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Information on EC 2.7.11.31 - [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase
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2.7.11.31 [hydroxymethylglutaryl-CoA reductase (NADPH)] kinaseIUBMB Comments
The enzyme is activated by AMP. EC 1.1.1.34, hydroxymethylglutaryl-CoA reductase (NADPH) is inactivated by the phosphorylation of the enzyme protein. Histones can also act as acceptors. The enzyme can also phosphorylate hepatic acetyl-CoA carboxylase (EC 6.4.1.2) and adipose hormone-sensitive lipase (EC 3.1.1.79) . Thr-172 within the catalytic subunit (alpha-subunit) is the major site phosphorylated by the AMP-activated protein kinase kinase . GTP can act instead of ATP
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Word Map
- 2.7.11.31
- metformin
- rapamycin
- peroxisome
- obesity
- aicar
- mtor
- carboxylase
-
proliferator-activated
- acetyl-coa
- endothelial
- cardiac
-
high-fat
- triglyceride
- adipocytes
- adiponectin
- glycogen
- agonist
- mellitus
-
obese
- sterol
- hypothalamic
- steatosis
- sirt1
-
antidiabetic
-
ampk-dependent
-
diet-induced
- sirtuins
- leptin
-
p-ampk
- 5-aminoimidazole-4-carboxamide
-
lipogenesis
-
insulin-stimulated
-
ampk-mediated
- myotubes
-
element-binding
-
hfd-induced
-
anti-obesity
- srebp-1c
- ulk1
- camkks
-
adipor1
- coactivator-1
-
palmitoyltransferase-1
- dorsomorphin
- drug development
-
phospho-ampk
- epitrochlearis
-
metformin-induced
- phenformin
-
energy-sensing
-
insulin-independent
- medicine
- industry
- pharmacology
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
adenosine monophosphate-activated protein kinase, amp-activated kinase, 5'-amp-activated protein kinase, prkaa1, snf1 kinase, adenosine 5'-monophosphate-activated protein kinase, ampkalpha1, reductase kinase, aak-2, ampk alpha2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-hydroxy-3-methylglutaryl coenzyme A reductase kinase
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3-hydroxy-3-methylglutaryl-CoA reductase kinase
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5'-AMP-activated protein kinase catalytic subunit alpha-1
adenosine monophosphate-activated protein kinase
AMP-activated protein kinase
AMP-activated protein kinase alpha
AMPK
AMPKalpha
AMPKalpha1
AMPKalpha2
beta-hydroxy-beta-methylglutaryl-CoA reductase kinase
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EC 2.7.1.109
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formerly
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hydroxymethylglutaryl coenzyme A reductase kinase
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hydroxymethylglutaryl coenzyme A reductase kinase (phosphorylating)
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reductase kinase
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Snf1
Snf1 kinase
SNF1-interacting protein 1
SNF1-interacting protein 2
SNF1-interacting protein 3
SNF4
[hydroxymethylglutaryl-CoA reductase (NADPH2)] kinase
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additional information
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AMPK is a member of the serine/threonin protein kinases, as well as of a metabolite-sensing kinase family
AMP-activated protein kinase
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AMP-activated protein kinase
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
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AMP-activated protein kinase
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AMP-activated protein kinase
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AMP-activated protein kinase
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AMPK
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AMPK
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
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AMPK
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AMPK
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AMPK
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)] = ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
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SYSTEMATIC NAME
IUBMB Comments
ATP:[hydroxymethylglutaryl-CoA reductase (NADPH)] phosphotransferase
The enzyme is activated by AMP. EC 1.1.1.34, hydroxymethylglutaryl-CoA reductase (NADPH) is inactivated by the phosphorylation of the enzyme protein. Histones can also act as acceptors. The enzyme can also phosphorylate hepatic acetyl-CoA carboxylase (EC 6.4.1.2) and adipose hormone-sensitive lipase (EC 3.1.1.79) [5]. Thr-172 within the catalytic subunit (alpha-subunit) is the major site phosphorylated by the AMP-activated protein kinase kinase [7]. GTP can act instead of ATP [4]
CAS REGISTRY NUMBER
COMMENTARY
172522-01-9
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 3-hydroxy-3-methyl-glutaryl-CoA reductase
ADP + [3-hydroxy-3-methyl-glutaryl-CoA reductase]phosphate
-
-
-
-
?
ATP + 3-mercaptopyruvate sulfurtransferase
ADP + phosphorylated 3-mercaptopyruvate sulfurtransferase
-
-
-
?
ATP + acetyl-CoA carboxylase 1
ADP + phosphorylated acetyl-CoA carboxylase 1
-
-
-
-
?
ATP + acylamino-acid-releasing enzyme
ADP + phosphorylated acylamino-acid-releasing enzyme
-
-
-
?
ATP + adenylate kinase isoenzyme 1
ADP + phosphorylated adenylate kinase isoenzyme 1
-
-
-
?
ATP + adipose hormone-sensitive lipase
ADP + adipose hormone-sensitive lipase phosphate
-
-
-
-
?
ATP + band 3 anion transport protein
ADP + phosphorylated band 3 anion transport protein
-
-
-
?
ATP + bis(5'-nucleosyl)-tetraphosphatase
ADP + [bis(5'-nucleosyl)-tetraphosphatase]phosphate
-
-
-
-
?
ATP + bisphosphoglycerate mutase
ADP + phosphorylated bisphosphoglycerate mutase
-
-
-
?
ATP + bovine serum albumin
ADP + [bovine serum albumin] phosphate
-
fraction V
-
-
?
ATP + carbonic anhydrase 1
ADP + phosphorylated carbonic anhydrase 1
-
-
-
?
ATP + collapsing response mediator protein-2
ADP + [collapsing response mediator protein-2]phosphate
-
-
-
-
?
ATP + cytoplasmic malate dehydrogenase
ADP + phosphorylated cytoplasmic malate dehydrogenase
-
-
-
?
ATP + dephospho-alpha,beta-tubulin
ADP + [alpha,beta-tubulin] phosphate
-
relative kinase activity high MW-kinase 15%
-
-
?
ATP + dihydropteridine reductase
ADP + phosphorylated dihydropteridine reductase
-
-
-
?
ATP + dihydropyrimidinase-like 2
ADP + [dihydropyrimidinase-like 2]phosphate
-
-
-
-
?
ATP + DNA damage-binding protein 1
ADP + phosphorylated DNA damage-binding protein 1
-
-
-
?
ATP + dynein intermediate chain 2
ADP + [dynein intermediate chain 2]phosphate
-
-
-
-
?
ATP + erythrocyte spectrin alpha chain
ADP + phosphorylated erythrocyte spectrin alpha chain
-
-
-
?
ATP + erythrocyte spectrin beta chain
ADP + phosphorylated erythrocyte spectrin beta chain
-
-
-
?
ATP + eukaryotic elongation factor 2 kinase
ADP + phosphorylated eukaryotic elongation factor 2 kinase
ATP + far upstream element binding protein 1
ADP + [far upstream element binding protein 1]phosphate
-
-
-
-
?
ATP + glial fibrillary acidic protein
ADP + [glial fibrillary acidic protein]phosphate
-
-
-
-
?
ATP + glutamate dehydrogenase 1
ADP + [glutamate dehydrogenase 1]phosphate
-
-
-
-
?
ATP + glutathione S-transferase omega-1
ADP + phosphorylated glutathione S-transferase omega-1
-
-
-
?
ATP + glutathione synthetase
ADP + phosphorylated glutathione synthetase
-
-
-
?
ATP + glyceraldehyde-3-phosphate dehydrogenase
ADP + [glyceraldehyde-3-phosphate dehydrogenase]phosphate
-
-
-
-
?
ATP + glycerophosphate acyltransferase
ADP + [glycerophosphate acyltransferase]phosphate
-
-
-
-
?
ATP + glycogen synthase
ADP + [glycogen synthase] phosphate
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relative kinase activity for low-MW kinase 7%, high MW-kinase 87%
-
-
?
ATP + heavy meromyosin
ADP + [heavy meromyosin] phosphate
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relative kinase activity for low-MW kinase 2%, high MW-kinase 100%
-
-
?
ATP + heterogeneous nuclear ribonucleoproteins A2/B1
ADP + [heterogeneous nuclear ribonucleoproteins A2/B1]phosphate
-
-
-
-
?
ATP + histone H1 (IIIS)
ADP + [histone H1 (IIIS)] phosphate
-
histones are better substrates for high-MW kinase than hydroxymethylglutaryl-CoA reductase, relative kinase activity for low-MW kinase 275%, high MW-kinase 103%
-
-
?
ATP + histone II-S
ADP + [histone II-S] phosphate
-
relative kinase activity for low-MW kinase 38%, high MW-kinase 159%
-
-
?
ATP + histone VIIIS
ADP + [histone VIIIS] phosphate
-
relative kinase activity for low-MW kinase 65%, high MW-kinase 141%
-
-
?
ATP + HMKSAMSGLHLVKRR
ADP + ?
-
synthetic SAMS-containing peptide as substrate
-
-
?
ATP + JAK1
ADP + phosphorylated JAK1
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phosphorylation at Ser515 and Ser518
-
-
?
ATP + MAP-2
ADP + MAP-2 phosphate
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relative kinase activity for low-MW kinase 14%, high MW-kinase 566%
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-
?
ATP + myelin basic protein
ADP + [myelin basic protein] phosphate
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moderate substrate for low-MW kinase, better than hydroxymethylglutaryl-CoA reductase for high-MW kinase, relative kinase activity for low-MW kinase 36%, high MW-kinase 238%
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-
?
ATP + myosin mixed light chains
ADP + [myosin mixed light chains] phosphate
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relative kinase activity for low-MW kinase 4%, high MW-kinase 27%
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-
?
ATP + neurofilament triplet L protein
ADP + [neurofilament triplet L protein]phosphate
-
-
-
-
?
ATP + Ngg1 interacting factor 3-like 1
ADP + [Ngg1 interacting factor 3-like 1]phosphate
-
-
-
-
?
ATP + NmrA-like family domain containing 1
ADP + [NmrA-like family domain containing 1]phosphate
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-
-
-
?
ATP + PFK2
ADP + phospho-PFK2
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phosphorylation at Ser466 induced by UV radiation and H2O2 treatment
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-
?
ATP + phosphoglycerate kinase 1
ADP + phosphorylated phosphoglycerate kinase 1
-
-
-
?
ATP + phosphoribosylformylglycinamidine synthase
ADP + phosphorylated phosphoribosylformylglycinamidine synthase
-
-
-
?
ATP + phosphorylase B
ADP + [phosphorylase B] phosphate
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relative kinase activity high MW-kinase 12%
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-
?
ATP + PKZeta
?
-
AMPK alpha phosphorylates PKZeta on residue Thr410 within the PKCzeta activation loop
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-
?
ATP + proteasome subunit alpha type-1
ADP + phosphorylated proteasome subunit alpha type-1
-
-
-
?
ATP + proteasome subunit alpha type-7
ADP + phosphorylated proteasome subunit alpha type-7
-
-
-
?
ATP + protein kinase C and casein kinase substrate in neurons protein 1
ADP + [protein kinase C and casein kinase substrate in neurons protein 1]phosphate
-
-
-
-
?
ATP + purine nucleoside phosphorylase
ADP + phosphorylated purine nucleoside phosphorylase
-
-
-
?
ATP + rabbit muscle glycogen synthase
ADP + [rabbit muscle glycogen synthase] phosphate
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rabbit muscle glycogen synthase
-
-
?
ATP + recombinant human Kv1.5 channel
ADP + phosphorylated recombinant human Kv1.5 channel
-
-
-
-
?
ATP + RNA-binding protein HUR
ADP + ?
-
inhibits the protein by phosphorylation
-
-
?
ATP + S-formylglutathione hydrolase
ADP + phosphorylated S-formylglutathione hydrolase
-
-
-
?
ATP + selenium binding protein 1
ADP + phosphorylated selenium binding protein 1
-
-
-
?
ATP + synapsin 1
ADP + [synapsin 1] phosphate
-
as good substrate as hydroxymethylglutaryl-CoA reductase, relative kinase activity for low-MW kinase 151%, high MW-kinase 103%
-
-
?
ATP + telomerase-binding protein p23
ADP + [telomerase-binding protein p23]phosphate
-
-
-
-
?
ATP + thioredoxin-like protein 1
ADP + phosphorylated thioredoxin-like protein 1
-
-
-
?
ATP + tripeptidyl-peptidase 2
ADP + [tripeptidyl-peptidase 2]phosphate
-
-
-
-
?
ATP + ubiquitin carboxyl-terminal hydrolase 13
ADP + phosphorylated ubiquitin carboxyl-terminal hydrolase 13
-
-
-
?
ATP + ubiquitin carboxyl-terminal hydrolase 14
ADP + phosphorylated ubiquitin carboxyl-terminal hydrolase 14
-
-
-
?
ATP + ubiquitin carboxyl-terminal hydrolase 5
ADP + phosphorylated ubiquitin carboxyl-terminal hydrolase 5
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-
-
?
ATP + ubiquitin-activating enzyme E1
ADP + phosphorylated ubiquitin-activating enzyme E1
-
-
-
?
ATP + valosin-containing protein
ADP + phosphorylated valosin-containing protein
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-
-
?
ATP + [acetyl-CoA carboxylase 2]
ADP + [acetyl-CoA carboxylase 2] phosphate
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phosphorylation at Ser79
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + phospho-[acetyl-CoA carboxylase]
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phosphorylation at Ser79
-
-
?
ATP + [endothelial nitic oxide synthase]
ADP + [endothelial nitic oxide synthase] phosphate
ATP + [endothelial nitric oxide synthase]
ADP + [endothelial nitric oxide synthase] phosphate
ATP + [eukaryotic elongation factor-2]
ADP + [eukaryotic elongation factor-2] phosphate
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phosphorylation at Ser259 and Ser498
-
-
?
ATP + [glucose hexokinase regulatory protein]
ADP + [glucose hexokinase regulatory protein] phosphate
ATP + [Golgi-specific brefeldin A resistance factor 1]
ADP + [Golgi-specific brefeldin A resistance factor 1] phosphate
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
ATP + [peptide QKFQRELSTKWVLN]
ADP + [peptide QKFQRELSTKWVLN] phosphate
-
a peptide derived from glucose hexokinase regulatory protein, residues 474-487
-
-
?
ATP + [smooth muscle myosin light chain kinase]
ADP + [smooth muscle myosin light chain kinase] phosphate
ATP + [sn-glycerol-3-phosphate acyltransferase]
ADP + [sn-glycerol-3-phosphate acyltransferase]phosphate
CTP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
CDP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
-
?
dATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
dADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
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phosphorylation at about 90% the rate of ATP
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-
?
GTP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
GDP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
ITP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
IDP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
UTP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
UDP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
ATP + acetyl-CoA carboxylase
ADP + phosphorylated acetyl-CoA carboxylase
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-
-
-
?
ATP + acetyl-CoA carboxylase
ADP + phosphorylated acetyl-CoA carboxylase
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the enzyme is involved in the regulation of hepatic lipids via its downstream effector acetyl-CoA carboxylase, enzyme inhibition leads to an increased level of triacylglycerols and accumulation of lipids, metformin decreases lipid accumulation, induced by high D-glucose levels, by activating the enzyme, the enzyme functions as energy intracellular sensor
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-
?
ATP + acetyl-CoA carboxylase
ADP + phosphorylated acetyl-CoA carboxylase
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phosphorylation at Ser79, phosphorylation inhibits the acetyl-CoA carboxylase
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-
?
ATP + acetyl-CoA carboxylase
ADP + phosphorylated acetyl-CoA carboxylase
-
-
-
-
?
ATP + acetyl-CoA carboxylase
ADP + phosphorylated acetyl-CoA carboxylase
-
-
-
-
?
ATP + acetyl-CoA carboxylase
ADP + phosphorylated acetyl-CoA carboxylase
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phosphorylation at Ser79
-
-
?
ATP + acetyl-CoA carboxylase
ADP + [acetyl-CoA carboxylase] phosphate
-
-
-
?
ATP + acetyl-CoA carboxylase
ADP + [acetyl-CoA carboxylase] phosphate
-
-
-
?
ATP + acetyl-CoA carboxylase
ADP + [acetyl-CoA carboxylase] phosphate
-
-
-
?
ATP + acetyl-CoA carboxylase
ADP + [acetyl-CoA carboxylase] phosphate
-
AMPK plays an important role in regulating malonyl-CoA levels through the phosphorylation of acetyl-CoA carboxylase
-
?
ATP + acetyl-CoA carboxylase
ADP + [acetyl-CoA carboxylase] phosphate
-
-
-
?
ATP + acetyl-CoA carboxylase
ADP + [acetyl-CoA carboxylase] phosphate
-
-
-
?
ATP + acetyl-CoA carboxylase
ADP + [acetyl-CoA carboxylase] phosphate
-
substrate Rattus norvegicus hepatic acetyl-CoA carboxylase, enzyme phosphorylates Ser-residues 79, 1200 and 1215
-
?
ATP + acetyl-CoA carboxylase
ADP + [acetyl-CoA carboxylase] phosphate
-
-
-
?
ATP + acetyl-CoA carboxylase
ADP + [acetyl-CoA carboxylase]phosphate
-
AMPK alpha phosphorylates at Ser79
-
-
?
ATP + acetyl-CoA carboxylase
ADP + [acetyl-CoA carboxylase]phosphate
-
AMPKalpha can phosphorylate Ser79 of acetyl-CoA carboxylase
-
-
?
ATP + acetyl-CoA carboxylase
ADP + [acetyl-CoA carboxylase]phosphate
-
-
-
-
?
ATP + acetyl-CoA carboxylase
ADP + [acetyl-CoA carboxylase]phosphate
-
-
-
-
?
ATP + acetyl-CoA carboxylase
ADP + [acetyl-CoA carboxylase]phosphate
-
-
-
-
?
ATP + adipose hormone-sensitive lipase
ADP + [adipose hormone-sensitive lipase] phosphate
-
-
-
-
?
ATP + adipose hormone-sensitive lipase
ADP + [adipose hormone-sensitive lipase] phosphate
-
-
-
-
?
ATP + ATF1
ADP + phospho-ATF1
-
important reaction in enhancement of transcriptional activity
-
-
?
ATP + ATF1
ADP + phospho-ATF1
-
phosphorylation at Ser63 and Ser267, recombinant AMPK composed by subunits alpha2beta2gamma2
-
-
?
ATP + ATF2
ADP + phospho-ATF2
-
recombinant AMPK composed by subunits alpha2beta2gamma2
-
-
?
ATP + biotin-GGHMRSAMSGLHLVKRR-NH2
ADP + phosphorylated biotin-GGHMRSAMpSGLHLVKRR-NH2
i.e. SAMS peptide, a peptide derived from residues 73-85 of rat acetyl-CoA carboxylase in which Ser77 is mutated to Ala and the AMPK phosphorylation site is Ser79
-
-
?
ATP + biotin-GGHMRSAMSGLHLVKRR-NH2
ADP + phosphorylated biotin-GGHMRSAMpSGLHLVKRR-NH2
i.e. SAMS peptide, a peptide derived from residues 73-85 of rat acetyl-CoA carboxylase in which Ser77 is mutated to Ala and the AMPK phosphorylation site is Ser79
-
-
?
ATP + casein
ADP + casein phosphate
-
relative kinase activity for low-MW kinase 8%, high MW-kinase 48%
-
-
?
ATP + casein
ADP + casein phosphate
-
relative kinase activity for low-MW kinase 8%, high MW-kinase 48%
-
-
?
ATP + CREB
ADP + phospho-CREB
-
important reaction in enhancement of transcriptional activity
-
-
?
ATP + CREB
ADP + phospho-CREB
-
phosphorylation at Ser98 and Ser133, recombinant AMPK composed by subunits alpha2beta2gamma2
-
-
?
ATP + CREB1
ADP + phospho-CREB1
-
AMPK competes with protein kinase A for the Ser119 phosphorylation site
-
-
?
ATP + CREB1
ADP + phospho-CREB1
-
phosphorylation at Ser119, recombinant AMPK composed by subunits alpha2beta2gamma2
-
-
?
ATP + CREBL2
ADP + phospho-CREBL2
-
recombinant AMPK composed by subunits alpha2beta2gamma2
-
-
?
ATP + CREM
ADP + phospho-CREM
-
important reaction in enhancement of transcriptional activity
-
-
?
ATP + CREM
ADP + phospho-CREM
-
phosphorylation at Ser71 and Ser192, recombinant AMPK composed by subunits alpha2beta2gamma2
-
-
?
ATP + eukaryotic elongation factor 2 kinase
ADP + phosphorylated eukaryotic elongation factor 2 kinase
-
phosphorylation at Ser398, the enzyme plays a regulatory role in eEF2 kinase activity, overview
-
-
?
ATP + eukaryotic elongation factor 2 kinase
ADP + phosphorylated eukaryotic elongation factor 2 kinase
-
phosphorylation at Ser398 activates the eukaryotic elongation factor 2 kinase, no activity with the substrate mutant S398A
-
-
?
ATP + HMRSAMSGLHLVKRR
ADP + ?
-
synthetic SAMS-containing peptide as substrate
-
-
?
ATP + HMRSAMSGLHLVKRR
ADP + ?
-
acetyl-CoA carboxylase-derived synthetic peptide substrate
-
-
?
ATP + HMRSAMSGLHLVKRR
ADP + ?
-
acetyl-CoA carboxylase-derived synthetic peptide substrate
-
-
?
ATP + hormone-sensitive lipase
ADP + phosphorylated hormone-sensitive lipase
-
-
-
-
?
ATP + hormone-sensitive lipase
ADP + phosphorylated hormone-sensitive lipase
-
HSL is a key enzyme in controlling lipolysis in adipocytes, phosphorylation at Ser565 by AMPK reduces its translocation toward lipid droplets
-
-
?
ATP + hormone-sensitive lipase
ADP + phosphorylated hormone-sensitive lipase
-
-
-
-
?
ATP + hormone-sensitive lipase
ADP + phosphorylated hormone-sensitive lipase
-
HSL is a key enzyme in controlling lipolysis in adipocytes, phosphorylation at Ser565 by AMPK reduces its translocation toward lipid droplets
-
-
?
ATP + Mig1 protein
ADP + phosphorylated Mig1 protein
-
-
-
?
ATP + Mig1 protein
ADP + phosphorylated Mig1 protein
a zinc-finger transcription factor, all three isoforms of Snf1 can mediate phosphorylation of Mig1
-
-
?
ATP + Mig1 protein
ADP + phosphorylated Mig1 protein
a zinc-finger transcriptions factor, all three isoforms of Snf1 can mediate phosphorylation of Mig1
-
-
?
ATP + Mig1 protein
ADP + phosphorylated Mig1 protein
-
-
-
?
ATP + Mig1 protein
ADP + phosphorylated Mig1 protein
a zinc-finger transcriptions factor, all three isoforms of Snf1 can mediate phosphorylation of Mig1
-
-
?
ATP + Mig1 protein
ADP + phosphorylated Mig1 protein
a zinc-finger transcription factor, all three isoforms of Snf1 can mediate phosphorylation of Mig1
-
-
?
ATP + Mig2 protein
ADP + phosphorylated Mig2 protein
alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2
-
-
?
ATP + Mig2 protein
ADP + phosphorylated Mig2 protein
a zinc-finger transcriptions factor, the Gal83 isoform is necessary and sufficient for phosphorylation of Mig2
-
-
?
ATP + Mig2 protein
ADP + phosphorylated Mig2 protein
alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2
-
-
?
ATP + Mig2 protein
ADP + phosphorylated Mig2 protein
a zinc-finger transcriptions factor, the Gal83 isoform is necessary and sufficient for phosphorylation of Mig2
-
-
?
ATP + p27
ADP + phospho-p27
-
loss of tuberin is associated with increased AMPK activity and altered p27 function leading to increased Cdk2 activity and resistance of the cells against apoptosis. Mislocation of p27 occurs in tuberin-deficient cells, possessing no functional gene tsc2, and can induced directly by activating AMPK physiologically via glucose deprivation or genetically via a constitutively active AMPK, overview
-
-
?
ATP + p27
ADP + phospho-p27
-
AMPK phosphorylates p27 function at least at three sites, Thr172, Thr170, and Ser83, Thr170 is localized near the nuclear localization signal sequence and its phosphorylation is responsible for p27 translocation to the cytoplasm
-
-
?
ATP + p38
ADP + phospho-p38
-
phosphorylation at Thr180/Thr182, p38 MAPK is a downstream signal of AMPK upon various stimuli, AMPK serves as a positive regulator for p38 Ser15 phosphorylation induced by UV radiation and H2O2 treatment
-
-
?
ATP + p53
ADP + phospho-p53
-
AMPK serves as a positive regulator for p38 Ser15 phosphorylation induced by UV radiation and H2O2 treatment
-
-
?
ATP + phosvitin
ADP + phosvitin phosphate
-
relative kinase activity for low-MW kinase 2%, high MW-kinase 2%
-
-
?
ATP + phosvitin
ADP + phosvitin phosphate
-
relative kinase activity for low-MW kinase 2%, high MW-kinase 2%
-
-
?
ATP + protamine
ADP + protamine phosphate
-
relative kinase activity for low-MW kinase 24%, high MW-kinase 38%
-
-
?
ATP + protamine
ADP + protamine phosphate
-
relative kinase activity for low-MW kinase 24%, high MW-kinase 38%
-
-
?
ATP + ubiquitin ligase Nedd4-2
ADP + phosphorylated ubiquitin ligase Nedd4-2
Q13131; Q9Y478; P54619
-
-
-
?
ATP + ubiquitin ligase Nedd4-2
ADP + phosphorylated ubiquitin ligase Nedd4-2
Q13131; Q9Y478; P54619
activation
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
-
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
inhibition of acetyl-CoA carboxylase
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
-
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
phosphorylation at Ser79
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
phosphorylation at Ser79
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
phosphorylation at Ser79
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
phosphorylation at Ser79
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
copper deficiency results in AMP-activated protein kinase activation and acetyl-CoA carboxylase phosphorylation in rat cerebellum, overview
-
-
?
ATP + [endothelial nitic oxide synthase]
ADP + [endothelial nitic oxide synthase] phosphate
-
activates nitric oxide synthesis, mechanism, overview
-
-
?
ATP + [endothelial nitic oxide synthase]
ADP + [endothelial nitic oxide synthase] phosphate
-
phosphorylation by AMPK at Ser1177
-
-
?
ATP + [endothelial nitric oxide synthase]
ADP + [endothelial nitric oxide synthase] phosphate
-
AMPK-eNOS signalling, overview
-
-
?
ATP + [endothelial nitric oxide synthase]
ADP + [endothelial nitric oxide synthase] phosphate
-
phosphorylation at Ser1177
-
-
?
ATP + [endothelial nitric oxide synthase]
ADP + [endothelial nitric oxide synthase] phosphate
-
-
-
-
?
ATP + [glucose hexokinase regulatory protein]
ADP + [glucose hexokinase regulatory protein] phosphate
-
-
-
-
?
ATP + [glucose hexokinase regulatory protein]
ADP + [glucose hexokinase regulatory protein] phosphate
-
phosphorylation by AMPK at a site in residues 474-487
-
-
?
ATP + [Golgi-specific brefeldin A resistance factor 1]
ADP + [Golgi-specific brefeldin A resistance factor 1] phosphate
-
phosphorylation at Thr1337 to induce disassembly of Golgi apparatus
-
-
?
ATP + [Golgi-specific brefeldin A resistance factor 1]
ADP + [Golgi-specific brefeldin A resistance factor 1] phosphate
-
a guanine nucleotide exchange factor for the ADP-ribosylation factor family associated with the Golgi apparatus, phosphorylation at Thr1337, phosphorylation site identification by mutational analysis
-
-
?
ATP + [histone deacetylase 5]
ADP + [histone deacetylase 5] phosphate
-
AMP-activated protein kinase regulates GLUT4 transcription by phosphorylating histone deacetylase 5
-
-
?
ATP + [histone deacetylase 5]
ADP + [histone deacetylase 5] phosphate
-
phosphorylation at Ser259 and Ser498
-
-
?
ATP + [HMG-CoA reductase]
ADP + [HMG-CoA reductase] phosphate
-
-
-
-
?
ATP + [HMG-CoA reductase]
ADP + [HMG-CoA reductase] phosphate
-
inhibition of HMG-CoA carboxylase
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
2 isoforms, major form A and minor form B, both phosphorylates mammalian HMG-CoA reductase
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
activated AMPK acts to down-regulate ATP-consuming pathways such as fatty acid synthesis by phosphorylating and inactivating acetyl-CoA carboxylase and protein synthesis by promoting the phosphorylation of eukaryotic elongation factor-2, in heart AMPK activation stimulates glycolysis by increasing glucose uptake
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
bicyclic phosphorylation system, enzyme is believed to be involved in protecting cells against ATP depletion due to environmental stress by inactivating several key biosynthetic enzymes
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
-
?
ATP + [malonylCoAdecarboxylase]
ADP + [malonylCoAdecarboxylase]phosphate
-
-
-
-
?
ATP + [malonylCoAdecarboxylase]
ADP + [malonylCoAdecarboxylase]phosphate
-
-
-
-
?
ATP + [O-GlcNAc transferase]
ADP + [O-GlcNAc transferase] phosphate
-
activation
-
-
?
ATP + [O-GlcNAc transferase]
ADP + [O-GlcNAc transferase] phosphate
-
AMP-activated protein kinase activates O-glucosaminyl-acylation of neuronal proteins, e.g. neurofilament H, during glucose deprivation involving activation of O-GlcNAc transferase, OGT, and induces OGT protein expression in Neuro-2a neuroblastoma cells, mechanism, overview
-
-
?
ATP + [peptide HMRSAMSGLHLVKRR]
ADP + [peptide HMRSAMSGLHLVKRR] phosphate
-
i.e. SAMS peptide
-
-
?
ATP + [peptide HMRSAMSGLHLVKRR]
ADP + [peptide HMRSAMSGLHLVKRR] phosphate
-
i.e. SAMS peptide
-
-
?
ATP + [peptide HMRSAMSGLHLVKRR]
ADP + [peptide HMRSAMSGLHLVKRR] phosphate
i.e. SAMS peptide
-
-
?
ATP + [smooth muscle myosin light chain kinase]
ADP + [smooth muscle myosin light chain kinase] phosphate
-
phosphorylation activates MLCK and increases its affinity for Ca2+ and calmodulin
-
-
?
ATP + [smooth muscle myosin light chain kinase]
ADP + [smooth muscle myosin light chain kinase] phosphate
-
phosphorylation in the CaM-binding domain at Ser815, substrate from chicken, determination of the phosphorylation site by mass spectrometric analysis
-
-
?
ATP + [sn-glycerol-3-phosphate acyltransferase]
ADP + [sn-glycerol-3-phosphate acyltransferase]phosphate
-
-
-
-
?
ATP + [sn-glycerol-3-phosphate acyltransferase]
ADP + [sn-glycerol-3-phosphate acyltransferase]phosphate
-
-
-
-
?
GTP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
GDP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
-
?
GTP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
GDP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
phosphorylation at about 30% the rate of ATP
-
-
?
ITP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
IDP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
-
?
ITP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
IDP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
phosphorylation at about 10% the rate of ATP
-
-
?
UTP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
UDP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
-
?
UTP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
UDP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
phosphorylation at about 5% the rate of ATP
-
-
?
additional information
?
-
-
AMPK can influence the behavior of Caenorhabditis elegans worms in addition to its well known function in metabolic control, aak-1 and aak-2 affect paraquat sensitivity of adult worms, overview
-
-
?
additional information
?
-
-
AMPK promotes ATP production and inhibits ATp consumption acting as a metabolic switch, mechanism, overview. AMPK is activated by phosphorylation through upstream kinases and 5'-AMP in response to various nutritional and stress signals, AMPK signaling pathways, overview
-
-
?
additional information
?
-
-
enzyme functions as a metabolic sensor that monitors cellular AMP and ATP levels
-
-
?
additional information
?
-
-
conditions that elevate the AMP:ATP ratio in cells, such as growth factor depletion, hypoglycemia, ischemia in heart muscle, exercise in skeletal muscle, as well as treatment with arsenite, azide, oxidative agents and the pharmacological agent AICAR, which mimics the effect of AMP can cause activation of AMPK
-
-
?
additional information
?
-
-
phosphorylates key target proteins that control flux through metabolic pathways of hepatic ketogenesis, cholesterol synthesis, adipocyte lipolysis and skeletal muscle fatty acid oxidation
-
-
?
additional information
?
-
-
AMP-activated protein kinase acts as a key energy sensor in regulating intracellular lysosomal protein degradation and is involved in proteasomal degradation of proteins, which allows the regulation of proteasomal activity under conditions of energy demand, mechanism, overview
-
-
?
additional information
?
-
-
AMP-activated protein kinase acts as a master regulator of cellular metabolism in skeletal muscle, biochemical regulation of AMPK by AMP, protein phosphatases, and its three known upstream kinases, LKB1, Ca2+/calmodulin-dependent protein kinase kinase, CaMKK, and transforming growth factor-beta activated kinase 1, TAK1. Physiological regulation of cellular metabolism in skeletal muscle, concerning glucose metabolism, glycogen synthesis, protein metabolism and degradation, lipid metabolism and lipolysis, detailed overview
-
-
?
additional information
?
-
-
AMP-activated protein kinase contributes to UV- and H2O2-induced apoptosis in human skin keratinocytes, AMPK serves as a negative feedback signal against UV-induced mammalian target of rapamycin, mTOR activation in a TSC2-dependent manner, AMPK plays important roles in UV-induced signal transduction ultimately leading to skin photoaging and even skin cancer, regulation, overview
-
-
?
additional information
?
-
-
AMP-activated protein kinase is involved in 8-chloro-cAMP-induced growth inhibition which proceeds via p38 MAPK and the metabolite 8-chloro-adenosine, AICAR must be phosphorylated to ZMP by adenosine kinases in order to activate AMPK, mechanism, overview
-
-
?
additional information
?
-
-
AMP-activated protein kinase is involved in regulation of the activation of the PGC-1alpha promoter and PGC-1alpha expression in skeletal muscle cells, effect of AMPK activation on DNA binding and protein expression, overview
-
-
?
additional information
?
-
-
AMP-activated protein kinase mediates glucocorticoid-induced metabolic changes representing a mechanism in Cushings syndrome, overview. activation of AMPK stimulates appetite in the hypothalamus and stimulates catabolic processes in the periphery
-
-
?
additional information
?
-
-
AMPK is a sensor of the cellular energy status, it also exerts modulation of the fibrogenic properties of hepatic stellate cells, physiological effects of AMPK activation and inhibition, mechanism, AMPK activation regulates intracellular signaling pathways in hepatic stellate cells, overview
-
-
?
additional information
?
-
-
AMPK is activated in response to changes in the cellular energy charge and cellular stress via increases in the ATP-to-AMP ratio
-
-
?
additional information
?
-
-
AMPK regulates the energy balance both at the cellular and whole body level, disorders of it are obesity, type 2 diabetes and the metabolic syndrome, overview. Activating mutations in AMPK can cause heart disease. AMPK is regulated by the AMP/ATP ratio and upstream kinases, e.g. CaMKKbeta and LBK1, overview. AMPK activation inhibits activation of the mammalian target-of-rapamycin pathway by the insulin/insulin-like growth factor-1 pathway, probably via phosphorylation of TSC2, an upstream regulator of mTOR
-
-
?
additional information
?
-
-
AMPK signaling influences glucose and lipid metabolisms, mitochondrial biogenesis, and gene transcription, playing a role in trained and obese physiological state, overview. AMPK is important in the molecular regulation of lipid oxidation in skeletal muscle and the energy balance through suppression of ATP-consuming anabolic pathways and enhancement of ATP-producing catabolic pathways, overview
-
-
?
additional information
?
-
-
lovostatin-induced endothelial progenitor cell to endothelial cell differentiation depends on AMPK, AMPK enhances the vasculogensis and angiogenesis of endothelial progenitor cells, overview
-
-
?
additional information
?
-
-
AMPK phosphorylates histone deacetylase 5 (HDAC5) at Ser259 and Ser498 in primary myocytes
-
-
?
additional information
?
-
-
AMPK phosphorylates site 2 on glycogen synthase in cell-free assays
-
-
?
additional information
?
-
identification of putative AMPK targets in hemoglobin-depleted lysates of erythrocytes, including metabolic enzymes, cytoskeletal proteins and enzymes involved in the oxidative stress response, cloning and recombinant expression
-
-
?
additional information
?
-
-
mechanism of lipolytic enzyme activity modulation, regulation, overview
-
-
?
additional information
?
-
-
AMP-activated protein kinase acts as an energy sensor able to adapt cellular metabolism in response to nutritional environmental variations, and it regulates lymphocyte responses to metabolic stress but is largely dispensable for immune cell development and function, overview
-
-
?
additional information
?
-
-
AMPK and calcineurin, a calcium-regulated serine/threonine protein phosphatase, regulate skeletal muscle metabolic gene expression programs in response to changes in the energy status and levels of neuronic input, respectively. AMPK activates metabolic genes, mitochondrial biogenesis, glucose uptake, lipid oxidation, and insulin sesitivity, but blocks protein synthesis, pathway and regulation, overview
-
-
?
additional information
?
-
-
AMPK is a regulator of gene transcription increasing mitochondrial proteins of oxidative metabolsim as well as hexokinase expression in muscles
-
-
?
additional information
?
-
-
AMPK is an important energy-sensing protein in skeletal muscle, it inhibits mTOR signaling thereby inhibiting protein synthesis initiation via S6K1 and 4E-BP1, regulation system, overview
-
-
?
additional information
?
-
-
AMPK regulates the energy balance both at the cellular and whole body level, disorders of it are obesity, type 2 diabetes and the metabolic syndrome, overview. Activating mutations in AMPK can cause heart disease. AMPK is regulated by the AMP/ATP ratio and upstream kinases, e.g. CaMKKbeta and LBK1, overview. AMPK activation inhibits activation of the mammalian target-of-rapamycin pathway by the insulin/insulin-like growth factor-1 pathway, probably via phosphorylation of TSC2, an upstream regulator of mTOR
-
-
?
additional information
?
-
-
AMP-activated protein kinase phosphorylates transcription factors of the CREB family
-
-
?
additional information
?
-
-
AMPK signalling pathways are downregulated and skeletal muscle development is impaired in fetuses of obese, over-nourished sheep without differences in energy status, i.e. the AMP/ATP ratio, overview. Decreased signalling of the AMPK system in skeletal muscle of fetuses of OB mothers may play a role in altered muscle development and development of insulin resistance in the offspring
-
-
?
additional information
?
-
-
autophosphorylation in absence of substrate
-
-
?
additional information
?
-
-
autophosphorylation in absence of substrate
-
-
?
additional information
?
-
-
protein kinase C and Ca2+/calmodulin dependent reductase kinases are no substrates
-
-
?
additional information
?
-
-
incorporates 0.5 mol phosphate/mol MW 53000 enzyme substrate fragment, 2 mol phosphate/mol native enzyme substrate
-
-
?
additional information
?
-
-
acetyl-CoA carboxylase kinase EC 2.7.1.128 and hydroxymethylglutaryl-CoA reductase kinase activity are catalyzed by the same enzyme
-
-
?
additional information
?
-
-
regulates triacylglycerolsynthesis and fatty acid oxidation in liver and muscle reciprocally
-
-
?
additional information
?
-
-
AMPK regulation, AMPK mediates the autophagy suppression of okadaic acid and other protein phosphatase-inhibitory toxins, overview
-
-
?
additional information
?
-
-
mechanism of lipolytic enzyme activity modulation, regulation, overview
-
-
?
additional information
?
-
-
the enzyme is regulated by the nucleoside diphosphate kinase, complex formation in vivo, e.g. between isozyme alpha1 and NDPK-H1, inhibits the enzyme, overview
-
-
?
additional information
?
-
-
activation of AMPK leads to activation of PKC-zeta and promotes Na,K-ATPase endocytosis. AMPK mediates CO2-induced Na,K-ATPase endocytosis and alveolar epithelial dysfunction, which can be prevented with beta-adrenergic agonists and cAMP
-
-
?
additional information
?
-
-
AMP-activated protein kinase acts as a master regulator of cellular metabolism in skeletal muscle, biochemical regulation of AMPK by AMP, protein phosphatases, and its three known upstream kinases, LKB1, Ca2+/calmodulin-dependent protein kinase kinase, CaMKK, and transforming growth factor-beta activated kinase 1, TAK1. Physiological regulation of cellular metabolism in skeletal muscle, concerning glucose metabolism, glycogen synthesis, protein metabolism and degradation, lipid metabolism and lipolysis, detailed overview
-
-
?
additional information
?
-
-
AMP-activated protein kinase is essential for survival in chronic hypoxia
-
-
?
additional information
?
-
-
AMPK inhibits hepatioc lipogenesis through multisite control, involving inhibition of glucose hexokinase translocation with consequent inhibition of flux through glucose phosphorylation and glycolysis, overview
-
-
?
additional information
?
-
-
AMPK is a cellular energy sensor that is activated during mitochondrial inhibition and shuts down biosynthetic processes to help conserve cellular ATP levels
-
-
?
additional information
?
-
-
AMPK plays a central role in the regulation of lipid metabolism, AMPK activity may have an important role in the development of alcoholic fatty liver, AMPK activator AICAR strongly inhibits the activity of acetyl-CoA carboxylase in hepatocyte preparations in parallel to fatty acid synthesis, but cells from ethanol-fed rats show significantly lower sensitivity to inhibition by AICAR, overview
-
-
?
additional information
?
-
-
AMPK regulates the energy balance both at the cellular and whole body level, disorders of it are obesity, type 2 diabetes and the metabolic syndrome, overview. Activating mutations in AMPK can cause heart disease. AMPK is regulated by the AMP/ATP ratio and upstream kinases, e.g. CaMKKbeta and LBK1, overview. AMPK activation inhibits activation of the mammalian target-of-rapamycin pathway by the insulin/insulin-like growth factor-1 pathway, probably via phosphorylation of TSC2, an upstream regulator of mTOR
-
-
?
additional information
?
-
-
anti-obesity effects of Juniperus chinensis extract are associated with increased AMP-activated protein kinase expression and phosphorylation in the visceral adipose tissue, overview
-
-
?
additional information
?
-
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
-
-
?
additional information
?
-
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
-
-
?
additional information
?
-
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
-
-
?
additional information
?
-
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
-
-
?
additional information
?
-
-
hypoxic pulmonary vasoconstriction is precipitated, at least in part, by the inhibition of mitochondrial oxidative phosphorylation by hypoxia, an increase in the AMP/ATP ratio and consequent activation of AMP-activated protein kinase, mechanism, overview
-
-
?
additional information
?
-
-
key role for AMP-activated protein kinase in the ventromedial hypothalamus in regulating counterregulatory hormone responses to acute hypoglycemia
-
-
?
additional information
?
-
-
neuronal AMPK responds to cellular energy requirements as well as whole body energy demands, mechanism, in patholgical brain AMPK responds globally in the brain to energy challenge, while in healthy brain only to changes in energy balance/food/intake, increased AMPK activity leads to inhibition of energy-using processes and, during ischemia, can lead to complete energy failure and death by stroke, overview. AMPK mediates the physiological effects of C75, an alpha-methylene-gamma-butyrolactone beta-ketoacyl synthase inhibitor, brain injection of C75 increases ATP levels in neurons, glucose oxidation FAS activity, CPT-1 activity, food intake and body weight in rodents, detailed overview
-
-
?
additional information
?
-
-
the thrifty metabolism that favors fat storage after caloric restriction involves AMPK activity, AMPK signaling is diminished during refeeding after caloric restriction rats. Isocaloric refeeding with a high-fat diet, which exacerbates the suppression of thermogenesis, results in further reduction and in impaired AMPK phosphorylation, overview
-
-
?
additional information
?
-
-
AMPK promotes reactivation of mitochondrial aconitase
-
-
?
additional information
?
-
-
autophosphorylation in absence of substrate
-
-
?
additional information
?
-
-
autophosphorylation in absence of substrate
-
-
?
additional information
?
-
-
incorporates 0.5 mol phosphate/mol MW 53000 enzyme substrate fragment, 2 mol phosphate/mol native enzyme substrate
-
-
?
additional information
?
-
-
regulates triacylglycerolsynthesis and fatty acid oxidation in liver and muscle reciprocally
-
-
?
additional information
?
-
-
acetyl-CoA carboxylase kinase EC 2.7.1.128 and hydroxymethylglutaryl-CoA reductase kinase activity are catalyzed by the same enzyme
-
-
?
additional information
?
-
-
AMP-activated protein kinase acts as a regulator in cellular metabolism, biochemical regulation of AMPK by AMP, protein phosphatases, and upstream kinases, e.g. LKB1, overview
-
-
?
additional information
?
-
alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2
-
-
?
additional information
?
-
alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2
-
-
?
additional information
?
-
alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2
-
-
?
additional information
?
-
-
alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2
-
-
?
additional information
?
-
alkaline stress results in the increased phosphorylation of Mig2 but decreased phosphorylation of Mig1. Alkaline stress also causes a reduced abundance of Mig1 but no change in the abundance of Mig2. In contrast, glucose stress causes an increased phosphorylation of both proteins and the opposite effect on the abundance of these proteins. Glucose stress leads to increased Mig1 abundance and decreased Mig2 abundance
-
-
?
additional information
?
