]
FUNCTION, ENZYME REGULATION, AND PHOSPHORYLATION AT THR-183.
PubMed=14511394; DOI=10.1186/1475-4924-2-28;
Hawley S.A., Boudeau J., Reid J.L., Mustard K.J., Udd L., Makela T.P.,
Alessi D.R., Hardie D.G.;
"Complexes between the LKB1 tumor suppressor, STRAD alpha/beta and
MO25 alpha/beta are upstream kinases in the AMP-activated protein
kinase cascade.";
J. Biol. 2:28.1-28.16(2003).
[14]
FUNCTION IN PHOSPHORYLATION OF HNF4A.
PubMed=12740371; DOI=10.1074/jbc.M304112200;
Hong Y.H., Varanasi U.S., Yang W., Leff T.;
"AMP-activated protein kinase regulates HNF4alpha transcriptional
activity by inhibiting dimer formation and decreasing protein
stability.";
J. Biol. Chem. 278:27495-27501(2003).
[15]
PHOSPHORYLATION AT THR-269 AND SER-496, MUTAGENESIS OF THR-183;
THR-269 AND SER-496, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=12764152; DOI=10.1074/jbc.M303946200;
Woods A., Vertommen D., Neumann D., Turk R., Bayliss J.,
Schlattner U., Wallimann T., Carling D., Rider M.H.;
"Identification of phosphorylation sites in AMP-activated protein
kinase (AMPK) for upstream AMPK kinases and study of their roles by
site-directed mutagenesis.";
J. Biol. Chem. 278:28434-28442(2003).
[16]
FUNCTION IN PHOSPHORYLATION OF EEF2K.
PubMed=14709557; DOI=10.1074/jbc.M309773200;
Browne G.J., Finn S.G., Proud C.G.;
"Stimulation of the AMP-activated protein kinase leads to activation
of eukaryotic elongation factor 2 kinase and to its phosphorylation at
a novel site, serine 398.";
J. Biol. Chem. 279:12220-12231(2004).
[17]
PHOSPHORYLATION AT THR-183, AND ENZYME REGULATION.
PubMed=16054095; DOI=10.1016/j.cmet.2005.05.009;
Hawley S.A., Pan D.A., Mustard K.J., Ross L., Bain J., Edelman A.M.,
Frenguelli B.G., Hardie D.G.;
"Calmodulin-dependent protein kinase kinase-beta is an alternative
upstream kinase for AMP-activated protein kinase.";
Cell Metab. 2:9-19(2005).
[18]
PHOSPHORYLATION AT THR-183, AND ENZYME REGULATION.
PubMed=16054096; DOI=10.1016/j.cmet.2005.06.005;
Woods A., Dickerson K., Heath R., Hong S.-P., Momcilovic M.,
Johnstone S.R., Carlson M., Carling D.;
"Ca2+/calmodulin-dependent protein kinase kinase-beta acts upstream of
AMP-activated protein kinase in mammalian cells.";
Cell Metab. 2:21-33(2005).
[19]
FUNCTION IN PHOSPHORYLATION OF SLC12A1.
PubMed=17341212; DOI=10.1042/BJ20061850;
Fraser S.A., Gimenez I., Cook N., Jennings I., Katerelos M.,
Katsis F., Levidiotis V., Kemp B.E., Power D.A.;
"Regulation of the renal-specific Na+-K+-2Cl- co-transporter NKCC2 by
AMP-activated protein kinase (AMPK).";
Biochem. J. 405:85-93(2007).
[20]
PHOSPHORYLATION BY ULK1 AND ULK, AND PHOSPHORYLATION AT SER-360;
THR-368; SER-397; SER-486 AND THR-488.
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]
FUNCTION IN PHOSPHORYLATION OF MAPT.
PubMed=21204788; DOI=10.1042/BJ20101485;
Thornton C., Bright N.J., Sastre M., Muckett P.J., Carling D.;
"AMP-activated protein kinase (AMPK) is a tau kinase, activated in
response to amyloid beta-peptide exposure.";
Biochem. J. 434:503-512(2011).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486; THR-490 AND
SER-496, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[23]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 405-557 IN COMPLEX WITH
PRKAB2 AND PRKAG1.