-
alkaline stress results in the increased phosphorylation of Mig2 but decreased phosphorylation of Mig1. Alkaline stress also causes a reduced abundance of Mig1 but no change in the abundance of Mig2. In contrast, glucose stress causes an increased phosphorylation of both proteins and the opposite effect on the abundance of these proteins. Glucose stress leads to increased Mig1 abundance and decreased Mig2 abundance
-
-
?
additional information
?
-
alkaline stress results in the increased phosphorylation of Mig2 but decreased phosphorylation of Mig1. Alkaline stress also causes a reduced abundance of Mig1 but no change in the abundance of Mig2. In contrast, glucose stress causes an increased phosphorylation of both proteins and the opposite effect on the abundance of these proteins. Glucose stress leads to increased Mig1 abundance and decreased Mig2 abundance
-
-
?
additional information
?
-
-
alkaline stress results in the increased phosphorylation of Mig2 but decreased phosphorylation of Mig1. Alkaline stress also causes a reduced abundance of Mig1 but no change in the abundance of Mig2. In contrast, glucose stress causes an increased phosphorylation of both proteins and the opposite effect on the abundance of these proteins. Glucose stress leads to increased Mig1 abundance and decreased Mig2 abundance
-
-
?
additional information
?
-
alkaline stress results in the increased phosphorylation of Mig2 but decreased phosphorylation of Mig1. Alkaline stress also causes a reduced abundance of Mig1 but no change in the abundance of Mig2. In contrast, glucose stress causes an increased phosphorylation of both proteins and the opposite effect on the abundance of these proteins. Glucose stress leads to increased Mig1 abundance and decreased Mig2 abundance
-
-
?
additional information
?
-
alkaline stress results in the increased phosphorylation of Mig2 but decreased phosphorylation of Mig1. Alkaline stress also causes a reduced abundance of Mig1 but no change in the abundance of Mig2. In contrast, glucose stress causes an increased phosphorylation of both proteins and the opposite effect on the abundance of these proteins. Glucose stress leads to increased Mig1 abundance and decreased Mig2 abundance
-
-
?
additional information
?
-
alkaline stress results in the increased phosphorylation of Mig2 but decreased phosphorylation of Mig1. Alkaline stress also causes a reduced abundance of Mig1 but no change in the abundance of Mig2. In contrast, glucose stress causes an increased phosphorylation of both proteins and the opposite effect on the abundance of these proteins. Glucose stress leads to increased Mig1 abundance and decreased Mig2 abundance
-
-
?
additional information
?
-
alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2
-
-
?
additional information
?
-
alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2
-
-
?
additional information
?
-
alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2
-
-
?
additional information
?
-
-
Snf4 subunit contains cystathionine-beta-synthase (CBS) sequence repeats. CBS4 can be occupied either by AMP, ZMP or ATP, and CBS2 by ADP
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + acetyl-CoA carboxylase 1
ADP + phosphorylated acetyl-CoA carboxylase 1
-
-
-
-
?
ATP + ATF1
ADP + phospho-ATF1
-
important reaction in enhancement of transcriptional activity
-
-
?
ATP + CREB
ADP + phospho-CREB
-
important reaction in enhancement of transcriptional activity
-
-
?
ATP + CREB1
ADP + phospho-CREB1
-
AMPK competes with protein kinase A for the Ser119 phosphorylation site
-
-
?
ATP + CREM
ADP + phospho-CREM
-
important reaction in enhancement of transcriptional activity
-
-
?
ATP + eukaryotic elongation factor 2 kinase
ADP + phosphorylated eukaryotic elongation factor 2 kinase
-
phosphorylation at Ser398, the enzyme plays a regulatory role in eEF2 kinase activity, overview
-
-
?
ATP + JAK1
ADP + phosphorylated JAK1
-
phosphorylation at Ser515 and Ser518
-
-
?
ATP + p27
ADP + phospho-p27
-
loss of tuberin is associated with increased AMPK activity and altered p27 function leading to increased Cdk2 activity and resistance of the cells against apoptosis. Mislocation of p27 occurs in tuberin-deficient cells, possessing no functional gene tsc2, and can induced directly by activating AMPK physiologically via glucose deprivation or genetically via a constitutively active AMPK, overview
-
-
?
ATP + p38
ADP + phospho-p38
-
phosphorylation at Thr180/Thr182, p38 MAPK is a downstream signal of AMPK upon various stimuli, AMPK serves as a positive regulator for p38 Ser15 phosphorylation induced by UV radiation and H2O2 treatment
-
-
?
ATP + p53
ADP + phospho-p53
-
AMPK serves as a positive regulator for p38 Ser15 phosphorylation induced by UV radiation and H2O2 treatment
-
-
?
ATP + PFK2
ADP + phospho-PFK2
-
phosphorylation at Ser466 induced by UV radiation and H2O2 treatment
-
-
?
ATP + recombinant human Kv1.5 channel
ADP + phosphorylated recombinant human Kv1.5 channel
-
-
-
-
?
ATP + ubiquitin ligase Nedd4-2
ADP + phosphorylated ubiquitin ligase Nedd4-2
Q13131; Q9Y478; P54619
activation
-
-
?
ATP + [acetyl-CoA carboxylase 2]
ADP + [acetyl-CoA carboxylase 2] phosphate
-
phosphorylation at Ser79
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + phospho-[acetyl-CoA carboxylase]
-
phosphorylation at Ser79
-
-
?
ATP + [endothelial nitic oxide synthase]
ADP + [endothelial nitic oxide synthase] phosphate
-
activates nitric oxide synthesis, mechanism, overview
-
-
?
ATP + [endothelial nitric oxide synthase]
ADP + [endothelial nitric oxide synthase] phosphate
ATP + [glucose hexokinase regulatory protein]
ADP + [glucose hexokinase regulatory protein] phosphate
-
-
-
-
?
ATP + [Golgi-specific brefeldin A resistance factor 1]
ADP + [Golgi-specific brefeldin A resistance factor 1] phosphate
-
phosphorylation at Thr1337 to induce disassembly of Golgi apparatus
-
-
?
ATP + [histone deacetylase 5]
ADP + [histone deacetylase 5] phosphate
-
AMP-activated protein kinase regulates GLUT4 transcription by phosphorylating histone deacetylase 5
-
-
?
ATP + [HMG-CoA reductase]
ADP + [HMG-CoA reductase] phosphate
-
inhibition of HMG-CoA carboxylase
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
ATP + [O-GlcNAc transferase]
ADP + [O-GlcNAc transferase] phosphate
-
AMP-activated protein kinase activates O-glucosaminyl-acylation of neuronal proteins, e.g. neurofilament H, during glucose deprivation involving activation of O-GlcNAc transferase, OGT, and induces OGT protein expression in Neuro-2a neuroblastoma cells, mechanism, overview
-
-
?
ATP + [smooth muscle myosin light chain kinase]
ADP + [smooth muscle myosin light chain kinase] phosphate
-
phosphorylation activates MLCK and increases its affinity for Ca2+ and calmodulin
-
-
?
ATP + acetyl-CoA carboxylase
ADP + phosphorylated acetyl-CoA carboxylase
-
-
-
-
?
ATP + acetyl-CoA carboxylase
ADP + phosphorylated acetyl-CoA carboxylase
-
the enzyme is involved in the regulation of hepatic lipids via its downstream effector acetyl-CoA carboxylase, enzyme inhibition leads to an increased level of triacylglycerols and accumulation of lipids, metformin decreases lipid accumulation, induced by high D-glucose levels, by activating the enzyme, the enzyme functions as energy intracellular sensor
-
-
?
ATP + hormone-sensitive lipase
ADP + phosphorylated hormone-sensitive lipase
-
HSL is a key enzyme in controlling lipolysis in adipocytes, phosphorylation at Ser565 by AMPK reduces its translocation toward lipid droplets
-
-
?
ATP + hormone-sensitive lipase
ADP + phosphorylated hormone-sensitive lipase
-
HSL is a key enzyme in controlling lipolysis in adipocytes, phosphorylation at Ser565 by AMPK reduces its translocation toward lipid droplets
-
-
?
ATP + Mig1 protein
ADP + phosphorylated Mig1 protein
-
-
-
?
ATP + Mig1 protein
ADP + phosphorylated Mig1 protein
-
-
-
?
ATP + Mig2 protein
ADP + phosphorylated Mig2 protein
alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2
-
-
?
ATP + Mig2 protein
ADP + phosphorylated Mig2 protein
alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
inhibition of acetyl-CoA carboxylase
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
-
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
phosphorylation at Ser79
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
phosphorylation at Ser79
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
phosphorylation at Ser79
-
-
?
ATP + [acetyl-CoA carboxylase]
ADP + [acetyl-CoA carboxylase] phosphate
-
copper deficiency results in AMP-activated protein kinase activation and acetyl-CoA carboxylase phosphorylation in rat cerebellum, overview
-
-
?
ATP + [endothelial nitric oxide synthase]
ADP + [endothelial nitric oxide synthase] phosphate
-
AMPK-eNOS signalling, overview
-
-
?
ATP + [endothelial nitric oxide synthase]
ADP + [endothelial nitric oxide synthase] phosphate
-
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
-
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
activated AMPK acts to down-regulate ATP-consuming pathways such as fatty acid synthesis by phosphorylating and inactivating acetyl-CoA carboxylase and protein synthesis by promoting the phosphorylation of eukaryotic elongation factor-2, in heart AMPK activation stimulates glycolysis by increasing glucose uptake
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
bicyclic phosphorylation system, enzyme is believed to be involved in protecting cells against ATP depletion due to environmental stress by inactivating several key biosynthetic enzymes
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate
-
inactivates EC 1.1.1.34 by phosphorylation
-
?
additional information
?
-
-
AMPK can influence the behavior of Caenorhabditis elegans worms in addition to its well known function in metabolic control, aak-1 and aak-2 affect paraquat sensitivity of adult worms, overview
-
-
?
additional information
?
-
-
AMPK promotes ATP production and inhibits ATp consumption acting as a metabolic switch, mechanism, overview. AMPK is activated by phosphorylation through upstream kinases and 5'-AMP in response to various nutritional and stress signals, AMPK signaling pathways, overview
-
-
?
additional information
?
-
-
AMP-activated protein kinase acts as a key energy sensor in regulating intracellular lysosomal protein degradation and is involved in proteasomal degradation of proteins, which allows the regulation of proteasomal activity under conditions of energy demand, mechanism, overview
-
-
?
additional information
?
-
-
AMP-activated protein kinase acts as a master regulator of cellular metabolism in skeletal muscle, biochemical regulation of AMPK by AMP, protein phosphatases, and its three known upstream kinases, LKB1, Ca2+/calmodulin-dependent protein kinase kinase, CaMKK, and transforming growth factor-beta activated kinase 1, TAK1. Physiological regulation of cellular metabolism in skeletal muscle, concerning glucose metabolism, glycogen synthesis, protein metabolism and degradation, lipid metabolism and lipolysis, detailed overview
-
-
?
additional information
?
-
-
AMP-activated protein kinase contributes to UV- and H2O2-induced apoptosis in human skin keratinocytes, AMPK serves as a negative feedback signal against UV-induced mammalian target of rapamycin, mTOR activation in a TSC2-dependent manner, AMPK plays important roles in UV-induced signal transduction ultimately leading to skin photoaging and even skin cancer, regulation, overview
-
-
?
additional information
?
-
-
AMP-activated protein kinase is involved in 8-chloro-cAMP-induced growth inhibition which proceeds via p38 MAPK and the metabolite 8-chloro-adenosine, AICAR must be phosphorylated to ZMP by adenosine kinases in order to activate AMPK, mechanism, overview
-
-
?
additional information
?
-
-
AMP-activated protein kinase is involved in regulation of the activation of the PGC-1alpha promoter and PGC-1alpha expression in skeletal muscle cells, effect of AMPK activation on DNA binding and protein expression, overview
-
-
?
additional information
?
-
-
AMP-activated protein kinase mediates glucocorticoid-induced metabolic changes representing a mechanism in Cushings syndrome, overview. activation of AMPK stimulates appetite in the hypothalamus and stimulates catabolic processes in the periphery
-
-
?
additional information
?
-
-
AMPK is a sensor of the cellular energy status, it also exerts modulation of the fibrogenic properties of hepatic stellate cells, physiological effects of AMPK activation and inhibition, mechanism, AMPK activation regulates intracellular signaling pathways in hepatic stellate cells, overview
-
-
?
additional information
?
-
-
AMPK is activated in response to changes in the cellular energy charge and cellular stress via increases in the ATP-to-AMP ratio
-
-
?
additional information
?
-
-
AMPK regulates the energy balance both at the cellular and whole body level, disorders of it are obesity, type 2 diabetes and the metabolic syndrome, overview. Activating mutations in AMPK can cause heart disease. AMPK is regulated by the AMP/ATP ratio and upstream kinases, e.g. CaMKKbeta and LBK1, overview. AMPK activation inhibits activation of the mammalian target-of-rapamycin pathway by the insulin/insulin-like growth factor-1 pathway, probably via phosphorylation of TSC2, an upstream regulator of mTOR
-
-
?
additional information
?
-
-
AMPK signaling influences glucose and lipid metabolisms, mitochondrial biogenesis, and gene transcription, playing a role in trained and obese physiological state, overview. AMPK is important in the molecular regulation of lipid oxidation in skeletal muscle and the energy balance through suppression of ATP-consuming anabolic pathways and enhancement of ATP-producing catabolic pathways, overview
-
-
?
additional information
?
-
-
lovostatin-induced endothelial progenitor cell to endothelial cell differentiation depends on AMPK, AMPK enhances the vasculogensis and angiogenesis of endothelial progenitor cells, overview
-
-
?
additional information
?
-
-
mechanism of lipolytic enzyme activity modulation, regulation, overview
-
-
?
additional information
?
-
-
AMP-activated protein kinase acts as an energy sensor able to adapt cellular metabolism in response to nutritional environmental variations, and it regulates lymphocyte responses to metabolic stress but is largely dispensable for immune cell development and function, overview
-
-
?
additional information
?
-
-
AMPK and calcineurin, a calcium-regulated serine/threonine protein phosphatase, regulate skeletal muscle metabolic gene expression programs in response to changes in the energy status and levels of neuronic input, respectively. AMPK activates metabolic genes, mitochondrial biogenesis, glucose uptake, lipid oxidation, and insulin sesitivity, but blocks protein synthesis, pathway and regulation, overview
-
-
?
additional information
?
-
-
AMPK is a regulator of gene transcription increasing mitochondrial proteins of oxidative metabolsim as well as hexokinase expression in muscles
-
-
?
additional information
?
-
-
AMPK is an important energy-sensing protein in skeletal muscle, it inhibits mTOR signaling thereby inhibiting protein synthesis initiation via S6K1 and 4E-BP1, regulation system, overview
-
-
?
additional information
?
-
-
AMPK regulates the energy balance both at the cellular and whole body level, disorders of it are obesity, type 2 diabetes and the metabolic syndrome, overview. Activating mutations in AMPK can cause heart disease. AMPK is regulated by the AMP/ATP ratio and upstream kinases, e.g. CaMKKbeta and LBK1, overview. AMPK activation inhibits activation of the mammalian target-of-rapamycin pathway by the insulin/insulin-like growth factor-1 pathway, probably via phosphorylation of TSC2, an upstream regulator of mTOR
-
-
?
additional information
?
-
-
AMPK signalling pathways are downregulated and skeletal muscle development is impaired in fetuses of obese, over-nourished sheep without differences in energy status, i.e. the AMP/ATP ratio, overview. Decreased signalling of the AMPK system in skeletal muscle of fetuses of OB mothers may play a role in altered muscle development and development of insulin resistance in the offspring
-
-
?
additional information
?
-
-
AMPK regulation, AMPK mediates the autophagy suppression of okadaic acid and other protein phosphatase-inhibitory toxins, overview
-
-
?
additional information
?
-
-
mechanism of lipolytic enzyme activity modulation, regulation, overview
-
-
?
additional information
?
-
-
activation of AMPK leads to activation of PKC-zeta and promotes Na,K-ATPase endocytosis. AMPK mediates CO2-induced Na,K-ATPase endocytosis and alveolar epithelial dysfunction, which can be prevented with beta-adrenergic agonists and cAMP
-
-
?
additional information
?
-
-
AMP-activated protein kinase acts as a master regulator of cellular metabolism in skeletal muscle, biochemical regulation of AMPK by AMP, protein phosphatases, and its three known upstream kinases, LKB1, Ca2+/calmodulin-dependent protein kinase kinase, CaMKK, and transforming growth factor-beta activated kinase 1, TAK1. Physiological regulation of cellular metabolism in skeletal muscle, concerning glucose metabolism, glycogen synthesis, protein metabolism and degradation, lipid metabolism and lipolysis, detailed overview
-
-
?
additional information
?
-
-
AMP-activated protein kinase is essential for survival in chronic hypoxia
-
-
?
additional information
?
-
-
AMPK inhibits hepatioc lipogenesis through multisite control, involving inhibition of glucose hexokinase translocation with consequent inhibition of flux through glucose phosphorylation and glycolysis, overview
-
-
?
additional information
?
-
-
AMPK is a cellular energy sensor that is activated during mitochondrial inhibition and shuts down biosynthetic processes to help conserve cellular ATP levels
-
-
?
additional information
?
-
-
AMPK plays a central role in the regulation of lipid metabolism, AMPK activity may have an important role in the development of alcoholic fatty liver, AMPK activator AICAR strongly inhibits the activity of acetyl-CoA carboxylase in hepatocyte preparations in parallel to fatty acid synthesis, but cells from ethanol-fed rats show significantly lower sensitivity to inhibition by AICAR, overview
-
-
?
additional information
?
-
-
AMPK regulates the energy balance both at the cellular and whole body level, disorders of it are obesity, type 2 diabetes and the metabolic syndrome, overview. Activating mutations in AMPK can cause heart disease. AMPK is regulated by the AMP/ATP ratio and upstream kinases, e.g. CaMKKbeta and LBK1, overview. AMPK activation inhibits activation of the mammalian target-of-rapamycin pathway by the insulin/insulin-like growth factor-1 pathway, probably via phosphorylation of TSC2, an upstream regulator of mTOR
-
-
?
additional information
?
-
-
anti-obesity effects of Juniperus chinensis extract are associated with increased AMP-activated protein kinase expression and phosphorylation in the visceral adipose tissue, overview
-
-
?
additional information
?
-
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
-
-
?
additional information
?
-
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
-
-
?
additional information
?
-
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
-
-
?
additional information
?
-
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
-
-
?
additional information
?
-
-
hypoxic pulmonary vasoconstriction is precipitated, at least in part, by the inhibition of mitochondrial oxidative phosphorylation by hypoxia, an increase in the AMP/ATP ratio and consequent activation of AMP-activated protein kinase, mechanism, overview
-
-
?
additional information
?
-
-
key role for AMP-activated protein kinase in the ventromedial hypothalamus in regulating counterregulatory hormone responses to acute hypoglycemia
-
-
?
additional information
?
-
-
neuronal AMPK responds to cellular energy requirements as well as whole body energy demands, mechanism, in patholgical brain AMPK responds globally in the brain to energy challenge, while in healthy brain only to changes in energy balance/food/intake, increased AMPK activity leads to inhibition of energy-using processes and, during ischemia, can lead to complete energy failure and death by stroke, overview. AMPK mediates the physiological effects of C75, an alpha-methylene-gamma-butyrolactone beta-ketoacyl synthase inhibitor, brain injection of C75 increases ATP levels in neurons, glucose oxidation FAS activity, CPT-1 activity, food intake and body weight in rodents, detailed overview
-
-
?
additional information
?
-
-
the thrifty metabolism that favors fat storage after caloric restriction involves AMPK activity, AMPK signaling is diminished during refeeding after caloric restriction rats. Isocaloric refeeding with a high-fat diet, which exacerbates the suppression of thermogenesis, results in further reduction and in impaired AMPK phosphorylation, overview
-
-
?
additional information
?
-
-
AMP-activated protein kinase acts as a regulator in cellular metabolism, biochemical regulation of AMPK by AMP, protein phosphatases, and upstream kinases, e.g. LKB1, overview
-
-
?
additional information
?
-
alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2
-
-
?
additional information
?
-
alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2
-
-
?
additional information
?
-
alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2
-
-
?
additional information
?
-
-
alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2
-
-
?
additional information
?
-
alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2
-
-
?
additional information
?
-
alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2
-
-
?
additional information
?
-
alkaline stress leads to the activation of all three isoforms yet only the Gal83 isoform translocates to the nucleus and phosphorylates Mig2
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Calmodulin
-
requirement, Ca2+/calmodulin dependent kinase, no phosphorylation of substrate observed in absence
AMP
-
dependent on, AMPK is activated by phosphorylation through upstream kinases and 5'-AMP in response to various nutritional and stress signals
ATP
-
-
662296, 663969, 665496, 690657, 690725, 691704, 692001, 692091, 692365, 693032, 693151, 693205, 693207, 693328, 694825, 701572
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
Ca2+
-
increases in intracellular Ca2+ levels activate AMPK is via the activation of CaMKKs, mechanism, overview
Ca2+
-
AMPK activation by phosphorylation through the Ca2+-calmodulin dependent protein kinase kinase, CaMKK
Ca2+
-
activation of AMPK is mediated by a CO2-triggered increase in intracellular Ca2+ concentration and Ca2+/calmodulin-dependent kinase kinase-beta, CaMKK-beta
Ca2+
-
increases in intracellular Ca2+ levels activate AMPK is via the activation of CaMKKs, mechanism, overview
Mg2+
-
-
Mg2+
-
Asp-157 within the DFG motif is required for binding the Mg2+ ion that co-ordinates beta and gamma phosphates of Mg2+-ATP in the active site
Mg2+
-
-
Mg2+
-
requirement, actual substrate: MgATP2-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(5Z)-2-[(3-hydroxyphenyl)amino]-5-(1H-indol-3-ylmethylidene)-1,3-thiazol-4(5H)-one
-
-
(Z)-2-(3-((4-((2-(diethylamino)ethyl)carbamoyl)-3,5-dimethyl-1H-pyrrol-2-yl)methylene)-2-oxoindolin-5-yl)ethyl acetate
-
-
(Z)-5-((5-(2-acetamidoethyl)-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
-
(Z)-5-((5-(2-azidoethyl)-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
-
(Z)-5-((5-(2-cyanoethyl)-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
-
(Z)-5-((5-(3-amino-3-oxopropyl)-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
potent and selective inhibitor; potent and selective inhibitor
(Z)-5-((5-cyano-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole3-carboxamide
-
-
(Z)-5-((5-fluoro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxylic acid
78% inhibition at 0.01 mM; 85% inhibition at 0.01 mM
(Z)-5-((5-fluoro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-N-propyl-1H-pyrrole-3-carboxamide
30% inhibition at 0.01 mM; 48% inhibition at 0.01 mM
(Z)-5-((6-bromo-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
-
(Z)-5-((6-chloro-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
-
(Z)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-5-((2-oxo-5-(ureidomethyl)indolin-3-ylidene)methyl)-1H-pyrrole-3-carboxamide
-
-
(Z)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-5-((2-oxoindolin-3-ylidene)methyl)-1H-pyrrole-3-carboxamide
-
(Z)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-5-((6-methyl-2-oxoindolin-3-ylidene)methyl)-1H-pyrrole-3-carboxamide
88% inhibition at 0.01 mM; 89% inhibition at 0.01 mM
(Z)-N-(2-(diethylamino)ethyl)-5-((5-(2-(dimethylamino)ethyl)-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
-
(Z)-N-(2-(diethylamino)ethyl)-5-((5-(2-hydroxyethyl)-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
potent and selective inhibitor; potent and selective inhibitor
(Z)-N-(2-(diethylamino)ethyl)-5-((5-(2-methoxyethyl)-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
-
-
(Z)-N-(2-(diethylamino)ethyl)-5-((5-fluoro-1-methyl-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
17% inhibition at 0.01 mM; 40% inhibition at 0.01 mM
(Z)-N-(2-(diethylamino)ethyl)-5-((6-ethyl-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
90% inhibition at 0.01 mM
(Z)-N-(2-(diethylamino)ethyl)-5-((6-fluoro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
-
(Z)-N-(2-(diethylamino)ethyl)-5-((6-isopropyl-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
69% inhibition at 0.01 mM; 70% inhibition at 0.01 mM
(Z)-N-(2-(dimethylamino)ethyl)-5-((5-floro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
-
(Z)-N-(2-(ethylamino)ethyl)-5-((5-fluoro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
-
(Z)-N-(2-aminoethyl)-5-((5-fluoro-2-oxoindolin-3-ylidene) methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
-
(Z)-N-(3-(diethylamino)propyl)-5-((5-fluoro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
-
(Z)-N-(3-(dimethylamino)propyl)-5-((5-fluoro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
-
A134974
-
at 1 nM ablates the stimulatory action of 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside with no effects on osteoclast formation in the absence of 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside
adenosine-5'-tetraphospho-5'-adenosine
-
i.e. AP4A, inhibits in the presence of AMP
C75
-
rapidly reduces the level of the phosphorylated AMPKalpha subunit in the hypothalamus. Also reduces pAMPK levels in fasted mice that have elevated hypothalamic pAMPK
Cu2+
-
copper deficiency results in AMP-activated protein kinase activation and acetyl-CoA carboxylase phosphorylation in rat cerebellum, overview
dexamethasone
-
decreases in AMPK activity in treated adipocytes. The inhibitory effect of dexamethasone on AMPK activity is antagonized by co-administration of metformin at 0.01 mM, which increases AMPK activity to 224% compared with dexamethasone treatment alone
hydroxymethylglutaryl-CoA
-
only with hydroxymethylglutaryl-CoA reductase as substrate
leptin
-
has a tissue-specific effect on AMPK, in the hypothalamus, it decreases hypothalamic AMPK activity
-
N-(2-[[2-(1H-indol-3-yl)ethyl]amino]-2-oxoethyl)-3-phenyl-2,1-benzoxazole-5-carboxamide
-
-
N-[2-(diethylamino)ethyl]-5-[(Z)-(6-fluoro-2-oxo-2,3-dihydro-1H-inden-1-ylidene)methyl]-2,4-dimethyl-1H-pyrrole-3-carboxamide
sunitinib, subunit AMPKalpha1 shows about 50% inhibition at 100 nM; sunitinib, subunit AMPKalpha2 shows 46% inhibition at 100 nM
nicotinamide
-
SIRT1 inhibitor, potentiates Tat-mediated reduction in AMPK activation and downstream acetyl-CoA carboxylase activation. Potentiates Tat-induced HIV-1 transactivation
propranolol
-
effects of interleukin-6 on both AMPK activity and energy state are inhibited by coincubation with propranolol, suggesting involvement of beta-adrenergic signaling
STO 609
molecular docking study, STO 609 docks in the compound-C binding pocket of AMPK
sucrose
-
sucrose-drinking animals have lower hypothalamic AMPK activity compared to saline-drinking control rats
sunitinib
subunit AMPKalpha1 shows about 50% inhibition at 100 nM; subunit AMPKalpha2 shows 46% inhibition at 100 nM
6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine
-
compound C, abolishes statin-induced reduction of O2- in BAEC
6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine
-
compound C, potent AMPK inhibitor, inhibition results in an increase in 1-methyl-4-pyridinium-induced cell death. Prevents the AMPK activation by 1-methyl-4-pyridinium and stimulates 1-methyl-4-pyridinium-induced cell death
6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine
-
compound C, AMPK-inhibitor, 0.02 mM does not significantly modify eryptosis under glucose-replete conditions but significantly augments the eryptotic effect of glucose withdrawal
6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine
-
compound C, inhibition of AMPK prevents at 0.05 mM, in part, the IFNgamma-induced decrease in transepithelial electrical resistance, the increased epithelial permeability, the decreased transepithelial electrical resistance, and the decrease in occludin and zonula occludens-1 caused by IFNgamma treatment of T84 cells
6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine
-
compound C, hypoxia-induced PKCzeta translocation to the plasma membrane and phosphorylation at Thr410 is prevented by pharmacological inhibition of AMPK
6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine
-
compound C, AMPK inhibitor, reduces puerarin-induced suppression of MDR1 expression
6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine
-
compound C, potentiates Tat-induced HIV-1 transactivation
6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine
-
compound C, at a concentration of 0.02 mM, suppresses the glucose-stimulated rise in cytoplasmic free Ca2+ concentration by 75%, and the cytoplasmic free Ca2+ concentration response to BLX-1002 is also significantly suppressed
6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine
-
inhibits AMPK in a dose dependent manner. Suppresses AMPK activity during the early phase of adipogenic differentiation, which indicates that suppressed activation of AMPK may inhibit the mitotic clonal expansion process of preadipocytes. Levels of phosphorylated AMPKalpha and total AMPKalpha are not affected by 6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine
6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine
-
compound C, inhibits AMPK, whereby restores acid secretion
6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine
-
compound C
compound C
-
i.e. dorsomorphin or 6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine
compound C
-
i.e. 6-[4-(2-piperidin-1-ylethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine, a cell-permeable pyrrazolopyrimidine compound that can act as a reversible and ATP competitive inhibitor of AMPK
compound C
-
i.e. AMPKi or 6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine, a specific inhibitor of AMPK, largely impairs the activation of p38 MAPK upon UV radiation
compound C
(6-[4-(2-piperidin-1-yl-ethoxy)-phenyl])-3-pyridin-4-yl-pyrazolo[1,5-a]pyrimidine, a selective inhibitor, inhibition of the AMP-activated protein kinase alpha2 subunit kinase domain. Compound C binding dramatically alters the conformation of the activation loop, which adopts an intermediate conformation between DFG-out and DFG-in. The induced fit forms a compound-C binding pocket composed of the N-lobe, the C-lobe and the hinge of the kinase domain. The pocket partially overlaps with the putative ATP-binding pocket. Binding structure analysis, overview
compound C
-
i.e. dorsomorphin or 6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine, a specific inhibitor of AMPK
compound C
-
i.e. dorsomorphin or 6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine
compound C
-
i.e. 6-[4-(2-piperidin-1-ylethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine, a cell-permeable pyrrazolopyrimidine compound that can act as a reversible and ATP competitive inhibitor of AMPK
compound C
-
i.e. dorsomorphin or 6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine, a specific inhibitor of AMPK
compound C
-
i.e. 6-[4-(2-piperidin-1-ylethoxy)phenyl]-3-pyridin-4-yl-pyrazolo[1,5-a]pyrimidine
glucocorticoid
-
treatment inhibits AMPK activity in rat adipose tissue and heart, while stimulating it in the liver and hypothalamus, similar to activity in vitro in the primary adipose and hypothalamic cells
-
glucocorticoid
-
treatment inhibits AMPK activity in rat adipose tissue and heart, while stimulating it in the liver and hypothalamus, similar to activity in vitro in the primary adipose and hypothalamic cells
-
metformin
-
can inhibit the stimulatory effect of dexamethasone in primary hypothalamic culture, blocks the AMPK phosphorylation induced by low glucose in primary cultures of hypothalamic neurones
additional information
-
genetic inhibition of LKB1 ablates statin-induced AMPK activation in endothelial cells
-
additional information
-
hypoxia decreases the expression level of AMPK beta1 isozyme by about 50%
-
additional information
-
insulin-resistance caused by high levels of D-glucose in the cell decreases the enzyme activity
-
additional information
-
activating phosphorylation of AMPK at Thr172 of the alpha-subunit, e.g. by CaMKKbeta or LBK1, inhibiting dephosphorylation by phosphatase PP2C
-
additional information
-
physiological effects of AMPK activation and inhibition, mechanism, overview
-
additional information
-
activation of p38 in response to UV or H2O2 is inhibited in AMPKalpha siRNA-treated HaCaT cells, EGFR inhibitor PD 153035 and AG 1478 inhibit UV-induced AMPK and LKB1 activation
-
additional information
-
when glycogen becomes depleted, the glycogen-bound pool of AMPK becomes inhibited due to binding to alpha1-6-linked branch points exposed by the action of phosphorylase and/or debranching enzyme
-
additional information
-
protein phosphatase 2A (PP2A) and protein phosphatase 2C (PP2C) inactivate the active and phosphorylated form of AMPK in cell-free assays. Dephosphorylation of AMPK by PP2Calpha is inhibited by 5'-AMP
-
additional information
-
SOCS3, an inhibitor of leptin-STAT3 signalling, inhibits leptin activation of AMPK in primary myotubes
-
additional information
-
overexpression of reactive oxygen species scavenger catalase prevents hypoxia-induced AMPK activation
-
additional information
-
a significant reduction in AMPK activation and downstream acetyl-CoA carboxylase activation in response to viral Tat protein treatment. Knockdown of SIRT1 by siRNA potentiates Tat-mediated reduction in AMPK activation and downstream acetyl-CoA carboxylase activation. Knockdown of AMPK by siRNA potentiates Tat-induced HIV-1 transactivation
-
additional information
-
activating phosphorylation of AMPK at Thr172 of the alpha-subunit, e.g. by CaMKKbeta or LBK1, inhibiting dephosphorylation by phosphatase PP2C
-
additional information
-
contraction in skeletal muscle in adenylate kinase null mice reduces AMPK activation due to lack of conversion of ADP to AMP
-
additional information
-
AMPK phosphorylation is significantly reduced in ob/ob mouse hearts compared with lean, wild-type controls and the reduction in active phosphorylated AMPKalpha is associated with an increase in protein phosphatase 2C (PP2C)
-
additional information
-
UCH-L3 is involved in a cell-autonomous down-regulation of AMPK activity
-
additional information
-
osteoclasts and macrophages generated from AMPK beta1-/- mice display no detectable AMPK activity
-
additional information
-
re-feeding after fasting inhibits AMPK activity in multiple hypothalamic regions. Diet-induced obesity mice have suppressed AMPK activity in the paraventricular nucleus of the hypothalamus, AMPK is suppressed to the level in leptin-treated chow-fed mice, and there is no further effect of leptin. In mice, diet-induced obesity alters the effect of leptin on AMPK activity not only in the hypothalamus, but also in the skeletal muscle. Adiponectin-deficient mice show decreased AMPK phosphorylation in the arcuate nucleus. In leptin-over-expressing transgenic mice on a high fat diet, muscle AMPK phosphorylation and acetyl-CoA carboxylase phosphorylation are reduced compared with standard diet leptin-over-expressing transgenic mice and are comparable to high fat diet-non-transgenic mice. Leptin i.c.v., in addition to transgenic hyperleptinaemia, is not able to restore the impaired AMPK signalling because of the induced generalised leptin resistance
-
additional information
-
in neurodegeneration model in which apoptotic neurodegeneration of neonatal mouse brains is induced by ethanol, AMPK activity is attenuated
-
additional information
-
no inhibition by adenosine-5'-pentaphospho-5'-adenosine
-
additional information
-
complex formation between isozyme alpha1 and NDPK-H1 inhibits the AMPK activity, inhibition by NDPK is reduced by addition of ADP or GTP, overview
-
additional information
-
prosurvival effects of rapamycin are consistent with mTOR inhibition being a critical downstream mediator of AMPK in persistent low oxygen
-
additional information
-
activating phosphorylation of AMPK at Thr172 of the alpha-subunit, e.g. by CaMKKbeta or LBK1, inhibiting dephosphorylation by phosphatase PP2C
-
additional information
-
inhibition or downregulation of AMPK via adenoviral delivery of dominant-negative AMPK-alpha prevents CO2-induced Na,K-ATPase endocytosis
-
additional information
-
AMPK phosphorylation is significantly reduced in Zucker diabetic fa/fa rats compared with lean, wild-type controls and the reduction in active phosphorylated AMPKalpha is associated with an increase in protein phosphatase 2C (PP2C). AMPK activity is reduced in aortic endothelium or skeletal muscle of obese rats compared with lean animals. Possibility that chronic exposure of cells to fatty acids may inhibit AMPK activation. Feeding of a high fat diet significantly decreases AMPK in the liver and muscles
-
additional information
-
lower basal AMPK activity in paraventricular nucleus may be due to effects of hyperinsulinaemia and/or hyperglycaemia, which suppress AMPK activity in multiple hypothalamic nuclei
-
additional information
-
autoinhibition of AMPK by the autoinhibitory domain. The autoinhibitory domain in the holoenzyme has a bona fide inhibiting role in the rate of phosphoryl transfer (kcat) as it does in the catalytic kinase domain/autoinhibitory domain fragments
-
additional information
-
kinase domain/autoinhibitory domain fragment is inactive in the unphosphorylated state, and exhibits low basal kinase activities when phosphorylated at residue Thr 210
-
additional information
-
kinase domain/autoinhibitory domain fragment is inactive in the unphosphorylated state, and exhibits low basal kinase activities when phosphorylated at residue Thr 189
-
additional information
-
dynamical mechanism of autoinhibition of AMP-activated protein kinase, molecular dynamics simulations and modelling, overview. Conformational switch model involving the movement of the kinase domain between an inactive unphosphorylated open state and an active or semi-active phosphorylated closed state, mediated by the autoinhibitory domain (AID). AID inhibits the catalytic function by restraining the kinase domain into an unproductive open conformation, thereby limiting local structural rearrangements, while mutations that disrupt the interactions between the kinase domain and AID allow for both the local structural rearrangement and global interlobe conformational transition. The AID also greatly impacts the structuring and mobility of the activation loop. Binding of AMP to the gamma-subunit changes the interactions between the AID and kinase domain to remove the inhibitory effect of AID to allow the interlobe conformational transition to the closed state. The unphosphorylated KD-AID fragment from Schizosaccharomycespombe (PDB ID 3H4J) is used as a model of the inactive-open state because of its open interlobe conformation, while the phosphorylated kinase domain fragment from Saccharomyces cerevisiae (PDB ID 3DAE) is used as the active-closed state reference, in accord with the experimental structural and mutagenesis analysis. AID inhibits catalytic function by restraining kinase domain to an inactive-open state
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(23E)-cucurbita-5,23,25-triene-3beta,7beta-diol
-
CH10, triterpene from the stem of bitter melon Momordica charantia, leads to the activation of AMPK in cells, overcomes insulin resistance
(5S)-3-[(13S)-13-hydroxy-14-(2-{[(2S)-2-hydroxydodecyl]oxy}ethoxy)tetradecyl]-5-methylfuran-2(5H)-one
-
i.e. AA005
-
1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine
-
activates AMPK, phosphorylation of AMPK-Thr172 is increased 2.8fold in the degenerated midbrain by 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-intoxication. AMPK activation is stimulated in the substantia nigra of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-intoxicated mice
1-methyl-4-phenylpyridinium
-
activates AMPK in SH-SY5Y cells. Increases phosphorylation level at Thr172 in the active site of AMPKalpha. AMPK is activated during the progression of cell death mediated by 1-methyl-4-pyridinium
2-deoxyglucose
-
blocks glucose utilization and increases the intracellular AMP concentration, activation is suppressed by compound C
24-hydroxyursolic acid
-
from the leaves of Diospyros kaki, strongly activates AMPK, inhibits cell proliferation
3beta,25-dihydroxy-7beta-methoxycucurbita-5,23(E)-diene
-
CH63, triterpene from the stem of bitter melon Momordica charantia, leads to the activation of AMPK in cells, overcomes insulin resistance
3beta,7beta,25-trihydroxycucurbita-5,23(E)-dien-19-al
-
CH93, triterpene from the stem of bitter melon Momordica charantia, leads to the activation of AMPK in cells, overcomes insulin resistance
5-aminoimidazole-4-carboxamide-1-beta-D-riboside
-
AICAR, activates AMPK, whereby significantly reduces secretagogue-induced acid secretion
A23187
-
0.01 mM significantly enhances the phosphorylation of AMPK-Thr172 in BAEC. Either STO-609 (0.001 mM) or BAPTA-AM (0.02 mM), significantly suppresses calcium inophore A23187-enhanced phosphorylation in BAEC
A769662
A769662 selectively activates beta1-containing AMPK isoforms
alpha,beta-methylene-ADP
-
allosteric activator, can replace ADP, with 66% efficiency with bovine serum albumin as substrate
BLX-1002
-
has no affinity to peroxisome proliferator-activated receptors (PPAR), stimulation of beta-cells with BLX-1002 induces activation of AMPK at high glucose. BLX-1002 selectively potentiates insulin secretion induced by high glucose in normal and diabetic islets in a PI3K-dependent manner. This effect is associated with an increased cytoplasmic free Ca2+ concentration mediated through Ca2+ mobilization, and an enhanced activation of AMPK
-
BLX-1015
-
0.01 mM significantly enhances AMPK phosphorylation, to an extent similar to that of BLX-1002. Potentiates pioglitazone-, but not fenofibrate-induced insulin secretion
-
calyculin A
-
stimulation of activating AMPK phosphorylation at Thr172, independent of narigin
cantharidin
-
stimulation of activating AMPK phosphorylation at Thr172, independent of narigin
Colchicine
at low concentration (10 nM) promotes phosphorylation of AMPKalpha and macrophage M2 polarisation and reduces activation of caspase-1 and release of IL-1beta and CXCL1 by monosodium urate crystals in BMDMs in vitro. Activation of AMPK is induced by certain drugs already in the clinic for arthritis and other diseases (e.g. methotrexate, high-dose aspirin, metformin) and by other agents, including the selective and direct activator A-769661
compound C
-
inhibits AMPK and phase II, but not phase I, of hypoxic pulmonary vasoconstriction
corticosterone
-
counteracts inhibiting effect of sucrose and increases hypothalamic AMPK activity to levels comparable with saline-drinking animals
dexamethasone
-
induces increase in AMPK in primary rat hypothalamic cell cultures, suggesting a direct effect of glucocorticoids on AMPK activity
Diethylamine NONOate
-
nitric oxide donor, stimulates rapid and transient AMPK phosphorylation in INS832/13 cells and islets
GINST
-
a hydrolyzed ginseng extract, phosphorylation of AMPKalpha increases 2.5fold by GINST after 360 min of treatment
-
hydrogen peroxide
-
sublethal oxidative stress inhibits retinal pigment epithelium cell phagocytosis and activates AMPK. 0.5 mM hydrogen peroxide dramatically activates AMPKalpha, reaches the peak within 15 min, and declines 1 h later. Thr172 phosphorylation of catalytic subunit AMPKalpha is required for AMPKalpha activation
IFNgamma
-
activates AMPK by phosphorylation of Thr172, independent of intracellular energy (ATP) levels. Phosphatidylinositol 3'-kinase inhibition by LY294002 partially prevents IFNgamma-induced activation of AMPK
-
Insulin
-
insulin-induced hypoglycaemia in rats increases AMPK phosphorylation and alpha2AMPK activity in the arcuate nucleus/dorso-mediobasal hypothalamus and paraventricular nucleus
-
Mito-TEMPOL
-
mitochondria-targeting superoxide dismutase mimetic, 0.01 mM markedly attenuates statin-enhanced phosphorylation of both AMPK-Thr172 and acetyl-CoA carboxylase-Ser79
MT-II
-
melanocortin 4 receptor agonist, significantly augments AMPK and acetyl-CoA carboxylase phosphorylation, MT-II is a potent AMPK activator in muscle, even in mice on a high fat diet
N-(3-hydroxyphenyl)adenosine
-
activates the enzyme with 1.4fold maximal activity at 0.001 mM
-
nitric oxide
-
AMPK is transiently activated by nitric oxide in insulinoma cells and rat islets following interleukin-1 treatment or by the exogenous addition of nitric oxide
O2
-
hypoxia leads to time-dependent AMPK activation in ATII cells. Maximal activation of AMPK after 10 min of 1.5% O2 exposure, whereas 3% O2 activates AMPK in a similar but slower manner. AMPK levels return to the baseline after 30 min of hypoxia exposure. Hypoxia-generated mitochondrial reactive oxygen species leads to the activation of the AMPK alpha1 isoform at Thr172. Hypoxia fails to activate AMPK in mitochondrion-deficient rho0-A549 cells
okadaic acid
-
stimulation of activating AMPK phosphorylation at Thr172, activation is antagonized by naringin
PKC-zeta
-
is required for statin-induced LKB1 nucleus export and AMPK activation in HUVEC cells
-
puerarin
-
stimulates AMPK, puerarin down-regulated MDR1 expression via nuclear factor kappa-B and cAMP-responsive element transcriptional activity-dependent up-regulation of AMPK in MCF-7/adr cells
tautomycin
-
stimulation of activating AMPK phosphorylation at Thr172, independent of narigin
vascular endothelial growth factor
-
activates AMPK in endothelial progenitor cells by phosphorylation at Ser172
-
[([5-(5-oxo-4,5-dihydro-1,2-oxazol-3-yl)furan-2-yl]phosphoryl)bis(oxy)methylene]bis(2-methylpropanoate)
-
i.e. C13
(+)-simvastatin
-
0.05 mM increases phosphorylation of AMPK at Thr172 by 2.6fold and acetyl-CoA carboxylase at Ser79 in BAEC. Ser428 phosphorylation of LKB1 is essential for statin-induced AMPK activation. Statin-induced AMPK activation in BAEC is independent of CaMKKbeta. Activation of AMPK by statin Is O2- or ONOO- dependent
(+)-simvastatin
-
LKB1 is required for statin-dependent AMPK activation. Transfection of LKB1-expressing plasmid is required for statin-induced AMPK activation in A-549 and HeLa S3 cell lines deficient in endogenous LKB1
(+)-simvastatin
-
in vivo administration of statin increases 3-nitrotyrosine and the phosphorylation of AMPK and acetyl-CoA carboxylase in wild-type mice but not in mice deficient in endothelial nitric-oxide synthase. PKC-zeta-dependent AMPK activation. In vivo transfection of PKC-zeta-specific small interfering RNA in mice significantly attenuates statin-enhanced phosphorylation of AMPK-Thr172, acetyl-CoA carboxylase-Ser79, and LKB1-Ser428
5'-AMP
-
the gamma subunit of AMPK contains adenine nucleotide binding sites that facilitate the direct interaction of AMP with the AMPK heterotrimer. AMP regulates the activity of AMPK via the inhibition of AMPK dephosphorylation by protein phosphatases
5'-AMP
-
up to 10fold activation, AMP also promotes net phosphorylation at a critical threonine residue Thr172 within the kinase domain that can generate a further 100fold activation, the combined effect being 1000fold
5'-AMP
-
up to 10fold activation, AMP also promotes net phosphorylation at a critical threonine residue Thr172 within the kinase domain that can generate a further 100fold activation, the combined effect being 1000fold
5'-AMP
-
-
5'-AMP
-
the gamma subunit of AMPK contains adenine nucleotide binding sites that facilitate the direct interaction of AMP with the AMPK heterotrimer. AMP regulates the activity of AMPK via the inhibition of AMPK dephosphorylation by protein phosphatases
5'-AMP
-
up to 10fold activation, AMP also promotes net phosphorylation at a critical threonine residue Thr172 within the kinase domain that can generate a further 100fold activation, the combined effect being 1000fold
5-aminoimidazole-4-carboxamide 1-beta-D-ribofuranoside
-
i.e. AICAR, the pharmacological compound transported into cells by the adenosine transporter, and then metabolized by the enzyme adenosine kinase into 5-aminoimidazole-4-carboxamide 1-b-D-ribofuranosyl monophosphate, ZMP, an AMP analogue, which then functions like endogenous AMP by binding to the Bateman domains of AMPK and promoting allosteric activation of the kinase, AICAR does not alter endogenous levels of AMP or ATP, ZMP might prevent the dephosphorylation of AMPK by inhibition of AMP-sensitive phosphatases
5-aminoimidazole-4-carboxamide 1-beta-D-ribofuranoside
-
i.e. AICAR, the pharmacological compound transported into cells by the adenosine transporter, and then metabolized by the enzyme adenosine kinase into 5-aminoimidazole-4-carboxamide 1-b-D-ribofuranosyl monophosphate, ZMP, an AMP analogue, which then functions like endogenous AMP by binding to the Bateman domains of AMPK and promoting allosteric activation of the kinase, AICAR does not alter endogenous levels of AMP or ATP, ZMP might prevent the dephosphorylation of AMPK by inhibition of AMP-sensitive phosphatase
5-aminoimidazole-4-carboxamide ribonucleoside
-
AICAR, AMPK activator, inhibits Tat-induced HIV-1 transactivation
5-aminoimidazole-4-carboxamide ribonucleoside
-
AICAR, has a proapoptotic effect in neuroblastoma cells. AICAR does not significantly change AMPK activity after prolonged exposure (48 h), when its apoptotic effect becomes evident
5-aminoimidazole-4-carboxamide ribonucleoside
-
AICAR, a potent activator of AMPK. If treated with small to moderate concentrations, embryonic hippocampal neurons cultured in conditions of glucose deprivation have improved survival
5-aminoimidazole-4-carboxamide ribonucleotide
Q13131; Q9Y478; P54619
i.e. AICAR, activation of AMPK in isolated perfused proximal renal tubules by AICAR
5-aminoimidazole-4-carboxamide riboside
-
AICAR, increases phosphorylation of alpha1 AMPK, resulting in inactivation of ACCalpha in MAC-T cells
5-aminoimidazole-4-carboxamide riboside
-
AICAR, activates AMPK, whereby increasing the rate of fatty acid oxidation in isolated human muscle strips and cultured human skeletal muscle cells. In isolated human muscle strips, AICAR induces glucose uptake, that is associated with increased translocation of the glucose transporter, GLUT4, to the plasma membrane
5-aminoimidazole-4-carboxamide riboside
-
AICAR, its activation of AMPK is abolished by preincubation with dipyridamole or 5-iodotubercidin
5-aminoimidazole-4-carboxamide riboside
-
AICAR is able to reverse both the inhibitory effect on pAMPK and the C75-induced anorexia
5-aminoimidazole-4-carboxamide riboside
-
AICAR, stimulates site 2 phosphorylation
5-aminoimidazole-4-carboxamide riboside
-
stimulation of activating AMPK phosphorylation at Thr172
5-aminoimidazole-4-carboxamide riboside
-
i.e. AICAR, a specific AMPK activator
5-aminoimidazole-4-carboxamide riboside
-
AICAR, activation of the alpha2 isoform of AMPK in response to treatment with the AMPK activator AICAR, is much greater in the glycogen-depleted state
5-aminoimidazole-4-carboxamide riboside
-
AICAR, in perfused hindlimb, AICAR induces glucose uptake, that is associated with increased translocation of the glucose transporter, GLUT4, to the plasma membrane. Reduces insulin-stimulated glycogen synthase activity in isolated skeletal muscle. Diminishes ectopic lipid deposition in liver and muscle of Zucker diabetic fatty rats and slows the progression to type 2 diabetes in these animals
5-aminoimidazole-4-carboxamide riboside
-
AICAR, increases phosphorylation of acetyl-CoA carboxylase and AMPK in INS832/13 cells
5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside
-
AICAR, increase in cytosolic Ca2+ activity by Ca2+ ionophore ionomycin triggeres eryptosis, an effect blunted by the AMPK activator 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside at 1 mM
5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside
-
AICAR, increases AMPK activity
5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside
-
i.e. AICAR, activates AMPK activity with substrate CREB about 3fold, and AMPK signaling in muscles but not in LBK1-KO mice, overview
5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside
-
activates AMPK in BMMs and RAW264.7 cells. While 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside greatly stimulates osteoclast formation, it acts through an AMPK-independent mechanism
5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside
-
AICAR, activating phosphorylation of alphaAMPK T172 in response to AICAR increases normally in muscle from obese mice fed a high-fat diet
5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside
-
AICAR, activates AMPK, wherby altering the expression of a variety of genes, including those for uncoupling protein (UCP)-3 and GLUT-4 in muscle, and fatty acid synthase and phosphoenolpyruvate carboxykinase in hepatocytes
5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside
-
AICAR, chronic AMPK activation with AICAR decreases blood pressure in rats displaying features of the insulin resistance syndrome
5-aminoimidazole-4-carboxamide-1-beta-D-ribonucleoside