PubMed=17851531; DOI=10.1038/nature06161;
Xiao B., Heath R., Saiu P., Leiper F.C., Leone P., Jing C.,
Walker P.A., Haire L., Eccleston J.F., Davis C.T., Martin S.R.,
Carling D., Gamblin S.J.;
"Structural basis for AMP binding to mammalian AMP-activated protein
kinase.";
Nature 449:496-500(2007).
[24]
X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 13-559 IN COMPLEX WITH
PRKAB2 AND PRKAG1, AND MUTAGENESIS OF 386-ARG--GLU-391.
PubMed=21399626; DOI=10.1038/nature09932;
Xiao B., Sanders M.J., Underwood E., Heath R., Mayer F.V., Carmena D.,
Jing C., Walker P.A., Eccleston J.F., Haire L.F., Saiu P.,
Howell S.A., Aasland R., Martin S.R., Carling D., Gamblin S.J.;
"Structure of mammalian AMPK and its regulation by ADP.";
Nature 472:230-233(2011).
-!- 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. 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
has tau-protein kinase activity: in response to amyloid beta A4
protein (APP) exposure, activated by CAMKK2, leading to
phosphorylation of MAPT/TAU; however the relevance of such data
remains unclear in vivo. Also phosphorylates CFTR, EEF2K, KLC1,
NOS3 and SLC12A1. {ECO:0000269|PubMed:10025949,
ECO:0000269|PubMed:11069105, ECO:0000269|PubMed:11598104,
ECO:0000269|PubMed:11724780, ECO:0000269|PubMed:12065600,
ECO:0000269|PubMed:12740371, ECO:0000269|PubMed:14511394,
ECO:0000269|PubMed:14709557, ECO:0000269|PubMed:17341212,
ECO:0000269|PubMed:21204788, ECO:0000269|PubMed:2369897,
ECO:0000269|PubMed:9029219}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:2369897, ECO:0000269|PubMed:9029219}.
-!- CATALYTIC ACTIVITY: ATP + [acetyl-CoA carboxylase] = ADP +
[acetyl-CoA carboxylase] phosphate. {ECO:0000269|PubMed:9029219}.
-!- CATALYTIC ACTIVITY: ATP + [hydroxymethylglutaryl-CoA reductase
(NADPH)] = ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
phosphate. {ECO:0000269|PubMed:2369897}.
-!- CATALYTIC ACTIVITY: ATP + [tau protein] = ADP + [tau protein]
phosphate. {ECO:0000305|PubMed:21204788}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- ENZYME REGULATION: Activated by phosphorylation on Thr-183.
Binding of AMP to non-catalytic gamma subunit (PRKAG1, PRKAG2 or
PRKAG3) results in allosteric activation, inducing phosphorylation
on Thr-183. AMP-binding to gamma subunit also sustains activity by
preventing dephosphorylation of Thr-183. ADP also stimulates Thr-
183 phosphorylation, without stimulating already phosphorylated
AMPK. ATP promotes dephosphorylation of Thr-183, 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. 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.
{ECO:0000269|PubMed:14511394, ECO:0000269|PubMed:14614828,
ECO:0000269|PubMed:16054095, ECO:0000269|PubMed:16054096,
ECO:0000269|PubMed:8910387}.
-!- 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. {ECO:0000269|PubMed:17851531,
ECO:0000269|PubMed:21399626, ECO:0000269|PubMed:7961907}.
-!- INTERACTION:
Q76JQ2:Flcn; NbExp=2; IntAct=EBI-7596967, EBI-7596839;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}. Note=In response to stress, recruited by p53/TP53
to specific promoters. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Low expression in kidney, liver, lung, heart
and brain.
-!- DOMAIN: The AIS (autoinhibitory sequence) region shows some
sequence similarity with the ubiquitin-associated domains and
represses kinase activity. {ECO:0000250}.
-!- PTM: Ubiquitinated. {ECO:0000250}.