-
i.e. AICAR
5-aminoimidazole-4-carboxamide-1-beta-D-ribonucleoside
-
i.e. AICAR, a potent agonist of AMPK, activates AMPK activation by p38 MAPK, AICAR must be phosphorylated itself to ZMP by adenosine kinases in order to activate AMPK
5-aminoimidazole-4-carboxamide-1-beta-D-ribonucleoside
-
i.e. AICAR, activates AMPK and increases PGC-1alpha expression
5-aminoimidazole-4-carboxamide-1-beta-D-ribonucleoside
-
i.e. AICAR, an AMP-activated protein kinase specific activator
5-aminoimidazole-4-carboxamide-1-beta-D-ribonucleoside
-
i.e. AICAR, decreases class III PI3-kinase binding to beclin-1, and this effect counteracts and reverses the known positive effect of AMPK activity on autophagy, and AICAR inhibits the proteasomal degradation of proteins in lysosomes by an AMPK-dependent mechanism, but inhibits autophagy by an AMPK-independent mechanism
5-aminoimidazole-4-carboxamide-1-beta-D-ribonucleoside
-
i.e. AICAR, the activation of AMPK negatively modulates the activated phenotype of hepatic stellate cells, AMPKactivation does not reduce PDGF-dependent activation of extracellular signal-regulated kinase, ERK, or Akt, but blocks in cell cycle progression, physiological effects of AMPK activation and inhibition, mechanism, overview
5-aminoimidazole-4-carboxamide-1-beta-D-ribonucleoside
-
i.e. AICAR, activates the phosphorylation of peptide QKFQRELSTKWVLN 4fold, kinetics, overview
A-769662
-
small molecule direct activator of AMPK, increases glucose uptake in both L6 myotubes and primary myotubes
A-769662
-
small molecule direct activator of AMPK, treatment of ob/ob mice for 5 days decreases plasma glucose and triglyceride concentrations, lowers hepatic triglyceride content and reduces expression of gluconeogenesis genes in the liver
A-769662
a selective pharmacological activator of AMPK. A-769662 promotes AMPK-dependent macrophage anti-inflammatory M2 polarisation and inhibits NLRP3 gene expression, activation of caspase-1 and IL-1beta
A-769662
-
activates the liver enzyme, binds to the enzyme, acts allosterically
A-769662
-
small molecule direct activator of AMPK, reduces fatty acid synthesis in primary hepatocytes
adiponectin
-
activation of AMPK, which is mediated via cell surface receptor AdipoR1
-
AMP
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
-
AMP
P54646; O43741; Q9UGI9
an allosteric activator for AMPK heterotrimeric complex (alpha2beta2gamma3)
AMP
phosphorylation of the activation-loop threonine (Thr172 of alpha2) or allosteric modulation by AMP binding is essential for AMPK activation
AMP
the alpha2-subunit-containing enzyme complexes are more readily activated by AMP than alpha1-complexes
AMP
-
-
AMP
-
wild-type is activated about 2fold in the presence of 0.2 mM. The catalytic activity and substrate binding affinity of AMPK are separately regulated by AMP binding and the assembly of beta- and gamma-subunits onto the alpha-subunit
Ca2+/calmodulin-dependent protein kinase kinase
-
i.e. CaMKKalpha/beta, increases AMPK activity regulating AMPK in a Ca2+/calmodulin-dependent, AMP-independent manner, overview
-
Ca2+/calmodulin-dependent protein kinase kinase
-
i.e. CaMKKalpha/beta, increases AMPK activity regulating AMPK in a Ca2+/calmodulin-dependent, AMP-independent manner, overview
-
Calmodulin
-
AMPK activation by phosphorylation through the Ca2+-calmodulin dependent protein kinase kinase, CaMKK
Calmodulin
-
activation of AMPK is mediated by a CO2-triggered increase in intracellular Ca2+ concentration and Ca2+/calmodulin-dependent kinase kinase-beta, CaMKK-beta
dinitrophenol
-
a cellular metabolic poison that activates AMPK in numerous cell types, including skeletal muscle, mechanism, overview
dinitrophenol
-
a cellular metabolic poison that activates AMPK in numerous cell types, including skeletal muscle, mechanism, overview
glucocorticoid
-
treatment inhibits AMPK activity in rat adipose tissue and heart, while stimulating it in the liver and hypothalamus, similar to activity in vitro in the primary adipose and hypothalamic cells
-
glucocorticoid
-
treatment inhibits AMPK activity in rat adipose tissue and heart, while stimulating it in the liver and hypothalamus, similar to activity in vitro in the primary adipose and hypothalamic cells
-
interleukin-6
-
activates AMPK in skeletal muscle by increasing the phosphorylation of Thr172 of AMPK
interleukin-6
-
activates AMPK in skeletal muscle by increasing the phosphorylation of Thr172 of AMPK
interleukin-6
-
directly activates AMPK in vivo and in vitro. Activates AMPK in skeletal muscle by increasing the concentration of cAMP and the AMP:ATP ratio. AMPK activation coincides temporally with a nearly 3fold increase in the AMP:ATP ratio in the extensor digitorum longus
leptin
-
the classical adipokine, released from adipocytes, stimulates the alpha2 isoform of AMPK and hence fatty acid oxidation in skeletal muscle
-
leptin
-
the classical adipokine, released from adipocytes, stimulates the alpha2 isoform of AMPK and hence fatty acid oxidation in skeletal muscle
-
leptin
-
the classical adipokine, released from adipocytes, stimulates the alpha2 isoform of AMPK and hence fatty acid oxidation in skeletal muscle
-
leptin
-
has a tissue-specific effect on AMPK. In the skeletal muscle, it stimulates AMPK activity
-
metformin
-
AMPK mediates the prevention of progression of heart failure by metformin. Protective effects of AMPK activation by metformin on cardiovascular disease
metformin
-
increases the activating phosphorylation of the enzyme at Thr172 of the alpha-subunit by 3.6fold
metformin
-
i.e. N,N-dimethylimidodicarbonimidic diamide, one of the most commonly prescribed drugs for the treatment of type 2 diabetes, increases the activity of AMPK in skeletal muscle, mechanism, loss of TAK1 protein prevents the metformin-induced activation of AMPK, overview
metformin
-
improves cardiac structure and function, which is associated with increases in AMPK and endothelial nitric oxide synthase phosphorylation, as well as increased peroxisome proliferator-activated receptor-gamma coactivator (PGC)-1alpha expression in cardiac myocytes. Cardioprotective effects of metformin are ablated in mice lacking functional AMPK or nitric oxide synthase
metformin
-
significantly increases AMPK activity in the aortas and hearts of wild-type mice but not those of eNOS-/-, although eNOS-/- mice express AMPK
metformin
-
stimulates AMPK, does not induce any significant change in glucose-stimulated insulin secretion
metformin
-
co-administration of dexamethasone and metformin decreases insulin-stimulated glucose uptake compared with metformin alone
metformin
-
i.e. N,N-dimethylimidodicarbonimidic diamide, one of the most commonly prescribed drugs for the treatment of type 2 diabetes, increases the activity of AMPK in skeletal muscle, mechanism, loss of TAK1 protein prevents the metformin-induced activation of AMPK, overview
pioglitazone
-
i.e. 5-((4-(2-(5-ethyl-2-pyridinyl)ethoxy)-phenyl)methyl)-(+)-2,4-thiazolidinedione, a drug that is used to treat type 2 diabetes, a thiazolidinedione, reduces blood glucose levels in humans via activation of AMPK in skeletal muscle
pioglitazone
-
i.e. 5-((4-(2-(5-ethyl-2-pyridinyl)ethoxy)-phenyl)methyl)-(+)-2,4-thiazolidinedione, a drug that is used to treat type 2 diabetes, a thiazolidinedione, reduces blood glucose levels in rodents via activation of AMPK in skeletal muscle
Reductase kinase kinase
-
activation, i.e. EC 2.7.1.110, in the presence of MgATP2-
-
Reductase kinase kinase
-
EC 2.7.1.110, activation in presence of MgATP2-
-
Reductase kinase kinase
-
activation, i.e. EC 2.7.1.110, in the presence of MgATP2-
-
resveratrol
-
reverses Tat-mediated reduction in AMPK activation and downstream acetyl-CoA carboxylase activation, inhibits Tat-induced HIV-1 transactivation
resveratrol
-
increases the phosphorylation status of AMPK in wild-type MEFs. Effect of resveratrol on AMPK is mediated via LKB1
resveratrol
-
resveratrol exerts anti-hypertrophic effects by activating AMPK via LKB1 and inhibiting Akt, thus suppressing protein synthesis and gene transcription. Level of phosphorylated AMPK is significantly increased in resveratrol-treated cardiac myocytes in the absence or presence of phenylephrine
rosiglitazone
-
i.e. 5-((4-(2-(methyl-2-pyridinylamino)ethoxy)phenyl)methyl)-2,4-thiazol-idinedione, a drug that is used to treat type 2 diabetes, a thiazolidinedione, reduces blood glucose levels in humans via activation of AMPK in skeletal muscle
rosiglitazone
-
stimulates an increase in the ADP/ATP ratio and AMPK activity essentially involving LKB1 and leading to activation of nitric oxide synthesis in human aortic endothelial cells, the stimulation of AMPK and NO synthesis by rosiglitazone is unaffected by the peroxisome proliferator-activated receptor-gamma inhibitor GW9662 or by STO-609, overview
rosiglitazone
-
i.e. 5-((4-(2-(methyl-2-pyridinylamino)ethoxy)phenyl)methyl)-2,4-thiazol-idinedione, a drug that is used to treat type 2 diabetes, a thiazolidinedione, reduces blood glucose levels in rodents via activation of AMPK in skeletal muscle
rotenone
-
a cellular metabolic poison that activates AMPK in numerous cell types, including skeletal muscle, mechanism, overview
rotenone
-
a cellular metabolic poison that activates AMPK in numerous cell types, including skeletal muscle, mechanism, overview
additional information
-
decreases in energy availability or rises in intracellular Ca2+ most likely activates AMPK in MAC-T cell
-
additional information
-
AAK-2 is phosphorylated at Thr243 and activated in response to paraquat treatment, the phosphorylation depends on PAR-4, the Caenorhabditis elegans LKB1 homologue
-
additional information
-
AMPK is activated by phosphorylation through upstream kinases and 5'-AMP in response to various nutritional and stress signals
-
additional information
the region flanking the regulatory T172 site of AMPKalpha subunit is phosphorylated by an upstream AMPKK. AMPK is activated during temperature stress. AMPK activity remains constant between 12 and 18°C, but increases up to 9.1fold between 18 and 30°C. Total AMPK protein expression levels do not vary significantly over this temperature range. Prolonged exposure for up to 6 h to the sublethal temperature of 26°C leads to a constant elevation of AMPK activity. Increase in AMPK activity above 18°C coincides with the decrease in reaction time
-
additional information
the region flanking the regulatory T172 site of AMPKalpha subunit is phosphorylated by an upstream AMPKK. AMPK is activated during temperature stress. AMPK activity remains constant between 12 and 18°C, but increases up to 9.1fold between 18 and 30°C. Total AMPK protein expression levels do not vary significantly over this temperature range. Prolonged exposure for up to 6 h to the sublethal temperature of 26°C leads to a constant elevation of AMPK activity. Increase in AMPK activity above 18°C coincides with the decrease in reaction time
-
additional information
-
AMPK activity increases 5.5fold in liver during hypoxic exposure accompanied by a change in the AMP/ATP ratio, but not in muscle, brain, heart, or gill, overview
-
additional information
-
activating phosphorylation of AMPK at Thr172 of the alpha-subunit, e.g. by CaMKKbeta or LBK1, dephosphorylation by phosphatase PP2C
-
additional information
-
activation of AMPK requires phosphorylation at Thr172 by an AMPK kinases, e.g. LKB1 and Ca2+/calmodulin-dependent kinase kinase, CaMKK
-
additional information
-
AMPKalpha needs to be activated by phosphorylation on Thr172
-
additional information
-
phosphorylation of AMPK at Thr172 of the alpha-subunit activates the enzyme
-
additional information
-
the enzyme is activated by phosphorylation at Thr172 in the alpha subunit activation T-loop
-
additional information
-
UV and H2O2 induce AMPK activation through Thr172 phosphorylation, UV and H2O2 also phosphorylate LKB1, an upstream signal of AMPK, in an epidermal growth factor receptor-dependent manner, overview. SB203580, a p38 inhibitor, does not affect AMPK activation
-
additional information
-
activation of the alpha2 isoform of AMPK in response to exercise in human muscle, is much greater in the glycogen-depleted state. In humans with McArdle's disease (glycogen storage disease V), the activation of AMPK-alpha2 in response to a moderate level of exercise (which is all these subjects can tolerate) is significantly higher than in the controls
-
additional information
-
in healthy humans, an acute bout of exercise activates AMPK in an isoform and intensity-dependent manner
-
additional information
-
LKB1, a serine-threonine kinase of 433 amino acids, which contains both a kinase domain and a nuclear localization signal in its N-terminal region, phosphorylates the T-loop of AMPK
-
additional information
all three nucleotides AMP, ADP and ATP can bind to sites 1 and 3 with similar affinities. Phosphorylation of Thr172/Thr174 of the alpha subunit activates the enzyme isozymes
-
additional information
Q13131; Q9Y478; P54619
ischemia stimulates the AMP-activated protein kinase (AMPK)
-
additional information
P54646; O43741; Q9UGI9
small molecule activator thienopyridone A-769662 has no ativating effect on AMPK heterotrimeric complex (alpha2beta2gamma3)
-
additional information
the enzyme is activated under circumstances with an increased cellular AMP:ATP ratio, such as metabolic stresses that inhibit ATP production (hypoxia, glucose deprivation, metabolic inhibitors etc.) and those that stimulate ATP consumption (exercise, cell growth and division etc.). Activation-loop conformation, overview
-
additional information
-
activating phosphorylation of AMPK at Thr172 of the alpha-subunit, e.g. by CaMKKbeta or LBK1, inhibiting dephosphorylation by phosphatase PP2C
-
additional information
-
phosphorylation at Thr172 activates the enzyme, the phosphorylation is activated by 5-aminoimidazole-4-carboxamide-1-beta-D-ribonucleoside
-
additional information
-
phosphorylation of AMPK at Thr172 of the alpha-subunit activates the enzyme
-
additional information
-
T cell receptor stimulation activates AMPK due to energy needs in case of cell division having regulatory function, overview. AMPK activation by phosphorylation through the Ca2+-calmodulin dependent protein kinase kinase, CaMKK
-
additional information
-
ADP does not directly control AMPK activity but can do so indirectly through the adenylate kinase equilibrium with AMP and ATP
-
additional information
-
in skeletal muscle of Uchl3-/- mice fed a normal chow diet, phosphorylated AMPK is significantly up-regulated, which indicates an increased activation of AMPK, in any feeding state. No AMPK activation in other major metabolic tissues, such as liver and white adipose tissue. Embryonic fibroblasts derived from Uchl3-/- mice also show increased activation of AMPK, indicating that UCH-L3 is involved in a cell-autonomous down-regulation of AMPK
-
additional information
-
methanol extracts from the fruit, seed, or stem of bitter melon Momordica charantia all contain components efficacious in improving glucose uptake of insulin-resistant cells involving activation of AMPK
-
additional information
-
mice subjected to moderate diet restriction (60% of the requirement) are characterized by AMPK activation. Drastic diet restriction (40% of the requirement) leads to further elevation in AMPK activity
-
additional information
-
overexpression of GDE in cells causes increased phosphorylation of the AMPK alpha subunit at Thr-172 and its consequent activation
-
additional information
phosphorylation on Thr172 and activation of AMPKalpha subunit
-
additional information
-
phosphorylation of AMPK at Thr172 of the alpha-subunit activates the enzyme
-
additional information
-
activated by phosphorylation by upstream protein kinases AMPKK and CaMKIK
-
additional information
-
AMPK can also be activated by hyperosmotic stress
-
additional information
-
stimulation by protein phosphatase-inhibitory toxins
-
additional information
-
activating phosphorylation of AMPK at Thr172 of the alpha-subunit, e.g. by CaMKKbeta or LBK1, inhibiting dephosphorylation by phosphatase PP2C
-
additional information
-
AMPKalpha needs to be activated by phosphorylation on Thr172. Reactive oxygen species contribute to AMPK activation, mechanism, overview
-
additional information
-
anti-obesity effects of Juniperus chinensis extract are associated with increased AMP-activated protein kinase expression and phosphorylation in the visceral adipose tissue, overview
-
additional information
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
-
additional information
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
-
additional information
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
-
additional information
cellular energy stress and other signals activate AMPK by various pathways, leading as a main consequence to compensatory measures that increase ATP generation and decrease ATP consumption
-
additional information
-
phosphorylation of AMPK at Thr172 of the alpha-subunit activates the enzyme
-
additional information
-
phosphorylation of AMPK at Thr172 of the alpha-subunit activates the enzyme
-
additional information
-
phosphorylation of AMPK at Thr172 of the alpha-subunit activates the enzyme, copper deficiency results in AMP-activated protein kinase activation and acetyl-CoA carboxylase phosphorylation in rat cerebellum, overview
-
additional information
-
the enzyme is activated by phosphorylation at Thr172
-
additional information
-
AMPK may be sensitive to the lipid status of a cell and activation may be influenced by intracellular fatty acid availability independent of cellular AMP levels
-
additional information
-
diabetic rats treated with cilostazol, a selective inhibitor of phosphodiesterase 3, exhibit normalization of endothelial function that is linked to AMPK activation producing increased endothelial nitric oxide synthase activity and NO production. In the ischemic heart, both catalytic alpha1-isoform and alpha2-isoform of AMPK containing regulatory gamma1-isoform or gamma2-isoform are activated
-
additional information
-
elevated phosphorylation of AMPK and R2-GABAB in the hippocampus of a rat ischemic in vivo model
-
additional information
-
inhibition of intracellular glucose utilisation through the administration of 2-deoxyglucose increases hypothalamic AMPK activity and food intake. Diabetic rats have enhanced AMPK activity, despite their high glucose levels, which should suppress hypothalamic AMPK. Thyroid hormones stimulate AMPK and acetyl-CoA carboxylase expression in skeletal muscle. 1 h of strenuous exercise in rats does not elicit significant changes in hypothalamic AMPK activity despite an increase in plasma ghrelin
-
additional information
-
adenosine (0.0001-0.5 mM) has no direct stimulating effect on enzyme activity
-
additional information
alkaline and glucose stress leads to the activation of all three isoforms
-
additional information
alkaline and glucose stress leads to the activation of all three isoforms
-
additional information
alkaline and glucose stress leads to the activation of all three isoforms
-
additional information
-
alkaline and glucose stress leads to the activation of all three isoforms
-
additional information
alkaline and glucose stress leads to the activation of all three isoforms, but only the Gal83 isoform of Snf1 is both necessary and sufficient for the phosphorylation of Mig2 protein in response to alkaline stress
-
additional information
alkaline and glucose stress leads to the activation of all three isoforms, but only the Gal83 isoform of Snf1 is both necessary and sufficient for the phosphorylation of Mig2 protein in response to alkaline stress
-
additional information
alkaline and glucose stress leads to the activation of all three isoforms, but only the Gal83 isoform of Snf1 is both necessary and sufficient for the phosphorylation of Mig2 protein in response to alkaline stress
-
additional information
-
alkaline and glucose stress leads to the activation of all three isoforms, but only the Gal83 isoform of Snf1 is both necessary and sufficient for the phosphorylation of Mig2 protein in response to alkaline stress
-
additional information
-
protein kinases Elm1, Pak1 and Tos3 phosphorylate and activate SNF1
-
additional information
-
hydrophobic contacts between the kinase domain and the autoinhibitory domain have a predominant role in controlling the conformational change between low- and high activity forms of AMPK
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02667
biotin-GGHMRSAMSGLHLVKRR-NH2
pH 7.5, 30°C, enzyme construct alpha1beta1gamma1
0.03207
biotin-GGHMRSAMSGLHLVKRR-NH2
pH 7.5, 30°C, enzyme construct alpha1beta1gamma1
0.03731
biotin-GGHMRSAMSGLHLVKRR-NH2
pH 7.5, 30°C, enzyme construct alpha1beta1gamma1
0.08003
biotin-GGHMRSAMSGLHLVKRR-NH2
pH 7.5, 30°C, enzyme construct alpha1beta1gamma1
0.1076
biotin-GGHMRSAMSGLHLVKRR-NH2
pH 7.5, 30°C, enzyme construct alpha1beta1gamma1
0.1214
biotin-GGHMRSAMSGLHLVKRR-NH2
pH 7.5, 30°C, enzyme construct alpha1beta1gamma1
additional information
additional information
glucosyl-beta-cyclodextrin binding kinetics, association and dissociation, and thermodynamics
-
additional information
additional information
glucosyl-beta-cyclodextrin binding kinetics, association and dissociation, and thermodynamics
-
additional information
additional information
theMichaelis-Menten enzyme kinetics and allosteric modulation of six recombinant AMPK isoforms, alpha1beta1gamma1, alpha1beta2gamma1, alpha1beta2gamma3, alpha2beta1gamma1, alpha2beta2gamma,1 and alpha2beta2gamma3 using known activators, A769662 and AMP. The alpha1-containing complexes exhibit higher specific activities and lower Km values for peptide substrate biotin-GGHMRSAMSGLHLVKRR-NH2 (SAMS) compared with alpha2-complexes. Binding affinities of AMP, ADP and ATP using surface plasmon resonance techniques, all three nucleotides AMP, ADP and ATP can bind to sites 1 and 3 with similar affinities, allosteric regulation
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000111 - 0.000418
(Z)-2-(3-((4-((2-(diethylamino)ethyl)carbamoyl)-3,5-dimethyl-1H-pyrrol-2-yl)methylene)-2-oxoindolin-5-yl)ethyl acetate
-
0.000108 - 0.000184
(Z)-5-((5-(2-acetamidoethyl)-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
0.000101 - 0.000139
(Z)-5-((5-(2-azidoethyl)-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
0.0000324 - 0.000164
(Z)-5-((5-(2-cyanoethyl)-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
0.0000607 - 0.000107
(Z)-5-((5-(3-amino-3-oxopropyl)-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
0.0000162 - 0.000093
(Z)-5-((5-cyano-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole3-carboxamide
-
0.0000825 - 0.000208
(Z)-5-((6-bromo-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
0.0000651 - 0.000217
(Z)-5-((6-chloro-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
0.0000836 - 0.000205
(Z)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-5-((2-oxo-5-(ureidomethyl)indolin-3-ylidene)methyl)-1H-pyrrole-3-carboxamide
-
0.0000885 - 0.000246
(Z)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-5-((2-oxoindolin-3-ylidene)methyl)-1H-pyrrole-3-carboxamide
0.000154 - 0.0021
(Z)-N-(2-(diethylamino)ethyl)-5-((5-(2-(dimethylamino)ethyl)-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
0.0000205 - 0.000173
(Z)-N-(2-(diethylamino)ethyl)-5-((5-(2-hydroxyethyl)-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
0.0000966 - 0.000296
(Z)-N-(2-(diethylamino)ethyl)-5-((5-(2-methoxyethyl)-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
-
0.000348
(Z)-N-(2-(diethylamino)ethyl)-5-((6-ethyl-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
0.0000494 - 0.00024
(Z)-N-(2-(diethylamino)ethyl)-5-((6-fluoro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
0.0000504 - 0.000136
(Z)-N-(2-(dimethylamino)ethyl)-5-((5-floro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
0.0000614 - 0.00018
(Z)-N-(2-(ethylamino)ethyl)-5-((5-fluoro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
0.000141 - 0.000393
(Z)-N-(2-aminoethyl)-5-((5-fluoro-2-oxoindolin-3-ylidene) methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
0.0000386 - 0.000152
(Z)-N-(3-(diethylamino)propyl)-5-((5-fluoro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
0.0000748 - 0.000221
(Z)-N-(3-(dimethylamino)propyl)-5-((5-fluoro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
0.000158 - 0.00617
N-[2-(diethylamino)ethyl]-5-[(Z)-(6-fluoro-2-oxo-2,3-dihydro-1H-inden-1-ylidene)methyl]-2,4-dimethyl-1H-pyrrole-3-carboxamide
0.000111
(Z)-2-(3-((4-((2-(diethylamino)ethyl)carbamoyl)-3,5-dimethyl-1H-pyrrol-2-yl)methylene)-2-oxoindolin-5-yl)ethyl acetate
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
-
0.000418
(Z)-2-(3-((4-((2-(diethylamino)ethyl)carbamoyl)-3,5-dimethyl-1H-pyrrol-2-yl)methylene)-2-oxoindolin-5-yl)ethyl acetate
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
-
0.000108
(Z)-5-((5-(2-acetamidoethyl)-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
0.000184
(Z)-5-((5-(2-acetamidoethyl)-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
0.000101
(Z)-5-((5-(2-azidoethyl)-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
0.000139
(Z)-5-((5-(2-azidoethyl)-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
0.0000324
(Z)-5-((5-(2-cyanoethyl)-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
0.000164
(Z)-5-((5-(2-cyanoethyl)-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
0.0000607
(Z)-5-((5-(3-amino-3-oxopropyl)-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
0.000107
(Z)-5-((5-(3-amino-3-oxopropyl)-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
0.0000162
(Z)-5-((5-cyano-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole3-carboxamide
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
-
0.000093
(Z)-5-((5-cyano-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
-
0.0000825
(Z)-5-((6-bromo-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
0.000208
(Z)-5-((6-bromo-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
0.0000651
(Z)-5-((6-chloro-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
0.000217
(Z)-5-((6-chloro-2-oxoindolin-3-ylidene)methyl)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
0.0000836
(Z)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-5-((2-oxo-5-(ureidomethyl)indolin-3-ylidene)methyl)-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
-
0.000205
(Z)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-5-((2-oxo-5-(ureidomethyl)indolin-3-ylidene)methyl)-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
-
0.0000885
(Z)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-5-((2-oxoindolin-3-ylidene)methyl)-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
0.000246
(Z)-N-(2-(diethylamino)ethyl)-2,4-dimethyl-5-((2-oxoindolin-3-ylidene)methyl)-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
0.000154
(Z)-N-(2-(diethylamino)ethyl)-5-((5-(2-(dimethylamino)ethyl)-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
0.0021
(Z)-N-(2-(diethylamino)ethyl)-5-((5-(2-(dimethylamino)ethyl)-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
0.0000205
(Z)-N-(2-(diethylamino)ethyl)-5-((5-(2-hydroxyethyl)-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
0.000173
(Z)-N-(2-(diethylamino)ethyl)-5-((5-(2-hydroxyethyl)-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
0.0000966
(Z)-N-(2-(diethylamino)ethyl)-5-((5-(2-methoxyethyl)-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
-
0.000296
(Z)-N-(2-(diethylamino)ethyl)-5-((5-(2-methoxyethyl)-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
-
0.0000494
(Z)-N-(2-(diethylamino)ethyl)-5-((6-fluoro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
0.00024
(Z)-N-(2-(diethylamino)ethyl)-5-((6-fluoro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
0.0000504
(Z)-N-(2-(dimethylamino)ethyl)-5-((5-floro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
0.000136
(Z)-N-(2-(dimethylamino)ethyl)-5-((5-floro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
0.0000614
(Z)-N-(2-(ethylamino)ethyl)-5-((5-fluoro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
0.00018
(Z)-N-(2-(ethylamino)ethyl)-5-((5-fluoro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
0.000141
(Z)-N-(2-aminoethyl)-5-((5-fluoro-2-oxoindolin-3-ylidene) methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
0.000393
(Z)-N-(2-aminoethyl)-5-((5-fluoro-2-oxoindolin-3-ylidene) methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
0.0000386
(Z)-N-(3-(diethylamino)propyl)-5-((5-fluoro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
0.000152
(Z)-N-(3-(diethylamino)propyl)-5-((5-fluoro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
0.0000748
(Z)-N-(3-(dimethylamino)propyl)-5-((5-fluoro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
0.000221
(Z)-N-(3-(dimethylamino)propyl)-5-((5-fluoro-2-oxoindolin-3-ylidene)methyl)-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
0.000158
N-[2-(diethylamino)ethyl]-5-[(Z)-(6-fluoro-2-oxo-2,3-dihydro-1H-inden-1-ylidene)methyl]-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha1, at pH 7.5 and 25°C
0.00617
N-[2-(diethylamino)ethyl]-5-[(Z)-(6-fluoro-2-oxo-2,3-dihydro-1H-inden-1-ylidene)methyl]-2,4-dimethyl-1H-pyrrole-3-carboxamide
Homo sapiens
subunit AMPKalpha2, at pH 7.5 and 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.6
5.9
subunit AMPK-beta, calculated from amino acid sequence
6
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
subunit AMPKgamma3, calculated from amino acid sequence
6.1
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
subunit AMPKgamma1, calculated from amino acid sequence
6.3
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
subunit AMPKbeta1b, calculated from amino acid sequence
6.6
7.1
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
subunit AMPKalpha1, calculated from amino acid sequence
7.3
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
subunit AMPKalpha2, calculated from amino acid sequence
8.6
subunit AMPK-alpha, calculated from amino acid sequence
9
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
subunit AMPKgamma2b, calculated from amino acid sequence
5.6
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
subunit AMPKbeta1a, calculated from amino acid sequence
5.6
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
subunit AMPKbeta2, calculated from amino acid sequence
6.6
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
subunit AMPKgamma2a, calculated from amino acid sequence
6.6
subunit AMPK-gamma, calculated from amino acid sequence
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
two alpha, two beta, and five gamma gene orthologues encoding the subunit variants
-
-
-
644981, 644984, 662296, 665496, 690657, 690725, 691704, 692001, 692091, 692365, 692554, 693032, 693151, 693205, 693207, 693328, 694825, 701571, 701572, 701573, 702079, 703102, 703277, 703348, 703612, 704431, 704459, 704545, 705267, 705694, 705799, 705939, 706364, 706902
-
-
-
644989, 665636, 687732, 690346, 691621, 692365, 693047, 694183, 701571, 701572, 701573, 701620, 702510, 703277, 703348, 703612, 703617, 704122, 704433, 704450, 705267, 705939, 706085
-
-
-
286565, 491403, 644952, 644953, 644954, 644956, 644957, 644959, 644961, 644963, 644964, 644971, 644972, 644973, 644976, 644977, 644978, 644979, 644983, 644988, 663952, 665636, 684366, 690726, 691556, 691704, 692365, 692682, 693207, 701572, 701573, 703277, 703348, 704433, 705267, 705884, 705939, 761360, 761734, 762101
-
-
male sprague-dawley rats
-
-
beta subunit Gal83, equivalent to subunit beta 3
UniProt
beta subunit Sip1, equivalent to subunit beta 1
UniProt
beta subunit Sip2, equivalent to subunit beta 2
UniProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
selective expression of the AMPKalpha1 catalytic subunit in lymphoid cells
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
-
additional information
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
-
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
-
-
visceral adipose tissue, the predominant AMPK subunit in adipose tissue is AMPKalpha1
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
-
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
highest expression of subunit AMPKbeta1a
-
AMPK is widely expressed throughout the brain, including several areas controlling food intake and neuroendocrine function
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
-
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
highest expression of subunit AMPKbeta1b
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
-
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
highest expression of subunit AMPKbeta2
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
highest expression of subunit AMPKgamma1
of female and male oysters, expression of AMP-activated protein kinase (AMPK) subunits during gametogenesis in the gonad, overview. AMPK beta transcripts in the gonad at different reproductive stages decrease from stage 1 to 3
of female and male oysters, expression of AMP-activated protein kinase (AMPK) subunits during gametogenesis in the gonad, overview. AMPK gamma transcripts amounts in the gonad at different reproductive stages are quit constant
of female and male oysters, expression of AMP-activated protein kinase (AMPK) subunits during gametogenesis in the gonad, overview. Subunit AMPK alpha mRNA levels are more abundant in males at the first stage of gametogenesis, when mitotic activity and the differentiation of germinal cells occur, and are always more abundant in males than in females. AMPKalpha Thr172 phosphorylation appears to be almost totally inhibited in mature female gonads at stage 3, at the time when accumulation of reserves in oocytes is promoted, while it remains at a high level in mature spermatozoa. Truncated (45-kDa) and entire (62-kDa) AMPK alpha proteins are detected in gonads of both males and females at all reproductive stages. In both males and females, AMPK alpha truncated protein is detected at a very low level, and its amount does not vary significantly during reproduction, while the entire AMPK alpha protein is detected at a high level, and its amount varies significantly during reproduction. AMPK alpha transcripts in the gonad at different reproductive stages decreases from stage 1 to 3
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
-
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
highest expression of subunit AMPKalpha2
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
highest expression of subunit AMPKgamma2a
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
highest expression of subunit AMPKgamma3
-
HeLa cells stably expressing wild type LKB1 or a kinase-inactive mutant LKB1
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
-
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
-
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
highest expression of subunit AMPKalpha1
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
-
-
the hibernating 13-lined ground squirrel actively increases its fat stores in the liver during the summer, and this is associated with relatively low enzyme (total AMP-activated protein kinase, P-AMPK) activity. During hibernation fat synthesis is turned off while fat oxidation is increased and P-AMPK is activated, especially during the IBA. During torpor activity of P-AMPK declines
-
-
286565, 490912, 491403, 644952, 644953, 644954, 644955, 644956, 644957, 644959, 644961, 644964, 644967, 644971, 644972, 644973, 644978, 644980, 644983, 644988, 663969, 684366, 691132, 691704, 692682, 693207, 701571, 704936
-
AMPK activity in the liver is significantly higher in corticosterone-treated rats compared with the untreated ones
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
-
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
highest expression of subunit AMPKgamma2b
-
different isozymes in muscles by different combinations of subunits, i.e. alpha1/beta2/gamma1, alpha2/beta2/gamma1, and alpha2/beta2/gamma3, overview
P54646; O43741; Q9UGI9
in human skeletal muscle, the alpha2beta2gamma3 complexes constitutes the majority of AMPK heterotrimers
-
gastrocnemius, tibialis anterior, heart, and epitrochlearis muscle
-
-
additional information
-
AMPKalpha1 and AMPKbeta1 genes are ubiquitously expressed in goldfish tissues, AMPKalpha1a is most highly expressed in brain, kidney, and intestine, AMPKalpha1b in brain, kideny, and gill, AMPKbeta1 is most highly expressed in brain
additional information
activity status of AMPK in the gonadic tissue of male and female oysters reared under natural conditions
additional information
activity status of AMPK in the gonadic tissue of male and female oysters reared under natural conditions
additional information
activity status of AMPK in the gonadic tissue of male and female oysters reared under natural conditions
additional information
the alpha2 isoform is abundant in cardiac and skeletal muscle
additional information
-
present in BMM cells. Osteoclasts and macrophages lack AMPK beta2 subunit expression
additional information
-
present in BMM cells. Osteoclasts and macrophages lack AMPK beta2 subunit expression
-
additional information
cells expressing only the Sip1 isoform of Snf1 kinase grow very poorly onmediawith glycerol/ethanol as the carbon source
additional information
cells expressing only the Sip1 isoform of Snf1 kinase grow very poorly onmediawith glycerol/ethanol as the carbon source
additional information
cells expressing only the Sip1 isoform of Snf1 kinase grow very poorly onmediawith glycerol/ethanol as the carbon source
additional information
-
cells expressing only the Sip1 isoform of Snf1 kinase grow very poorly onmediawith glycerol/ethanol as the carbon source
additional information
-
cells expressing only the Sip1 isoform of Snf1 kinase grow very poorly onmediawith glycerol/ethanol as the carbon source
-
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
at prophase, P-AMPKalpha-Thr172 associates with the two asters of microtubules that begin to nucleate from mature centrosomes. Overlapping localization of P-AMPKalpha-Thr172 with the mitotic centrosomal Aurora-A kinase on the microtubules near the spindle poles in metaphase and in early anaphase. Localization of P-AMPKalpha-Thr172 at the central spindle and midbody persists during the furrowing process and at the completion of telophase. P-AMPKalpha-Thr172 localization at centrosomes requires dynamic microtubules
-
AMPK alpha and beta subunits are located both in the cytosol (associated to the rough endoplasmic reticulum) and in close association with rosettes of glycogen particles. Labeling for the alpha(1) and alpha(2) subunits of AMPK is about 2fold greater over glycogen than over cytosol, whereas labeling for beta(1) is 8fold higher over the glycogen particles than over the cytosol. The beta(1) subunits are located at the periphery of the glycogen rosettes
-
additional information
-
-
-
AMPK alpha and beta subunits are located both in the cytosol (associated to the rough endoplasmic reticulum) and in close association with rosettes of glycogen particles. Labeling for the alpha(1) and alpha(2) subunits of AMPK is about 2fold greater over glycogen than over cytosol, whereas labeling for beta(1) is 8fold higher over the glycogen particles than over the cytosol
beta subunit Gal83-containing isozyme after activation by alkaline stress, when the Gal83 isoform is activated by the other Snf1-activating kinases, Tos3 and Elm1, the Gal83 isoform is unable to translocate to the nucleus
-
beta subunit Gal83-containing isozyme after activation by alkaline stress, when the Gal83 isoform is activated by the other Snf1-activating kinases, Tos3 and Elm1, the Gal83 isoform is unable to translocate to the nucleus
-
additional information
-
differential localization patterns of AMPKalpha 1 and AMPKalpha2
-
additional information
-
differential localization patterns of AMPKalpha 1 and AMPKalpha2
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
Saccharomyces cerevisiae expresses three isoforms of Snf1 kinase that differ by which beta subunit is present, Gal83, Sip1 or Sip2, abundance, activation, localization and signaling specificity of the three Snf1 isoforms, by quantitative immunoblotting and fluorescence microscopy, overview. The Gal83 containing isoform is the most abundant in all assays while the abundance of the Sip1 and Sip2 isoforms is typically underestimated especially in glass-bead extractions
evolution
the AMPK beta-subunit CBM has a beta-sandwich fold with the conserved residues Trp100, Lys126 and Trp133 (residue numbers according to beta1-CBM), classifying it under the CBM48 family
evolution
the genes encoding the three subunits of AMPK are highly conserved in eukaryotic species for which complete genome sequences are available, including vertebrates, invertebrates, plants, fungi, and protozoa
evolution
-
Saccharomyces cerevisiae expresses three isoforms of Snf1 kinase that differ by which beta subunit is present, Gal83, Sip1 or Sip2, abundance, activation, localization and signaling specificity of the three Snf1 isoforms, by quantitative immunoblotting and fluorescence microscopy, overview. The Gal83 containing isoform is the most abundant in all assays while the abundance of the Sip1 and Sip2 isoforms is typically underestimated especially in glass-bead extractions
-
malfunction
-
Agouti-related peptide alpha2 AMPK-KO mice show decreased body weight even though there are no changes in food intake or energy expenditure and, the difference in body weight is lost when the animals are fed a high fat diet. Pro-opiomelanocortin alpha2 AMPK-KO animals show increased body weight and adiposity, which is further enhanced by a high fat diet
malfunction
-
AMPK gamma2 mutations are associated with hypertrophic cardiomyopathy
malfunction
-
germline deletion of either AMPK beta1 or beta2 subunit isoforms results in reduced trabecular bone density and mass, but without effects on osteoclast or osteoblast numbers, as compared to wild-type littermate controls
malfunction
-
in the liver from beta1 knockout mice the gamma1 subunit is present but alpha1 and alpha2 are degraded
malfunction
-
mice deficient in AMPKalpha-2 have smaller infarct volumes after middle cerebral artery occlusion, whereas AMPKalpha-1 deficiency has no effect compared to wild-type
malfunction
-
mice lacking either the alpha1 or alpha2 AMPK catalytic subunits demonstrate that AMPK is required for the effect of AICAR on glucose uptake. Transgenic mice expressing an inactive form of AMPK alpha2 subunit specifically in skeletal muscle develop impaired whole-body glucose tolerance and iInsulin resistance in skeletal muscle, particularly when fed a high-fat diet
malfunction
-
mutations in the gamma2 and gamma3 subunits result in glycogen storage disease
malfunction
-
mutations in the gamma2 and gamma3 subunits result in glycogen storage disease. Ten point mutations in gamma2 are associated with a glycogen storage cardiomyopathy and ventricular pre-excitation
malfunction
deletion of the SAK1 gene blocks nuclear translocation of Gal83 and signaling to Mig2
malfunction
knockout of AMPKalpha1 enhances, and, conversely, activator A-769662 inhibits monosodium urate crystal-induced inflammatory responses including IL-1beta and CXCL1 release in vitro and in vivo
malfunction
stabilization of MAPO1 occurs in AMPKalpha-knockdown cells even without N-methyl-N-nitrosourea treatment. Knockdown of the Flcn and Ampkalpha genes by specific siRNAs significantly suppresses an apoptotic response to N-methyl-N-nitrosourea
malfunction
the absence of functional AMPK may consequently cause a failure of distinct signaling pathways in red bood cells
malfunction
-
enzyme ablation increases Zika virus replication and reduces innate antiviral responses
malfunction
Mus musculus C57BL/6/129
-
knockout of AMPKalpha1 enhances, and, conversely, activator A-769662 inhibits monosodium urate crystal-induced inflammatory responses including IL-1beta and CXCL1 release in vitro and in vivo
-
malfunction
-
germline deletion of either AMPK beta1 or beta2 subunit isoforms results in reduced trabecular bone density and mass, but without effects on osteoclast or osteoblast numbers, as compared to wild-type littermate controls
-
malfunction
-
deletion of the SAK1 gene blocks nuclear translocation of Gal83 and signaling to Mig2
-
metabolism
-
active AMPK promotes the functional recovery of beta-cell oxidative metabolism and abrogates the induction of pathways that mediate cell death such as caspase-3 activation following exposure to nitric oxide
metabolism
-
is a key regulator of cellular and whole-body energy homeostasis that co-ordinates metabolic pathways in order to balance nutrient supply with energy demand
metabolism
-
is a key regulator of cellular and whole-body energy homeostasis that co-ordinates metabolic pathways in order to balance nutrient supply with energy demand
metabolism
-
is a key regulator of cellular and whole-body energy homeostasis that co-ordinates metabolic pathways in order to balance nutrient supply with energy demand
metabolism
-
is a key regulator of cellular and whole-body energy homeostasis that co-ordinates metabolic pathways in order to balance nutrient supply with energy demand
metabolism
-
is a metabolic energy regulator that can switch acid secretion off as cellular ATP levels fall. Secretagogue-induced acid secretion can be significantly reduced with AMPK activation and restored with its deactivation
metabolism
-
plays an important role in the regulation of both lipid and glucose metabolism. Direct link between AMPK activation and fatty acid metabolism. Has the potential of ameliorating insulin resistance and improving glucose homeostasis. A gain-of-function mutation in the gene encoding AMPK gamma3-subunit is reported to confer beneficial effects on muscle fuel metabolism
metabolism
-
SNF1 protein kinase cascade, sharing functional similarities with mammalian AMPK, which plays an important role in adapting the unicellular eukaryote to glucose starvation
physiological function
-
activation of AMPK alpha is necessary for hypoxia-induced AMPK-PKCzeta binding in alveolar epithelial cells. Overexpression of a dominant-negative AMPK alpha subunit construct prevents hypoxia-induced endocytosis of Na,K-ATPase, hypoxia-induced PKCzeta translocation to the plasma membrane and phosphorylation at Thr410
physiological function
-
activation of AMPK may prevent neuronal cell death and play a role as a survival factor in Parkinson's disease
physiological function
-
activation of AMPK may prevent neuronal cell death and play a role as a survival factor in Parkinson's disease. Overexpression of AMPK increases cell viability after exposure to 1-methyl-4-pyridinium in SH-SY5Y cells
physiological function
-
AMPK activation alters the expression of a variety of genes, including phosphoenolpyruvate carboxykinase in hepatocytes. Reduced AMPK activation may play an important role in the lipid accumulation and genesis of endothelial dysfunction in obese rats. Endothelial AMPK activity may inhibit glycerol-3-phosphate acyltransferase, required for de novo synthesis of diacylglycerol
physiological function
-
AMPK activation and subsequent increases in fatty acid beta-oxidation in skeletal muscle leads to increased energy expenditure in Uchl3-/- mice
physiological function
-
AMPK activation dramatically decreases de novo fatty acid synthesis and inactivates ACCalpha. AMPK activation modifies lipogenic gene expression including fatty acid synthase, glycerol-3-phosphate acyltransferase, and fatty acid binding protein-3. AMPK is able to inhibit fatty acid synthesis, an energy consuming process, in response to decreases in energy supply
physiological function
-
AMPK activation during oxidative stress may switch retinal pigment epithelium cells to a self-protected status. Alpha2 but not alpha1 AMPK is involved in retinal pigment epithelium cell phagocytosis and activation of alpha2 AMPK contributes to the inhibition of retinal pigment epithelium cell phagocytosis by oxidative stress
physiological function
-
AMPK activation induces vasodilatation and blood flow regulation in wild-type mice and this effect is abolished in AMPKalpha1 knockout mice. Chronic activation of AMPK in vivo attenuates ROS-mediated c-Jun N-terminal kinase activation and endothelial dysfunction in response to angiotensin II, which is abrogated in mice lacking the endothelial isoform of AMPKalpha1 or peroxisome proliferator gamma coactivator-1alpha, a target of AMPK that controls mitochondrial biogenesis. AMPK-deficient mice demonstrate impairment in postischemic fatty acid oxidation. In the setting of systolic pressure overload, left ventricular hypertrophy ensues and AMPKalpha2 knockout mice exhibit significantly increased overload-induced ventricular hypertrophy and decreased left ventricular ejection fraction. Isolated hearts of AMPK-deleted mice show increased apoptosis and dysfunction after ischemia/reperfusion. Role of AMPK in regulation of apoptosis that is an important mechanism of heart failure
physiological function
-
AMPK activation inhibits endothelial apoptosis in cultured cells. AMPK activation suppresses the basal and angiotensin II-enhanced superoxide anions in BAEC
physiological function
-
AMPK activation inhibits ICAM-1 mediated migration of lymphocytes across primary microvascular endothelial cells
physiological function
-
AMPK activation inhibits TNFa-stimulated leukocyte adhesion to aortic endothelial cells and ICAM-1 mediated migration of lymphocytes across primary microvascular endothelial cells
physiological function
-
AMPK is required for proper cell division and faithful chromosomal segregation during mitosis. Active form of the alpha-catalytic AMPK subunit (P-AMPKalpha-Thr172), but not its total form (AMPKalpha), transiently associates with several mitotic structures including centrosomes, spindle poles, the central spindle midzone and the midbody throughout all of the mitotic stages and cytokinesis in human cancer-derived epithelial cells
physiological function
-
AMPK is required to maintain normal bone density, but not through bone cell differentiation, and does not mediate powerful osteolytic effects of 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside
physiological function
-
AMPK is responsible for phosphorylation of site 2 in vivo. Both basal and 5-aminoimidazole-4-carboxamide riboside (AICAR)-stimulated site 2 phosphorylation is greatly reduced in muscles of AMPK-alpha2 knockout mice
physiological function
-
AMPK may play an important role in protecting endothelial cells against adverse effects of sustained hyperglycaemia, such as alterations in fatty acid metabolism, impaired Akt activation by insulin, increased caspase 3 activity and apoptosis. It may modulate endothelial cell energy supply. The AMPK-acetyl CoA carboxylase-malonyl CoA-carnitine palmitoyl-transferase 1 mechanism for regulating long-chain fatty acid oxidation, similar to that of muscle, operates in the endothelial cell and is regulated by AMPK under physiological conditions. One way to deal with endothelial lipotoxicity is to promote free fatty acid oxidation and ameliorate lipid accumulation in endothelial cells, which can be achieved by activating endothelial AMPK. AMPK inhibits fatty acid-induced increases in NF-kappaB transactivation in cultured human umbilical vein endothelial cells
physiological function
-
AMPK mediates cold-induced resistance to anorexigenic signalling in the hypothalamus. Activation of AMPK can contribute to hyperphagia. Inhibition of AMPK inhibits the hypoglycaemia-induced increase in the counter-regulatory hormones glucagon, corticosterone and catecholamines, causing a severe and prolonged hypoglycaemia
physiological function
-
critical role of AMPK in the survival of circulating erythrocytes. As compared with erythrocytes from wild-type littermates (ampk+/+), erythrocytes from AMPKalpha1-deficient mice (ampk-/-) are significantly more susceptible to the eryptotic effect of energy depletion. The ampk-/- mice are anemic despite excessive reticulocytosis, and they suffer from severe splenomegaly
physiological function
-
overexpression or ablation of the AMPK gamma3 subunit does not appear to play a critical role in defining mitochondrial content in resting skeletal muscle. Skeletal muscle mitochondrial content is unaltered in AMPK gamma3-/- mice
physiological function
-
plays a crucial role in carbon catabolite repression in yeast. cRKIN1 gene product from rye can rescue SNF1 mutation
physiological function
-
role for AMPK, in concert with other signals induced by IFNgamma, in mediating reduced epithelial barrier function in a cell model of chronic intestinal inflammation
physiological function
-
role of AMPK is that it monitors cellular energy status by sensing the relative cellular concentrations of AMP and ATP. The beta-subunits of AMPK contain a glycogen-binding domain, which is a regulatory domain that allows AMPK to act as a sensor of the status of cellular reserves of energy in the form of glycogen. The pool of AMPK that is bound to the glycogen particle is in an active state when glycogen particles are fully synthesized, causing phosphorylation of glycogen synthase at site 2 and providing a feedback inhibition of further extension of the outer chains of glycogen
physiological function
-
transgenic littermates overexpressing an alpha2AMPK kinase-dead (KD) have reduced skeletal muscle alpha2AMPK activity (50% in gastrocnemius and more than 80% in soleus and extensor digitorum longus) and acetyl-CoA carboxylase-2 Ser228 phosphorylation (90% in gastrocnemius). Obesity in response to high-fat feeding is not associated with impaired AMPK actions, obesity-induced lipid accumulation and insulin resistance are not exacerbated in AMPK KD mice
physiological function
AMP-activated protein kinase (AMPK) is a serine/threonine kinase that functions as a sensor to maintain energy balance at both the cellular and the whole-body levels. The enzyme is activated under circumstances with an increased cellular AMP:ATP ratio, such as metabolic stresses that inhibit ATP production (hypoxia, glucose deprivation, metabolic inhibitors etc.) and those that stimulate ATP consumption (exercise, cell growth and division etc.)