-!- PTM: Phosphorylated at Thr-183 by STK11/LKB1 in complex with
STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Also
phosphorylated at Thr-183 by CAMKK2; triggered by a rise in
intracellular calcium ions, without detectable changes in the
AMP/ATP ratio. CAMKK1 can also phosphorylate Thr-183, but at a
much lower level. Dephosphorylated by protein phosphatase 2A and
2C (PP2A and PP2C). Phosphorylated by ULK1 and ULK2; leading to
negatively regulate AMPK activity and suggesting the existence of
a regulatory feedback loop between ULK1, ULK2 and AMPK. There is
some ambiguity for some phosphosites: Ser-360/Thr-368 and Ser-
486/Thr-488. Dephosphorylated by PPM1A and PPM1B (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. SNF1 subfamily. {ECO:0000305}.
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EMBL; CH474048; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; U40819; AAC52355.1; -; mRNA.
RefSeq; NP_062015.2; NM_019142.2.
UniGene; Rn.87789; -.
PDB; 2V8Q; X-ray; 2.10 A; A=407-559.
PDB; 2V92; X-ray; 2.40 A; A=407-559.
PDB; 2V9J; X-ray; 2.53 A; A=407-559.
PDB; 2Y8L; X-ray; 2.50 A; A=407-555.
PDB; 2Y8Q; X-ray; 2.80 A; A=407-555.
PDB; 2YA3; X-ray; 2.51 A; A=407-555.
PDB; 4CFH; X-ray; 3.24 A; A=13-481, C=535-559.
PDB; 4EAI; X-ray; 2.28 A; A=405-479, A=540-559.
PDB; 4EAJ; X-ray; 2.61 A; A=405-479, A=540-559.
PDB; 4EAK; X-ray; 2.50 A; A=405-479, A=540-559.
PDB; 4EAL; X-ray; 2.51 A; A=405-479, A=540-559.
PDB; 4F2L; X-ray; 1.50 A; A=295-347.
PDB; 4QFG; X-ray; 3.46 A; A=11-480, A=536-559.
PDB; 4QFR; X-ray; 3.34 A; A=11-480, A=536-559.
PDB; 4QFS; X-ray; 3.55 A; A=11-479, A=536-559.
PDB; 5KQ5; X-ray; 3.41 A; A=11-480, A=536-559.
PDB; 5T5T; X-ray; 3.46 A; A=11-480, A=536-559.
PDB; 5UFU; X-ray; 3.45 A; A=269-559.
PDBsum; 2V8Q; -.
PDBsum; 2V92; -.
PDBsum; 2V9J; -.
PDBsum; 2Y8L; -.
PDBsum; 2Y8Q; -.
PDBsum; 2YA3; -.
PDBsum; 4CFH; -.
PDBsum; 4EAI; -.
PDBsum; 4EAJ; -.
PDBsum; 4EAK; -.
PDBsum; 4EAL; -.
PDBsum; 4F2L; -.
PDBsum; 4QFG; -.
PDBsum; 4QFR; -.
PDBsum; 4QFS; -.
PDBsum; 5KQ5; -.
PDBsum; 5T5T; -.
PDBsum; 5UFU; -.
ProteinModelPortal; P54645; -.
SMR; P54645; -.
BioGrid; 249325; 5.
CORUM; P54645; -.
DIP; DIP-57168N; -.
IntAct; P54645; 314.
MINT; MINT-4566241; -.
STRING; 10116.ENSRNOP00000017626; -.
BindingDB; P54645; -.
ChEMBL; CHEMBL4533; -.
iPTMnet; P54645; -.
PhosphoSitePlus; P54645; -.
PaxDb; P54645; -.
PRIDE; P54645; -.
Ensembl; ENSRNOT00000017626; ENSRNOP00000017626; ENSRNOG00000012799.
GeneID; 65248; -.
KEGG; rno:65248; -.
CTD; 5562; -.
RGD; 3387; Prkaa1.
eggNOG; KOG0586; Eukaryota.
eggNOG; ENOG410XNQ0; LUCA.
GeneTree; ENSGT00900000140875; -.
HOGENOM; HOG000233016; -.
HOVERGEN; HBG050432; -.
InParanoid; P54645; -.
KO; K07198; -.
OMA; QGVRRAK; -.
OrthoDB; EOG091G03TG; -.
PhylomeDB; P54645; -.
TreeFam; TF314032; -.
BRENDA; 2.7.11.1; 5301.
BRENDA; 2.7.11.31; 5301.
Reactome; R-RNO-1632852; Macroautophagy.
Reactome; R-RNO-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
Reactome; R-RNO-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-RNO-6804756; Regulation of TP53 Activity through Phosphorylation.
SABIO-RK; P54645; -.
EvolutionaryTrace; P54645; -.
PRO; PR:P54645; -.
Proteomes; UP000002494; Chromosome 2.
Bgee; ENSRNOG00000012799; -.
Genevisible; P54645; RN.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005622; C:intracellular; ISO:RGD.
GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
GO; GO:0031588; C:nucleotide-activated protein kinase complex; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:RGD.
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; IDA:RGD.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0042557; F:eukaryotic elongation factor-2 kinase activator activity; NAS:UniProtKB.
GO; GO:0035174; F:histone serine kinase activity; ISS:UniProtKB.
GO; GO:0019900; F:kinase binding; IPI:RGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
GO; GO:0004672; F:protein kinase activity; ISO:RGD.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:RGD.
GO; GO:0050321; F:tau-protein kinase activity; IEA:UniProtKB-EC.
GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO; GO:0061762; P:CAMKK-AMPK signaling cascade; ISO:RGD.
GO; GO:0071361; P:cellular response to ethanol; IEP:RGD.
GO; GO:0042149; P:cellular response to glucose starvation; ISS:UniProtKB.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEP:RGD.
GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
GO; GO:0031669; P:cellular response to nutrient levels; ISS:UniProtKB.
GO; GO:0071417; P:cellular response to organonitrogen compound; IEP:RGD.
GO; GO:0071380; P:cellular response to prostaglandin E stimulus; ISO:RGD.
GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0009631; P:cold acclimation; IDA:RGD.
GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0055089; P:fatty acid homeostasis; IDA:UniProtKB.
GO; GO:0019395; P:fatty acid oxidation; ISO:RGD.
GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
GO; GO:0006006; P:glucose metabolic process; ISO:RGD.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0008610; P:lipid biosynthetic process; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
GO; GO:2001274; P:negative regulation of glucose import in response to insulin stimulus; IMP:RGD.
GO; GO:0050995; P:negative regulation of lipid catabolic process; ISS:UniProtKB.
GO; GO:0032007; P:negative regulation of TOR signaling; ISS:UniProtKB.
GO; GO:0017148; P:negative regulation of translation; NAS:UniProtKB.
GO; GO:0010508; P:positive regulation of autophagy; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:RGD.
GO; GO:0046321; P:positive regulation of fatty acid oxidation; NAS:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
GO; GO:0045722; P:positive regulation of gluconeogenesis; NAS:UniProtKB.
GO; GO:0046326; P:positive regulation of glucose import; NAS:UniProtKB.
GO; GO:0045821; P:positive regulation of glycolytic process; IDA:UniProtKB.
GO; GO:0048643; P:positive regulation of skeletal muscle tissue development; ISO:RGD.
GO; GO:0051291; P:protein heterooligomerization; IDA:RGD.
GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
GO; GO:2000505; P:regulation of energy homeostasis; IDA:UniProtKB.
GO; GO:0033135; P:regulation of peptidyl-serine phosphorylation; ISO:RGD.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0060627; P:regulation of vesicle-mediated transport; IMP:RGD.
GO; GO:0014823; P:response to activity; IDA:RGD.
GO; GO:0031000; P:response to caffeine; IDA:RGD.
GO; GO:1901563; P:response to camptothecin; ISO:RGD.
GO; GO:0010332; P:response to gamma radiation; ISS:UniProtKB.
GO; GO:0042542; P:response to hydrogen peroxide; ISO:RGD.
GO; GO:0009411; P:response to UV; ISO:RGD.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
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_sf.