physiological function
AMP-activated protein kinase (AMPK) is a serine/threonine protein kinase that is essential in regulating energy metabolism in all eukaryotic cells
physiological function
AMP-activated protein kinase (AMPK) is a serine/threonine protein kinase that serves as a pleotropic regulator of whole body energy homoeostasis. The enzyme is allosterically regulated, kinetic analysis, overview. Binding of activator AMP to the gamma-subunit allows a small regulatory segment of the alpha-subunit (alpha2 residues 365-371) called the alpha-hook or alpha-RIM2 to directly interact with bound AMP and create an allosteric conformational change at the catalytic active site. As a consequence, the phosphorylated alpha-Thr172/174 can be protected from dephosphorylation by phosphatases and sustain its kinase activity for an extended period
physiological function
P54646; O43741; Q9UGI9
AMP-activated protein kinase (AMPK) is an energy-sensing serine/threonine protein kinase that plays a central role in whole-body energy homeostasis. The muscle-specific AMPK heterotrimeric complex (alpha2beta2gamma3) is involved in glucose and fat metabolism in skeletal muscle
physiological function
AMP-activated protein kinase (AMPK) is metabolic biosensor with anti-inflammatory activities. Gout is commonly associated with excesses in soluble urate and in nutrition, both of which suppress tissue AMPK activity. Gout is driven by macrophage-mediated inflammation transduced partly by NLRP3 inflammasome activation and interleukin-1beta release. AMP-activated protein kinase suppresses urate crystal-induced inflammation and transduces colchicine effects in macrophages. Activated AMPK is anti-inflammatory partly through inhibition of NF-kappaB
physiological function
-
AMP-activated protein kinase (AMPK) maintains the balance between ATP production and energy consumption in eukaryotic cells by responding to the rise of intracellular AMP
physiological function
AMPK is a cellular energy sensor that negatively regulates cell growth and proliferation. MAPO1, identified as a component involved in the induction of apoptosis, is stabilized by interaction with AMP-activated protein kinase (AMPK) and folliculin (FLCN). AMPK is activated during the process of O6-methylguanine-induced apoptosis and this activation is dependent on MAPO1 and folliculin. It is likely that the kinase activity of AMPK is involved in the degradation of MAPO1
physiological function
AMPK is a metabolic stress-sensing kinase with important functions for red blood cell survival. Identification of putative AMPK targets in hemoglobin-depleted lysates of erythrocytes, including metabolic enzymes, cytoskeletal proteins and enzymes involved in the oxidative stress response, cloning and recombinant expression. AMPK aids the function of red blood cells
physiological function
Q13131; Q9Y478; P54619
ischemia stimulates the AMP-activated protein kinase (AMPK), a serine/threonine kinase, sensing energy depletion and stimulating several cellular mechanisms to enhance energy production and to limit energy utilization. AMPK downregulates the epithelial Na+ channel ENaC mediated by the ubiquitin ligase Nedd4-2. AMPK regulates the heterotetrameric K+-channel KCNQ1/KCNE1. Wild-type and constitutively active AMPK significantly reduce KCNQ1/KCNE1-mediated currents and reduce KCNQ1 abundance in the cell membrane of transfected Xenopus laevis oocytes, overview. AMPK decreased the KCNQ1 protein abundance in the cell membrane via ubiquitin ligase Nedd4-2
physiological function
sex-specific regulation of AMP-activated protein kinase alpha in the Pacific oyster Crassostrea gigas. AMPKalpha activation might play a sex-dependent role in management of energy during gametogenesis in oyster
physiological function
sex-specific regulation of AMP-activated protein kinase in the Pacific oyster Crassostrea gigas
physiological function
Snf1 signaling specificity is mediated by localization of the different Snf1 isoforms. The phosphorylation of both zinc-finger transcriptions factors Mig1 and Mig2 is Snf1-dependent. Any of the three isoforms is capable of phosphorylating Mig1 in response to glucose stress. In contrast, the Gal83 isoform of Snf1 is both necessary and sufficient for the phosphorylation of Mig2 protein in response to alkaline stress
physiological function
Snf1 signaling specificity is mediated by localization of the different Snf1 isoforms. The phosphorylation of both zinc-finger transcriptions factors Mig1 and Mig2 is Snf1-dependent. Any of the three isoforms is capable of phosphorylating Mig1 in response to glucose stress. In contrast, the Gal83 isoform of Snf1 is both necessary and sufficient for the phosphorylation of Mig2 protein in response to alkaline stress. The nuclear localization of the Gal83 isoform of Snf1 is necessary for its ability to phosphorylate Mig2
physiological function
-
enzyme phosphorylation inhibits the activation of human hepatic stellate cell line LX-2. Enzyme activation in LX-2 cells inhibits autophagosome formation. Enzyme activation inhibits transforming growth factor-beta-induced intracellular lipid droplet depletion, which relies on increased autophagic flux, and finally inhibits transforming growth factor-beta-induced hepatic stellate cell activation
physiological function
-
intrinsic activation of the enzyme has functional protective effects in the reperfused atria when glucose is the only available energetic substrate whereas it is deleterious when palmitate is also available
physiological function
-
once activated, the enzyme suppresses the necessary enzymes involved in ATP-consuming anabolic pathways and enhances cellular ATP supply. Enzyme activation can facilitate bacterial eradication in sepsis and related inflammatory conditions associated with the inhibition of neutrophil activation and chemotaxis. The enzyme also inhibits nuclear factor-kappaB signaling and inflammation
physiological function
-
the enzyme couples inhibition of mitochondrial metabolism by hypoxia to acute hypoxic pulmonary vasoconstriction and progression of pulmonary hypertension. Inhibition of complex I of the mitochondrial electron transport chain activates the enzyme and inhibits Kv1.5 channels in pulmonary arterial myocytes. The enzyme is the primary mediator of reductions in Kv1.5 channels following inhibition of mitochondrial oxidative phosphorylation during hypoxia and by mitochondrial poisons
physiological function
-
the enzyme has an antiviral effect on Zika virus replication. The anti-Zika virus effect of enzyme signaling in endothelial cells is mediated by reduction of viral-induced glycolysis and enhanced innate antiviral responses
physiological function
Mus musculus C57BL/6/129
-
AMP-activated protein kinase (AMPK) is metabolic biosensor with anti-inflammatory activities. Gout is commonly associated with excesses in soluble urate and in nutrition, both of which suppress tissue AMPK activity. Gout is driven by macrophage-mediated inflammation transduced partly by NLRP3 inflammasome activation and interleukin-1beta release. AMP-activated protein kinase suppresses urate crystal-induced inflammation and transduces colchicine effects in macrophages. Activated AMPK is anti-inflammatory partly through inhibition of NF-kappaB
-
physiological function
-
AMPK is required to maintain normal bone density, but not through bone cell differentiation, and does not mediate powerful osteolytic effects of 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside
-
physiological function
-
Snf1 signaling specificity is mediated by localization of the different Snf1 isoforms. The phosphorylation of both zinc-finger transcriptions factors Mig1 and Mig2 is Snf1-dependent. Any of the three isoforms is capable of phosphorylating Mig1 in response to glucose stress. In contrast, the Gal83 isoform of Snf1 is both necessary and sufficient for the phosphorylation of Mig2 protein in response to alkaline stress
-
physiological function
-
Snf1 signaling specificity is mediated by localization of the different Snf1 isoforms. The phosphorylation of both zinc-finger transcriptions factors Mig1 and Mig2 is Snf1-dependent. Any of the three isoforms is capable of phosphorylating Mig1 in response to glucose stress. In contrast, the Gal83 isoform of Snf1 is both necessary and sufficient for the phosphorylation of Mig2 protein in response to alkaline stress. The nuclear localization of the Gal83 isoform of Snf1 is necessary for its ability to phosphorylate Mig2
-
additional information
alpha1-subunit containing AMPK isoforms possess higher basal activity and are less sensitive to desphosphorylation by phosphatases compared with alpha2-subunit containing heterotrimers. The alpha2-subunit-containing complexes are more readily activated by AMP than alpha1-complexes. Enzymatic activity, phosphatase sensitivity and kinetics of alpha1- and alpha2-containing AMPK isoforms, differential effect of activators, overview
additional information
-
residues Glu42, Arg81, Asp156, and Phe175 of the isolated kinase domain fragment have greater conformational flexibility in the closed state, with the hinge residue Gly116 exhibiting two conformational basins in the closed state, and Gly115 already in an active-closed state conformation even when the interlobe conformation is open
additional information
Saccharomyces cerevisiae expresses three isoforms of Snf1 kinase that differ by which beta subunit is present, Gal83, Sip1 or Sip2, abundance, activation, localization and signaling specificity of the three Snf1 isoforms, by quantitative immunoblotting and fluorescence microscopy, overview. The Gal83 containing isoform is the most abundant in all assays while the abundance of the Sip1 and Sip2 isoforms is typically underestimated especially in glass-bead extractions
additional information
Saccharomyces cerevisiae expresses three isoforms of Snf1 kinase that differ by which beta subunit is present, Gal83, Sip1 or Sip2, abundance, activation, localization and signaling specificity of the three Snf1 isoforms, by quantitative immunoblotting and fluorescence microscopy, overview. The Gal83 containing isoform is the most abundant in all assays while the abundance of the Sip1 and Sip2 isoforms is typically underestimated especially in glass-bead extractions
additional information
Saccharomyces cerevisiae expresses three isoforms of Snf1 kinase that differ by which beta subunit is present, Gal83, Sip1 or Sip2, abundance, activation, localization and signaling specificity of the three Snf1 isoforms, by quantitative immunoblotting and fluorescence microscopy, overview. The Gal83 containing isoform is the most abundant in all assays while the abundance of the Sip1 and Sip2 isoforms is typically underestimated especially in glass-bead extractions
additional information
-
Saccharomyces cerevisiae expresses three isoforms of Snf1 kinase that differ by which beta subunit is present, Gal83, Sip1 or Sip2, abundance, activation, localization and signaling specificity of the three Snf1 isoforms, by quantitative immunoblotting and fluorescence microscopy, overview. The Gal83 containing isoform is the most abundant in all assays while the abundance of the Sip1 and Sip2 isoforms is typically underestimated especially in glass-bead extractions
additional information
the AMPK alpha2 kinase domain exhibits a typical bilobal kinase fold and exists as a monomer in the crystal. Like the wild-type apo form, the T172D mutant apo form adopts the autoinhibited structure of the DFG-out conformation, with the Phe residue of the DFG motif anchored within the putative ATP-binding pocket
additional information
the beta-subunit exists in two isoforms (beta1 and beta2) and contains a carbohydrate-binding module (CBM) that interacts with glycogen. The two CBM isoforms (beta1- and beta2-CBM) are near identical in sequence and structure, yet show differences in carbohydrate-binding affinity. beta2-4CBM binds linear carbohydrates with -fold greater affinity than beta1-CBM and binds single alpha1,6-branched carbohydrates up to 30fold tighter
additional information
the beta-subunit exists in two isoforms (beta1 and beta2) and contains a carbohydrate-binding module (CBM) that interacts with glycogen. The two CBM isoforms (beta1- and beta2-CBM) are near identical in sequence and structure, yet show differences in carbohydrate-binding affinity. beta2-4CBM binds linear carbohydrates with -fold greater affinity than beta1-CBM and binds single alpha1,6-branched carbohydrates up to 30fold tighter
additional information
-
Saccharomyces cerevisiae expresses three isoforms of Snf1 kinase that differ by which beta subunit is present, Gal83, Sip1 or Sip2, abundance, activation, localization and signaling specificity of the three Snf1 isoforms, by quantitative immunoblotting and fluorescence microscopy, overview. The Gal83 containing isoform is the most abundant in all assays while the abundance of the Sip1 and Sip2 isoforms is typically underestimated especially in glass-bead extractions
-
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). AAPK1_HUMAN
559
0
64009
Swiss-Prot
other Location (Reliability: 4)
AAPK1_MOUSE
559
0
63929
Swiss-Prot
other Location (Reliability: 4)
AAPK1_PIG
385
0
44226
Swiss-Prot
other Location (Reliability: 2)
AAPK1_PONAB
554
0
63393
Swiss-Prot
other Location (Reliability: 3)
AAPK1_RAT
559
0
63973
Swiss-Prot
other Location (Reliability: 4)
AAPK2_HUMAN
552
0
62320
Swiss-Prot
other Location (Reliability: 1)
AAPK2_MOUSE
552
0
62022
Swiss-Prot
other Location (Reliability: 1)
AAPK2_PIG
552
0
62325
Swiss-Prot
other Location (Reliability: 1)
AAPK2_PONAB
552
0
62302
Swiss-Prot
other Location (Reliability: 1)
AAPK2_RAT
552
0
62258
Swiss-Prot
other Location (Reliability: 1)
A0A0M4FMJ6_ORENI
557
0
62788
TrEMBL
other Location (Reliability: 2)
A0A250Y2Q7_CASCN
552
0
62419
TrEMBL
other Location (Reliability: 1)
A0A6J0AP28_VICPA
415
0
47283
TrEMBL
other Location (Reliability: 2)
A0A8C1IZ68_CYPCA
562
0
64335
TrEMBL
other Location (Reliability: 3)
A0A8C0M2F3_CANLF
552
0
62310
TrEMBL
other Location (Reliability: 1)
A0A8B8SC13_CAMFR
415
0
47283
TrEMBL
other Location (Reliability: 2)
B4F6W2_XENTR
551
0
62377
TrEMBL
other Location (Reliability: 1)
A0A671QZG0_9TELE
560
0
63832
TrEMBL
other Location (Reliability: 2)
A0A8B9Z5H1_9AVES
516
0
59061
TrEMBL
other Location (Reliability: 4)
A0A7K6ZEZ1_9AVES
517
0
59170
TrEMBL
other Location (Reliability: 3)
A0A8C0BJN6_9AVES
563
0
65200
TrEMBL
other Location (Reliability: 1)
A0A2K5R140_CEBIM
574
0
65591
TrEMBL
other Location (Reliability: 4)
H9FBH3_MACMU
551
0
62922
TrEMBL
other Location (Reliability: 1)
A0A7L1YC84_9PASS
552
0
62374
TrEMBL
other Location (Reliability: 1)
F7D386_MACMU
552
0
62320
TrEMBL
other Location (Reliability: 1)
A0A8C7L8N3_ONCKI
536
0
61264
TrEMBL
other Location (Reliability: 2)
A0A8C7I269_ONCKI
558
0
63562
TrEMBL
other Location (Reliability: 2)
A0A7K8FIQ4_9CORV
561
0
63983
TrEMBL
other Location (Reliability: 5)
A0A091UJS9_PHALP
462
0
52815
TrEMBL
other Location (Reliability: 3)
A0A662YSH4_ACIRT
490
0
54981
TrEMBL
other Location (Reliability: 1)
H2PZ45_PANTR
552
0
62320
TrEMBL
other Location (Reliability: 1)
A0A7K8MEQ0_9CORV
551
0
62193
TrEMBL
other Location (Reliability: 1)
A0A669DJ57_ORENI
561
0
63571
TrEMBL
other Location (Reliability: 2)
A0A7L0J553_PIPCL
561
0
64011
TrEMBL
other Location (Reliability: 5)
A0A8C8J0Y2_ONCTS
566
0
64193
TrEMBL
other Location (Reliability: 2)
A0A852I7P6_9PASS
551
0
62165
TrEMBL
other Location (Reliability: 1)
A0A5F5XED4_FELCA
530
0
60149
TrEMBL
other Location (Reliability: 2)
A0A2Y9HRW6_NEOSC
559
0
64008
TrEMBL
other Location (Reliability: 4)
A0A671V1A8_SPAAU
557
0
62727
TrEMBL
other Location (Reliability: 2)
A0A8C8SZ19_PERMB
522
0
59682
TrEMBL
other Location (Reliability: 3)
A0A7L1N9A6_RHICY
560
0
64113
TrEMBL
other Location (Reliability: 5)
A0A7J8F328_ROUAE
550
0
62793
TrEMBL
other Location (Reliability: 1)
A0A7L3M460_9PASS
554
0
63162
TrEMBL
other Location (Reliability: 5)
A0A7K9H6V9_9AVES
552
0
62389
TrEMBL
other Location (Reliability: 2)
A0A6P6CZ59_PTEVA
536
0
60780
TrEMBL
other Location (Reliability: 3)
A0A2Y9G4G5_TRIMA
565
0
64431
TrEMBL
other Location (Reliability: 1)
A0A3Q1IUA2_ANATE
557
0
62731
TrEMBL
other Location (Reliability: 2)
A0A6J2E423_ZALCA
574
0
65592
TrEMBL
other Location (Reliability: 4)
A0A672RWB3_SINGR
459
0
52592
TrEMBL
other Location (Reliability: 1)
A0A6P8VV18_GYMAC
573
0
64721
TrEMBL
other Location (Reliability: 2)
A0A6P8PWB1_GEOSA
460
0
52729
TrEMBL
other Location (Reliability: 1)
L8IZB9_9CETA
569
0
64964
TrEMBL
other Location (Reliability: 2)
A0A341CC44_NEOAA
462
0
52084
TrEMBL
other Location (Reliability: 1)
A0A5N3WAK0_MUNMU
552
0
62321
TrEMBL
other Location (Reliability: 1)
A0A8I3MG89_CANLF
574
0
65640
TrEMBL
other Location (Reliability: 4)
A0A1A6HCU4_NEOLE
497
0
56579
TrEMBL
other Location (Reliability: 3)
A0A7K5R3T8_9PASE
547
0
61853
TrEMBL
other Location (Reliability: 2)
A0A8C7XWL1_9TELE
572
0
64601
TrEMBL
other Location (Reliability: 2)
A0A6P9BJP3_PANGU
487
0
55371
TrEMBL
other Location (Reliability: 2)
A0A665WZ01_ECHNA
573
0
64791
TrEMBL
other Location (Reliability: 2)
A0A665WZ01_ECHNA
573
0
64791
TrEMBL
other Location (Reliability: 2)
A0A8C3QIU7_9PASS
561
0
63983
TrEMBL
other Location (Reliability: 5)
A0A8C2EKR6_CYPCA
559
0
63053
TrEMBL
other Location (Reliability: 2)
A0A8C1Q9X6_CYPCA
616
0
70082
TrEMBL
other Location (Reliability: 2)
A0A8C6PL33_NOTFU
570
0
64253
TrEMBL
other Location (Reliability: 4)
A0A8D0DEE2_SANLU
498
0
56679
TrEMBL
other Location (Reliability: 2)
A0A7J6BYD1_9TELE
529
0
59764
TrEMBL
other Location (Reliability: 2)
A0A8I5ZZZ5_RAT
528
0
60667
TrEMBL
other Location (Reliability: 1)
A0A1S3KHY4_SALSA
558
0
62962
TrEMBL
other Location (Reliability: 2)
A0A1S3KY68_SALSA
583
0
65672
TrEMBL
other Location (Reliability: 2)
A0A7L1UYT0_SITEU
517
0
59173
TrEMBL
other Location (Reliability: 3)
A0A7K7VU43_9AVES
517
0
59170
TrEMBL
other Location (Reliability: 3)
A0A6P8PWF0_GEOSA
365
0
42023
TrEMBL
Secretory Pathway (Reliability: 3)
A0A8C1DKR0_CYPCA
566
0
64547
TrEMBL
other Location (Reliability: 2)
A0A7N6A9P4_ANATE
573
0
64724
TrEMBL
other Location (Reliability: 2)
A0A7N6A9P4_ANATE
573
0
64724
TrEMBL
other Location (Reliability: 2)
A0A7N5P827_AILME
559
0
64012
TrEMBL
other Location (Reliability: 4)
U6CQI5_NEOVI
386
0
44100
TrEMBL
other Location (Reliability: 2)
A0A3B1KK92_ASTMX
573
0
65079
TrEMBL
other Location (Reliability: 2)
A0A671Q8H5_9TELE
573
0
65133
TrEMBL
other Location (Reliability: 2)
A0A7L3Y699_9AVES
551
0
62208
TrEMBL
other Location (Reliability: 1)
A0A8C4BA89_9TELE
555
0
63356
TrEMBL
other Location (Reliability: 2)
A0A6P7EWT1_SHEEP
415
0
47297
TrEMBL
other Location (Reliability: 2)
A0A3P9KIN2_ORYLA
600
0
67383
TrEMBL
Mitochondrion (Reliability: 3)
A0A091RWQ0_NESNO
459
0
52226
TrEMBL
other Location (Reliability: 3)
A0A6J0TDB9_9SAUR
554
0
62567
TrEMBL
other Location (Reliability: 5)
A0A2I0MCC0_COLLI
480
0
54892
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8B9G7Q8_9PSIT
532
0
61032
TrEMBL
other Location (Reliability: 5)
M7AZT2_CHEMY
530
0
60189
TrEMBL
other Location (Reliability: 1)
A0A315VTW8_GAMAF
620
0
69688
TrEMBL
other Location (Reliability: 2)
A0A8C0V1L7_CYACU
556
0
63346
TrEMBL
other Location (Reliability: 1)
A0A7L0RY48_GLABR
560
0
63996
TrEMBL
other Location (Reliability: 4)
A0A8C3GYA3_9CORV
692
0
75838
TrEMBL
other Location (Reliability: 1)
A0A8C8G9C4_ONCTS
558
0
63396
TrEMBL
other Location (Reliability: 4)
A0A7F8R694_LEPWE
462
0
52093
TrEMBL
other Location (Reliability: 1)
A0A7K5B9U1_9FURN
561
0
63983
TrEMBL
other Location (Reliability: 5)
A0A7L1NQY4_RHICY
432
0
49131
TrEMBL
other Location (Reliability: 1)
A0A851MDR3_9DEND
538
0
61337
TrEMBL
other Location (Reliability: 3)
A0A8I5NY83_PAPAN
574
0
65652
TrEMBL
other Location (Reliability: 4)
A0A6I9YV94_9SAUR
537
0
60924
TrEMBL
other Location (Reliability: 3)
A0A4W5QE66_9TELE
560
0
63156
TrEMBL
other Location (Reliability: 2)
A0A3Q0S3J3_AMPCI
551
0
62148
TrEMBL
other Location (Reliability: 2)
A0A3Q1JRI8_ANATE
562
0
63545
TrEMBL
other Location (Reliability: 2)
A0A7K8A1M6_9PASE
561
0
63983
TrEMBL
other Location (Reliability: 5)
A0A8C3JTT8_9CHAR
452
0
51511
TrEMBL
other Location (Reliability: 2)
A0A8C3K6V7_9CHAR
516
0
59112
TrEMBL
other Location (Reliability: 4)
A0A8J6AJL1_GALPY
631
0
71562
TrEMBL
other Location (Reliability: 4)
A0A8J6AC73_GALPY
552
0
62242
TrEMBL
other Location (Reliability: 1)
U6CXD0_NEOVI
390
0
43747
TrEMBL
other Location (Reliability: 2)
A0A091X7X0_OPIHO
458
0
52482
TrEMBL
other Location (Reliability: 3)
A0A091WQJ5_OPIHO
517
0
59213
TrEMBL
other Location (Reliability: 3)
A0A6I9KPC4_CHRAS
574
0
65578
TrEMBL
other Location (Reliability: 4)
C9W108_PIG
552
0
62325
TrEMBL
other Location (Reliability: 1)
A0A2K6A384_MANLE
559
0
63995
TrEMBL
other Location (Reliability: 4)
A0A8B7QGV6_HIPAR
559
0
64022
TrEMBL
other Location (Reliability: 4)
A0A8B9W0V5_BOSMU
528
0
59754
TrEMBL
other Location (Reliability: 1)
A0A0S7L6D5_9TELE
591
0
66756
TrEMBL
other Location (Reliability: 5)
A0A7K6FFF9_9CORV
517
0
59183
TrEMBL
other Location (Reliability: 3)
A0A8C0SJ73_CANLF
559
0
64008
TrEMBL
other Location (Reliability: 4)
A0A5A9P916_9TELE
570
0
64718
TrEMBL
other Location (Reliability: 2)
A0A8B9CXM9_9AVES
552
0
62387
TrEMBL
other Location (Reliability: 1)
A0A834AFX9_9CHIR
462
0
52064
TrEMBL
other Location (Reliability: 1)
A0A668AX07_9TELE
560
0
63581
TrEMBL
other Location (Reliability: 2)
A0A151MX04_ALLMI
547
0
62535
TrEMBL
other Location (Reliability: 1)
A0A811ZMG0_NYCPR
552
0
62340
TrEMBL
other Location (Reliability: 1)
A0A6P4XSL6_PANPR
536
0
61276
TrEMBL
other Location (Reliability: 3)
A0A665VW28_ECHNA
576
0
64776
TrEMBL
other Location (Reliability: 4)
A0A7K4QYZ1_9TYRA
552
0
62404
TrEMBL
other Location (Reliability: 1)
A0A3Q7WCR7_URSAR
559
0
64042
TrEMBL
other Location (Reliability: 4)
A0A091QC28_MERNU
521
0
59015
TrEMBL
other Location (Reliability: 3)
A0A8D0KXI9_STROC
543
0
61326
TrEMBL
other Location (Reliability: 1)
A0A8C2VDM5_CHILA
536
0
61376
TrEMBL
other Location (Reliability: 2)
A0A7L2ENU7_ANTMN
552
0
62334
TrEMBL
other Location (Reliability: 1)
A0A7L1MEN2_BOMGA
471
0
53842
TrEMBL
other Location (Reliability: 2)
A0A8B8U7T1_CAMFR
552
0
62336
TrEMBL
other Location (Reliability: 1)
A0A7L3AIS6_9AVES
560
0
63982
TrEMBL
other Location (Reliability: 4)
A0A7K8E2V0_LEURO
561
0
63983
TrEMBL
other Location (Reliability: 5)
A0A3P9CWR9_9CICH
557
0
62804
TrEMBL
other Location (Reliability: 2)
A0A3B4DG22_PYGNA
552
0
62208
TrEMBL
other Location (Reliability: 2)
A0A6J3B628_VICPA
538
0
61103
TrEMBL
other Location (Reliability: 4)
A0A6P3VZP8_CLUHA
568
0
64577
TrEMBL
other Location (Reliability: 2)
A0A8C5WPE5_LATLA
560
0
63191
TrEMBL
other Location (Reliability: 1)
A0A091KC63_9GRUI
521
0
58994
TrEMBL
other Location (Reliability: 3)
A0A8C3TJU9_CHESE
551
0
62208
TrEMBL
other Location (Reliability: 1)
A0A0P7Z231_SCLFO
558
0
63459
TrEMBL
other Location (Reliability: 2)
A0A8B9K5F2_ASTMX
566
0
63690
TrEMBL
other Location (Reliability: 3)
V8P811_OPHHA
528
0
59849
TrEMBL
Secretory Pathway (Reliability: 3)
A0A671N781_9TELE
535
0
60602
TrEMBL
Secretory Pathway (Reliability: 5)
A0A851NW99_9GALL
552
0
62353
TrEMBL
other Location (Reliability: 1)
G3HHG7_CRIGR
477
0
55465
TrEMBL
other Location (Reliability: 4)
A0A3L8S7I3_CHLGU
561
0
63922
TrEMBL
other Location (Reliability: 5)
A0A7K4LNU4_9AVES
561
0
64023
TrEMBL
other Location (Reliability: 4)
A0A7L1YS96_9PASS
473
0
53972
TrEMBL
other Location (Reliability: 3)
A0A8C4BEQ6_9TELE
571
0
64850
TrEMBL
other Location (Reliability: 2)
A0A7L4J2R1_9PASS
551
0
62223
TrEMBL
other Location (Reliability: 1)
A0A3P9KKC7_ORYLA
572
0
64617
TrEMBL
other Location (Reliability: 2)
A0A8B7AR71_ORYAF
574
0
65570
TrEMBL
other Location (Reliability: 4)
A0A7K8WWE3_9FURN
552
0
62374
TrEMBL
other Location (Reliability: 1)
A0A8C5EKS0_9TELE
528
0
60247
TrEMBL
other Location (Reliability: 2)
A0A6A5EFT9_PERFL
572
0
64626
TrEMBL
other Location (Reliability: 2)
A0A8C3V8V3_CATUS
561
0
63983
TrEMBL
other Location (Reliability: 5)
A0A091NP37_APAVI
400
0
44880
TrEMBL
other Location (Reliability: 2)
A0A8C8Z7Q1_PROSS
559
0
64036
TrEMBL
other Location (Reliability: 4)
A0A3Q3F1Z4_9LABR
557
0
62744
TrEMBL
other Location (Reliability: 2)
A0A851WA43_9CORV
551
0
62253
TrEMBL
other Location (Reliability: 1)
A0A4D9EHU0_9SAUR
551
0
62277
TrEMBL
other Location (Reliability: 1)
A0A2I2UPC3_FELCA
552
0
62300
TrEMBL
other Location (Reliability: 1)
A0A7M4FC76_CROPO
528
0
60568
TrEMBL
other Location (Reliability: 1)
A0A671UY80_SPAAU
552
0
62211
TrEMBL
other Location (Reliability: 2)
A0A803TI08_ANOCA
732
0
83479
TrEMBL
other Location (Reliability: 1)
A0A7J8F2I0_ROUAE
415
0
47285
TrEMBL
other Location (Reliability: 2)
A0A3B4VKP8_SERDU
557
0
62785
TrEMBL
other Location (Reliability: 2)
A0A8C9HS96_9PRIM
630
0
70851
TrEMBL
other Location (Reliability: 2)
A0A8C2XQD6_CYCLU
556
0
62390
TrEMBL
other Location (Reliability: 2)
A0A8C7TAY8_ONCMY
569
0
64043
TrEMBL
other Location (Reliability: 3)
A0A8B9VTI0_9AVES
559
0
63901
TrEMBL
other Location (Reliability: 4)
K7F737_PELSI
461
0
51941
TrEMBL
other Location (Reliability: 1)
K7F737_PELSI
461
0
51941
TrEMBL
other Location (Reliability: 1)
A0A8C6EAJ7_MOSMO
574
0
65548
TrEMBL
other Location (Reliability: 5)
A0A6J2W752_CHACN
563
0
64075
TrEMBL
other Location (Reliability: 2)
A0A7K4KBR2_9AVES
502
0
56323
TrEMBL
other Location (Reliability: 3)
A0A7N8Y2G1_9TELE
563
0
63712
TrEMBL
other Location (Reliability: 2)
A0A091VTI2_NIPNI
517
0
59253
TrEMBL
other Location (Reliability: 3)
A0A091G1U3_9AVES
560
0
63966
TrEMBL
other Location (Reliability: 4)
A0A2I4CPB4_9TELE
557
0
62810
TrEMBL
other Location (Reliability: 2)
A0A7K5PD53_9CORV
552
0
62338
TrEMBL
other Location (Reliability: 1)
A0A668AE57_9TELE
541
0
61742
TrEMBL
other Location (Reliability: 2)
A0A673ZYL5_SALTR
536
0
61253
TrEMBL
other Location (Reliability: 2)
A0A667Z4H9_9TELE
551
1
62476
TrEMBL
other Location (Reliability: 2)
A0A673Y6E9_SALTR
558
0
62814
TrEMBL
other Location (Reliability: 2)
A0A8C3RKV5_CHESE
551
0
62859
TrEMBL
other Location (Reliability: 1)
G1PPL4_MYOLU
517
0
59182
TrEMBL
other Location (Reliability: 3)
A0A7L2AKZ4_9GRUI
517
0
59283
TrEMBL
other Location (Reliability: 3)
A0A7L1W254_9PASS
561
0
63970
TrEMBL
Mitochondrion (Reliability: 5)
A0A6P7QKZ1_MUSCR
415
0
47236
TrEMBL
other Location (Reliability: 2)
A0A6P9DVW7_PANGU
550
0
62742
TrEMBL
other Location (Reliability: 2)
A0A6P4X6F4_PANPR
471
0
53959
TrEMBL
other Location (Reliability: 4)
A0A6P4WFD6_PANPR
Felis pardus
477
0
53814
TrEMBL
other Location (Reliability: 1)
A0A6P4WFD6_PANPR
477
0
53814
TrEMBL
other Location (Reliability: 1)
A0A665VVR9_ECHNA
533
0
60136
TrEMBL
other Location (Reliability: 2)
A0A452GMZ9_9SAUR
551
0
62300
TrEMBL
other Location (Reliability: 1)
A0A8C5C502_GADMO
574
0
64719
TrEMBL
other Location (Reliability: 4)
A0A8C2BR95_CYPCA
552
0
63088
TrEMBL
other Location (Reliability: 2)
A0A8B8U6Q7_CAMFR
431
0
49092
TrEMBL
other Location (Reliability: 1)
A0A2K6SQ69_SAIBB
566
0
64538
TrEMBL
other Location (Reliability: 1)
A0A2K6GBP0_PROCO
559
0
64045
TrEMBL
other Location (Reliability: 4)
A0A2K6SQ72_SAIBB
458
0
52435
TrEMBL
other Location (Reliability: 1)
A0A087RDG0_APTFO
517
0
59199
TrEMBL
other Location (Reliability: 3)
A0A7K8AYM6_9CORV
561
0
64025
TrEMBL
other Location (Reliability: 5)
A0A7L2VPM3_9AVES
551
0
62202
TrEMBL
other Location (Reliability: 1)
A0A7J8AAR3_PIPKU
439
0
49466
TrEMBL
Mitochondrion (Reliability: 4)
A0A2K5JE08_COLAP
545
0
61392
TrEMBL
other Location (Reliability: 2)
A0A6J2PGZ0_COTGO
557
0
62832
TrEMBL
other Location (Reliability: 2)
A0A7J7F5H2_DICBM
488
0
55231
TrEMBL
other Location (Reliability: 2)
A0A850YG92_AEGCA
383
0
43402
TrEMBL
other Location (Reliability: 3)
A0A1S3LVS0_SALSA
563
0
63597
TrEMBL
other Location (Reliability: 4)
A0A146P626_FUNHE
564
0
63842
TrEMBL
other Location (Reliability: 2)
A0A6J1ZCV9_ACIJB
462
0
52090
TrEMBL
other Location (Reliability: 1)
F7IRM3_CALJA
552
0
62290
TrEMBL
other Location (Reliability: 1)
A0A6P3EDP8_SHEEP
559
0
64006
TrEMBL
other Location (Reliability: 4)
A0A8B9KD07_ASTMX
573
0
65079
TrEMBL
other Location (Reliability: 2)
H0VFT6_CAVPO
552
0
62368
TrEMBL
other Location (Reliability: 1)
A0A091KH79_EGRGA
517
0
59170
TrEMBL
other Location (Reliability: 3)
A0A6P3IIF3_BISBI
552
0
62321
TrEMBL
other Location (Reliability: 1)
A0A7L3SYV7_RISTR
551
0
62217
TrEMBL
other Location (Reliability: 1)
A0A672TWI1_STRHB
462
0
52092
TrEMBL
other Location (Reliability: 1)
A0A3P8V0Y9_CYNSE
551
0
62235
TrEMBL
other Location (Reliability: 2)
A0A8C7FLD3_ONCKI
559
0
63139
TrEMBL
other Location (Reliability: 2)
A0A8C4BE20_9TELE
572
0
65047
TrEMBL
other Location (Reliability: 2)
A0A093K585_STRCA
464
0
53051
TrEMBL
other Location (Reliability: 3)
A0A8C0ETA9_BUBBB
462
0
52096
TrEMBL
other Location (Reliability: 1)
H2PFE9_PONAB
630
0
70964
TrEMBL
other Location (Reliability: 2)
A0A6D2W979_PANTR
552
0
62320
TrEMBL
other Location (Reliability: 1)
A0A7L2QHG6_9PASS
390
0
44296
TrEMBL
other Location (Reliability: 2)
A0A484CF87_PERFV
837
0
95205
TrEMBL
other Location (Reliability: 2)
A0A851KB81_VIDCH
551
0
62223
TrEMBL
other Location (Reliability: 1)
A0A8C8J4R1_ONCTS
545
0
62255
TrEMBL
other Location (Reliability: 2)
A0A7K8CZI4_9CORV
561
0
64013
TrEMBL
other Location (Reliability: 5)
A0A851VBL2_9PASS
560
0
63171
TrEMBL
other Location (Reliability: 2)
A0A8C9PED3_SPEDA
554
1
63856
TrEMBL
Mitochondrion (Reliability: 5)
A0A8C4M6F8_EQUAS
552
0
62346
TrEMBL
other Location (Reliability: 1)
A0A096MX27_PAPAN
557
0
62907
TrEMBL
other Location (Reliability: 1)
A0A8C3WXI6_9CETA
552
0
62331
TrEMBL
other Location (Reliability: 1)
A0A3Q0CDP0_MESAU
559
0
63982
TrEMBL
other Location (Reliability: 4)
A0A7N6FK50_ANATE
566
0
64153
TrEMBL
other Location (Reliability: 1)
A0A8C7A6F3_NEOVI
559
0
64040
TrEMBL
other Location (Reliability: 4)
A0A556TV28_BAGYA
923
0
104428
TrEMBL
other Location (Reliability: 3)
A0A226PAG8_COLVI
560
0
64121
TrEMBL
other Location (Reliability: 5)
A0A672FP20_SALFA
502
0
56479
TrEMBL
other Location (Reliability: 2)
A0A3Q3CN78_HAPBU
571
0
64552
TrEMBL
other Location (Reliability: 2)
A0A6B0RZY3_9CETA
640
0
72809
TrEMBL
other Location (Reliability: 1)
A0A4Z2GKR1_9TELE
576
0
64823
TrEMBL
other Location (Reliability: 2)
A0A3M0KTW7_HIRRU
529
0
60164