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; Direct protein sequencing;
Fatty acid biosynthesis; Fatty acid metabolism; Kinase;
Lipid biosynthesis; Lipid metabolism; Magnesium; Metal-binding;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Steroid biosynthesis;
Steroid metabolism; Sterol biosynthesis; Sterol metabolism;
Transcription; Transcription regulation; Transferase; Ubl conjugation;
Wnt signaling pathway.
CHAIN 1 559 5'-AMP-activated protein kinase catalytic
subunit alpha-1.
/FTId=PRO_0000085593.
DOMAIN 27 279 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 33 41 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 302 381 AIS. {ECO:0000250}.
ACT_SITE 150 150 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 56 56 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 32 32 Phosphothreonine.
{ECO:0000250|UniProtKB:Q13131}.
MOD_RES 183 183 Phosphothreonine; by LKB1 and CaMKK2.
{ECO:0000269|PubMed:14511394,
ECO:0000269|PubMed:14614828,
ECO:0000269|PubMed:16054095,
ECO:0000269|PubMed:16054096,
ECO:0000269|PubMed:8910387}.
MOD_RES 269 269 Phosphothreonine.
{ECO:0000269|PubMed:12764152}.
MOD_RES 355 355 Phosphothreonine.
{ECO:0000250|UniProtKB:Q13131}.
MOD_RES 356 356 Phosphoserine.
{ECO:0000250|UniProtKB:Q13131}.
MOD_RES 360 360 Phosphoserine; by ULK1.
{ECO:0000305|PubMed:21460634}.
MOD_RES 368 368 Phosphothreonine; by ULK1.
{ECO:0000305|PubMed:21460634}.
MOD_RES 382 382 Phosphothreonine.
{ECO:0000250|UniProtKB:Q13131}.
MOD_RES 397 397 Phosphoserine; by ULK1.
{ECO:0000269|PubMed:21460634}.
MOD_RES 467 467 Phosphoserine.
{ECO:0000250|UniProtKB:Q13131}.
MOD_RES 486 486 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 486 486 Phosphoserine; by ULK1.
{ECO:0000244|PubMed:22673903,
ECO:0000305|PubMed:21460634}.
MOD_RES 488 488 Phosphothreonine; by ULK1.
{ECO:0000305|PubMed:21460634}.
MOD_RES 490 490 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 496 496 Phosphoserine.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:12764152}.
MOD_RES 508 508 Phosphoserine.
{ECO:0000250|UniProtKB:Q13131}.
MOD_RES 524 524 Phosphoserine.
{ECO:0000250|UniProtKB:Q13131}.
MOD_RES 527 527 Phosphoserine.
{ECO:0000250|UniProtKB:Q13131}.
MUTAGEN 183 183 T->E: Hinders activation.
{ECO:0000269|PubMed:12764152}.
MUTAGEN 269 269 T->A: Hinders activation.
{ECO:0000269|PubMed:12764152}.
MUTAGEN 269 269 T->D: Retains activation ability.
{ECO:0000269|PubMed:12764152}.
MUTAGEN 386 391 RHTLDE->AHALAA: Allosterically activated
by AMP but is not protected against
dephosphorylation by AMP or ADP.
{ECO:0000269|PubMed:21399626}.
MUTAGEN 496 496 S->A: Hinders activation.
{ECO:0000269|PubMed:12764152}.
MUTAGEN 496 496 S->D: Retains activation ability.
{ECO:0000269|PubMed:12764152}.
CONFLICT 13 14 Missing (in Ref. 2; AAC52355).
{ECO:0000305}.
CONFLICT 473 473 D -> L (in Ref. 2; AA sequence).
{ECO:0000305}.
STRAND 27 34 {ECO:0000244|PDB:4CFH}.
STRAND 37 39 {ECO:0000244|PDB:4CFH}.
STRAND 41 46 {ECO:0000244|PDB:4CFH}.
TURN 47 49 {ECO:0000244|PDB:4CFH}.
STRAND 52 59 {ECO:0000244|PDB:4CFH}.