TrEMBL
other Location (Reliability: 5)
A0A852GE59_9CHAR
551
0
62217
TrEMBL
other Location (Reliability: 1)
A0A8B9MJW8_9AVES
527
0
60255
TrEMBL
other Location (Reliability: 2)
A0A5A9NIR0_9TELE
580
0
65749
TrEMBL
other Location (Reliability: 3)
A0A8C4I2Y7_DICLA
562
0
63684
TrEMBL
other Location (Reliability: 2)
A0A7L4JQT0_9AVES
551
0
62275
TrEMBL
other Location (Reliability: 1)
A0A7K5PNC7_9CORV
517
0
59160
TrEMBL
other Location (Reliability: 3)
A0A673WMQ1_SALTR
544
0
61371
TrEMBL
other Location (Reliability: 2)
A0A7J5ZK76_AMEME
546
0
61616
TrEMBL
other Location (Reliability: 1)
A0A2K5UX98_MACFA
552
0
62320
TrEMBL
other Location (Reliability: 1)
A0A7L2H529_SAGSE
560
0
63972
TrEMBL
other Location (Reliability: 3)
A0A6J3JD70_SAPAP
552
0
62320
TrEMBL
other Location (Reliability: 1)
A0A3Q1ERL7_9TELE
573
0
64770
TrEMBL
other Location (Reliability: 2)
A0A8C8DNI7_9TELE
582
0
65815
TrEMBL
other Location (Reliability: 2)
A0A7L0KV72_9SYLV
551
0
62122
TrEMBL
other Location (Reliability: 1)
A0A8B8X863_BALMU
415
0
47240
TrEMBL
other Location (Reliability: 2)
A0A091KB32_COLST
517
0
59277
TrEMBL
other Location (Reliability: 3)
A0A6P9DLK6_PANGU
526
0
60241
TrEMBL
other Location (Reliability: 3)
A0A6P4XML6_PANPR
574
0
65566
TrEMBL
other Location (Reliability: 4)
H2UY55_TAKRU
575
0
64932
TrEMBL
other Location (Reliability: 4)
A0A674NAF6_TAKRU
558
0
63454
TrEMBL
other Location (Reliability: 2)
A0A8D0H810_SPHPU
552
0
62528
TrEMBL
other Location (Reliability: 2)
H0YVD1_TAEGU
538
0
61139
TrEMBL
other Location (Reliability: 2)
A0A8C5D0C6_GADMO
606
0
67767
TrEMBL
other Location (Reliability: 1)
A0A8C2BT18_CYPCA
523
0
59837
TrEMBL
other Location (Reliability: 2)
A0A8C1PMW3_CYPCA
559
0
63033
TrEMBL
other Location (Reliability: 2)
A0A8C1TMR1_CYPCA
627
0
71396
TrEMBL
other Location (Reliability: 2)
A0A8C6PL42_NOTFU
567
0
63881
TrEMBL
other Location (Reliability: 2)
A0A7J8A9R2_PIPKU
552
0
62391
TrEMBL
other Location (Reliability: 2)
A0A1U7S978_ALLSI
563
0
64400
TrEMBL
other Location (Reliability: 4)
A0A668VUD4_OREAU
577
0
64985
TrEMBL
other Location (Reliability: 2)
A0A8D0ACS6_SANLU
545
0
61940
TrEMBL
other Location (Reliability: 2)
A0A3P8PRU8_ASTCA
557
0
62804
TrEMBL
other Location (Reliability: 2)
A0A8D2NMZ2_ZOSLA
540
0
61056
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8C9ER30_PAVCR
552
0
62417
TrEMBL
other Location (Reliability: 2)
A0A8C5TL76_9PASS
537
0
60206
TrEMBL
Mitochondrion (Reliability: 2)
A0A7K9GS94_LOXLE
561
0
63899
TrEMBL
other Location (Reliability: 4)
A0A4W4G5E1_ELEEL
548
0
62439
TrEMBL
other Location (Reliability: 2)
A0A5E4C6F2_MARMO
552
0
62389
TrEMBL
other Location (Reliability: 1)
Q5U5E3_XENLA
560
0
64057
TrEMBL
other Location (Reliability: 4)
A0A6P4XMM9_PANPR
473
0
53962
TrEMBL
other Location (Reliability: 1)
A0A4U5VCU2_COLLU
576
0
65137
TrEMBL
other Location (Reliability: 1)
A0A4X1T2X0_PIG
574
0
65488
TrEMBL
other Location (Reliability: 4)
A0A8B7QHE1_HIPAR
458
0
52418
TrEMBL
other Location (Reliability: 1)
A0A4W2FCL1_BOBOX
559
0
64006
TrEMBL
other Location (Reliability: 4)
A8D245_SHEEP
552
0
62303
TrEMBL
other Location (Reliability: 1)
A0A8B9KCY9_ASTMX
542
0
62044
TrEMBL
other Location (Reliability: 2)
A0A7K5YXP1_9AVES
560
0
63954
TrEMBL
other Location (Reliability: 4)
A0A6I9ZKA1_ACIJB
536
0
61282
TrEMBL
other Location (Reliability: 3)
A0A663F6C0_AQUCH
454
0
51794
TrEMBL
other Location (Reliability: 1)
A0A6P6RPZ4_CARAU
566
0
63847
TrEMBL
other Location (Reliability: 3)
A0A851X5X4_EOLRO
551
0
62287
TrEMBL
other Location (Reliability: 1)
A0A4U1EK47_MONMO
452
0
52517
TrEMBL
other Location (Reliability: 4)
A0A8C7L2U7_ONCKI
559
0
63328
TrEMBL
other Location (Reliability: 2)
W5PHS9_SHEEP
559
0
64006
TrEMBL
other Location (Reliability: 4)
A0A7J5XDK7_DISMA
549
0
61932
TrEMBL
other Location (Reliability: 2)
A0A8D3AEH2_SCOMX
564
0
64123
TrEMBL
other Location (Reliability: 3)
A0A8I5TUE9_PONAB
615
0
69160
TrEMBL
other Location (Reliability: 2)
A0A444TX80_ACIRT
742
0
84144
TrEMBL
other Location (Reliability: 2)
U3JH39_FICAL
561
0
63983
TrEMBL
other Location (Reliability: 5)
A0A7K7B633_9AVES
517
0
59170
TrEMBL
other Location (Reliability: 3)
A0A851MVA3_9DEND
517
0
59236
TrEMBL
other Location (Reliability: 3)
A0A8C3VNT4_9CETA
559
0
63992
TrEMBL
other Location (Reliability: 4)
A0A7J8F2J5_ROUAE
458
0
52390
TrEMBL
other Location (Reliability: 1)
A0A8C3W0Y0_9CETA
574
0
65492
TrEMBL
other Location (Reliability: 4)
A0A3Q7NY54_CALUR
559
0
64022
TrEMBL
other Location (Reliability: 4)
A0A8C8SUI5_9SAUR
551
0
62190
TrEMBL
other Location (Reliability: 1)
A0A8C6ZW59_NOTPE
549
0
61842
TrEMBL
other Location (Reliability: 2)
A0A4W5QCY5_9TELE
572
0
64516
TrEMBL
other Location (Reliability: 1)
A0A2U4AXF2_TURTR
559
0
63976
TrEMBL
other Location (Reliability: 4)
A0A3Q1APT7_AMPOC
573
0
64751
TrEMBL
other Location (Reliability: 2)
A0A8C7T2E9_ONCMY
572
0
64358
TrEMBL
other Location (Reliability: 4)
A0A8C2ZJZ8_CYCLU
575
0
64762
TrEMBL
other Location (Reliability: 2)
I3MFA4_ICTTR
552
0
62403
TrEMBL
other Location (Reliability: 1)
A0A8C7SZM5_ONCMY
553
0
62289
TrEMBL
other Location (Reliability: 2)
A0A3N0XHV4_ANAGA
570
0
64778
TrEMBL
other Location (Reliability: 2)
A0A673CCJ6_9TELE
552
0
62002
TrEMBL
other Location (Reliability: 1)
A0A6J2DWT3_ZALCA
462
0
52117
TrEMBL
other Location (Reliability: 1)
K9K2H2_HORSE
414
0
47140
TrEMBL
other Location (Reliability: 2)
A0A7K5S295_LANLU
517
0
59129
TrEMBL
other Location (Reliability: 3)
A0A3Q4GTY3_NEOBR
487
0
54494
TrEMBL
other Location (Reliability: 2)
A0A8C9MZ09_SERCA
458
0
52247
TrEMBL
other Location (Reliability: 1)
A0A8C9MGI6_SERCA
549
0
62647
TrEMBL
other Location (Reliability: 2)
A0A8C9MGG5_SERCA
556
0
63692
TrEMBL
other Location (Reliability: 3)
A0A7L1J2R6_SMUAF
Smutsornis africanus
474
0
53949
TrEMBL
other Location (Reliability: 3)
A0A452F0I9_CAPHI
559
0
64006
TrEMBL
other Location (Reliability: 4)
A0A6P8PA61_GEOSA
461
0
51982
TrEMBL
other Location (Reliability: 1)
A0A2K5XK42_MANLE
538
0
60919
TrEMBL
other Location (Reliability: 2)
A0A8B7Q793_HIPAR
552
0
62376
TrEMBL
other Location (Reliability: 1)
A0A8C0A2D7_BOSMU
552
0
62321
TrEMBL
other Location (Reliability: 1)
A0A5N3VUW3_MUNMU
574
0
65650
TrEMBL
other Location (Reliability: 4)
A0A8C4NW06_DICLA
582
0
65849
TrEMBL
other Location (Reliability: 2)
A0A3B3Q7B2_9TELE
573
0
64823
TrEMBL
other Location (Reliability: 2)
A0A674EW14_SALTR
575
0
65133
TrEMBL
other Location (Reliability: 2)
A0A7J5ZTW5_AMEME
611
0
69025
TrEMBL
other Location (Reliability: 4)
A0A7K9BXU4_9PICI
556
0
62779
TrEMBL
other Location (Reliability: 2)
A0A6P5JMZ7_PHACI
461
0
52006
TrEMBL
other Location (Reliability: 1)
A0A8C9AYE4_PHOSS
552
0
62334
TrEMBL
other Location (Reliability: 1)
G1SEA7_RABIT
656
0
74466
TrEMBL
other Location (Reliability: 2)
A0A6P9DLI0_PANGU
378
0
43329
TrEMBL
Secretory Pathway (Reliability: 1)
A0A7K9J1Q4_9CORV
517
0
59183
TrEMBL
other Location (Reliability: 3)
A0A3Q3VTH1_MOLML
573
0
64835
TrEMBL
other Location (Reliability: 2)
A0A093CZ17_TAUER
462
0
52815
TrEMBL
other Location (Reliability: 3)
A0A452RAE5_URSAM
525
0
59669
TrEMBL
other Location (Reliability: 3)
A0A8C4Z879_GADMO
560
0
63114
TrEMBL
other Location (Reliability: 3)
A0A8C3NZ89_9PASS
563
0
64061
TrEMBL
other Location (Reliability: 4)
A0A8J5C8Q0_CLAMG
489
0
56568
TrEMBL
other Location (Reliability: 2)
A0A8C2CII8_CYPCA
552
0
62349
TrEMBL
other Location (Reliability: 2)
A0A8D0EM13_STROC
539
0
61620
TrEMBL
other Location (Reliability: 2)
A0A8C6PK91_NOTFU
544
0
61317
TrEMBL
other Location (Reliability: 2)
A0A384AY40_BALAS
447
0
50949
TrEMBL
other Location (Reliability: 3)
A0A383YNN3_BALAS
524
0
59425
TrEMBL
other Location (Reliability: 2)
A0A2K5JE31_COLAP
539
0
60731
TrEMBL
other Location (Reliability: 2)
M3YTI3_MUSPF
517
0
59301
TrEMBL
other Location (Reliability: 3)
A0A6P7I3Y6_9TELE
557
0
62665
TrEMBL
other Location (Reliability: 2)
A0A3B4ELK3_PYGNA
573
0
65004
TrEMBL
other Location (Reliability: 2)
A0A8C6TFT5_9GOBI
566
0
63749
TrEMBL
other Location (Reliability: 3)
A0A2Y9Q9L7_DELLE
559
0
63990
TrEMBL
other Location (Reliability: 4)
A0A8D2QUY1_ZOSLA
527
0
60143
TrEMBL
other Location (Reliability: 2)
A0A341C8Y2_NEOAA
458
0
52372
TrEMBL
other Location (Reliability: 1)
A0A4W2HHU8_BOBOX
574
0
65608
TrEMBL
other Location (Reliability: 4)
A0A1A8B983_NOTFU
571
0
64670
TrEMBL
other Location (Reliability: 2)
A0A384AXT4_BALAS
458
0
52372
TrEMBL
other Location (Reliability: 1)
B1H2Z8_XENTR
551
0
62934
TrEMBL
other Location (Reliability: 2)
A0A3Q7NNB4_CALUR
473
0
53990
TrEMBL
other Location (Reliability: 1)
A0A6J2AQJ3_ACIJB
574
0
65578
TrEMBL
other Location (Reliability: 4)
A0A7J8J1E7_MOLMO
550
0
62777
TrEMBL
other Location (Reliability: 1)
A0A8C0AVE3_9AVES
501
0
56745
TrEMBL
other Location (Reliability: 5)
A0A1V4KDI9_PATFA
796
0
90619
TrEMBL
other Location (Reliability: 4)
A0A3L8SQ37_CHLGU
545
0
61536
TrEMBL
other Location (Reliability: 3)
A0A8C4CMT8_9TELE
525
0
59525
TrEMBL
other Location (Reliability: 2)
A0A3Q7UXT4_VULVU
415
0
47299
TrEMBL
other Location (Reliability: 2)
A0A2I0LTY0_COLLI
560
0
63964
TrEMBL
other Location (Reliability: 4)
A0A8C5EKF1_9TELE
560
0
63522
TrEMBL
other Location (Reliability: 2)
A0A2Y9IWE1_ENHLU
552
0
62304
TrEMBL
other Location (Reliability: 1)
E4XT71_OIKDI
515
0
58867
TrEMBL
other Location (Reliability: 1)
A0A8D2AXB3_SCIVU
559
0
64064
TrEMBL
other Location (Reliability: 4)
A0A663D732_PONAB
552
0
62320
TrEMBL
other Location (Reliability: 1)
A0A6D2VTX0_PANTR
574
0
65523
TrEMBL
other Location (Reliability: 4)
A0A852A7Y0_CALOR
547
0
61823
TrEMBL
other Location (Reliability: 2)
A0A8C8IVN7_ONCTS
597
0
67342
TrEMBL
Mitochondrion (Reliability: 2)
A0A7K8DSK8_9CORV
552
0
62298
TrEMBL
other Location (Reliability: 1)
A0A671W2A7_SPAAU
571
0
64624
TrEMBL
other Location (Reliability: 2)
F7FPU2_MONDO
551
0
62213
TrEMBL
other Location (Reliability: 2)
A0A515J4H7_CTEID
570
0
64702
TrEMBL
other Location (Reliability: 2)
A0A852KQ93_UROIN
401
0
45850
TrEMBL
other Location (Reliability: 3)
A0A2K5E9P7_AOTNA
574
0
65580
TrEMBL
other Location (Reliability: 4)
A0A340XU30_LIPVE
552
0
62318
TrEMBL
other Location (Reliability: 1)
A0A2R9BBM3_PANPA
574
0
65523
TrEMBL
other Location (Reliability: 4)
A0A3B4U0L0_SERDU
573
0
64746
TrEMBL
other Location (Reliability: 2)
A0A8D0DXM6_9SAUR
552
0
62480
TrEMBL
other Location (Reliability: 2)
A0A3B3CSP7_ORYME
474
0
53128
TrEMBL
other Location (Reliability: 4)
A0A4W5K217_9TELE
549
0
62331
TrEMBL
other Location (Reliability: 2)
A0A7L1BNX9_9PASS
561
0
64017
TrEMBL
other Location (Reliability: 5)
A0A8C2ZK53_CYCLU
563
0
63416
TrEMBL
other Location (Reliability: 2)
A0A8C2ZKR9_CYCLU
561
0
63448
TrEMBL
other Location (Reliability: 2)
I3MB35_ICTTR
544
0
62447
TrEMBL
other Location (Reliability: 3)
A0A8C3LKF4_CHRPC
560
0
63970
TrEMBL
other Location (Reliability: 4)
A0A7N6BJM1_ANATE
562
0
63403
TrEMBL
other Location (Reliability: 4)
K7G581_PELSI
560
0
64077
TrEMBL
other Location (Reliability: 4)
A0A7K8J313_9PASS
551
0
62239
TrEMBL
other Location (Reliability: 1)
H2Z923_CIOSA
556
0
63119
TrEMBL
other Location (Reliability: 3)
A0A672RWA8_SINGR
574
0
65245
TrEMBL
other Location (Reliability: 2)
A0A851YCZ3_9AVES
551
0
62233
TrEMBL
other Location (Reliability: 1)
A0A8C9N0E0_SERCA
534
0
61393
TrEMBL
other Location (Reliability: 5)
A0A6I9JAX7_CHRAS
552
0
62308
TrEMBL
other Location (Reliability: 1)
A0A8C0QZU1_CANLU
559
0
64008
TrEMBL
other Location (Reliability: 4)
A0A6P5DLV0_BOSIN
443
0
50116
TrEMBL
other Location (Reliability: 4)
A0A8B9N4V2_9AVES
552
0
62330
TrEMBL
other Location (Reliability: 1)
A0A8C4I2X8_DICLA
562
0
63844
TrEMBL
other Location (Reliability: 2)
A0A8C4DY18_DICLA
563
0
63493
TrEMBL
other Location (Reliability: 4)
A0A2I4CP75_9TELE
465
0
52248
TrEMBL
other Location (Reliability: 1)
A0A673Y6H3_SALTR
561
0
63363
TrEMBL
other Location (Reliability: 2)
A0A8B9IPG7_ANSCY
Anser cygnoid
552
0
62387
TrEMBL
other Location (Reliability: 1)
A0A6J1TYD8_9SAUR
553
0
62393
TrEMBL
other Location (Reliability: 2)
A0A8C6NDG8_MELUD
509
0
57826
TrEMBL
other Location (Reliability: 3)
A0A3Q3VYJ2_MOLML
557
0
62722
TrEMBL
other Location (Reliability: 2)
A0A452SK24_URSAM
559
0
64042
TrEMBL
other Location (Reliability: 4)
A0A8C1BRL7_CYPCA
527
0
59464
TrEMBL
other Location (Reliability: 2)
S7Q3D7_MYOBR
614
0
68957
TrEMBL
other Location (Reliability: 2)
A0A485NRS4_LYNPA
415
0
47285
TrEMBL
other Location (Reliability: 2)
A0A553R5W9_9TELE
537
0
60617
TrEMBL
other Location (Reliability: 2)
A0A8D0A413_SANLU
581
0
65612
TrEMBL
other Location (Reliability: 2)
A0A3P9B4M7_9CICH
571
0
64552
TrEMBL
other Location (Reliability: 2)
A0A8C6SHY1_9GOBI
561
0
64069
TrEMBL
other Location (Reliability: 2)
A0A8B7K0B6_9AVES
560
0
63881
TrEMBL
other Location (Reliability: 3)
A0A1S3PAZ4_SALSA
556
0
62630
TrEMBL
other Location (Reliability: 2)
A0A8D2QUE4_ZOSLA
522
0
59937
TrEMBL
other Location (Reliability: 2)
A0A7L0M239_9PSIT
517
0
59199
TrEMBL
other Location (Reliability: 3)
A0A7K8G129_ORTSP
569
0
64899
TrEMBL
other Location (Reliability: 5)
Q8UVW8_XENLA
560
0
64050
TrEMBL
other Location (Reliability: 4)
U3CBS5_CALJA
559
0
63981
TrEMBL
other Location (Reliability: 3)
A0A3Q7T641_VULVU
458
0
52404
TrEMBL
other Location (Reliability: 1)
A0A8B9K3I7_ASTMX
569
0
63867
TrEMBL
other Location (Reliability: 2)
W5L1L0_ASTMX
560
0
62938
TrEMBL
other Location (Reliability: 2)
A0A8B9K3W1_ASTMX
539
0
60726
TrEMBL
other Location (Reliability: 2)
A0A2K6QKX6_RHIRO
697
0
77744
TrEMBL
other Location (Reliability: 1)
Q4SQH4_TETNG
569
0
64551
TrEMBL
other Location (Reliability: 1)
A0A7J8FAU7_MOLMO
552
0
62305
TrEMBL
other Location (Reliability: 1)
A0A1N6LXS7_BABMR
Babesia microti (strain RI)
443
0
51184
TrEMBL
Mitochondrion (Reliability: 3)
A0A6P3ILW7_BISBI
559
0
64006
TrEMBL
other Location (Reliability: 4)
A0A851YED9_EOLRO
564
0
64897
TrEMBL
other Location (Reliability: 4)
A0A8C7LG77_ONCKI
556
0
63035
TrEMBL
other Location (Reliability: 1)
A0A3Q7SLJ1_VULVU
552
0
62370
TrEMBL
other Location (Reliability: 1)
A0A8B7ADQ4_ORYAF
552
0
62343
TrEMBL
other Location (Reliability: 1)
A0A8J6H0V6_MICOH
559
0
63979
TrEMBL
other Location (Reliability: 4)
A0A7L0QL19_SETKR
552
0
62380
TrEMBL
other Location (Reliability: 1)
A0A093GPB3_DRYPU
512
0
58259
TrEMBL
other Location (Reliability: 3)
A0A8C8MCH5_ONCTS
568
0
64213
TrEMBL
other Location (Reliability: 2)
A0A8C8IN00_ONCTS
575
0
65044
TrEMBL
other Location (Reliability: 3)
A0A8C8G5L6_ONCTS
583
0
65761
TrEMBL
other Location (Reliability: 2)
A0A671UXJ7_SPAAU
565
0
63643
TrEMBL
other Location (Reliability: 2)
A0A8C9PE30_SPEDA
371
0
41925
TrEMBL
Secretory Pathway (Reliability: 3)
A0A2Y9SM69_PHYMC
559
0
63976
TrEMBL
other Location (Reliability: 4)
A0A6Q2ZLJ6_ESOLU
577
0
64936
TrEMBL
other Location (Reliability: 1)
A0A1A8EN68_9TELE
570
0
64252
TrEMBL
other Location (Reliability: 3)
A0A3Q2ZMJ5_KRYMA
557
0
62680
TrEMBL
other Location (Reliability: 2)
A0A4W5K200_9TELE
582
0
65585
TrEMBL
other Location (Reliability: 2)
A0A8C2ZK87_CYCLU
574
0
64631
TrEMBL
other Location (Reliability: 2)
A0A2U4BXN6_TURTR
499
0
57132
TrEMBL
other Location (Reliability: 1)
A0A087YBI1_POEFO
564
0
63858
TrEMBL
other Location (Reliability: 2)
A0A7K7BLV5_APHCE
551
0
62222
TrEMBL
other Location (Reliability: 1)
A0A6J2V1M4_CHACN
555
0
62466
TrEMBL
other Location (Reliability: 2)
K7F734_PELSI
520
0
58826
TrEMBL
other Location (Reliability: 3)
A0A8C9MGE5_SERCA
458
0
52366
TrEMBL
other Location (Reliability: 1)
A0A7N8XIC6_9TELE
527
0
60178
TrEMBL
other Location (Reliability: 2)
A0A2D0QC90_ICTPU
611
0
69107
TrEMBL
other Location (Reliability: 3)
A0A8D0PUW0_PIG
550
0
62791
TrEMBL
other Location (Reliability: 1)
D0G7E1_PIG
550
0
62791
TrEMBL
other Location (Reliability: 1)
A0A8D0MD51_PIG
529
0
59722
TrEMBL
other Location (Reliability: 2)
G3RWH8_GORGO
559
0
64037
TrEMBL
other Location (Reliability: 4)
A0A8C5ZPI0_MARMA
520
0
58924
TrEMBL
other Location (Reliability: 4)
A0A667GTC1_LYNCA
574
0
65566
TrEMBL
other Location (Reliability: 4)
A0A8D2MMZ1_ZONAL
561
0
63925
TrEMBL
other Location (Reliability: 5)
A0A8C4NW49_DICLA
561
0
63727
TrEMBL
other Location (Reliability: 2)
A0A7K7PU28_ACRAR
551
0
62253
TrEMBL
other Location (Reliability: 1)
A0A673ZYJ7_SALTR
583
0
65642
TrEMBL
other Location (Reliability: 2)
A0A7K5W4T8_9SYLV
392
0
45503
TrEMBL
other Location (Reliability: 3)
G5APP8_HETGA
572
0
64518
TrEMBL
Mitochondrion (Reliability: 2)
A0A8C9BJE4_PHOSS
559
0
63950
TrEMBL
other Location (Reliability: 4)
A0A6I9PBK0_9TELE
482
0
54328
TrEMBL
other Location (Reliability: 1)
A0A851ASM8_SULDA
521
0
59005
TrEMBL
other Location (Reliability: 3)
A0A2I0T995_LIMLA
288
0
32415
TrEMBL
other Location (Reliability: 5)
A0A6A1Q6H1_BALPH
516
0
59110
TrEMBL
other Location (Reliability: 4)
A0A452RAF3_URSAM
502
0
56891
TrEMBL
other Location (Reliability: 5)
A0A8C1L1A6_CYPCA
558
0
63055
TrEMBL
other Location (Reliability: 2)
A0A6G1R891_9GRUI
551
0
62870
TrEMBL
other Location (Reliability: 1)
A0A7L0A255_9CORV
561
0
63983
TrEMBL
other Location (Reliability: 5)
A0A6J2QPT6_COTGO
573
0
64746
TrEMBL
other Location (Reliability: 2)
A0A4W3GX81_CALMI
438
0
49621
TrEMBL
other Location (Reliability: 3)
A0A7L1R5A2_9PASS
561
0
63983
TrEMBL
other Location (Reliability: 5)
A0A8D2L6K5_VARKO
552
0
62519
TrEMBL
other Location (Reliability: 2)
A0A8C6SIN7_9GOBI
575
0
65582
TrEMBL
other Location (Reliability: 3)
A0A8D2EV05_THEGE
574
0
65652
TrEMBL
other Location (Reliability: 4)
A0A8C3NPW3_GEOPR
552
0
62382
TrEMBL
other Location (Reliability: 1)
A0A147A6B7_FUNHE
557
0
62686
TrEMBL
other Location (Reliability: 2)
A0A671FLT0_RHIFE
559
0
64052
TrEMBL
other Location (Reliability: 4)
A0A384C7K3_URSMA
473
0
54010
TrEMBL
other Location (Reliability: 1)
A0A671Q6X3_9TELE
554
0
62867
TrEMBL
other Location (Reliability: 2)
A0A671MTJ3_9TELE
552
0
62308
TrEMBL
other Location (Reliability: 2)
H3CPW6_TETNG
581
0
65807
TrEMBL
other Location (Reliability: 1)
A0A6P4Z7D2_BRABE
554
0
62154
TrEMBL
other Location (Reliability: 3)
A0A7K5VC87_9CORV
561
0
63957
TrEMBL
other Location (Reliability: 5)
A0A401RZ21_CHIPU
372
0
42475
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8C7L8L5_ONCKI
583
0
65652
TrEMBL
other Location (Reliability: 2)
A0A8C7GM43_ONCKI
561
0
63177
TrEMBL
other Location (Reliability: 2)
A0A3P9IY16_ORYLA
557
0
62808
TrEMBL
other Location (Reliability: 2)
H2L8J1_ORYLA
557
0
62822
TrEMBL
other Location (Reliability: 2)
H2LFH6_ORYLA
572
0
64601
TrEMBL
other Location (Reliability: 2)
A0A6A5EZ80_PERFL
557
0
62712
TrEMBL
other Location (Reliability: 2)
A0A315VBY5_GAMAF
534
0
60129
TrEMBL
other Location (Reliability: 1)
A0A7L1RXM6_9PASS
561
0
63983
TrEMBL
other Location (Reliability: 5)
A0A4W6BQH4_LATCA
573
0
64788
TrEMBL
other Location (Reliability: 2)
A0A1A8C9K0_9TELE
466
0
53052
TrEMBL
other Location (Reliability: 2)
A0A7K5TA49_9FRIN
561
0
63939
TrEMBL
other Location (Reliability: 5)
A0A7K9NU63_9CORV
551
0
62209
TrEMBL
other Location (Reliability: 1)
A0A8C8IWG4_ONCTS
570
0
64704
TrEMBL
other Location (Reliability: 3)
A0A7L2MVS5_9PASS
561
0
63983
TrEMBL
other Location (Reliability: 5)
G1KJX3_ANOCA
560
0
64624
TrEMBL
other Location (Reliability: 1)
A0A8C5XQN3_MICMU
662
0
75269
TrEMBL
other Location (Reliability: 4)
A0A2R9B7U6_PANPA
559
0
64009
TrEMBL
other Location (Reliability: 4)
A0A8C9HHT7_9PRIM
599
0
67405
TrEMBL
other Location (Reliability: 2)
A0A8C6XK41_NAJNA
553
0
62356
TrEMBL
other Location (Reliability: 2)
A0A8C6XGC8_NAJNA
550
0
62823
TrEMBL
other Location (Reliability: 2)
A0A4W5MLE4_9TELE
592
0
66938
TrEMBL
other Location (Reliability: 2)
A0A8C7SZJ2_ONCMY
568
0
63977
TrEMBL
other Location (Reliability: 1)
A0A8B9PI68_APTOW
560
0
63917
TrEMBL
other Location (Reliability: 3)
A0A7K9SWG7_9AVES
560
0
64000
TrEMBL
other Location (Reliability: 4)
A0A7L2PG54_PYCJO
561
0
63995
TrEMBL
other Location (Reliability: 5)
A0A7K9SJ14_9AVES
552
0
62375
TrEMBL
other Location (Reliability: 2)
A0A835ND88_9PASS
506
0
57506
TrEMBL
Mitochondrion (Reliability: 5)
A0A7K7QXY8_POEAT
551
0
62175
TrEMBL
other Location (Reliability: 1)
A0A6J2E1U9_ZALCA
524
0
59359
TrEMBL
other Location (Reliability: 2)
A0A672T5H3_SINGR
527
0
59759
TrEMBL
other Location (Reliability: 2)
A0A8C6IMK5_MUSSI
386
0
43989
TrEMBL
other Location (Reliability: 2)
A0A8C2PBV5_CAPHI
535
0
60992
TrEMBL
other Location (Reliability: 5)
A0A091MUX5_CARIC
462
0
52815
TrEMBL
other Location (Reliability: 3)
A0A218UWT3_9PASE
585
0
65998
TrEMBL
other Location (Reliability: 1)
G1MAA9_AILME
521
0
59746
TrEMBL
other Location (Reliability: 3)
A0A674EXW1_SALTR
588
0
66349
TrEMBL
other Location (Reliability: 2)
A0A2K5TNN8_MACFA
510
0
59149
TrEMBL
other Location (Reliability: 4)
A0A6P5L0Y0_PHACI
559
0
64093
TrEMBL
other Location (Reliability: 5)
L5K413_PTEAL
574
0
65678
TrEMBL
other Location (Reliability: 4)
A0A6P5PK01_MUSCR
552
0
61994
TrEMBL
other Location (Reliability: 1)
A0A6J2IZA5_9PASS
552
0
62374
TrEMBL
other Location (Reliability: 1)
A0A8C7XUU3_9TELE
557
0
62822
TrEMBL
other Location (Reliability: 2)
A0A091KIK3_COLST
521
0
59051
TrEMBL
other Location (Reliability: 3)
A0A4Z2BIQ0_9TELE
572
0
64843
TrEMBL
other Location (Reliability: 2)
A0A8D0HGZ7_SPHPU
523
0
59875
TrEMBL
other Location (Reliability: 4)
A0A8C1S783_CYPCA
563
0
64306
TrEMBL
other Location (Reliability: 4)
S9Y4B1_CAMFR
481
0
54722
TrEMBL
other Location (Reliability: 1)
A0A8C6M243_NOTFU
579
0
65506
TrEMBL
other Location (Reliability: 3)
A0A2K6V8H5_SAIBB
555
1
63088
TrEMBL
other Location (Reliability: 2)
A0A2K6GM52_PROCO
553
0
62377
TrEMBL
other Location (Reliability: 1)
M3Y782_MUSPF
524
0
59318
TrEMBL
other Location (Reliability: 2)
A0A6P7NX82_BETSP
573
0
64830
TrEMBL
other Location (Reliability: 2)
A0A8C6TEK4_9GOBI
579
0
65313
TrEMBL
other Location (Reliability: 3)
A0A4W2DEJ0_BOBOX
552
0
62321
TrEMBL
other Location (Reliability: 1)
A0A6P6HWL6_PUMCO
471
0
53959
TrEMBL
other Location (Reliability: 4)
A0A8C5W9T9_MICMU
458
0
52432
TrEMBL
other Location (Reliability: 1)
A0A3B5LL84_9TELE
564
0
63800
TrEMBL
other Location (Reliability: 2)
A0A7L0FDI5_CORCN
551
0
62247
TrEMBL
other Location (Reliability: 1)
G1NG26_MELGA
544
0
61749
TrEMBL
other Location (Reliability: 3)
A0A8C7L468_ONCKI
552
0
62700
TrEMBL
other Location (Reliability: 2)
A0A8C6CFQ3_MONMO
552
0
62334
TrEMBL
other Location (Reliability: 1)
F7HR67_MACMU
581
0
65961
TrEMBL
other Location (Reliability: 2)
A0A8C4CT01_9TELE
552
0
62250
TrEMBL
other Location (Reliability: 2)
W5PHS8_SHEEP
574
0
65578
TrEMBL
other Location (Reliability: 4)
H0X5V2_OTOGA
559
0
64036
TrEMBL
other Location (Reliability: 4)
A0A093RJ11_PYGAD
517
0
59199
TrEMBL
other Location (Reliability: 3)
A0A8C9CUV1_PANLE
574
0
65566
TrEMBL
other Location (Reliability: 4)
A0A8C5G938_9TELE
547
0
62283
TrEMBL
other Location (Reliability: 2)
A0A8D3CG64_SCOMX
573
0
64670
TrEMBL
other Location (Reliability: 2)
A0A673LQV7_9TELE
557
0
63793
TrEMBL
other Location (Reliability: 4)
A0A673J3J1_9TELE
545
0
62060
TrEMBL
other Location (Reliability: 2)
A0A0A0A120_CHAVO
517
0
59170
TrEMBL
other Location (Reliability: 3)
F6RCR9_CIOIN
554
0
62835
TrEMBL
other Location (Reliability: 2)
A0A8J6GUW8_MICOH
641
0
71817
TrEMBL
other Location (Reliability: 1)
A0A8C9AMF2_PROSS
552
0
62317
TrEMBL
other Location (Reliability: 1)
A0A4W6CUD2_LATCA
557
0
62708
TrEMBL
other Location (Reliability: 2)
I3J3R8_ORENI
550
0
61983
TrEMBL
other Location (Reliability: 2)
A0A2K5N8D5_CERAT
574
0
65638
TrEMBL
other Location (Reliability: 4)
G1KFT1_ANOCA
452
0
51369
TrEMBL
other Location (Reliability: 1)
A0A7K5ZL84_ONYCO
551
0
62231
TrEMBL
other Location (Reliability: 1)
A0A8C5V1D8_MICMU
669
0
76116
TrEMBL
other Location (Reliability: 4)
G3W3Y1_SARHA
551
0
62188
TrEMBL
other Location (Reliability: 1)
A0A8C8SXC9_9SAUR
523
0
59185
TrEMBL
other Location (Reliability: 2)
A0A7L4FQH2_9COLU
402
0
45835
TrEMBL
other Location (Reliability: 2)
A0A8C2ZK41_CYCLU
583
0
65655
TrEMBL
other Location (Reliability: 3)
A0A8C2XSB2_CYCLU
559
0
62880
TrEMBL
other Location (Reliability: 2)
A0A8C4QYB0_EPTBU
453
0
50201
TrEMBL
other Location (Reliability: 1)
A0A673B8V7_9TELE
569
0
64490
TrEMBL
other Location (Reliability: 2)
A0A673BAM3_9TELE
557
0
63096
TrEMBL
other Location (Reliability: 2)
A0A670XT18_PSETE
553
0
62371
TrEMBL
other Location (Reliability: 2)
A0A672PXB9_SINGR
502
0
56872
TrEMBL
other Location (Reliability: 2)
A0A7L0WKN2_ALELA
434
0
49360
TrEMBL
other Location (Reliability: 1)
A0A8C2QVI0_CAPHI
524
0
59423
TrEMBL
other Location (Reliability: 2)
A0A7N8Y586_9TELE
553
0
62162
TrEMBL
other Location (Reliability: 2)
A0A8D0HTE7_PIG
531
0
60050
TrEMBL
other Location (Reliability: 2)
M4A9Q8_XIPMA
629
0
70592
TrEMBL
Secretory Pathway (Reliability: 4)
A0A2I3GRR2_NOMLE
574
0
65549
TrEMBL
other Location (Reliability: 4)
A0A6G1B2N5_CROCR
521
0
58876
TrEMBL
other Location (Reliability: 3)
G3R126_GORGO
552
0
62320
TrEMBL
other Location (Reliability: 1)
A0A8C5ZV61_MARMA
510
0
58745
TrEMBL
Mitochondrion (Reliability: 4)
A0A8D2M848_ZONAL
552
0
62380
TrEMBL
other Location (Reliability: 1)
A0A7K7T8A0_9TYRA
551
0
62245
TrEMBL
other Location (Reliability: 1)
A0A8B9CYQ2_9AVES
527
0
59836
TrEMBL
other Location (Reliability: 3)
A0A834B9B7_9CHIR
574
0
65606
TrEMBL
other Location (Reliability: 4)
A0A668AA92_9TELE
559
0
63450
TrEMBL
other Location (Reliability: 2)
A0A6P6HX10_PUMCO
415
0
47285
TrEMBL
other Location (Reliability: 2)
A0A6J3HXI4_SAPAP
574
0
65581
TrEMBL
other Location (Reliability: 4)
A0A3Q1GLR4_9TELE
557
0
62711
TrEMBL
other Location (Reliability: 2)
A0A8C8B975_9STRI
560
0
63982
TrEMBL
other Location (Reliability: 4)
A0A6J2G5H8_9PASS
579
0
65526
TrEMBL
Mitochondrion (Reliability: 3)
A0A8C7XSN6_9TELE
564
0
63709
TrEMBL
other Location (Reliability: 2)
A0A4Z2B5S1_9TELE
588
0
65958
TrEMBL
other Location (Reliability: 4)
A0A665VVR1_ECHNA
565
0
63536
TrEMBL
other Location (Reliability: 2)
A0A7K6LQA3_9CORV
551
0
62209
TrEMBL
other Location (Reliability: 1)
A0A674GWE4_TAEGU
528
0
59764
TrEMBL
other Location (Reliability: 3)
A0A8C1YRG9_CYPCA
562
0
64321
TrEMBL
other Location (Reliability: 3)
A0A2K6SQ46_SAIBB
550
0
62838
TrEMBL
other Location (Reliability: 1)
A0A091TTR8_PELCR
365
0
41207
TrEMBL
Secretory Pathway (Reliability: 3)
A0A2U3WK21_ODORO
528
0
62852
TrEMBL
other Location (Reliability: 4)
A0A8D2EZB7_THEGE
501
0
57948
TrEMBL
other Location (Reliability: 1)
A0A091EKF1_CORBR
517
0
59067
TrEMBL
other Location (Reliability: 3)
A0A1S2ZEB6_ERIEU
572
0
64492
TrEMBL
other Location (Reliability: 1)
A0A4W4HCN0_ELEEL
552
0
62029
TrEMBL
other Location (Reliability: 2)
A0A6J2ASS5_ACIJB
473
0
53974
TrEMBL
other Location (Reliability: 1)
A0A2G9QN46_LITCT
360
0
40785
TrEMBL
Secretory Pathway (Reliability: 3)
A0A8C1IYX7_CYPCA
627
0
71410
TrEMBL
other Location (Reliability: 2)
A0A6J2LNI6_9CHIR
552
0
62304
TrEMBL
other Location (Reliability: 1)
A0A7E6D9V9_9CHIR
415
0
47341
TrEMBL
other Location (Reliability: 2)
A0A8B9KFE2_ASTMX
541
0
61863
TrEMBL
other Location (Reliability: 2)
A0A851PCY7_9GALL
560
0
63988
TrEMBL
other Location (Reliability: 4)
A0A8C7GQC5_ONCKI
568
0
63981
TrEMBL
other Location (Reliability: 3)
A0A8C7MN29_ONCKI
574
0
65009
TrEMBL
other Location (Reliability: 1)
A0A3P9JJL0_ORYLA
603
0
67850
TrEMBL
other Location (Reliability: 2)
A0A7K6JJF7_9CORV
561
0
64011
TrEMBL
other Location (Reliability: 5)
A0A8D3CEN6_SCOMX
581
0
65709
TrEMBL
other Location (Reliability: 2)
A0A2J8NHX8_PANTR
552
0
62320
TrEMBL
other Location (Reliability: 1)
A0A669DX47_ORENI
577
0
65110
TrEMBL
other Location (Reliability: 4)
I3JZ78_ORENI
580
0
65536
TrEMBL
other Location (Reliability: 2)
A0A8C8IVC9_ONCTS
563
0
63631
TrEMBL
other Location (Reliability: 3)
A0A8C8HJI6_ONCTS
529
1
59559
TrEMBL
other Location (Reliability: 2)
M3XDB1_FELCA
573
0
65469
TrEMBL
other Location (Reliability: 4)
A0A2Y9HK62_NEOSC
574
0
65580
TrEMBL
other Location (Reliability: 4)
A0A6J0E228_PERMB
530
0
59949
TrEMBL
other Location (Reliability: 3)
A0A455B8N7_PHYMC
552
0
62282
TrEMBL
other Location (Reliability: 1)
A0A2K5F9L2_AOTNA
552
0
62350
TrEMBL
other Location (Reliability: 1)
A0A498LRJ7_LABRO
573
0
65005
TrEMBL
other Location (Reliability: 2)
A0A7L1C963_9PASS
470
0
52158
TrEMBL
other Location (Reliability: 4)
A0A3Q0QZJ5_AMPCI
571
0
64598
TrEMBL
other Location (Reliability: 2)
A0A6J3R2A6_TURTR
447
0
50975
TrEMBL
other Location (Reliability: 3)
A0A3Q1CNW8_AMPOC
557
0
62654
TrEMBL
other Location (Reliability: 2)
A0A8C7LLG3_ONCMY
596
0
67339
TrEMBL
other Location (Reliability: 2)
A0A7J7Y1S2_MYOMY
550
0
62742
TrEMBL
other Location (Reliability: 1)
A0A8C3BGM5_CAIMO
552
0
62400
TrEMBL
other Location (Reliability: 1)
A0A673BAG1_9TELE
577
0
65451
TrEMBL
other Location (Reliability: 3)
R0JT95_ANAPL
521
0
59034
TrEMBL
other Location (Reliability: 3)
G3PTT2_GASAC
582
0
65714
TrEMBL
other Location (Reliability: 1)
A0A673T856_SURSU
560
0
64005
TrEMBL
other Location (Reliability: 3)
A0A0D9S759_CHLSB
552
0
62350
TrEMBL
other Location (Reliability: 1)
A0A672HJT2_SALFA
581
0
65709
TrEMBL
other Location (Reliability: 2)
U3IIN8_ANAPP
552
0
62400
TrEMBL
other Location (Reliability: 1)
A0A2K5XK45_MANLE
542
0
61119
TrEMBL
other Location (Reliability: 5)
A0A091WIE7_NIPNI
517
0
59170
TrEMBL
other Location (Reliability: 3)
A0A8I3MP14_CANLF
721
0
80566
TrEMBL
Mitochondrion (Reliability: 3)
A0A3B3RVB5_9TELE
609
0
68554
TrEMBL
other Location (Reliability: 4)
A0A093EZD2_GAVST
517
0
59211
TrEMBL
other Location (Reliability: 3)
A0A6J0HZ04_9PASS
561
0
64037
TrEMBL
other Location (Reliability: 5)
A0A091HFQ4_BUCRH
517
0
59154
TrEMBL
other Location (Reliability: 3)
A0A8C8B4L0_9STRI
552
0
62346
TrEMBL
other Location (Reliability: 1)
A0A7J7Y619_RHIFE
415
0
47313
TrEMBL
other Location (Reliability: 2)
A0A452TP49_URSMA
500
0
57477
TrEMBL
Mitochondrion (Reliability: 5)
A0A2K6LPW9_RHIBE
574
0
65561
TrEMBL
other Location (Reliability: 4)
A0A2K6MRP5_RHIBE
534
0
60228
TrEMBL
other Location (Reliability: 2)
A0A674N143_TAKRU
558
0
63474
TrEMBL
other Location (Reliability: 2)
A0A7L0BSJ2_9AVES
552
0
62330
TrEMBL
other Location (Reliability: 1)
A0A674HEW4_TAEGU
561
0
63922
TrEMBL
other Location (Reliability: 5)
A0A8C5CEW0_GADMO
566
0
63719
TrEMBL
other Location (Reliability: 4)
H0ZH19_TAEGU
552
0
62304
TrEMBL
other Location (Reliability: 1)
A0A8C1N7Q5_CYPCA
578
0
65343
TrEMBL
other Location (Reliability: 2)
A0A669PHJ1_PHACC
560
0
64002
TrEMBL
other Location (Reliability: 4)
A0A1A7ZIS0_NOTFU
574
0
64821
TrEMBL
other Location (Reliability: 4)
A0A668SZ85_OREAU
561
0
63601
TrEMBL
other Location (Reliability: 2)
A0A668SXK7_OREAU
580
0
65566
TrEMBL
other Location (Reliability: 2)
A0A668VQU9_OREAU
577
0
65068
TrEMBL
other Location (Reliability: 4)
A0A8D0AB90_SANLU
567
0
64121
TrEMBL
other Location (Reliability: 5)
A0A6P7I8U3_9TELE
465
0
52103
TrEMBL
other Location (Reliability: 1)
A0A7L0Z8J4_9PASS
517
0
59203
TrEMBL
other Location (Reliability: 3)
A0A4W3JXC8_CALMI
550
0
62239
TrEMBL
other Location (Reliability: 1)
A0A8C6WGP7_9GOBI
552
0
62991
TrEMBL
other Location (Reliability: 2)
A0A8F5SR04_SCHPR
570
0
64553
TrEMBL
other Location (Reliability: 2)
A0A8C6SHN4_9GOBI
543
0
62155
TrEMBL
other Location (Reliability: 2)
A0A8I6A5W8_RAT
521
0
58848
TrEMBL
other Location (Reliability: 3)
A0A8D2ETT2_THEGE
552
0
62320
TrEMBL
other Location (Reliability: 1)
A0A7L0MVX4_9PSIT
552
0
62386
TrEMBL
other Location (Reliability: 1)
A0A4W4G5D6_ELEEL
560
0
63820
TrEMBL
other Location (Reliability: 2)
A0A2U4BXM6_TURTR
523
0
59260
TrEMBL
other Location (Reliability: 2)
A0A6P8QL60_GEOSA
375
0
43163
TrEMBL
other Location (Reliability: 4)
A0A674JRJ2_TERCA
551
0
62315
TrEMBL
other Location (Reliability: 1)
D2HJX7_AILME
574
0
65584
TrEMBL
other Location (Reliability: 4)
Q2LGF9_HORSE
552
0
62388
TrEMBL
other Location (Reliability: 1)
A0A671DKG1_RHIFE
552
0
62386
TrEMBL
other Location (Reliability: 1)
A0A8C4VCH6_FALTI
629
0
70061
TrEMBL
Mitochondrion (Reliability: 3)
A0A671QZ84_9TELE
539
0
61412
TrEMBL
other Location (Reliability: 2)
A0A2K6QKY2_RHIRO
576
0
65755
TrEMBL
other Location (Reliability: 2)
A0A2K6QX69_RHIRO
560
0
63126
TrEMBL
other Location (Reliability: 4)
A0A6J0YE89_ODOVR
552
0
62319
TrEMBL
other Location (Reliability: 1)
A0A5A4DW27_TACFU
546
0
61771
TrEMBL
other Location (Reliability: 2)
A0A8C7L6N6_ONCKI
558
0
63322
TrEMBL
other Location (Reliability: 4)
A0A8C7I1K9_ONCKI
597
0
67521
TrEMBL
other Location (Reliability: 2)
A0A6J3DH53_AYTFU
552
0
62400
TrEMBL
other Location (Reliability: 1)
A0A850XN46_PIACA
551
0
62261
TrEMBL
other Location (Reliability: 1)
A0A3Q7UXS8_VULVU
559
0
64008
TrEMBL
other Location (Reliability: 4)
A0A8C5G927_9TELE
572
0
64615
TrEMBL
other Location (Reliability: 2)
A0A8C8Z1B1_PROSS
574
0
65672
TrEMBL
other Location (Reliability: 4)
A0A6F9A552_9TELE
524
0
59057
TrEMBL
other Location (Reliability: 1)
A0A3B4A0M6_9GOBI
559
0
63040
TrEMBL
other Location (Reliability: 2)
A0A3P9QDJ6_POERE
637
0
71951
TrEMBL
other Location (Reliability: 2)
A0A7F8R8D5_LEPWE
419
0
46995
TrEMBL
other Location (Reliability: 2)
A0A2Y9GKJ8_NEOSC
552
0
62343
TrEMBL
other Location (Reliability: 1)
A0A8C4M4T2_EQUAS
559
0
63981
TrEMBL
other Location (Reliability: 4)
A0A7J8KEX7_ROUAE
552
0
62353
TrEMBL
other Location (Reliability: 2)
A0A8C3HL65_CHRPI
539
0
61048
TrEMBL
other Location (Reliability: 1)
A0A2G9GVG4_9LAMI
188
0
21037
TrEMBL
other Location (Reliability: 3)
A0A6P6CZ27_PTEVA
462
0
52131
TrEMBL
other Location (Reliability: 1)
A0A7N6FHS9_ANATE
565
0
63744
TrEMBL
other Location (Reliability: 4)
A0A556TSZ3_BAGYA
493
0
55471
TrEMBL
other Location (Reliability: 2)
A0A226PR02_COLVI
444
0
50977
TrEMBL
other Location (Reliability: 4)
A0A8C9N1G8_SERCA
536
0
61441
TrEMBL
other Location (Reliability: 4)
A0A452EL67_CAPHI
552
0
62321
TrEMBL
other Location (Reliability: 1)
A0A672HJQ7_SALFA
567
0
64236
TrEMBL
other Location (Reliability: 2)
A0A672HJY1_SALFA
560
0
63291
TrEMBL
other Location (Reliability: 2)
A0A3Q2WZG7_HAPBU
557
0
62804
TrEMBL
other Location (Reliability: 2)
A0A6P5BP33_BOSIN
552
0
62321
TrEMBL
other Location (Reliability: 1)
A0A7L1PZZ4_ORIOR
552
0
62294
TrEMBL
other Location (Reliability: 1)
A0A7L0E9P2_TROML
547
0
61801
TrEMBL
other Location (Reliability: 2)
A0A6I9HVD1_GEOFO
515
0
59032
TrEMBL
other Location (Reliability: 4)
A0A2I4CPA4_9TELE
449
0
50446
TrEMBL
other Location (Reliability: 2)
A0A7E6DCT0_9CHIR
458
0
52446
TrEMBL
other Location (Reliability: 1)
A0A834BBZ4_9CHIR
475
0
54434
TrEMBL
other Location (Reliability: 3)
K9IYL0_DESRO
552
0
62210
TrEMBL
other Location (Reliability: 1)
G7P7E7_MACFA
532
0
60899
TrEMBL
other Location (Reliability: 4)
G5C4R6_HETGA
547
0
62909
TrEMBL
other Location (Reliability: 5)
A0A6P6IS08_PUMCO
462
0
52090
TrEMBL
other Location (Reliability: 1)
A0A7K6GBV3_9PASS
551
0
62207
TrEMBL
other Location (Reliability: 1)
A0A6P5R8L4_MUSCR
559
0
63945
TrEMBL
other Location (Reliability: 4)
A0A3Q2CD60_CYPVA
557
0
62699
TrEMBL
other Location (Reliability: 2)
A0A8B8X3R5_BALMU
447
0
50922
TrEMBL
other Location (Reliability: 3)
A0A665WZ44_ECHNA
561
0
63599
TrEMBL
other Location (Reliability: 2)
A0A4U5UJF1_COLLU
591
0
66797
TrEMBL
other Location (Reliability: 3)
A0A7K6HGX9_9PASS
561
0
63983
TrEMBL
other Location (Reliability: 5)
A0A5N3X6J9_MUNRE
574
0
65650
TrEMBL
other Location (Reliability: 4)
A0A8C1S5T6_CYPCA
572
0
64891
TrEMBL
other Location (Reliability: 2)
A0A1A8UJ16_NOTFU
572
0
64536
TrEMBL
other Location (Reliability: 3)
A0A485NW32_LYNPA
458
0
52390
TrEMBL
other Location (Reliability: 1)
A0A087RHV6_APTFO
521
0
59024
TrEMBL
other Location (Reliability: 3)
A0A7J8AAV7_PIPKU
552
0
62390
TrEMBL
other Location (Reliability: 1)
A0A7K9WUT7_9PASS
561
0
63983
TrEMBL
other Location (Reliability: 5)
A0A091NTY7_HALAL
517
0
59146
TrEMBL
other Location (Reliability: 3)
C3YCL4_BRAFL
492
0
55732
TrEMBL
other Location (Reliability: 2)
L9JWD5_TUPCH
423
0
48785
TrEMBL
Mitochondrion (Reliability: 5)
A0A7L0VHP6_9PASE
552
0
62292
TrEMBL
other Location (Reliability: 1)
A0A2U3WYR5_ODORO
552
0
62339
TrEMBL
other Location (Reliability: 1)
A0A8C9JK06_PANTA
542
0
61562
TrEMBL
Secretory Pathway (Reliability: 4)
A0A091CVZ6_FUKDA
460
0
51841
TrEMBL
other Location (Reliability: 1)
A0A091EPW8_CORBR
444
0
50903
TrEMBL
other Location (Reliability: 3)
A0A7L1ZA38_LEILU
561
0
64015
TrEMBL
other Location (Reliability: 5)
A0A2P4TAK8_BAMTH
522
0
60605
TrEMBL
other Location (Reliability: 5)
A0A5E4C2Z4_MARMO
559
0
64064
TrEMBL
other Location (Reliability: 4)
A0A6P4W122_PANPR
462
0
52082
TrEMBL
other Location (Reliability: 1)
A0A7F8QS87_LEPWE
458
0
52404
TrEMBL
other Location (Reliability: 1)
A0A6J2M1L8_9CHIR
559
0
64050
TrEMBL
other Location (Reliability: 4)
A0A6P9BT32_PANGU
553
0
62270
TrEMBL
other Location (Reliability: 2)
A0A8C4TWV3_FALTI
527
0
60249
TrEMBL
other Location (Reliability: 2)
A0A6P6K635_CARAU
573
0
65139
TrEMBL
other Location (Reliability: 2)
A0A7L4ESC7_HIRRU
551
0
62223
TrEMBL
other Location (Reliability: 1)
A0A8C7I442_ONCKI
588
0
66444
TrEMBL
other Location (Reliability: 2)
G7MV52_MACMU
532
0
60899
TrEMBL
other Location (Reliability: 4)
A0A8C0IBJ0_BUBBB
526
0
59624
TrEMBL
other Location (Reliability: 2)
A0A8C4B8N6_9TELE
577
0
65618
TrEMBL
other Location (Reliability: 2)
W5PDB5_SHEEP
546
0
62018
TrEMBL
other Location (Reliability: 5)
A0A8C3V1C9_CATUS
562
0
64076
TrEMBL
other Location (Reliability: 4)
A0A8C3U3R9_CATUS
552
0
62290
TrEMBL
other Location (Reliability: 1)
A0A8I5TS24_PONAB
574
0
65523
TrEMBL
other Location (Reliability: 4)
A0A673JE98_9TELE
573
0
65035
TrEMBL
other Location (Reliability: 2)
A0A673J9I8_9TELE
541
0
61575
TrEMBL
other Location (Reliability: 2)
A0A444U4T9_ACIRT
775
0
87619
TrEMBL
other Location (Reliability: 2)
A0A7K4U9M7_9SYLV
561
0
63983
TrEMBL
other Location (Reliability: 5)
A0A7L2QBE9_9PASS
552
0
62382
TrEMBL
other Location (Reliability: 1)
L5LLC8_MYODS
457
0
52182
TrEMBL
other Location (Reliability: 2)
A0A7M4EE85_CROPO
461
0
52037
TrEMBL
other Location (Reliability: 1)
A0A7M4FC45_CROPO
617
0
69751
TrEMBL
other Location (Reliability: 2)
A0A337S7J7_FELCA
520
0
59607
TrEMBL
other Location (Reliability: 3)
A0A671UY70_SPAAU
553
0
62117
TrEMBL
other Location (Reliability: 2)
A0A5J5CQN1_9PERO
544
0
61323
TrEMBL
other Location (Reliability: 2)
A0A2K5E9M7_AOTNA
559
0
64009
TrEMBL
other Location (Reliability: 4)
A0A2U3V6N5_TURTR
552
0
62334
TrEMBL
other Location (Reliability: 1)
A0A8C7TPT4_ONCMY
592
0
67022
TrEMBL
other Location (Reliability: 3)
A0A7K9HER3_9AVES
560
0
64007
TrEMBL
other Location (Reliability: 4)
A0A8B9PG48_APTOW
508
0
56699
TrEMBL
other Location (Reliability: 3)
A0A8C2T8U2_COTJA
560
0
64018
TrEMBL
other Location (Reliability: 4)
A0A673C3C4_9TELE
572
0
64591
TrEMBL
other Location (Reliability: 3)
A0A673C3D0_9TELE
557
0
62712
TrEMBL
other Location (Reliability: 2)
H2Z921_CIOSA
562
0
63708
TrEMBL
other Location (Reliability: 3)
A0A672PXA7_SINGR
513
0
57915
TrEMBL
other Location (Reliability: 2)
A0A7N9AVJ7_9TELE
576
0
64850
TrEMBL
other Location (Reliability: 2)
A0A7K5IJJ3_TOXRE
552
0
62348
TrEMBL
other Location (Reliability: 1)
A0A6B0QPZ5_9CETA
559
0
64006
TrEMBL
other Location (Reliability: 4)
A0A3M0K6G5_HIRRU
568
0
64016
TrEMBL
other Location (Reliability: 1)
A0A7K7E092_9SYLV
551
0
62209
TrEMBL
other Location (Reliability: 1)
A0A091UVR0_NIPNI
521
0
58964
TrEMBL
other Location (Reliability: 3)
A0A8C0M4B9_CANLF
721
0
80566
TrEMBL
Mitochondrion (Reliability: 3)
A0A091UFA3_PHORB
474
0
54138
TrEMBL
other Location (Reliability: 3)
A0A8C4DYF9_DICLA
556
0
62649
TrEMBL
other Location (Reliability: 2)
A0A8C4DY41_DICLA
568
0
64179
TrEMBL
other Location (Reliability: 2)
A0A3B3Q7D2_9TELE
552
0
62842
TrEMBL
other Location (Reliability: 2)
A0A8C0GZ81_CHEAB
551
0
62235
TrEMBL
other Location (Reliability: 1)
A0A2K5TNP6_MACFA
559
0
63995
TrEMBL
other Location (Reliability: 4)
G1PPM6_MYOLU
528
0
59934
TrEMBL
other Location (Reliability: 3)
G1SMV0_RABIT
537
0
60904
TrEMBL
other Location (Reliability: 3)
A0A8C7XS84_9TELE
571
0
64509
TrEMBL
other Location (Reliability: 2)
A0A8B8WQ06_BALMU
523
0
59263
TrEMBL
other Location (Reliability: 2)
A0A8C7XV17_9TELE
555
0
62861
TrEMBL
other Location (Reliability: 2)
A0A665WZL8_ECHNA
526
0
60228
TrEMBL
other Location (Reliability: 2)
A0A1S3FM67_DIPOR
537
0
60905
TrEMBL
other Location (Reliability: 1)
A0A8C3P338_9PASS
486
0
55877
TrEMBL
other Location (Reliability: 4)
A0A8C1NAN8_CYPCA
556
0
63101
TrEMBL
other Location (Reliability: 2)
A0A8C1S7L4_CYPCA
523
0
59942
TrEMBL
other Location (Reliability: 2)
A0A8C2YLN7_CHILA
552
0
62336
TrEMBL
other Location (Reliability: 1)
A0A8C6LT26_NOTFU
565
0
64434
TrEMBL
other Location (Reliability: 4)
A0A3Q0HKG3_ALLSI
554
0
63336
TrEMBL
other Location (Reliability: 3)
A0A8C5L894_JACJA
518
0
59353
TrEMBL
other Location (Reliability: 3)
A0A668VTW3_OREAU
550
0
61941
TrEMBL
other Location (Reliability: 2)
A0A8D0A9S0_SANLU
557
0
62686
TrEMBL
other Location (Reliability: 2)
A0A2R3ZDC3_9TELE
552
0
62343
TrEMBL
other Location (Reliability: 2)
A0A6P3VDD0_OCTDE
462
0
52074
TrEMBL
other Location (Reliability: 1)
A0A7K6RDX2_9GRUI
517
0
59170
TrEMBL
other Location (Reliability: 3)
A0A1S3KIB7_SALSA
563
0
63488
TrEMBL
other Location (Reliability: 2)
A0A1S2ZEB5_ERIEU
552
0
62322
TrEMBL
other Location (Reliability: 1)
A0A7C8ZVM6_OPUST
301
0
33400
TrEMBL
other Location (Reliability: 4)
A0A7K9B8B1_DRONO
560
0
63940
TrEMBL
other Location (Reliability: 3)
A0A6P3R6G6_PTEVA
458
0
52418
TrEMBL
other Location (Reliability: 1)
A0A1A8QTW0_9TELE
571
0
64724
TrEMBL
other Location (Reliability: 2)
A0A8C0MEY4_CANLF
574
0
65640
TrEMBL
other Location (Reliability: 4)
A0A8B7HU07_MICMU
552
0
62316
TrEMBL
other Location (Reliability: 1)
A0A8C4TU21_FALTI
560
0
63995
TrEMBL
other Location (Reliability: 4)
A0A091J289_EGRGA
462
0
52831
TrEMBL
other Location (Reliability: 3)
A0A6J0WG00_ODOVR
462
0
53244
TrEMBL
other Location (Reliability: 2)
A0A6P4ZNF5_BRABE
555
0
62278
TrEMBL
other Location (Reliability: 3)
A0A061IFT2_CRIGR
451
0
51831
TrEMBL
Mitochondrion (Reliability: 5)
A0A663F8K0_AQUCH
544
0
62257
TrEMBL
other Location (Reliability: 4)
A0A8C2LE67_CRIGR
559
0
63987
TrEMBL
other Location (Reliability: 4)
A0A6P6LZU1_CARAU
462
0
52044
TrEMBL
other Location (Reliability: 1)
A0A3P8WA64_CYNSE
557
0
63243
TrEMBL
other Location (Reliability: 2)
A0A8C7I374_ONCKI
586
0
66226
TrEMBL
other Location (Reliability: 1)
A0A7K5EXQ3_PROAR
552
0
62358
TrEMBL
other Location (Reliability: 1)
A0A6P3TG25_SHEEP
458
0
52402
TrEMBL
other Location (Reliability: 1)
H0WLB8_OTOGA
521
0
58962
TrEMBL
other Location (Reliability: 3)
A0A8B7AL51_ORYAF
559
0
63998
TrEMBL
other Location (Reliability: 4)
A0A8C4RXP8_ERPCA
826
0
93705
TrEMBL
other Location (Reliability: 2)
A0A5N4EBL7_CAMDR
572
0
65411
TrEMBL
other Location (Reliability: 4)
A0A4D9F0J4_9SAUR
560
0
63981
TrEMBL
other Location (Reliability: 4)
A0A3P9QAU1_POERE
557
0
62730
TrEMBL
other Location (Reliability: 2)
A0A7K6YN61_ALCTO
517
0
59194
TrEMBL
other Location (Reliability: 3)
A0A6J0E0S2_PERMB
462
0
52071
TrEMBL
other Location (Reliability: 1)
A0A2Y9EKU6_PHYMC
523
0
59208
TrEMBL
other Location (Reliability: 2)
A0A2Y9SHI1_PHYMC
458
0
52372
TrEMBL
other Location (Reliability: 1)
A0A6Q2XPR3_ESOLU
579
0
65152
TrEMBL
other Location (Reliability: 1)
A0A3P8XQ51_ESOLU
596
0
66751
TrEMBL
other Location (Reliability: 2)
A0A8B7H987_MICMU
550
0
62835
TrEMBL
other Location (Reliability: 1)
A0A8C3H966_CHRPI
560
0
63974
TrEMBL
other Location (Reliability: 4)
A0A4W5MNQ0_9TELE
532
0
60111
TrEMBL
other Location (Reliability: 2)
A0A8C7U874_ONCMY
536
0
61255
TrEMBL
other Location (Reliability: 2)
A0A060VX13_ONCMY
559
0
63260
TrEMBL
other Location (Reliability: 2)
A0A8C2ZK90_CYCLU
577
0
65033
TrEMBL
other Location (Reliability: 2)
A0A7J8A0D8_MYOMY
552
0
62418
TrEMBL
other Location (Reliability: 1)
A0A8C4QV73_EPTBU
546
0
60820
TrEMBL
other Location (Reliability: 2)
R0JHK5_ANAPL
524
0
59986
TrEMBL
other Location (Reliability: 3)
A0A2Y9QS64_TRIMA
390
0
43803
TrEMBL
other Location (Reliability: 2)
A0A8C6QP32_NANGA
558
0
63878
TrEMBL
other Location (Reliability: 4)
A0A6J2DYJ6_ZALCA
552
0
62367
TrEMBL
other Location (Reliability: 1)
A0A8C7AZA4_NEOVI
552
0
62326
TrEMBL
other Location (Reliability: 1)
A0A672PYV1_SINGR
512
0
58058
TrEMBL
other Location (Reliability: 2)
A0A672T5N6_SINGR
636
0
71642
TrEMBL
Secretory Pathway (Reliability: 5)
A0A7K7UT99_EUDEL
560
0
63998
TrEMBL
other Location (Reliability: 4)
A0A673TD25_SURSU
534
0
60503
TrEMBL
Secretory Pathway (Reliability: 5)
A0A7K6TG43_CALNI
552
0
62326
TrEMBL
other Location (Reliability: 1)
A0A341C6E9_NEOAA
559
0
63976
TrEMBL
other Location (Reliability: 4)
A0A1W5T6Y0_MEGAM
570
0
64752
TrEMBL
other Location (Reliability: 2)
A0A6G0I147_LARCR
576
0
65147
TrEMBL
other Location (Reliability: 2)
W5MQQ0_LEPOC
551
0
62247
TrEMBL
other Location (Reliability: 2)
A0A7K5VXW9_9SYLV
469
0
53571
TrEMBL
other Location (Reliability: 2)
A0A6J1TVZ7_9SAUR
378
0
43380
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6J3HWD5_SAPAP
559
0
64009
TrEMBL
other Location (Reliability: 4)
A0A6J3HWD5_SAPAP
559
0
64009
TrEMBL
other Location (Reliability: 4)
A0A6P7QTU2_MUSCR
462
0
51744
TrEMBL
other Location (Reliability: 1)
L5K5X1_PTEAL
462
0
52145
TrEMBL
other Location (Reliability: 1)
A0A665VVV7_ECHNA
557
0
62635
TrEMBL
other Location (Reliability: 2)
A0A8C2BY47_CYPCA
560
0
64025
TrEMBL
other Location (Reliability: 1)
A0A8C1N7W2_CYPCA
523
0
59851
TrEMBL
other Location (Reliability: 2)
A0A8C2BRJ7_CYPCA
563
0
64201
TrEMBL
other Location (Reliability: 4)
A0A8C1N9B5_CYPCA
552
0
63037
TrEMBL
other Location (Reliability: 2)
A0A7K9AAL6_9PASS
516
0
58058
TrEMBL
other Location (Reliability: 4)
A0A3P8T1P0_AMPPE
557
0
62654
TrEMBL
other Location (Reliability: 2)
A0A383YNJ7_BALAS
523
0
59249
TrEMBL
other Location (Reliability: 2)
A0A485P1W8_LYNPA
550
0
62793
TrEMBL
other Location (Reliability: 1)
A0A8D0DED4_SANLU
564
0
63470
TrEMBL
other Location (Reliability: 2)
A0A8D2H2U4_UROPR
559
0
64064
TrEMBL
other Location (Reliability: 4)
A0A6P7J9T3_9TELE
571
0
64753
TrEMBL
other Location (Reliability: 2)
A0A6P7MBM1_BETSP
557
0
62717
TrEMBL
other Location (Reliability: 2)
A0A6P8FU03_CLUHA
552
0
62421
TrEMBL
other Location (Reliability: 2)
A0A8C5WNC6_LATLA
515
0
59092
TrEMBL
other Location (Reliability: 4)
A0A7L1ZI03_LEILU
552
0
62322
TrEMBL
other Location (Reliability: 1)
A0A8C9ESR3_PAVCR
483
0
55343
TrEMBL
other Location (Reliability: 2)
A0A5E4C4J5_MARMO
415
0
47355
TrEMBL
other Location (Reliability: 2)
A0A2K5NFN6_CERAT
552
0
62320
TrEMBL
other Location (Reliability: 1)
Q2PUH1_CHICK
560
0
64098
TrEMBL
other Location (Reliability: 5)
A0A1A8FWY5_9TELE
571
0
64734
TrEMBL
other Location (Reliability: 2)
A0A6P9DVX0_PANGU
457
0
52232
TrEMBL
other Location (Reliability: 1)
A0A0Q3UQW1_AMAAE
552
0
62406
TrEMBL
other Location (Reliability: 1)
A0A2K6QX75_RHIRO
534
0
60288
TrEMBL
other Location (Reliability: 4)
A0A6P3IR06_BISBI
462
0
52071
TrEMBL
other Location (Reliability: 1)
A0A6P4ZSI4_BRABE
557
0
62504
TrEMBL
other Location (Reliability: 3)
A0A6P4ZF65_BRABE
546
0
61375
TrEMBL
other Location (Reliability: 3)
A0A6P6M0N7_CARAU
552
0
62322
TrEMBL
other Location (Reliability: 2)
A0A6P6N740_CARAU
387
0
43887
TrEMBL
other Location (Reliability: 4)
A0A6P6N728_CARAU
570
0
64673
TrEMBL
other Location (Reliability: 2)
A3RLM9_MELGA
551
0
62974
TrEMBL
other Location (Reliability: 1)
A0A7L1YTU8_9PASS
561
0
64011
TrEMBL
other Location (Reliability: 5)
F1MBG5_BOVIN
559
0
64006
TrEMBL
other Location (Reliability: 4)
A0A8C4BBM9_9TELE
558
0
63294
TrEMBL
other Location (Reliability: 2)
W5PDB6_SHEEP
536
0
60802
TrEMBL
other Location (Reliability: 5)
H2LFH8_ORYLA
557
0
63169
TrEMBL
other Location (Reliability: 2)
A0A8C8XIH4_PANLE
552
0
62332
TrEMBL
other Location (Reliability: 1)
A0A7K8W5X9_9FURN
473
0
54165
TrEMBL
other Location (Reliability: 3)
A0A2U6EK48_SCOMX
573
0
64916
TrEMBL
other Location (Reliability: 2)
A0A8D3B2K0_SCOMX
567
0
63853
TrEMBL
other Location (Reliability: 3)
A0A673LVH4_9TELE
549
0
62696
TrEMBL
other Location (Reliability: 2)
A0A8C8HFX4_ONCTS
540
1
60981
TrEMBL
other Location (Reliability: 2)
A0A7K5N4Y6_CHRMC
551
0
62217
TrEMBL
other Location (Reliability: 1)
A0A8C8IXP8_ONCTS
576
0
65187
TrEMBL
other Location (Reliability: 2)
A0A2I2UD13_FELCA
558
0
63897
TrEMBL
other Location (Reliability: 4)
A0A2U3XPM9_LEPWE
548
0
62635
TrEMBL
other Location (Reliability: 2)
A0A6Q2YX82_ESOLU
566
0
64264
TrEMBL
other Location (Reliability: 2)
A0A096N9P0_PAPAN
533
0
61059
TrEMBL
other Location (Reliability: 2)
A0A2R9CJR2_PANPA
542
0
61179
TrEMBL
other Location (Reliability: 5)
A0A7J8F3Z3_ROUAE
574
0
65606
TrEMBL
other Location (Reliability: 4)
A0A8D0E0J0_9SAUR
550
0
62799
TrEMBL
other Location (Reliability: 1)
A0A3B3C1N3_ORYME
572
0
64702
TrEMBL
other Location (Reliability: 2)
A0A6I9X5A9_9SAUR
550
0
62674
TrEMBL
other Location (Reliability: 2)
A0A8C6YMQ1_NOTPE
560
0
63926
TrEMBL
other Location (Reliability: 3)
A0A8C7ND94_ONCMY
545
0
62269
TrEMBL
other Location (Reliability: 2)
A0A8C9WEE7_SCLFO
567
0
63846
TrEMBL
other Location (Reliability: 1)
A0A5C6MVV1_9TELE
626
0
70427
TrEMBL
Mitochondrion (Reliability: 3)
A0A5N5LB17_PANHP
546
0
61554
TrEMBL
other Location (Reliability: 2)
A0A8C2TMY5_COTJA
552
0
62403
TrEMBL
other Location (Reliability: 2)
A0A8C3M438_CHRPC
552
0
62417
TrEMBL
other Location (Reliability: 2)
A0A8B9SYK4_ANAPL
559
0
63901
TrEMBL
other Location (Reliability: 4)
A0A8B9ZPU0_9AVES
552
0
62400
TrEMBL
other Location (Reliability: 1)
A0A673CAR7_9TELE
541
0
61089
TrEMBL
other Location (Reliability: 2)
Q2LGG0_HORSE
550
0
62780
TrEMBL
other Location (Reliability: 1)
A0A3Q4IG85_NEOBR
555
0
62576
TrEMBL
other Location (Reliability: 2)
A0A672RW86_SINGR
574
0
65240
TrEMBL
other Location (Reliability: 2)
G3N889_GASAC
552
0
62079
TrEMBL
other Location (Reliability: 1)
A0A7L0WC70_ALELA
560
0
63942
TrEMBL
other Location (Reliability: 4)
A0A8C6IEP9_MUSSI
532
0
59755
TrEMBL
other Location (Reliability: 3)
A0A0D9RWH7_CHLSB
501
0
57922
TrEMBL
other Location (Reliability: 1)
A0A672HKS2_SALFA
572
0
64684
TrEMBL
other Location (Reliability: 2)
A0A7L1T0H5_ARAGA
436
0
50651
TrEMBL
other Location (Reliability: 3)
A0A8I3NR33_CANLF
552
0
62310
TrEMBL
other Location (Reliability: 1)
A0A091HK93_CALAN
521
0
59020
TrEMBL
other Location (Reliability: 3)
A0A667I8W0_LYNCA
552
0
62300
TrEMBL
other Location (Reliability: 1)
W5MZI1_LEPOC
561
0
63990
TrEMBL
other Location (Reliability: 2)
A0A8C4I5A9_DICLA
573
0
64847
TrEMBL
other Location (Reliability: 2)
A0A7L4JIH9_9AVES
517
0
59224
TrEMBL
other Location (Reliability: 3)
A0A674EXY3_SALTR
566
0
64449
TrEMBL
other Location (Reliability: 3)
A0A8C4JY18_DRONO
514
0
58020
TrEMBL
other Location (Reliability: 3)
A0A6J1U2Y6_9SAUR
457
0
52283
TrEMBL
other Location (Reliability: 1)
A0A2K6BJ02_MACNE
559
0
63995
TrEMBL
other Location (Reliability: 4)
A0A7L2FBF9_QUIME
561
0
63883
TrEMBL
other Location (Reliability: 4)
A0A6A1Q8B8_BALPH
590
0
66711
TrEMBL
other Location (Reliability: 1)
A0A8C5CU66_GADMO
575
0
64994
TrEMBL
other Location (Reliability: 1)
A0A8J4U7L8_CLAMG
466
0
53127
TrEMBL
other Location (Reliability: 2)
A0A8C1TQC7_CYPCA
539
0
61502
TrEMBL
other Location (Reliability: 2)
A0A8C1PMR1_CYPCA
552
0
62234
TrEMBL
other Location (Reliability: 2)
A0A2K6V8G1_SAIBB
462
0
52069
TrEMBL
other Location (Reliability: 1)
A0A7K8B9T3_9CORV
552
0
62336
TrEMBL
other Location (Reliability: 1)
A0A3Q0HGG8_ALLSI
461
0
52748
TrEMBL
other Location (Reliability: 1)
A0A668VTV5_OREAU
557
0
62746
TrEMBL
other Location (Reliability: 2)
A0A8D0ACV9_SANLU
509
0
58009
TrEMBL
other Location (Reliability: 2)
A0A3P8RGJ6_ASTCA
571
0
64552
TrEMBL
other Location (Reliability: 2)
A0A7L1A3Q3_9PASS
561
0
64038
TrEMBL
other Location (Reliability: 5)
A0A8C9M4S4_PANTA
538
0
60907
TrEMBL
other Location (Reliability: 2)
A0A7L4H1Y8_PODST
551
0
62284
TrEMBL
other Location (Reliability: 1)
A0A091DF85_FUKDA
791
0
90190
TrEMBL
other Location (Reliability: 3)
G3V715_RAT
526
0
59344
TrEMBL
other Location (Reliability: 3)
A0A3Q0DTV9_CARSF
534
0
61048
TrEMBL
other Location (Reliability: 2)
A0A3Q7VNM4_URSAR
536
0
61318
TrEMBL
other Location (Reliability: 3)
A0A2U9C3U2_SCOMX
557
0
62755
TrEMBL
other Location (Reliability: 2)
A0A8C1DJW0_CYPCA
573
0
65085
TrEMBL
other Location (Reliability: 2)
A0A671FVJ5_RHIFE
574
0
65696
TrEMBL
other Location (Reliability: 4)
A0A8C0C867_BALMU
559
0
63949
TrEMBL
other Location (Reliability: 4)
Q3TUQ7_MOUSE
550
0
62728
TrEMBL
other Location (Reliability: 1)
A0A0Q3PLM7_AMAAE
449
0
52222
TrEMBL
other Location (Reliability: 5)
A0A671QZF1_9TELE
567
0
64578
TrEMBL
other Location (Reliability: 2)
A0A671QZG4_9TELE
573
0
65000
TrEMBL
other Location (Reliability: 2)
A0A6P4ZF61_BRABE
566
0
63407
TrEMBL
other Location (Reliability: 3)
A0A8C6F2Q6_MONMO
559
0
63990
TrEMBL
other Location (Reliability: 4)
A0A8C7GS44_ONCKI
566
0
63769
TrEMBL
other Location (Reliability: 3)
A0A8C4XE67_ERPCA
531
0
60016
TrEMBL
other Location (Reliability: 2)
A0A6G1QHD4_9TELE
571
0
64619
TrEMBL
other Location (Reliability: 2)
A0A8D3D6X9_SCOMX
581
0
65784
TrEMBL
other Location (Reliability: 3)
A0A091QVW6_LEPDC
521
0
59063
TrEMBL
other Location (Reliability: 3)
A0A6D2WLV9_PONAB
559
0
64009
TrEMBL
other Location (Reliability: 4)
A0A673ICI8_9TELE
552
0
62213
TrEMBL
other Location (Reliability: 2)
A0A3Q3GP96_9LABR
573
0
64830
TrEMBL
other Location (Reliability: 2)
A0A093G9M5_DRYPU
517
0
59123
TrEMBL
other Location (Reliability: 3)
A0A7L2LIU8_9SYLV
561
0
63983
TrEMBL
other Location (Reliability: 5)
A0A8C8IXN3_ONCTS
588
0
66404
TrEMBL
other Location (Reliability: 2)
A0A7K6BE70_UPUEP
560
0
64055
TrEMBL
other Location (Reliability: 5)
A0A7F8QSC6_LEPWE
415
0
47299
TrEMBL
other Location (Reliability: 2)
A0A6Q2XMQ8_ESOLU
579
0
65284
TrEMBL
other Location (Reliability: 2)
A0A7K7K151_AGEPH
547
0
61823
TrEMBL
other Location (Reliability: 2)
A0A3Q3JPV4_MONAL
559
0
63453
TrEMBL
other Location (Reliability: 2)
A0A7N4PKM2_SARHA
559
0
64107
TrEMBL
other Location (Reliability: 4)
A0A3Q7Q4E9_CALUR
574
0
65594
TrEMBL
other Location (Reliability: 4)
A0A3Q3A7J3_KRYMA
573
0
64714
TrEMBL
other Location (Reliability: 2)
A0A8C8RAB3_9SAUR
560
0
64071
TrEMBL
other Location (Reliability: 4)
A0A8C9LR15_9PRIM
581
0
66005
TrEMBL
other Location (Reliability: 2)
A0A852MAH9_9PASS
551
0
62165
TrEMBL
other Location (Reliability: 1)
A0A2Y9R3R0_TRIMA
368
0
41453
TrEMBL
other Location (Reliability: 1)
A0A8C3K1B5_9CHAR
528
0
60302
TrEMBL
other Location (Reliability: 2)
A0MZF5_HUMAN
552
0
62306
TrEMBL
other Location (Reliability: 1)
A0A7K8X1B9_9PICI
552
0
62280
TrEMBL
other Location (Reliability: 1)
L8I6G9_9CETA
532
0
60391
TrEMBL
other Location (Reliability: 5)
A0A093R531_PHACA
511
0
57813
TrEMBL
other Location (Reliability: 3)
G3RZF9_GORGO
574
0
65551
TrEMBL
other Location (Reliability: 4)
A0A852LHS0_9AVES
551
0
62247
TrEMBL
other Location (Reliability: 1)
A0A7K7IKE0_LOXCU
547
0
61823
TrEMBL
other Location (Reliability: 2)
A0A667G364_LYNCA
521
0
59698
TrEMBL
other Location (Reliability: 3)
A0A7K9DKC5_9AVES
551
0
62233
TrEMBL
other Location (Reliability: 1)
A0A3Q3D6R9_HIPCM
569
0
64091
TrEMBL
other Location (Reliability: 2)
A0A852IPG1_9PICI
551
0
62183
TrEMBL
other Location (Reliability: 1)
A0A6I9P5H2_9TELE
475
0
54221
TrEMBL
other Location (Reliability: 2)
A0A6I9PIH1_9TELE
573
0
64735
TrEMBL
other Location (Reliability: 2)
A0A7K4ZI38_9AVES
551
0
62247
TrEMBL
other Location (Reliability: 1)
A0A3B4F2R3_9CICH
506
0
57588
TrEMBL
other Location (Reliability: 2)
A0A6P4VTJ5_PANPR
552
0
62332
TrEMBL
other Location (Reliability: 1)
A0A665WZ47_ECHNA
539
0
61506
TrEMBL
other Location (Reliability: 2)
A0A5J5MZ28_MUNRE
560
0
63254
TrEMBL
other Location (Reliability: 2)
A0A851SRV5_9AVES
517
0
59170
TrEMBL
other Location (Reliability: 3)
A0A8C5ARH6_GADMO
582
0
65538
TrEMBL
other Location (Reliability: 1)
A0A8C1TS43_CYPCA
566
0
64533
TrEMBL
other Location (Reliability: 2)
A0A7L2E842_ANTMN
392
0
45517
TrEMBL
other Location (Reliability: 3)
A0A8B8SAT8_CAMFR
559
0
63992
TrEMBL
other Location (Reliability: 4)
A0A7L1LTA2_BOMGA
562
0
64077
TrEMBL
other Location (Reliability: 5)
A0A2K6GBM4_PROCO
574
0
65709
TrEMBL
other Location (Reliability: 4)
A0A485MH76_LYNPA
536
0
60934
TrEMBL
other Location (Reliability: 1)
A0A437CV87_ORYJA
572
0
64669
TrEMBL
other Location (Reliability: 2)
A0A8C9K527_PANTA
574
0
65514
TrEMBL
other Location (Reliability: 5)
A0A8C6TEG1_9GOBI
566
0
63481
TrEMBL
other Location (Reliability: 3)
A0A7K4W1A7_9TYRA
551
0
62261
TrEMBL
other Location (Reliability: 1)
A0A6P7YHB4_9AMPH
551
0
62392
TrEMBL
other Location (Reliability: 2)
A0A6I8S1E5_XENTR
560
0
64038
TrEMBL
other Location (Reliability: 4)
A0A8C3MG11_GEOPR
561
0
63925
TrEMBL
other Location (Reliability: 5)
A0A4W4G156_ELEEL
560
0
64036
TrEMBL
other Location (Reliability: 3)
A0A6P4WVS2_PANPR
536
0
61270
TrEMBL
other Location (Reliability: 3)
A0A6P4X6I1_PANPR
486
0
55531
TrEMBL
other Location (Reliability: 4)
A0A3Q7WCS4_URSAR
415
0
47333
TrEMBL
other Location (Reliability: 2)
A0A6P3IBZ1_BISBI
458
0
52402
TrEMBL
other Location (Reliability: 1)
A0A2U9CH74_SCOMX
572
0
64683
TrEMBL
other Location (Reliability: 2)
A0A6I9LNF6_PERMB
552
0
62321
TrEMBL
other Location (Reliability: 1)
A0A1A8LAJ7_9TELE
571
0
64720
TrEMBL
other Location (Reliability: 2)
A0A8B9RBP0_ASTMX
560
0
62938
TrEMBL
other Location (Reliability: 2)
H3CMP8_TETNG
554
0
62583
TrEMBL
other Location (Reliability: 2)
A0A6J1ZC82_ACIJB
477
0
53789
TrEMBL
other Location (Reliability: 1)
A0A7K7KPW5_9AVES
551
0
62287
TrEMBL
other Location (Reliability: 1)
A0A5A4DW65_TACFU
573
0
65053
TrEMBL
other Location (Reliability: 2)
A0A663FLL7_AQUCH
552
0
62330
TrEMBL
other Location (Reliability: 1)
A0A7K9X9E9_9GRUI
517
0
59227
TrEMBL
other Location (Reliability: 3)
A0A3B4ZRS8_9TELE
557
0
62654
TrEMBL
other Location (Reliability: 2)
G7MH95_MACMU
521
0
58973
TrEMBL
other Location (Reliability: 3)
U3CGM7_CALJA
552
0
62316
TrEMBL
other Location (Reliability: 2)
A0A7J5YIN9_DISMA
502
0
57612
TrEMBL
other Location (Reliability: 2)
A0A093NH83_PYGAD
521
0
58994
TrEMBL
other Location (Reliability: 3)
A0A6G1PLR2_9TELE
581
0
65596
TrEMBL
other Location (Reliability: 1)
A0A8C5D3S1_9TELE
561
0
63365
TrEMBL
other Location (Reliability: 2)
A0A2Y9IKW5_ENHLU
574
0
65612
TrEMBL
other Location (Reliability: 4)
A0A8D3BVN6_SCOMX
542
0
61188
TrEMBL
other Location (Reliability: 2)
A0A2J8V963_PONAB
552
0
62320
TrEMBL
other Location (Reliability: 1)
A0A673LXZ9_9TELE
568
0
65001
TrEMBL
other Location (Reliability: 3)
A0A673LY34_9TELE
573
0
65106
TrEMBL
other Location (Reliability: 2)
A0A8C0UG01_CYACU
528
0
59680
TrEMBL
other Location (Reliability: 3)
A0A7L3L9C2_9CHAR
547
0
61934
TrEMBL
other Location (Reliability: 1)
A0A7L0U660_CHOAC
551
0
62229
TrEMBL
other Location (Reliability: 1)
A0A091MFB3_9PASS
438
0
49998
TrEMBL
other Location (Reliability: 4)
A0A7L3VH18_MOLAT
547
0
61867
TrEMBL
other Location (Reliability: 2)
A0A8C8J4X9_ONCTS
578
0
65443
TrEMBL
other Location (Reliability: 2)
A0A8C8G8M3_ONCTS
556
0
63095
TrEMBL
other Location (Reliability: 1)
E7F9C4_DANRE
553
0
62420
TrEMBL
other Location (Reliability: 2)
E7F9C4_DANRE
553
0
62420
TrEMBL
other Location (Reliability: 2)
A0A671UX38_SPAAU
562
0
63338
TrEMBL
other Location (Reliability: 3)
A0A7L4NFD1_9AVES
551
0
62217
TrEMBL
other Location (Reliability: 1)
A0A6Q2YY37_ESOLU
573
0
64815
TrEMBL
other Location (Reliability: 3)
A0A3B3U603_9TELE
551
0
62558
TrEMBL
other Location (Reliability: 2)
A0A890CAI7_TRASE
560
0
64044
TrEMBL
other Location (Reliability: 4)
A0A2R9B7S7_PANPA
496
0
57068
TrEMBL
other Location (Reliability: 4)
A0A7L1JSQ7_RYNNI
479
0
55403
TrEMBL
other Location (Reliability: 4)
A0A7L1JS42_RYNNI
476
0
54985
TrEMBL
other Location (Reliability: 3)
A0A8C9HG47_9PRIM
533
0
61073
TrEMBL
other Location (Reliability: 2)
A0A7K8NLD7_CASCA
560
0
63940
TrEMBL
other Location (Reliability: 3)
A0A4W5QIT6_9TELE
561
0
63173
TrEMBL
other Location (Reliability: 2)
A0A5C6NJX1_9TELE
572
0
64843
TrEMBL
other Location (Reliability: 2)
A0A670YLF0_PSETE
551
0
62877
TrEMBL
other Location (Reliability: 2)
G3TA29_LOXAF
552
0
62390
TrEMBL
other Location (Reliability: 1)
A0A672RX30_SINGR
558
0
63890
TrEMBL
other Location (Reliability: 4)
A0A7N8Y831_9TELE
566
0
64451
TrEMBL
other Location (Reliability: 3)
A0A7N8WNC5_9TELE
561
0
63283
TrEMBL
other Location (Reliability: 4)
B2RA25_HUMAN
552
0
62330
TrEMBL
other Location (Reliability: 1)
A0A6P8NU89_GEOSA
551
0
62244
TrEMBL
other Location (Reliability: 1)
U3IZ67_ANAPP
539
0
61650
TrEMBL
other Location (Reliability: 4)
A0A7L1D6F6_9PASS
561
0
63981
TrEMBL
other Location (Reliability: 5)
A0A8B9YPC4_BOSMU
559
0
64006
TrEMBL
other Location (Reliability: 4)
A0A218UVK5_9PASE
478
0
54957
TrEMBL
other Location (Reliability: 5)
A0A6P5JEC9_PHACI
551
0
62226
TrEMBL
other Location (Reliability: 2)
A0A7L3FCL9_9GRUI
517
0
59241
TrEMBL
other Location (Reliability: 3)
A0A7K7H583_ERIRU
562
0
63238
TrEMBL
other Location (Reliability: 2)
A0A2K6BJ13_MACNE
574
0
65638
TrEMBL
other Location (Reliability: 4)
A0A674M9Y6_TAKRU
527
0
60181
TrEMBL
other Location (Reliability: 2)
A0A091QF83_MERNU
517
0
59199
TrEMBL
other Location (Reliability: 3)
A0A452H7H3_9SAUR
659
0
74924
TrEMBL
other Location (Reliability: 4)