HELIX 60 63 {ECO:0000244|PDB:4CFH}.
TURN 64 67 {ECO:0000244|PDB:4CFH}.
HELIX 69 80 {ECO:0000244|PDB:4CFH}.
STRAND 90 95 {ECO:0000244|PDB:4CFH}.
STRAND 97 105 {ECO:0000244|PDB:4CFH}.
TURN 112 117 {ECO:0000244|PDB:4CFH}.
STRAND 118 121 {ECO:0000244|PDB:4CFH}.
HELIX 124 143 {ECO:0000244|PDB:4CFH}.
STRAND 146 149 {ECO:0000244|PDB:4QFG}.
STRAND 155 158 {ECO:0000244|PDB:4CFH}.
STRAND 164 166 {ECO:0000244|PDB:4CFH}.
HELIX 169 171 {ECO:0000244|PDB:5KQ5}.
STRAND 188 190 {ECO:0000244|PDB:4CFH}.
HELIX 193 196 {ECO:0000244|PDB:4CFH}.
HELIX 204 220 {ECO:0000244|PDB:4CFH}.
HELIX 230 238 {ECO:0000244|PDB:4CFH}.
HELIX 250 259 {ECO:0000244|PDB:4CFH}.
TURN 264 266 {ECO:0000244|PDB:4CFH}.
HELIX 270 274 {ECO:0000244|PDB:4CFH}.
HELIX 277 280 {ECO:0000244|PDB:4CFH}.
STRAND 287 289 {ECO:0000244|PDB:4CFH}.
HELIX 301 311 {ECO:0000244|PDB:4F2L}.
HELIX 315 323 {ECO:0000244|PDB:4F2L}.
HELIX 330 347 {ECO:0000244|PDB:4F2L}.
HELIX 349 351 {ECO:0000244|PDB:4CFH}.
HELIX 372 374 {ECO:0000244|PDB:4CFH}.
HELIX 376 381 {ECO:0000244|PDB:4CFH}.
STRAND 407 413 {ECO:0000244|PDB:2V8Q}.
HELIX 417 430 {ECO:0000244|PDB:2V8Q}.
STRAND 434 439 {ECO:0000244|PDB:2V8Q}.
STRAND 442 448 {ECO:0000244|PDB:2V8Q}.
TURN 450 452 {ECO:0000244|PDB:2V8Q}.
STRAND 455 464 {ECO:0000244|PDB:2V8Q}.
STRAND 466 468 {ECO:0000244|PDB:2V8Q}.
STRAND 470 477 {ECO:0000244|PDB:2V8Q}.
HELIX 542 555 {ECO:0000244|PDB:2V8Q}.
SEQUENCE 559 AA; 63973 MW; A869C340A85785ED CRC64;
MRRLSSWRKM ATAEKQKHDG RVKIGHYILG DTLGVGTFGK VKVGKHELTG HKVAVKILNR
QKIRSLDVVG KIRREIQNLK LFRHPHIIKL YQVISTPSDI FMVMEYVSGG ELFDYICKNG
RLDEKESRRL FQQILSGVDY CHRHMVVHRD LKPENVLLDA HMNAKIADFG LSNMMSDGEF
LRTSCGSPNY AAPEVISGRL YAGPEVDIWS SGVILYALLC GTLPFDDDHV PTLFKKICDG
IFYTPQYLNP SVISLLKHML QVDPMKRATI KDIREHEWFK QDLPKYLFPE DPSYSSTMID
DEALKEVCEK FECSEEEVLS CLYNRNHQDP LAVAYHLIID NRRIMNEAKD FYLATSPPDS
FLDDHHLTRP HPERVPFLVA ETPRARHTLD ELNPQKSKHQ GVRKAKWHLG IRSQSRPNDI
MAEVCRAIKQ LDYEWKVVNP YYLRVRRKNP VTSTFSKMSL QLYQVDSRTY LLDFRSIDDE
ITEAKSGTAT PQRSGSISNY RSCQRSDSDA EAQGKPSEVS LTSSVTSLDS SPVDVAPRPG
SHTIEFFEMC ANLIKILAQ


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