A0A8C1TNS6_CYPCA
573
0
65071
TrEMBL
other Location (Reliability: 2)
A0A7K9A8F5_9PASS
561
0
63997
TrEMBL
other Location (Reliability: 5)
A0A8C1S5R0_CYPCA
552
0
63128
TrEMBL
other Location (Reliability: 1)
A0A485NVV1_LYNPA
521
0
59698
TrEMBL
other Location (Reliability: 3)
A0A4X2JVK3_VOMUR
559
0
64093
TrEMBL
other Location (Reliability: 5)
A0A6P8FPP4_CLUHA
574
0
64725
TrEMBL
other Location (Reliability: 2)
A0A6P6DDE4_OCTDE
598
0
67491
TrEMBL
other Location (Reliability: 1)
A0A8I6GCD0_RAT
517
0
59266
TrEMBL
other Location (Reliability: 3)
A0A7L4CUP0_9AVES
517
0
59199
TrEMBL
other Location (Reliability: 3)
A0A094KP75_ANTCR
521
0
58988
TrEMBL
other Location (Reliability: 3)
A0A8C0XA28_CASCN
559
0
63996
TrEMBL
other Location (Reliability: 5)
A0A2R3ZDC6_9TELE
570
0
64700
TrEMBL
other Location (Reliability: 2)
A0A6P5DKP9_BOSIN
458
0
52402
TrEMBL
other Location (Reliability: 1)
A1E4B7_MELGA
552
0
62403
TrEMBL
other Location (Reliability: 2)
F1MQV7_BOVIN
552
0
62321
TrEMBL
other Location (Reliability: 1)
A0A8C0ERN9_BUBBB
528
0
60418
TrEMBL
other Location (Reliability: 2)
A0A7K5FVQ7_PROAR
560
0
63987
TrEMBL
other Location (Reliability: 4)
A0A836D6H5_SHEEP
415
0
47208
TrEMBL
Mitochondrion (Reliability: 4)
A0A8C4T406_ERPCA
538
0
60728
TrEMBL
other Location (Reliability: 2)
A0A8C8W9H5_PANLE
559
0
63994
TrEMBL
other Location (Reliability: 4)
A0A7K8F3B7_9CORV
552
0
62336
TrEMBL
other Location (Reliability: 1)
A0A2U6EJK6_SCOMX
557
0
62752
TrEMBL
other Location (Reliability: 2)
A0A8D3D198_SCOMX
579
0
65938
TrEMBL
Secretory Pathway (Reliability: 1)
A0A7K7Y109_THRLU
401
0
45797
TrEMBL
other Location (Reliability: 3)
A0A1A8ICZ7_NOTKU
475
0
54106
TrEMBL
other Location (Reliability: 2)
A0A673JDU9_9TELE
539
0
61447
TrEMBL
other Location (Reliability: 2)
A0A673J6C1_9TELE
556
0
63649
TrEMBL
other Location (Reliability: 3)
A0A8C4Y2X2_9SAUR
560
0
64015
TrEMBL
other Location (Reliability: 4)
A0A669C0S0_ORENI
560
0
63251
TrEMBL
other Location (Reliability: 5)
A0A8C8GA36_ONCTS
557
0
63381
TrEMBL
other Location (Reliability: 2)
A0A8C8INQ9_ONCTS
560
0
63252
TrEMBL
other Location (Reliability: 2)
A0A2U3XPK0_LEPWE
559
0
64008
TrEMBL
other Location (Reliability: 4)
A0A851FIQ4_PITSO
562
0
64108
TrEMBL
Mitochondrion (Reliability: 5)
A0A3P8XFA6_ESOLU
564
0
63975
TrEMBL
other Location (Reliability: 2)
A0A6Q2XY03_ESOLU
553
0
62992
TrEMBL
other Location (Reliability: 2)
A0A3B3VHV3_9TELE
564
0
63828
TrEMBL
other Location (Reliability: 2)
A0A3B3V6E5_9TELE
557
0
62685
TrEMBL
other Location (Reliability: 2)
A0A340YE61_LIPVE
574
0
65562
TrEMBL
other Location (Reliability: 4)
A0A834C8U8_ORYME
422
0
47123
TrEMBL
other Location (Reliability: 2)
A0A8C7SYL2_ONCMY
568
0
63860
TrEMBL
other Location (Reliability: 5)
A0A8C3CZ52_CAIMO
650
0
73677
TrEMBL
other Location (Reliability: 4)
A0A087YBV4_POEFO
557
0
62601
TrEMBL
other Location (Reliability: 2)
A0A673BCC0_9TELE
577
0
65357
TrEMBL
other Location (Reliability: 2)
A0A673BAD5_9TELE
577
0
65497
TrEMBL
other Location (Reliability: 3)
A0A3Q1JRD2_ANATE
574
0
64892
TrEMBL
other Location (Reliability: 2)
A0A8C6EFQ0_MOSMO
559
0
63976
TrEMBL
other Location (Reliability: 5)
A0A8C6ZYD1_NEOVI
574
0
65626
TrEMBL
other Location (Reliability: 4)
A0A672RX49_SINGR
540
0
61616
TrEMBL
other Location (Reliability: 2)
A0A6P8PWC0_GEOSA
388
0
44392
TrEMBL
other Location (Reliability: 2)
A0A6P8V723_GYMAC
556
0
62688
TrEMBL
other Location (Reliability: 2)
A0A6P8Q013_GEOSA
551
0
63030
TrEMBL
other Location (Reliability: 2)
A0A1W5T6Y8_MEGAM
545
0
61530
TrEMBL
other Location (Reliability: 1)
G1RX86_NOMLE
552
0
62293
TrEMBL
other Location (Reliability: 1)
A0A6P5DJE0_BOSIN
559
0
64006
TrEMBL
other Location (Reliability: 4)
A0A668AX19_9TELE
529
0
60261
TrEMBL
other Location (Reliability: 2)
A0A673ZYQ9_SALTR
559
0
63318
TrEMBL
other Location (Reliability: 2)
A0A673WCR3_SALTR
565
0
63614
TrEMBL
other Location (Reliability: 2)
A0A8C0GXU0_CHEAB
551
0
62987
TrEMBL
other Location (Reliability: 1)
A0A151M4H2_ALLMI
527
0
60194
TrEMBL
other Location (Reliability: 1)
A0A6F9DNX7_9ASCI
558
0
62960
TrEMBL
other Location (Reliability: 2)
A0A099ZHU0_TINGU
390
0
44355
TrEMBL
other Location (Reliability: 2)
A0A6J0GBY6_9PASS
474
0
53240
TrEMBL
other Location (Reliability: 1)
A0A811YEK3_NYCPR
574
0
65656
TrEMBL
other Location (Reliability: 4)
A0A8C7XW46_9TELE
582
0
65762
TrEMBL
other Location (Reliability: 2)
A0A8C7XU55_9TELE
562
0
63540
TrEMBL
other Location (Reliability: 2)
A0A2K6MRR4_RHIBE
539
0
60731
TrEMBL
other Location (Reliability: 2)
A0A8C1ZR69_CYPCA
552
0
62250
TrEMBL
other Location (Reliability: 2)
A0A8C1ZLC2_CYPCA
552
0
62372
TrEMBL
other Location (Reliability: 2)
A0A7K8ZCG8_9PASS
552
0
62330
TrEMBL
other Location (Reliability: 1)
A0A7K9YKD9_9GALL
551
0
62260
TrEMBL
other Location (Reliability: 1)
A0A8C1S814_CYPCA
556
0
63254
TrEMBL
other Location (Reliability: 3)
A0A8C6LSX6_NOTFU
578
0
65635
TrEMBL
other Location (Reliability: 4)
H3A9U2_LATCH
553
0
62312
TrEMBL
other Location (Reliability: 1)
L9KYH0_TUPCH
391
0
44692
TrEMBL
other Location (Reliability: 1)
V9KQW7_CALMI
549
0
62224
TrEMBL
other Location (Reliability: 2)
A0A2G9S1I9_LITCT
419
0
48767
TrEMBL
other Location (Reliability: 4)
A0A1S2ZDE0_ERIEU
460
0
52428
TrEMBL
other Location (Reliability: 1)
A0A8J7NYB9_ATRSP
559
0
63533
TrEMBL
other Location (Reliability: 2)
W5UDD8_ICTPU
546
0
61647
TrEMBL
other Location (Reliability: 2)
A0A8C0C6K2_BALMU
552
0
62337
TrEMBL
other Location (Reliability: 1)
A0A1A8E1G7_9TELE
571
0
64670
TrEMBL
other Location (Reliability: 2)
A0A671Q6V8_9TELE
553
0
63344
TrEMBL
other Location (Reliability: 2)
A0A7K7HCV1_9PASS
551
0
62277
TrEMBL
other Location (Reliability: 1)
A0A3L7I5D2_CRIGR
519
0
59493
TrEMBL
other Location (Reliability: 2)
A0A8J8XCP7_CALJA
574
0
65553
TrEMBL
other Location (Reliability: 3)
A0A8C6AU35_MONMO
574
0
65566
TrEMBL
other Location (Reliability: 4)
A0A8B9FDI1_9PSIT
552
0
62386
TrEMBL
other Location (Reliability: 1)
A0A8B9FDI1_9PSIT
552
0
62386
TrEMBL
other Location (Reliability: 1)
A0A8C5D0A8_9TELE
570
0
64430
TrEMBL
Mitochondrion (Reliability: 5)
A0A6D2XY28_PANTR
559
0
64009
TrEMBL
other Location (Reliability: 4)
A0A0A0AG54_CHAVO
521
0
58993
TrEMBL
other Location (Reliability: 3)
A0A6F9B8V5_9TELE
566
0
63617
TrEMBL
other Location (Reliability: 2)
A0A8C3GX66_9CORV
647
0
72493
TrEMBL
Mitochondrion (Reliability: 2)
A0A7L0ILZ7_PIPCL
552
0
62344
TrEMBL
other Location (Reliability: 1)
A0A2K5N892_CERAT
559
0
63995
TrEMBL
other Location (Reliability: 4)
A0A7K8CC22_9CORV
561
0
63983
TrEMBL
other Location (Reliability: 5)
A0A515J4J2_CTEID
552
0
62286
TrEMBL
other Location (Reliability: 2)
A0A2I3NFU9_PAPAN
532
0
60794
TrEMBL
other Location (Reliability: 3)
A0A3Q0CTZ5_MESAU
552
0
62236
TrEMBL
other Location (Reliability: 1)
A0A851TWT3_9PASS
551
0
62123
TrEMBL
other Location (Reliability: 1)
A0A851TWT3_9PASS
551
0
62123
TrEMBL
other Location (Reliability: 1)
A0A8C9HFT3_9PRIM
574
0
65553
TrEMBL
other Location (Reliability: 4)
A0A8C9HPJ9_9PRIM
552
0
62320
TrEMBL
other Location (Reliability: 1)
A0A7K9LPN7_9PASS
553
0
62391
TrEMBL
other Location (Reliability: 1)
A0A4W5K233_9TELE
538
0
61410
TrEMBL
other Location (Reliability: 2)
A0A8C7U2F5_ONCMY
556
0
63421
TrEMBL
other Location (Reliability: 3)
A0A8C5QBM4_9ANUR
537
0
60372
TrEMBL
other Location (Reliability: 2)
A0A401PEE6_SCYTO
501
1
56695
TrEMBL
Secretory Pathway (Reliability: 4)
A0A8C3KA52_9CHAR
552
0
62330
TrEMBL
other Location (Reliability: 1)
F6V6T6_HORSE
633
0
71302
TrEMBL
other Location (Reliability: 2)
A0A672PX66_SINGR
511
0
57876
TrEMBL
other Location (Reliability: 2)
A0A672RWT4_SINGR
569
0
64990
TrEMBL
other Location (Reliability: 2)
A0A672T6U1_SINGR
551
0
62175
TrEMBL
other Location (Reliability: 2)
A0A8C9MUP0_SERCA
462
0
52128
TrEMBL
other Location (Reliability: 1)
A0A7N8YPN5_9TELE
566
0
64093
TrEMBL
other Location (Reliability: 2)
A0A7N8XVM1_9TELE
565
0
63611
TrEMBL
other Location (Reliability: 2)
A0A7K5IED2_TOXRE
561
0
63983
TrEMBL
other Location (Reliability: 5)
A0A8D0JF14_PIG
525
0
60246
TrEMBL
Secretory Pathway (Reliability: 5)
I3LJD8_PIG
559
0
63992
TrEMBL
other Location (Reliability: 4)
A0A093PZ53_9PASS
521
0
59068
TrEMBL
other Location (Reliability: 3)
A0A667YSH6_9TELE
556
0
62689
TrEMBL
other Location (Reliability: 2)
A0A668AKJ9_9TELE
575
0
65213
TrEMBL
other Location (Reliability: 4)
A0A8B9EP78_ANSCY
Anser cygnoid
521
0
59600
TrEMBL
other Location (Reliability: 3)
A0A6J1U0Q8_9SAUR
552
0
62935
TrEMBL
other Location (Reliability: 2)
A0A8C6JUV0_MELUD
561
0
64127
TrEMBL
other Location (Reliability: 4)
A0A8C5NIK1_JUNHY
552
0
62350
TrEMBL
other Location (Reliability: 1)
A0A5F9CCC4_RABIT
642
0
72990
TrEMBL
other Location (Reliability: 2)
A0A8C7XVP0_9TELE
558
0
63327
TrEMBL
other Location (Reliability: 2)
A0A384C8M9_URSMA
536
0
61318
TrEMBL
other Location (Reliability: 3)
A0A452VAN0_URSMA
390
0
43761
TrEMBL
other Location (Reliability: 2)
A0A6P9BLW0_PANGU
371
0
41809
TrEMBL
Secretory Pathway (Reliability: 3)
A0A2K6B0E8_MACNE
552
0
62320
TrEMBL
other Location (Reliability: 1)
A0A8C3QLR2_9PASS
591
0
66641
TrEMBL
other Location (Reliability: 1)
A0A8C2HH02_CYPCA
552
0
62223
TrEMBL
other Location (Reliability: 2)
A0A8D0EN19_STROC
458
0
52360
TrEMBL
other Location (Reliability: 1)
A0A384AYR8_BALAS
415
0
47267
TrEMBL
other Location (Reliability: 2)
A0A2K6V8H8_SAIBB
537
0
60999
TrEMBL
Secretory Pathway (Reliability: 5)
A0A7K7NFU7_HALAL
551
0
62231
TrEMBL
other Location (Reliability: 1)
A0A7L0K3X3_CHATO
517
0
59170
TrEMBL
other Location (Reliability: 3)
A0A3S2ULZ1_ORYJA
557
0
62722
TrEMBL
other Location (Reliability: 2)
A0A8D2EQ04_THEGE
559
0
63995
TrEMBL
other Location (Reliability: 4)
A0A7K9G5A6_LOXLE
517
0
59189
TrEMBL
other Location (Reliability: 3)
A0A091LPW3_9GRUI
517
0
59110
TrEMBL
other Location (Reliability: 3)
A0A4W4G1S1_ELEEL
542
0
62157
TrEMBL
other Location (Reliability: 2)
A0A4X1T2W0_PIG
559
0
63992
TrEMBL
other Location (Reliability: 4)
A0A8C2D6S2_CYPCA
539
0
61516
TrEMBL
other Location (Reliability: 2)
A0A1A8IMF6_NOTKU
571
0
64698
TrEMBL
other Location (Reliability: 2)
Q2LAI0_CHICK
552
0
62387
TrEMBL
other Location (Reliability: 2)
H2R5J0_PANTR
559
0
64009
TrEMBL
other Location (Reliability: 4)
A0A3Q0GRF5_ALLSI
461
0
52041
TrEMBL
other Location (Reliability: 1)
A0A6J1ZEW7_ACIJB
552
0
62340
TrEMBL
other Location (Reliability: 1)
A0A7J8FCF1_MOLMO
419
0
46943
TrEMBL
other Location (Reliability: 2)
A0A8B9Z3R5_9AVES
527
0
60251
TrEMBL
other Location (Reliability: 2)
A0A2K5S359_CEBIM
552
0
62320
TrEMBL
other Location (Reliability: 1)
F7HR71_MACMU
574
0
65638
TrEMBL
other Location (Reliability: 4)
F7HR74_MACMU
550
0
62794
TrEMBL
other Location (Reliability: 1)
H9FBH4_MACMU
550
0
62117
TrEMBL
other Location (Reliability: 1)
A0A6J3EHW2_AYTFU
559
0
63901
TrEMBL
other Location (Reliability: 4)
A0A7K8WSC1_9FURN
562
0
64340
TrEMBL
other Location (Reliability: 5)
A0A7L1BAA7_GYMTI
517
0
59146
TrEMBL
other Location (Reliability: 3)
A0A8D3EC59_SCOMX
600
0
67941
TrEMBL
other Location (Reliability: 2)
A0A091Q8D2_LEPDC
517
0
59156
TrEMBL
other Location (Reliability: 3)
A0A2J8WBH7_PONAB
574
0
65523
TrEMBL
other Location (Reliability: 4)
H2N793_PONAB
552
0
62320
TrEMBL
other Location (Reliability: 1)
A0A7L0R7V2_SETKR
561
0
63939
TrEMBL
other Location (Reliability: 5)
A0A7L0R7V2_SETKR
561
0
63939
TrEMBL
other Location (Reliability: 5)
A0A250YIM3_CASCN
458
0
52422
TrEMBL
other Location (Reliability: 1)
A0A8C0XK01_CASCN
532
0
60331
TrEMBL
Secretory Pathway (Reliability: 5)
F7BFG2_MONDO
559
0
64093
TrEMBL
other Location (Reliability: 5)
A0A7L2MKG4_9PASS
473
0
53893
TrEMBL
other Location (Reliability: 3)
A0A803TFR2_ANOCA
460
0
52091
TrEMBL
other Location (Reliability: 1)
A0A3Q3IZ16_MONAL
582
0
65552
TrEMBL
other Location (Reliability: 2)
A0A7L3C4X2_PELUR
551
0
62220
TrEMBL
other Location (Reliability: 1)
A0A2R9CJS1_PANPA
520
0
58855
TrEMBL
other Location (Reliability: 4)
A0A340Y7S7_LIPVE
559
0
63976
TrEMBL
other Location (Reliability: 4)
A0A3Q7Q4F5_CALUR
415
0
47313
TrEMBL
other Location (Reliability: 2)
A0A8C7UBG8_ONCMY
568
0
64394
TrEMBL
other Location (Reliability: 2)
A0A8C7U050_ONCMY
583
0
65644
TrEMBL
other Location (Reliability: 2)
A0A8C7ND88_ONCMY
580
0
65676
TrEMBL
other Location (Reliability: 2)
A0A0P7Z2K6_SCLFO
550
0
61771
TrEMBL
other Location (Reliability: 2)
A0A8C5LTH6_9ANUR
563
0
63956
TrEMBL
other Location (Reliability: 3)
A0A8B9VMX4_9AVES
539
0
61650
TrEMBL
other Location (Reliability: 4)
A0A673C9B3_9TELE
556
0
62609
TrEMBL
other Location (Reliability: 2)
A0A673BAL8_9TELE
569
0
64488
TrEMBL
other Location (Reliability: 2)
A0A2Y9QS59_TRIMA
462
0
52164
TrEMBL
other Location (Reliability: 1)
A0A7L1EY67_SYLBO
470
0
53904
TrEMBL
other Location (Reliability: 3)
A0A2Y9D797_TRIMA
552
0
62390
TrEMBL
other Location (Reliability: 1)
A0A8C6QC40_NANGA
527
0
59418
TrEMBL
other Location (Reliability: 2)
A0A7K4KQB6_9AVES
560
0
63973
TrEMBL
other Location (Reliability: 4)
A0A8C6IAM1_MUSSI
520
0
58557
TrEMBL
other Location (Reliability: 4)
A0A7N8YBU0_9TELE
565
0
64034
TrEMBL
other Location (Reliability: 2)
A0A672HKI0_SALFA
571
0
64553
TrEMBL
other Location (Reliability: 2)
M4AQX8_XIPMA
564
0
63800
TrEMBL
other Location (Reliability: 2)
A0A8D0LP20_PIG
573
0
65280
TrEMBL
other Location (Reliability: 5)
A0A091HXC3_CALAN
517
0
59245
TrEMBL
other Location (Reliability: 3)
A0A093PXV6_9PASS
517
0
59212
TrEMBL
other Location (Reliability: 3)
A0A8C4I529_DICLA
585
0
66148
TrEMBL
other Location (Reliability: 2)
A0A2I4B2W1_9TELE
573
0
64877
TrEMBL
other Location (Reliability: 2)
A0A668AA87_9TELE
577
0
65194
TrEMBL
other Location (Reliability: 2)
A0A674EWX3_SALTR
555
0
63055
TrEMBL
other Location (Reliability: 2)
A0A663N4X3_ATHCN
516
0
59115
TrEMBL
other Location (Reliability: 4)
A0A091GUS4_BUCRH
367
0
41417
TrEMBL
Secretory Pathway (Reliability: 3)
A0A3B4FLF8_9CICH
557
0
62790
TrEMBL
other Location (Reliability: 2)
A0A7K8KPF4_9GRUI
551
0
62247
TrEMBL
other Location (Reliability: 1)
A0A3Q2CI19_CYPVA
564
0
63887
TrEMBL
other Location (Reliability: 2)
A0A8C0C8K8_BALMU
574
0
65535
TrEMBL
other Location (Reliability: 4)
A0A3B4WZ77_SERLL
556
1
62828
TrEMBL
Secretory Pathway (Reliability: 1)
A0A6P4X6E4_PANPR
559
0
63994
TrEMBL
other Location (Reliability: 4)
A0A8C2D6S7_CYPCA
566
0
64520
TrEMBL
other Location (Reliability: 2)
A0A8C2BVV2_CYPCA
572
0
64786
TrEMBL
other Location (Reliability: 2)
A0A2K6V8F5_SAIBB
541
0
60980
TrEMBL
other Location (Reliability: 2)
A0A212CF59_CEREH
448
0
50449
TrEMBL
other Location (Reliability: 1)
A0A668SZJ0_OREAU
571
0
64559
TrEMBL
other Location (Reliability: 2)
A0A674I0R3_TERCA
551
0
62874
TrEMBL
other Location (Reliability: 1)
A0A7K8QBZ0_9PASS
551
0
62245
TrEMBL
other Location (Reliability: 1)
A0A8C6WGQ7_9GOBI
545
0
62351
TrEMBL
other Location (Reliability: 2)
A0A8C6TDN1_9GOBI
559
0
62899
TrEMBL
other Location (Reliability: 2)
A0A3Q0DT06_CARSF
651
0
72353
TrEMBL
other Location (Reliability: 2)
A0A3P4S9H7_GULGU
458
0
52436
TrEMBL
other Location (Reliability: 1)
A0A7C8ZXE2_OPUST
299
0
33198
TrEMBL
other Location (Reliability: 5)
F6YST6_ORNAN
630
0
70799
TrEMBL
Mitochondrion (Reliability: 4)
A0A5E4C512_MARMO
475
0
54448
TrEMBL
other Location (Reliability: 3)
A0A1A7Y4H3_9TELE
571
0
64709
TrEMBL
other Location (Reliability: 2)
A0A8B8WLU3_BALMU
462
0
52087
TrEMBL
other Location (Reliability: 1)
Q4STJ7_TETNG
543
0
61408
TrEMBL
other Location (Reliability: 2)
A0A6J2AT85_ACIJB
559
0
63994
TrEMBL
other Location (Reliability: 4)
A0A671QZD1_9TELE
522
0
59847
TrEMBL
other Location (Reliability: 2)
A0A7J8J1G3_MOLMO
458
0
52374
TrEMBL
other Location (Reliability: 1)
A0A3B5LQ72_9TELE
557
0
62653
TrEMBL
other Location (Reliability: 2)
A0A8C2MIR1_CRIGR
552
0
62295
TrEMBL
other Location (Reliability: 1)
A0A3B5BJ40_9TELE
573
0
64812
TrEMBL
other Location (Reliability: 2)
A0A093HXN0_STRCA
507
0
57953
TrEMBL
other Location (Reliability: 3)
A0A091RTF8_NESNO
517
0
59167
TrEMBL
other Location (Reliability: 3)
A0A7L1AFA8_GYMTI
561
0
64039
TrEMBL
other Location (Reliability: 5)
A0A8D2CMC6_SCIVU
574
0
65636
TrEMBL
other Location (Reliability: 4)
A0A7L0NPQ4_9PASS
551
0
62233
TrEMBL
other Location (Reliability: 1)
A0A8C0V6X2_CYACU
544
0
62028
TrEMBL
other Location (Reliability: 3)
A0A6I9MD94_PERMB
522
0
59753
TrEMBL
other Location (Reliability: 3)
A0A6Q2YHW7_ESOLU
577
0
64993
TrEMBL
other Location (Reliability: 2)
A0A7J8F3H1_ROUAE
386
0
44054
TrEMBL
other Location (Reliability: 2)
A0A3Q7P154_CALUR
552
0
62367
TrEMBL
other Location (Reliability: 1)
A0A4W5MNP5_9TELE
565
0
63813
TrEMBL
other Location (Reliability: 2)
A0A484GN97_SOUCH
528
0
59844
TrEMBL
other Location (Reliability: 3)
A0A8C4QFI4_EPTBU
395
0
44173
TrEMBL
other Location (Reliability: 2)
H2Z922_CIOSA
531
0
60442
TrEMBL
other Location (Reliability: 2)
H2Z922_CIOSA
531
0
60442
TrEMBL
other Location (Reliability: 2)
A0A8C2PC75_CAPHI
458
0
52401
TrEMBL
other Location (Reliability: 1)
A0A0E3JX30_SINCH
557
0
62683
TrEMBL
other Location (Reliability: 2)
G1S3D1_NOMLE
559
0
64009
TrEMBL
other Location (Reliability: 4)
A0A091GM20_9AVES
521
0
59022
TrEMBL
other Location (Reliability: 3)
D2HX61_AILME
521
0
58974
TrEMBL
other Location (Reliability: 3)
A0A7L1PM55_ORIOR
547
0
62470
TrEMBL
other Location (Reliability: 1)
A0A674EXV2_SALTR
588
0
66304
TrEMBL
other Location (Reliability: 2)
A0A674EXK9_SALTR
560
0
63737
TrEMBL
other Location (Reliability: 2)
A0A8B9ETW6_ANSCY
Anser cygnoid
560
0
63944
TrEMBL
other Location (Reliability: 4)
A0A8B8X3M3_BALMU
458
0
52345
TrEMBL
other Location (Reliability: 1)
A0A1L8GM16_XENLA
551
0
62440
TrEMBL
other Location (Reliability: 1)
A0A7K9VHN1_ANSSE
517
0
59160
TrEMBL
other Location (Reliability: 3)
A0A3B4XUQ9_SERLL
573
0
64746
TrEMBL
other Location (Reliability: 2)
A0A1S3FD39_DIPOR
697
0
78815
TrEMBL
other Location (Reliability: 3)
A0A093IL55_FULGA
517
0
59184
TrEMBL
other Location (Reliability: 3)
A0A8C5FPA8_GADMO
557
0
62744
TrEMBL
other Location (Reliability: 2)
A0A8C1ZRD7_CYPCA
559
0
63080
TrEMBL
other Location (Reliability: 2)
A0A8C6PM18_NOTFU
568
0
64005
TrEMBL
other Location (Reliability: 2)
A0A670I2J8_PODMU
552
0
62561
TrEMBL
other Location (Reliability: 2)
A0A8C6VWC7_NOTFU
625
0
70735
TrEMBL
Mitochondrion (Reliability: 4)
A0A212C888_CEREH
383
0
43924
TrEMBL
other Location (Reliability: 1)
A0A8C5KV37_JACJA
537
0
60676
TrEMBL
other Location (Reliability: 1)
G9KII3_MUSPF
515
0
59073
TrEMBL
other Location (Reliability: 4)
V9KW60_CALMI
478
0
55083
TrEMBL
other Location (Reliability: 2)
A0A7J7E8J3_DICBM
496
0
57514
TrEMBL
other Location (Reliability: 4)
A0A8I6ACB8_RAT
504
0
57013
TrEMBL
other Location (Reliability: 2)
A0A7L1V3C9_SITEU
473
0
53919
TrEMBL
other Location (Reliability: 3)
A0A093HXD3_TYTAL
517
0
59227
TrEMBL
other Location (Reliability: 3)
A0A4W4G4X6_ELEEL
574
0
65142
TrEMBL
other Location (Reliability: 2)
A0A2U4AXX3_TURTR
458
0
52372
TrEMBL
other Location (Reliability: 1)
A5WUM0_DANRE
573
0
65021
TrEMBL
other Location (Reliability: 2)
A0A1A7WI81_9TELE
418
0
46534
TrEMBL
other Location (Reliability: 2)
A0A072UZP8_MEDTR
300
0
34017
TrEMBL
Chloroplast (Reliability: 3)
A0A2Y9NQ82_DELLE
523
0
59260
TrEMBL
other Location (Reliability: 2)
H2R5J1_PANTR
574
0
65523
TrEMBL
other Location (Reliability: 4)
A0A8B9KCP1_ASTMX
557
0
63611
TrEMBL
other Location (Reliability: 2)
H0V5H1_CAVPO
559
0
64081
TrEMBL
other Location (Reliability: 4)
A0A6J2ATA0_ACIJB
415
0
47285
TrEMBL
other Location (Reliability: 2)
A0A6P4YT01_BRABE
563
0
63057
TrEMBL
other Location (Reliability: 3)
A0A672TTX8_STRHB
551
0
62842
TrEMBL
other Location (Reliability: 1)
A0A2K5R157_CEBIM
559
0
64009
TrEMBL
other Location (Reliability: 4)
A0A3P8WCG7_CYNSE
574
0
64784
TrEMBL
other Location (Reliability: 2)
A0A8J8XQW4_CALJA
693
0
77760
TrEMBL
other Location (Reliability: 1)
A0A4U1F3L6_MONMO
520
0
58869
TrEMBL
other Location (Reliability: 4)
A0A6P7DSS3_SHEEP
532
0
60671
TrEMBL
other Location (Reliability: 1)
A0A6J0SZW8_9SAUR
550
0
62812
TrEMBL
other Location (Reliability: 1)
A0A852C240_9PICI
570
0
64184
TrEMBL
other Location (Reliability: 2)
A0A7K4U3J5_9SYLV
473
0
53953
TrEMBL
other Location (Reliability: 3)
A0A8C4YSN8_9SAUR
551
0
62364
TrEMBL
other Location (Reliability: 1)
A0A484CYP2_PERFV
557
0
62641
TrEMBL
other Location (Reliability: 2)
U3KCR2_FICAL
543
0
60937
TrEMBL
other Location (Reliability: 5)
A0A0M4G4N9_ORENI
571
0
64529
TrEMBL
other Location (Reliability: 2)
A0A8C8IM73_ONCTS
557
0
62992
TrEMBL
other Location (Reliability: 2)
A0A3P9QB00_POERE
546
0
61512
TrEMBL
Secretory Pathway (Reliability: 5)
A0A7L4CPD1_9AVES
479
0
55485
TrEMBL
other Location (Reliability: 4)
A0A455BB20_PHYMC
499
0
57007
TrEMBL
other Location (Reliability: 1)
A0A803T6Q0_ANOCA
550
0
62859
TrEMBL
other Location (Reliability: 1)
A0A7J8F2Z0_ROUAE
475
0
54378
TrEMBL
other Location (Reliability: 3)
A0A8C7TH28_ONCMY
566
0
63694
TrEMBL
other Location (Reliability: 3)
A0A8C5QAV3_9ANUR
550
0
61999
TrEMBL
other Location (Reliability: 2)
A0A7L2Z6J3_JACJC
560
0
63982
TrEMBL
other Location (Reliability: 4)
A0A835NSJ0_9PASS
532
0
59752
TrEMBL
other Location (Reliability: 2)
A0A3Q4IAL8_NEOBR
557
0
62804
TrEMBL
other Location (Reliability: 2)
A0A8C7ALE9_NEOVI
539
0
61074
TrEMBL
Secretory Pathway (Reliability: 1)
A0A672HJU5_SALFA
563
0
63831
TrEMBL
other Location (Reliability: 2)
A0A3Q3SN91_9TELE
574
0
64829
TrEMBL
other Location (Reliability: 2)
A0A7N8XLN6_9TELE
569
0
64724
TrEMBL
other Location (Reliability: 4)
A0A7N8XGU1_9TELE
554
0
62329
TrEMBL
other Location (Reliability: 2)
A0A673T851_SURSU
575
0
65506
TrEMBL
other Location (Reliability: 3)
A0A8C0R002_CANLU
552
0
62310
TrEMBL
other Location (Reliability: 1)
A0A8B9YVW7_BOSMU
574
0
65608
TrEMBL
other Location (Reliability: 4)
A0A850WAE9_FREMA
498
0
56898
TrEMBL
other Location (Reliability: 3)
A0A2I2YTB3_GORGO
525
0
60705
TrEMBL
other Location (Reliability: 4)
G1MFV1_AILME
532
0
60300
TrEMBL
Secretory Pathway (Reliability: 5)
A0A7K5K1J5_9TYRA
551
0
62231
TrEMBL
other Location (Reliability: 1)
A0A8C4E3J4_DICLA
555
0
62432
TrEMBL
other Location (Reliability: 2)
A0A673WP67_SALTR
578
0
65097
TrEMBL
Mitochondrion (Reliability: 4)
A0A673ZYP9_SALTR
560
0
63267
TrEMBL
other Location (Reliability: 2)
A0A226NAE3_CALSU
475
0
54541
TrEMBL
other Location (Reliability: 2)
A0A7K5LLA1_VIRAL
551
0
62259
TrEMBL
other Location (Reliability: 1)
G7NVZ7_MACFA
521
0
58954
TrEMBL
other Location (Reliability: 3)
A0A663M2U1_ATHCN
505
0
57269
TrEMBL
other Location (Reliability: 5)
A0A663N611_ATHCN
552
0
63039
TrEMBL
other Location (Reliability: 3)
A0A3B3WHM4_9TELE
540
0
61610
TrEMBL
other Location (Reliability: 2)
A0A2K6LPW4_RHIBE
559
0
63995
TrEMBL
other Location (Reliability: 4)
A0A8J1KJ30_XENLA
418
0
47033
TrEMBL
other Location (Reliability: 2)
A0A1L8GFI4_XENLA
551
0
62434
TrEMBL
other Location (Reliability: 1)
A0A7L1EJE4_OENON
562
0
63190
TrEMBL
other Location (Reliability: 3)
A0A3Q7X853_URSAR
574
0
65614
TrEMBL
other Location (Reliability: 4)
A0A8C1NA18_CYPCA
563
0
64215
TrEMBL
other Location (Reliability: 4)
A0A669PF02_PHACC
552
0
62417
TrEMBL
other Location (Reliability: 2)
A0A7L2DDU6_CATFU
561
0
63957
TrEMBL
other Location (Reliability: 5)
A0A2K5I4J8_COLAP
559
0
63995
TrEMBL
other Location (Reliability: 4)
A0A553N294_9TELE
569
0
64634
TrEMBL
other Location (Reliability: 2)
A0A7L4KXI3_9CORV
551
0
62214
TrEMBL
other Location (Reliability: 1)
A0A1S3PAQ3_SALSA
561
0
63157
TrEMBL
other Location (Reliability: 2)
A0A2Y9NJB6_DELLE
552
0
62334
TrEMBL
other Location (Reliability: 1)
A0A8D2PSI7_ZOSLA
516
0
59084
TrEMBL
other Location (Reliability: 4)
A0A8C5U7W9_9PASS
552
0
62264
TrEMBL
other Location (Reliability: 1)
A0A4W4G3Z3_ELEEL
567
0
64441
TrEMBL
other Location (Reliability: 2)
A0A8D0I681_PIG
540
0
61484
TrEMBL
Mitochondrion (Reliability: 5)
A0A3Q7X859_URSAR
473
0
54010
TrEMBL
other Location (Reliability: 1)
A0A2Y9Q5E0_DELLE
458
0
52386
TrEMBL
other Location (Reliability: 1)
A8E649_BOVIN
458
0
52402
TrEMBL
other Location (Reliability: 1)
A0A7K5VKD8_9CORV
552
0
62244
TrEMBL
other Location (Reliability: 1)
A0A7K5V1P2_9CORV
473
0
53985
TrEMBL
other Location (Reliability: 3)
G3GTJ7_CRIGR
747
0
85199
TrEMBL
other Location (Reliability: 1)
F6YDC4_CALJA
708
0
79332
TrEMBL
other Location (Reliability: 1)
A0A8J4I2J6_SPHME
401
0
45807
TrEMBL
other Location (Reliability: 3)
A0A8C5EKS6_9TELE
567
0
64322
TrEMBL
other Location (Reliability: 2)
A0A2Y9IPI6_ENHLU
559
0
64040
TrEMBL
other Location (Reliability: 4)
A0A8D2ALS1_SCIVU
552
0
62361
TrEMBL
other Location (Reliability: 1)
A0A091TL34_PHALP
436
0
50687
TrEMBL
other Location (Reliability: 3)
A0A673J988_9TELE
567
0
64818
TrEMBL
other Location (Reliability: 4)
A0A673M0G4_9TELE
539
0
61519
TrEMBL
other Location (Reliability: 2)
A0A673N110_9TELE
535
0
60309
TrEMBL
other Location (Reliability: 2)
M7BL98_CHEMY
433
0
49480
TrEMBL
other Location (Reliability: 3)
A0A852P6S0_9PASS
547
0
61749
TrEMBL
other Location (Reliability: 2)
A0A7K5MRA8_CARCD
561
0
63925
TrEMBL
other Location (Reliability: 5)
A0A7K9KH71_9PASE
548
0
61913
TrEMBL
other Location (Reliability: 2)
A0A7L0RDW3_GLABR
551
0
62233
TrEMBL
other Location (Reliability: 1)
A0A3B3ZN56_9GOBI
565
0
64249
TrEMBL
other Location (Reliability: 2)
I3J3R7_ORENI
542
0
60963
TrEMBL
other Location (Reliability: 2)
A0A2K5NF49_CERAT
390
0
43709
TrEMBL
other Location (Reliability: 2)
A0A2K5N897_CERAT
458
0
52391
TrEMBL
other Location (Reliability: 1)
A0A7K9TK45_9AVES
517
0
59203
TrEMBL
other Location (Reliability: 3)
A0A6Q2WVG1_ESOLU
563
0
63459
TrEMBL
other Location (Reliability: 2)
A0A096NP50_PAPAN
581
0
65960
TrEMBL
other Location (Reliability: 3)
A0A851MJ76_9DEND
552
0
62360
TrEMBL
other Location (Reliability: 1)
A0A3B4TYY2_SERDU
552
0
62595
TrEMBL
other Location (Reliability: 2)
A0A060YAF5_ONCMY
573
0
64668
TrEMBL
Secretory Pathway (Reliability: 4)
A0A8C2XSC4_CYCLU
575
0
64798
TrEMBL
other Location (Reliability: 3)
A0A287CRX6_ICTTR
561
0
64230
TrEMBL
Mitochondrion (Reliability: 3)
A0A8C9V5F1_SCLFO
553
0
63185
TrEMBL
other Location (Reliability: 2)
A0A5N5JTV3_PANHP
574
0
65030
TrEMBL
other Location (Reliability: 2)
A0A8B9TML3_ANAPL
540
0
61055
TrEMBL
other Location (Reliability: 1)
A0A7L1F4J2_SYLBO
561
0
63975
TrEMBL
other Location (Reliability: 5)
A0A8C6DII7_MOSMO
532
0
60235
TrEMBL
other Location (Reliability: 1)
G3TJJ9_LOXAF
559
0
64029
TrEMBL
other Location (Reliability: 4)
A0A672LQP9_SINGR
553
0
62588
TrEMBL
other Location (Reliability: 2)
A0A8C9MTU1_SERCA
504
0
57187
TrEMBL
other Location (Reliability: 4)
A0A3Q3MVI6_9TELE
557
0
62716
TrEMBL
other Location (Reliability: 2)
A0A6I9KIH0_CHRAS
559
0
64064
TrEMBL
other Location (Reliability: 4)
A0A8D1GSM5_PIG
559
0
63974
TrEMBL
other Location (Reliability: 5)
A0A091LZW1_CARIC
517
0
59209
TrEMBL
other Location (Reliability: 3)
A0A8C5ZTI9_MARMA
552
0
63965
TrEMBL
Mitochondrion (Reliability: 3)
A0A8B9BMS2_9AVES
640
0
72233
TrEMBL
other Location (Reliability: 3)
A0A3Q2Z3Y3_HIPCM
548
0
61591
TrEMBL
other Location (Reliability: 2)
A0A673Y657_SALTR
561
0
63173
TrEMBL
other Location (Reliability: 2)
A0A673Y673_SALTR
570
0
64220
TrEMBL
other Location (Reliability: 3)
A0A7N9D4G5_MACFA
574
0
65638
TrEMBL
other Location (Reliability: 4)
A0A7L2XJ94_9PASS
389
0
44141
TrEMBL
other Location (Reliability: 2)
A0A8C9DXS3_PHOSS
574
0
65526
TrEMBL
other Location (Reliability: 4)
A0A6P6HWJ9_PUMCO
458
0
52390
TrEMBL
other Location (Reliability: 1)
A0A3B3Y5N7_9TELE
564
0
63888
TrEMBL
other Location (Reliability: 2)
A0A3B3YM75_9TELE
555
0
62373
TrEMBL
other Location (Reliability: 2)
A0A3B4WZ67_SERLL
536
0
60693
TrEMBL
other Location (Reliability: 2)
H2VDB7_TAKRU
572
0
64817
TrEMBL
other Location (Reliability: 2)
A0A674MSN7_TAKRU
588
0
65974
TrEMBL
other Location (Reliability: 4)
A0A3Q7WHR6_URSAR
552
0
62374
TrEMBL
other Location (Reliability: 1)
A0A8J6FID7_ELECQ
460
0
52581
TrEMBL
other Location (Reliability: 1)
A0A8J6B6L2_ELECQ
458
0
51942
TrEMBL
other Location (Reliability: 1)
A0A7L0CYG3_9CHAR
551
0
62247
TrEMBL
other Location (Reliability: 1)
A0A8C4YZE6_GADMO
564
0
63780
TrEMBL
other Location (Reliability: 1)
A0A3P8UA76_AMPPE
573
0
64737
TrEMBL
other Location (Reliability: 2)
A0A670JP56_PODMU
634
0
71988
TrEMBL
Mitochondrion (Reliability: 3)
A0A4X2KJ10_VOMUR
551
0
62177
TrEMBL
other Location (Reliability: 2)
A0A7K8ASY2_9CORV
517
0
59081
TrEMBL
other Location (Reliability: 3)
A0A7J7YYN4_PIPKU
550
0
62714
TrEMBL
other Location (Reliability: 1)
A0A7K8EKV1_LEURO
521
0
58954
TrEMBL
other Location (Reliability: 3)
A0A091P554_HALAL
442
0
50721
TrEMBL
other Location (Reliability: 3)
A0A2K5I4F9_COLAP
574
0
65564
TrEMBL
other Location (Reliability: 4)
H3A2S9_LATCH
552
0
62703
TrEMBL
other Location (Reliability: 2)
A0A8D2I6R5_UROPR
552
0
62435
TrEMBL
other Location (Reliability: 1)
A0A6P7MDL9_BETSP
562
0
63298
TrEMBL
other Location (Reliability: 2)
A0A2U3ZV84_ODORO
545
0
61618
TrEMBL
other Location (Reliability: 1)
A0A8D2LQP7_VARKO
549
0
62783
TrEMBL
other Location (Reliability: 2)
A0A6P3FPE0_OCTDE
550
0
62898
TrEMBL
other Location (Reliability: 1)
A0A8C9K8D0_PANTA
559
0
63943
TrEMBL
other Location (Reliability: 5)
A0A8C6SFG0_9GOBI
520
0
59860
TrEMBL
other Location (Reliability: 2)
A0A8C6SEV9_9GOBI
565
0
64299
TrEMBL
other Location (Reliability: 2)
A0A091EFN1_CORBR
517
0
59239
TrEMBL
other Location (Reliability: 3)
A0A7L3NAL7_9AVES
517
0
59277
TrEMBL
other Location (Reliability: 3)
A0A4W4G160_ELEEL
571
0
64785
TrEMBL
other Location (Reliability: 2)
SIP1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
815
0
91071
Swiss-Prot
other Location (Reliability: 4)
SIP2_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
415
0
46405
Swiss-Prot
-
AAKB1_RAT
270
0
30394
Swiss-Prot
other Location (Reliability: 4)
GAL83_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
417
0
46648
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
155000
P54646; O43741; Q9UGI9
recombinant His-tagged full-length alpha2beta2gamma3 heterotrimeric AMPK complex, gel filtration
35000
-
1 * 63000 + 1 * 38000 + 1 * 35000, 3 subunits alpha, beta and gamma, SDS-PAGE
36000
-
1 * 63000 * ? + 1 * 38000 + 1 * 36000, alpha, beta, gamma, SDS-PAGE
38000
58000
63000
38000
-
1 * 63000 + 1 * 38000 + 1 * 35000, 3 subunits alpha, beta and gamma, SDS-PAGE
38000
-
1 * 63000 * ? + 1 * 38000 + 1 * 36000, alpha, beta, gamma, SDS-PAGE
63000
-
1 * 63000 + 1 * 38000 + 1 * 35000, 3 subunits alpha, beta and gamma, SDS-PAGE
63000
-
1 * 63000 * ? + 1 * 38000 + 1 * 36000, alpha, beta, gamma, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterotrimer
trimer
additional information
?
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
x * 29230, subunit AMPKbeta1b, calculated from amino acid sequence
?
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
x * 29620, subunit AMPKbeta2, calculated from amino acid sequence
?
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
x * 30410, subunit AMPKbeta1a, calculated from amino acid sequence
?
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
x * 38260, subunit AMPKgamma3, calculated from amino acid sequence
?
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
x * 39130, subunit AMPKgamma1, calculated from amino acid sequence
?
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
x * 55530, subunit AMPKgamma2a, calculated from amino acid sequence
?
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
x * 60380, subunit AMPKgamma2b, calculated from amino acid sequence
?
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
x * 62290, subunit AMPKalpha2, calculated from amino acid sequence
?
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
x * 64700, subunit AMPKalpha1, calculated from amino acid sequence
?
x * 37953, recombinant phosphorylated AMPK alpha1 subunit, mass spectrometry
?
x * 110700, subunit AMPK-gamma, calculated from amino acid sequence
?
x * 33000, subunit AMPK-beta, calculated from amino acid sequence
?
x * 58800, subunit AMPK-alpha, calculated from amino acid sequence
heterotrimer
AMPK is a heterotrimeric kinase composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma
heterotrimer
P54646; O43741; Q9UGI9
1 * 64000, recombinant His-tagged alpha2 subunit, + 1 * 54000, recombinant His-tagged beta2 subunit, + 1* 33000, recombinant His-tagged gamma3 subunit, SDS-PAGE
heterotrimer
AMPK exists as a heterotrimeric complex, composed of a catalytic subunit (alpha) and two regulatory subunits (beta and gamma), each present as multiple isoforms
heterotrimer
enzyme AMPK is a heterotrimeric protein complex composed of a catalytic subunit (alpha) and two regulatory subunits (beta and gamma)
heterotrimer
enzyme AMPK is composed of AMPKalpha, beta and gamma subunits
heterotrimer
-
1 * 63000 + 1 * 38000 + 1 * 35000, 3 subunits alpha, beta and gamma, SDS-PAGE
heterotrimer
-
1 * 63000 * ? + 1 * 38000 + 1 * 36000, alpha, beta, gamma, SDS-PAGE
heterotrimer
AMPK is heterotrimer with alphabetagamma structure
trimer
-
AMPK exists as heterotrimeric complexes comprising catalytic alpha subunits and regulatory beta and gamma subunits
trimer
-
AMPK exists as heterotrimeric complexes comprising catalytic alpha subunits and regulatory beta and gamma subunits
trimer
-
AMPK exists as heterotrimeric complexes comprising catalytic alpha subunits and regulatory beta and gamma subunits
trimer
-
AMPK exists as heterotrimeric complexes comprising catalytic alpha subunits and regulatory beta and gamma subunits
trimer
-
AMPK exists as heterotrimeric complexes comprising catalytic alpha subunits and regulatory beta and gamma subunits
trimer
-
alphabetagamma heterotrimer composed of different alpha, beta, and gamma subunit variants
trimer
-
AMPK exists as heterotrimeric complexes comprising catalytic alpha subunits and regulatory beta and gamma subunits, with multiple genes encoding each subunit in mammals, alpha1, alpha2, beta1, beta2, gamma1, gamma2, gamma3
trimer
-
different heterotrimers resulting in different isozymes, the alphabetagamma composition can be formed by two different alpha subunit variants, two different beta and three different gamma subunits, overview
trimer
-
heterotrimeric AMPK consists of a catalytic alpha subunit, and regulatory beta and gamma subunits
trimer
-
in human skeletal muscle, the alpha2beta2gamma3 complexes constitute the majority of AMPK heterotrimers
trimer
-
alphabetagamma heterotrimer composed of different alpha, beta, and gamma subunit variants
trimer
-
AMPK exists as heterotrimeric complexes comprising catalytic alpha subunits and regulatory beta and gamma subunits, with multiple genes encoding each subunit in mammals, alpha1, alpha2, beta1, beta2, gamma1, gamma2, gamma3
trimer
-
AMPK exists as heterotrimeric complexes comprising catalytic alpha subunits and regulatory beta and gamma subunits
trimer
-
a heterotrimeric enzyme with a catalytic alpha subunit, and regulatory beta and gamma subunits, of which exists different variants
trimer
-
AMPK exists as heterotrimeric complexes comprising catalytic alpha subunits and regulatory beta and gamma subunits, with multiple genes encoding each subunit in mammals, alpha1, alpha2, beta1, beta2, gamma1, gamma2, gamma3
trimer
heterotrimer, complex structure determination and analysis by mass spectrometry, dynamic light and small-angle X-ray scattering and transmission electrom microscopy, modeling, overview
trimer
-
in rat skeletal muscle, the alpha2beta2gamma1 complexes constitute the majority of AMPK heterotrimers
trimer
-
AMPK exists as heterotrimeric complexes comprising catalytic alpha subunits and regulatory beta and gamma subunits
trimer
-
AMPK exists as heterotrimeric complexes comprising catalytic alpha subunits and regulatory beta and gamma subunits
trimer
-
AMPK exists as heterotrimeric complexes comprising catalytic alpha subunits and regulatory beta and gamma subunits
additional information
-
heterotrimeric serine/threonine kinase consists of a catalytic alpha-subunit and 2 regulatory subunits beta and gamma, each subunit exists as multiple isoforms, alpha1, alpha2, beta1, beta2, gamma1, gamma2 and gamma3, giving 12 different possible combinantions of holoenzyme with different tissue distribution and subcellular localization
additional information
-
heterotrimeric serine/threonine kinase consists of a catalytic alpha-subunit and 2 regulatory subunits beta and gamma, each subunit exists as multiple isoforms, alpha1, alpha2, beta1, beta2, gamma1, gamma2 and gamma3, giving 12 different possible combinantions of holoenzyme with different tissue distribution and subcellular localization
additional information
-
AMPK consists of a catalytic alpha subunit and two non-catalytic subunits,beta and gamma, each with multiple isoforms that form active 1:1:1 heterotrimers
additional information
-
several isoforms for each of the three AMPK subunits, including alpha1, alpha2, beta1, beta2, gamma1, gamma2, and gamma3, AMPKalpha subunit possesses a highly conserved, N-terminal catalytic domain that contains the activating phosphorylation site Thr172, an autoinhibitory domain, and a C-terminus that contains the domains required for binding with the beta and gamma subunits, subunit structures, overview
additional information
P54646; O43741; Q9UGI9
AMPK is a heterotrimeric enzyme with a catalytic (alpha) subunit and two regulatory (beta and gamma) subunits
additional information
the AMPK alpha2 kinase domain exhibits a typical bilobal kinase fold and exists as a monomer in the crystal. Like the wild-type apo form, the T172D mutant apo form adopts the autoinhibited structure of the DFG-out conformation, with the Phe residue of the DFG motif anchored within the putative ATP-binding pocket. Three-dimensional structure analysis, overview. The kinase domain structures display the typical bilobal protein-kinase fold
additional information
-
the alpha1-subunit isoform accounts for 90% of the total AMPK in vascular smooth muscle
additional information
-
heterotrimeric serine/threonine kinase consists of a catalytic alpha-subunit and 2 regulatory subunits beta and gamma, each subunit exists as multiple isoforms, alpha1, alpha2, beta1, beta2, gamma1, gamma2 and gamma3, giving 12 different possible combinantions of holoenzyme with different tissue distribution and subcellular localization
additional information
-
AMPK consists of a catalytic alpha subunit and two non-catalytic subunits,beta and gamma, each with multiple isoforms that form active 1:1:1 heterotrimers, beta1-Thr263 and beta1-Tyr267 are required for beta1gamma1 subunit association
additional information
-
several isoforms for each of the three AMPK subunits, including alpha1, alpha2, beta1, beta2, gamma1, gamma2, and gamma3, AMPKalpha subunit possesses a highly conserved, N-terminal catalytic domain that contains the activating phosphorylation site Thr172, an autoinhibitory domain, and a C-terminus that contains the domains required for binding with the beta and gamma subunits, subunit structures, overview
additional information
the beta-subunit exists in two isoforms (beta1 and beta2) and contains a carbohydrate-binding module (CBM). The two CBM isoforms (beta1- and beta2-CBM) are near identical in sequence and structure, determination of the NMR solution structure, structure analysis
additional information
the beta-subunit exists in two isoforms (beta1 and beta2) and contains a carbohydrate-binding module (CBM). The two CBM isoforms (beta1- and beta2-CBM) are near identical in sequence and structure, determination of the NMR solution structure, structure analysis
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
lipoprotein
the subunit beta sequence contains an N-myristoylation site
phosphoprotein
phosphoprotein
-
AAK-2 is phosphorylated at Thr243 in response to paraquat treatment, the phosphorylation depends on PAR-4, the Caenorhabditis elegans LKB1 homologue
phosphoprotein
-
AMPK is activated by phosphorylation through upstream kinases and 5'-AMP in response to various nutritional and stress signals
phosphoprotein
phosphorylation of the catalytic AMPK alpha protein at threonine 172
phosphoprotein
serine 108 and serine 182 phosphorylation sites in subunit beta
phosphoprotein
A0A514YC25, A0A515J4H7, A0A515J4I2, A0A515J4I4, A0A515J4J0, A0A515J4J2, A0A515J4J3, A0A515J4V2, A0A515J4V7
-
phosphoprotein
-
the enzyme is phosphorylated at Thr172 of its alpha-subunit, phosphorylation activates the enzyme, metformin increases the enzyme phosphorylation
phosphoprotein
-
8-chloro-cAMP and no 5-aminoimidazole-4-carboxamide-1-beta-D-ribonucleoside induce AMPK phosphorylation
phosphoprotein
-
activating phosphorylation of AMPK at Thr172 of the alpha-subunit, e.g. by CaMKKbeta or LBK1, dephosphorylation by phosphatase PP2C
phosphoprotein
-
activation of AMPK requires phosphorylation at Thr172 by an AMPK kinases, e.g. LKB1 and Ca2+/calmodulin-dependent kinase kinase, CaMKK
phosphoprotein
-
phosphorylation at alpha1-Thr172 by CaMKKbeta, and at alpha1-Ser485, beta1-Ser108, and beta1-Ser182 in Sf21 cells, determination of phosphorylation sites by mass spectrometry, phosphorylation also by LKB1, overview
phosphoprotein
-
phosphorylation of AMPK at Thr172 of the alpha-subunit inducd by 5-aminoimidazole-4-carboxamide-1-beta-D-ribonucleoside
phosphoprotein
-
the enzyme is activated by phosphorylation at Thr172 in the alpha subunit activation T-loop
phosphoprotein
-
UV and H2O2 induce AMPK activation through Thr172 phosphorylation
phosphoprotein
activation of the enzyme by phosphorylation of Thr172 of the alpha subunit. Thr172 is the only site phosphorylated by its upstream kinase, liver kinase B1, and the phosphorylation dramatically increases the kinase activity of the catalytic domain/alpha-subunit. Phosphorylation of AMPK alpha1 on Thr172 by LKB1/Ste20-related adaptor (STRAD)/mouse protein 25(MO25) complex. Top-down mass spectrometric analysis, overview. Ser18 and Ser22 in the His-tag region as well as Thr196 (equivalent to Thr172 in the unmodified enzyme) in the sequence of the AMPK catalytic domain are the three phosphorylation sites
phosphoprotein
autophosphorylation of 5'-AMP-activated protein kinase catalytic subunit alpha-1
phosphoprotein
enzyme activation by phosphorylation on Thr172, LKB1, Ca2+/calmodulin-dependent protein kinase kinase, ATM and TAK1 are AMPK kinases
phosphoprotein
phosphorylation of Thr172/Thr174 of the alpha subunit activates the enzyme isozymes
phosphoprotein
-
the enzyme can be activated by direct phosphorylation by the upstream kinase liver kinase B1 at the site of Thr172 on the alpha-subunit, or through indirect allosteric changes of the gamma-subunit, thereby regulating the phosphorylation state of the alpha-subunit
phosphoprotein
-
Zika virus infection results in a decrease in AMPKalpha phosphorylation at Thr172
phosphoprotein
-
activating phosphorylation of AMPK at Thr172 of the alpha-subunit, e.g. by CaMKKbeta or LBK1, dephosphorylation by phosphatase PP2C
phosphoprotein
-
phosphorylation at Thr172 activates the enzyme, the phosphorylation is activated by 5-aminoimidazole-4-carboxamide-1-beta-D-ribonucleoside
phosphoprotein
phosphorylation on Thr172 and activation of AMPKalpha subunit
phosphoprotein
-
protein kinase B increases the phosphorylation of AMPKalpha1 subunit at Ser485/Ser491, which subsequently prevents the phosphorylation of the enzyme at Thr172 by liver kinase B1 and thus suppresses the activation of the enzyme
phosphoprotein
-
upstream kinases boost phosphorylation of the enzyme on threonine 172 at the alpha catalytic subunit for enzymatic activation
phosphoprotein
Mus musculus C57BL/6/129
-
phosphorylation on Thr172 and activation of AMPKalpha subunit
-
phosphoprotein
-
the enzyme is activated by phosphorylation at Thr172, which is inhibited by naringin
phosphoprotein
-
activating phosphorylation of AMPK at Thr172 of the alpha-subunit, e.g. by CaMKKbeta or LBK1, dephosphorylation by phosphatase PP2C
phosphoprotein
-
AMPK is activated by phosphorylation, induced e.g. by leptin
phosphoprotein
-
AMPKalpha needs to be activated by phosphorylation on Thr172
phosphoprotein
-
phosphorylation by CaMKKbeta and LKB1, determination of phosphorylation sites by mass spectrometry, overview
phosphoprotein
-
phosphorylation of AMPK at Thr172 of the alpha-subunit
phosphoprotein
when the Gal83 isoform is activated by the other Snf1-activating kinases, Tos3 and Elm1, the Gal83 isoform is unable to translocate to the nucleus
phosphoprotein
-
when the Gal83 isoform is activated by the other Snf1-activating kinases, Tos3 and Elm1, the Gal83 isoform is unable to translocate to the nucleus
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the inactive, apo-form of AMPK alpha2 subunit N-terminal kinase catalytic domain (KCD, residues 10-278 inclusive), shows that it adopts a canonical bilobal structure with the active site forming a cleft between the two lobes. The small N-terminal lobe (residues 1-97) is composed of a five-stranded beta-sheet (beta1-beta5), with an alpha-helix (termed the C-helix) positioned between strands beta3 and beta4 and lying to one side of the beta sheet. Glu-64 within the C-helix is important for aligning the phosphates of ATP in the correct orientation for catalysis. A Gly-X-Gly-X-X-Gly P-loop motif connecting strands beta1 and beta2 is evident in the structure. This interacts with the beta phosphate group of ATP when the active site is occupied. The larger C-terminal lobe is predominantly (63%) alpha-helical (alphaD-alphaI) and contains determinants and structural features that dictate protein substrate binding. The two lobes are connected via a short, flexible hinge region that allows rotation of the two lobes relative to each other
-
purified AMPK alpha2 subunit in apoform and in complex with compound C inhibitor, for the apoform: hanging-drop vapour diffusion method, mixing of 2.8 mg/ml protein in 20 mM Tris-HCl, pH 8.5, 0.3 M NaCl, 10% glycerol, 2 mM DTT, 5 mM MgCl2, and 5 mM AMPPNP, with reservoir solution consisting of 0.1 M Tris-HCl pH 8.9, 15% 2-propanol, 0.1 M ammonium sulfate, and 16% PEG 4000, for the complexed form: sitting-drop vapour-diffusion method, mixing of 2.8 mg/mlprotien in 20 mM Tris-HCl, pH 8.5, 0.3 M NaCl, 10% glycerol, 2 mM DTT, 5 mM MgCl2, and 0.5 mM compound C, with reservoir solution consisting of 0.1 M Bis-Tris, pH 6.5, 1.5 M ammonium sulfate, and 0.1 M NaCl, 20°C, X-ray diffraction structure determination and analysis at 2.08-3.0 A resolution, molecular replacement, modelling, overview
crystal structure of AMPK beta1 subunit-carbohydrate-binding module in complex with the cyclic sugar beta-cyclodextrin shows that the domain consists of a beta-hairpin loop extending from a beta-sandwich containing two anti-parallel beta-sheets. The sugar ring is held in position by the beta-hairpin loop, which protrudes the ring with Leu-146 at its centre. Within the sugarbinding pocket an extensive network of hydrophobic stacking interactions, mediated by Trp100 and Trp133, and carbohydrate-protein hydrogen bonds are formed with five of the seven glucose units. Although Leu-146 is prominent in the beta7-beta8 hairpin and interacts extensively with beta-cyclodextrin, it is not essential for glycogen binding
-
purified subunit beta1 carbohydrate-binding module CBD in complex with glucosyl-beta-cyclodextrin, sitting-drop vapour-diffusion method, mixing of 0.001 ml of 13 mg/ml protein in 20 mM HEPES, pH 7.0, and 6 mM gBCD, with 0.001 ml of reservoir solution containing 0.2 M lithium sulfate, 25% w/v PEG 8000, and 0.1 M sodium acetate, pH 4.5, X-ray diffraction structure determination and analysis at 1.72 A resolution, molecular replacement
purified subunit beta2 carbohydrate-binding module, sitting-drop vapour-diffusion method, mixing of 0.001 ml of 13 mg/ml protein in 20 mM HEPES, pH 7.0, with or without 6 mM glucosyl-beta-cyclodextrin, with 0.001 ml of reservoir solution, which contains for the unliganded enzyme 0.17 M ammonium sulfate, 15% v/v glycerol and 25.5% w/v PEG 4000, or contains 0.2 M lithium chloride, 20% w/v PEG 6000 and 0.1 M sodium HEPES, pH 7.0 for the complex with gBCD, X-ray diffraction structure determination and analysis at 1.6-2.0 A reolution, molecular replacement
crystals grown by mixing proteins with ammonium formate. Crystal structure of phosphorylated kinase domain, to 2.9 A resolution. Phosphorylated kinase domain displays a closed conformation
-
crystal structures for full-length Snf4. In the subunit crystal structure ADP can be co-crystallized and occupies site 2, the unoccupied site present in mammalian gamma1
-
crystals grown by mixing proteins with ammonium sulphate. Crystal structure of an unphosphorylated fragment of the AMPK alpha-subunit that contains both the catalytic kinase domain and an autoinhibitory domain, to 2.8 A resolution. The unphosphorylated kinase domain of catalytic kinase domain/autoinhibitory domain fragment adopts an open inactive conformation. Kinase domain/autoinhibitory domain is jammed into its active site, and the critical catalytic residues make several intra- and intermolecular contacts
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K45R
R225W
-
naturally occuring mutation of the gamma3 subunit, which leads to a 2fold increased AMPK activity, a 90% increase in skeletal muscle glycogen content and a 30% decrease in triglycerides
R70Q
T172D
R225Q
D157A
D329K
-
catalytic kinase domain/autoinhibitory domain mutant, shows enhanced specific activity
F300E
-
catalytic kinase domain/autoinhibitory domain mutant, shows enhanced specific activity
H150R
-
constitutively active AMPKgamma1 mutant, stimulates the concentration-dependent increase of substrate phosphorylation
I327D
-
catalytic kinase domain/autoinhibitory domain mutant, shows enhanced specific activity
K45R
-
dominant negative AMPKalpha2 mutant, results in a concentration-dependent inhibition in the phosphorylation of the AMPK substrate, inhibits endogenous AMPK activation. Inhibition of AMPK attenuates recovery of aconitase activity and promotes caspase-3 activation during recovery
L326D
-
catalytic kinase domain/autoinhibitory domain mutant, shows enhanced specific activity
N330A
-
catalytic kinase domain/autoinhibitory domain mutant, shows little or no effect on specific activity
R263A
-
catalytic kinase domain/autoinhibitory domain mutant, shows little or no effect on specific activity
V296D
-
catalytic kinase domain/autoinhibitory domain mutant, shows enhanced specific activity
Y267A
-
the mutation almost completely abrogates the beta1gamma1 interaction in comparison to wild type enzyme
Y267F
-
the mutation affects the beta1gamma1 interaction in comparison to wild type enzyme
Y267H
-
the mutation affects the beta1gamma1 interaction in comparison to wild type enzyme
Y267S
-
the mutation affects the beta1gamma1 interaction in comparison to wild type enzyme
H379A
site-directed mutagenesis, mutation of beta subunit Gal83 with little effect on Gal83 function
H380A
site-directed mutagenesis, mutation of beta subunit Sip2, mutation does not affect heterotrimer association
H384A
site-directed mutagenesis, mutation of beta subunit Gal83 causing a severe loss of function when assayed for growth on alternative carbon sources, the mutation does not affect heterotrimer association
H772A
site-directed mutagenesis, mutation of beta subunit Sip1 does not affect Sip1 function
H379A
-
site-directed mutagenesis, mutation of beta subunit Gal83 with little effect on Gal83 function
-
H380A
-
site-directed mutagenesis, mutation of beta subunit Sip2, mutation does not affect heterotrimer association
-
H384A
-
site-directed mutagenesis, mutation of beta subunit Gal83 causing a severe loss of function when assayed for growth on alternative carbon sources, the mutation does not affect heterotrimer association
-
H772A
-
site-directed mutagenesis, mutation of beta subunit Sip1 does not affect Sip1 function
-
E344K
-
mutation in the autoinhibitory domain, disruption of the hydrophilic interactions, yields a modest but marked increase in basal activity
L312D
-
mutation in the autoinhibitory domain, leads to marked enzymatic activation
L341D
-
mutation in the autoinhibitory domain, catalytic efficiency is increased approximately 10fold, comparable to that of the wild-type kinase domain
L342D
-
mutation in the autoinhibitory domain, catalytic efficiency is increased approximately 10fold, comparable to that of the wild-type kinase domain
L88A
-
mutation in the kinase domain, has decreased catalytic activity
M316E
-
mutation in the autoinhibitory domain, catalytic efficiency is increased approximately 10fold, comparable to that of the wild-type kinase domain
R149E
-
mutation in the kinase domain, has decreased catalytic activity
R280A
-
mutation in the autoinhibitory domain, has no effect on kinase activity
additional information
K45R
-
site-directed mutagenesis, a dominant-negative mutant, expression leads to accumulation of lipids in cells
K45R
Q13131; Q9Y478; P54619
site-directed mutagenesis, a kinase dead mutant AMPK, the mutant is ineffective in inhibiting heterotetrameric K+-channel KCNQ1/KCNE1
R70Q
-
site-directed mutagenesis, marked increase in activity, largely AMP-independent
R70Q
Q13131; Q9Y478; P54619
site-directed mutagenesis, the constitutively active mutant is more effective in inhibiting heterotetrameric K+-channel KCNQ1/KCNE1 than the wild-type enzyme
T172D
-
site-directed mutagenesis, constitutively active mutant of AMPK, insensitive to metformin
T172D
site-directed mutagenesis of AMPK subunit alpha2, a phosphorylated-state mimic mutant. The activity of the T172D mutant kinase domain with and without AMPK kinase is about 40fold higher than that of the wild-type kinase domain treated with protein phosphatase 2A. The apo-form structure of the T172D mutant is essentially identical to that published for the wild type
R225Q
-
the mutation in gamma3 subunit leads to enhanced expression of Cd36 and cytochrome c in transgenic mice
R225Q
-
gain-of-function mutation, overexpression of the AMPK gamma3 subunit mutant increases mitochondrial biogenesis in glycolytic skeletal muscle, which is associated with an increase in expression of the co-activator PGC-1alpha and several transcription factors that regulate mitochondrial biogenesis, including NRF-1, NRF-2, and TFAM. Succinate dehydrogenase is also increased in transversal skeletal muscle sections of white gastrocnemius muscle, independent of changes in fiber type composition
D157A
-
AMPKalpha2 mutant, expression of a dominant-negative AMPK alpha results in a decreased ATP level and significantly compromised survival in hypoxia
additional information
-
aak-2 mutation and par-4 knockdown increase the sensitivity of worms to paraquat, and the double deficiency does not further increase sensitivity
additional information
-
a dominant negative AMP-activated protein kinase mutant abrogates rosiglitazone-stimulated Ser1177 phosphorylation and NO production in endothelial cells
additional information
-
activating mutations in AMPK can cause heart disease, detailed overview
additional information
-
AMPK silencing increases PDGF-induced proliferation of hepatic stellate cells
additional information
-
enzyme inhibition by expression of a dominant negative expression vector with kinase-dead form of AMPKalpha2
additional information
-
overexpression of the kinase-negative AMPK inhibits enzyme activation by 2-deoxyglucose
additional information
C-terminal truncation of AMPKalpha at residue 312 yields a protein that is active upon phosphorylation of Thr172 in the absence of beta and gamma subunits, which is refered to as the AMPK catalytic domain and commonly used to substitute for AMPK heterotrimeric complex in in vitro kinase assays
additional information
-
lipolysis is reduced in mutant with expression of a dominant-negative AMPK of in a null-mutant
additional information
-
AMPK subunit alpha2 and gamma3 knockoout mice show reduced inhibition of mTOR phosphorylation/activation and reduced mTOR signaling, overview
additional information
-
cells deficient in Tsc2, a tuberin encoded by gene tsc2, show cytoplasmic mislocalization of p27, which is reversible by inhibitors of the LKB1/AMPK pathway
additional information
-
construction of AMPK deficient ob/ob mice as a model for the metabolic syndrome, phenotype, overview. Activating mutations in AMPK can cause heart disease, detailed overview
additional information
-
construction of AMPKalpha1-KO mice, which show a splenomegaly possibly due to the massive amplification of erythroid nucleated cells, AMPKalpha1-KO mice are fully immunocompetent in vivo and display normal cell proliferation, humoral, cytotoxic and delayed-type hypersensitivity responses following antigen injection, phenotype, overview. AMPKalpha1-KO cells display increasing sensitivity to energetic stress in vitro, and are unable to maintain adequate ATP levels in response to ATP synthase inhibition, but the cells are able to respond to antigen stimulation in vitro, overview
additional information
-
construction of AMPKgamma3-knockout mice, which show impaired fasting-induced expression of skeletal musclelipid oxidative genes, while in mice overexpressing AMPKgamma3, an upregulation of lipid metabolic and mitochondrial gene expression occurs, overexpression or deletion of AMPKalpha2 subunit leads to abolishment of mitochondrial gene expression activation
additional information
-
LBK1-KO mice mutants show reduced phospho-AMPK content and AMPK activity, e.g. with substrate CREB, overview
additional information
-
lipolysis is reduced in mutant with expression of a dominant-negative AMPK of in a null-mutant
additional information
-
AMPK deficiency leads to ATP depletion in hepatocytes
additional information
-
construction of AMPK deficient fa/fa rats as a model for the metabolic syndrome, phenotype, overview. Activating mutations in AMPK can cause heart disease, detailed overview
additional information
-
defective AMPK signaling reduces the rate of substrate cycling between de novo lipogenesis and lipid oxidation, leading to suppressed thermogenesis, which accelerates body fat recovery and furthermore sensitizes skeletal muscle to dietary fat-induced impairments in PI3K/AMPK signaling, overview
additional information
-
downregulation of AMPK by microinjection of AMPK-RNAi in ventromedial hypothalamus results in suppressed glucagon and reduction of AMPKalpha-2 isozyme, but not of AMPKalpha-1 isozyme
additional information
-
overexpression of constitutively active AMPK leads to activation of PKC-zeta and promotes Na,K-ATPase endocytosis, downregulation of AMPK via adenoviral delivery of dominant-negative AMPK-alpha prevents CO2-induced Na,K-ATPase endocytosis
additional information
point mutations in Gal83 and Sip2 and a 17 amino acid C-terminal truncation of Sip1 to inactivate specific isoforms without affecting their abundance or association with the other subunits. Generation of truncated beta subunit mutants
additional information
point mutations in Gal83 and Sip2 and a 17 amino acid C-terminal truncation of Sip1 to inactivate specific isoforms without affecting their abundance or association with the other subunits. Generation of truncated beta subunit mutants
additional information
point mutations in Gal83 and Sip2 and a 17 amino acid C-terminal truncation of Sip1 to inactivate specific isoforms without affecting their abundance or association with the other subunits. Generation of truncated beta subunit mutants
additional information
-
point mutations in Gal83 and Sip2 and a 17 amino acid C-terminal truncation of Sip1 to inactivate specific isoforms without affecting their abundance or association with the other subunits. Generation of truncated beta subunit mutants
additional information
point mutations in Gal83 and Sip2 and a 17 amino acid C-terminal truncation of Sip1 to inactivate specific isoforms without affecting their abundance or association with the other subunits. Generation of truncated beta subunit mutants. Truncation of the C-terminal 17 amino acids of the Sip1 protein, the Sip1-Q798 protein still assembles into Snf1 kinase complexes
additional information
point mutations in Gal83 and Sip2 and a 17 amino acid C-terminal truncation of Sip1 to inactivate specific isoforms without affecting their abundance or association with the other subunits. Generation of truncated beta subunit mutants. Truncation of the C-terminal 17 amino acids of the Sip1 protein, the Sip1-Q798 protein still assembles into Snf1 kinase complexes
additional information
point mutations in Gal83 and Sip2 and a 17 amino acid C-terminal truncation of Sip1 to inactivate specific isoforms without affecting their abundance or association with the other subunits. Generation of truncated beta subunit mutants. Truncation of the C-terminal 17 amino acids of the Sip1 protein, the Sip1-Q798 protein still assembles into Snf1 kinase complexes
additional information
-
point mutations in Gal83 and Sip2 and a 17 amino acid C-terminal truncation of Sip1 to inactivate specific isoforms without affecting their abundance or association with the other subunits. Generation of truncated beta subunit mutants. Truncation of the C-terminal 17 amino acids of the Sip1 protein, the Sip1-Q798 protein still assembles into Snf1 kinase complexes
additional information
-
point mutations in Gal83 and Sip2 and a 17 amino acid C-terminal truncation of Sip1 to inactivate specific isoforms without affecting their abundance or association with the other subunits. Generation of truncated beta subunit mutants. Truncation of the C-terminal 17 amino acids of the Sip1 protein, the Sip1-Q798 protein still assembles into Snf1 kinase complexes
-
additional information
-
point mutations in Gal83 and Sip2 and a 17 amino acid C-terminal truncation of Sip1 to inactivate specific isoforms without affecting their abundance or association with the other subunits. Generation of truncated beta subunit mutants
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
2 h, inactivation, MgATP2- in a low, not high salt buffer restores activity, not cAMP or in phosphate buffer
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, in 0.05 M Tris-HCl, pH 7.5, 0.05 M NaF, 0.005 M diphosphate, 1 mM EDTA, 1 mM EGTA and 1 mM DTT, 0.1 mM PMSF, soybean trypsin inhibitor, benzamidine, Brij-35, 50% w/v glycerol, stable for at least 2 months
-
-70°C, 0.5 mg protein/ml, frozen in liquid nitrogen, can be stored with no loss of activity
-
-80C, glycerol
-80°C, in 0.05 M Tris-HCl buffer, pH 7.4, 0.05 M NaF, 0.003 M EDTA, 0.002 M EGTA, 0.005 M DTT, 0.5 mM PMSF, 10% v/v glycerol, remains stable for at least 3 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
different recombinant His6-tagged subunit constructs from Escherichia coli strain BL21-CodonPlusTM (DE3)-RIPL by nickel affinity chromatography and dialysis
functional full-length recombinant alpha2beta2gamma3 heterotrimeric complex of human AMP-activated protein kinase from Escherichia coli strain CodonPlus(DE3)-RIPL by nickel affinity chromatography, dialysis and two steps of gel filtration
P54646; O43741; Q9UGI9
isozymes alpha1 and alpha2 from liver homogenates by subcellular fractionation and immunoprecipitation
-
kinase domain and catalytic kinase domain/autoinhibitory domain fragments of AMPK alpha-subunit
-
kinase domain and kinase domain/autoinhibitory domain fragments of AMPK alpha-subunit
-
kinase domain and kinase domain/autoinhibitory fragments of AMPK alpha-subunit
-
partial
recombinant GST-tagged isozyme AMPK alpha1beta1gamma1 from Spodoptera frugiperda Sf21 cells by glutathione affinity and anion exchange chromatography, and gel filtration
-
recombinant GST-tagged isozyme AMPK beta1-alpha1 subunits fusion protein from COS-7 cells by glutathione affinity exchange chromatography
-
recombinant GST-tagged subunit beta1 from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography, gel filtration, anion exchange chromatography, and ultrafiltration
recombinant His-tagged AMPK alpha2 mutant by affinity chromatography and gel filtration
recombinant His-tagged isozymes alpha1 and alpha2 from Escherichia coli by nickel affinity chromatography
-
recombinant untagged protein by automated multidimensional purification including adsorption chromatography and gel filtration, overview
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
adenoviral expression of wild-type, dominant negative or constitutively active AMPK mutants. Transduction of INS832/13 cells
-
alpha, beta and subunit encoding genes, phylogenetic trees
AMPK alpha subunits (alpha1 and alpha2) tagged with green fluorescent protein at the N-terminus and co-expressed with beta and gamma subunits in CCL13 cells
-
ATII cells infected with a hemagglutinin-tagged adenovirus carrying the dominant-negative mutant K45R of the AMPK alpha1 subunit or with an adenovirus expressing a constitutively active AMPK alpha variant or with an adenovirus expressing a constitutively active AMPK alpha variant in which Thr172 is replaced with aspartate in the truncated AMPK alpha subunit, comprising residues 1 to 312. A549 cells transfected with AMPK alpha1
-
cardiac-specific transgenic mice overexpressing a dominant-negative AMPKalpha2 subunit
-
cDNA identified with porcine cDNA
DNA and amino acid sequence determination and analysis, phylogenetic tree, real-time PCR expression analysis of the AMPK alpha, beta, and gamma subunits, overview
expression of a dominant negative kinase-dead form of AMPKalpha2 in HeLa cells
-
expression of a dominant-negative mutant or of a constitutively active mutant of AMPK in adipocytes via adenovirus transfection
expression of alpha1 subunit alone or in combination with other subunits in Escherichia coli
expression of alpha2 subunit alone or in combination with other subunits in Escherichia coli
expression of beta1 subunit alone or in combination with other subunits in Escherichia coli
expression of beta2 subunit alone or in combination with other subunits in Escherichia coli
expression of gamma1 subunit alone or in combination with other subunits in Escherichia coli
expression of GST-fused constitutively active form of AMPK alpha1, residues 1-312, and of the kinase-dead mutant AMPK in HEK-193 cells
-
expression of GST-tagged wild-type AMPK beta1-alpha1 subunits fusion protein in COS-7 cells, and expression of beta1 residue 367 mutants in fusion to gamma1 subunit in COS-7 cells
-
expression of His6-tagged beta1(186-270)gamma1 complex and of GST-tagged isozyme AMPK alpha1beta1gamma1 in Spodoptera frugiperda Sf21 cells
-
expression of mutant enzymes in Escherichia coli and, via adenovirus transfection, in Hep-G2 cells
-
expression of short hairpin RNA for GFP-tagged AMPHalpha subunit in rat ventromedial hypothalamus via injection of the adeno-associated viral vector
-
expression of the AMPKalpha1 dominant negative mutant D175A in fibroblasts as GFP-tagged enzyme using an adenoviral transfection system
-
expression of wild-type and mutant AMPKalpha2 in human BJ fibroblast cells and in 786-0 renal carcinoma cells
-
functional His-tagged full-length recombinant alpha2beta2gamma3 heterotrimeric complex of human AMP-activated protein kinase is recombinantly expressed in Escherichia coli strain CodonPlus(DE3)-RIPL. All three subunits of AMPK alpha2beta2gamma3 are transcribed as a single tricistronic transcript driven by the T7 RNA polymerase promoter, allowing spontaneous formation of the heterotrimeric complex in the bacterial cytosol
P54646; O43741; Q9UGI9
gene PRKAA2, recombinant expression of kinase domain (residues 6-279) of the AMPK alpha2 mutant with an N-terminal His-tag and a tobacco etch virus (TEV) protease cleavage site via Escherichia coli cell-free system using the dialysis method
gene Prkab1, recombinant expression of GST-tagged subunit beta1 in Escherichia coli strain BL21(DE3)
gene Prkab2, recombinant expression of GST-tagged subunit beta2 in Escherichia coli strain BL21(DE3)
kinase domain and catalytic kinase domain/autoinhibitory domain fragments of AMPK alpha-subunit. AMPK holoenzyme expressed in a tricistronic vector
-
kinase domain and kinase domain/autoinhibitory domain fragments of AMPK alpha-subunit
quantitative AMPK expression analysis in different tissues with or without glucocorticosteroid treatment, overview
recombinant coexpression of different His6-tagged subunit constructs in Escherichia coli strain BL21-CodonPlusTM (DE3)-RIPL, coexpression with biotin-ligase (BirA)
recombinant expression of C-terminally HA-tagged or N-terminally triple-FLAG-tagged isozyme in an enzyme-deficient Saccharomyces cerevisiae strain, expression of C-terminally GFP-tagged isozyme in haploid Saccharomyces cerevisiae
recombinant expression of His-tagged AMPK catalytic domain in Escherichia coli strain Rossetta (DE3)
transgenic mice overexpressing either the wild-type or the R225Q mutant subunit and knock-out mice
-
transgenic mouse constructed by injection of Rattus norvegicus alpha2 subunit cDNA
-
transient expression of wild-type and mutant enzymes in COS-7 cells, co-expression with histone deacetylase 5
-
wild-type HA-tagged AMPKalpha1, FLAG-tagged AMPKbeta1, HA-tagged AMPKgamma1, constitutively active HA-tagged AMPKgamma1 mutant R70Q , kinase dead mutant HA-tagged AMPKalpha1 mutant K45R, and wild type HA-tagged AMPK alpha2, recombinant expression in Xenopus laevis oocytes. Coexpression with human KCNQ1/KCNE1. AMPK inhibites voltage-gated outward currents in KCNQ1/KCNE1-expressing Xenopus oocytes. Coexpression of the AMP-activated protein kinase, i.e. AMPKalpha1, AMPKbeta1, and AMPKgamma1
Q13131; Q9Y478; P54619
expression of a dominant-negative mutant or of a constitutively active mutant of AMPK in adipocytes via adenovirus transfection
-
expression of a dominant-negative mutant or of a constitutively active mutant of AMPK in adipocytes via adenovirus transfection
-
kinase domain and kinase domain/autoinhibitory domain fragments of AMPK alpha-subunit
-
kinase domain and kinase domain/autoinhibitory domain fragments of AMPK alpha-subunit
-
quantitative AMPK expression analysis in different tissues with or without glucocorticosteroid treatment, overview
-
quantitative AMPK expression analysis in different tissues with or without glucocorticosteroid treatment, overview
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
3 days of recurrent insulin-induced hypoglycaemia results in an increase in the gene expression of alpha1- and alpha2AMPK in the whole hypothalamus and in the dorso-mediobasal hypothalamus
-
alpha1 and alpha2 AMPK siRNAs selectively suppress AMPKalpha1 and AMPKalpha2 protein, respectively. AMPKalpha1 and AMPKalpha2 proteins are reduced to 6 and 1% of respective controls. Combined treatment with both alpha1 and alpha2 AMPK siRNAs lead to 66 and 92% reduction of AMPKalpha1 and AMPKalpha2 protein, respectively
-
AMPKalpha mRNA levels increase continuously throughout exposure to 26°C, reaching 5.6times more after 6 h at 26°C than in the 12°C controls
AMPKalpha1 repression causes a 37% compensational increase in AMPKalpha2 protein
-
enzyme activity significantly increases during ischemia, remaining activated during reperfusion
-
in the muscle subunit AMPK-gamma mRNA is significantly up-regulated at low salinity relative to controls. Muscle and hepatopancreas show increases in enzyme protein after 6 h exposure to low salinity, but there are no differences seen after long term acclimation
loss of AMPK beta-subunit expression in beta1-/- and beta2-/- mice, leading to a low-bone-mass phenotype
overexpression of AMPK dominant negative mutant abolishes statin-induced reduction of O2- in BAEC
-
relative expression of alpha, beta, and gamma isoforms of AMPK is greatest in muscle and MAC-T cells
-
siRNA knockdown of AMPK, which ameliorates the IFNgamma-induced increase in epithelial permeability and decrease in transepithelial electrical resistance
-
the expression of enzyme isoform AMPKalpha2 significantly increases in the hepatopancreas of fish exposed to 1 week of overwinter starvation conditions. The expression of isoform AMPKalpha2 significantly increases in the adipose tissue of fish exposed to 4 week of overwinter starvation conditions. The mRNA levels of enzyme isoforms in hepatocytes and adipocytes change significantly with in the first 24 h of exposure to the overwinter starvation conditions
the expression of enzyme isoform AMPKbeta1b significantly increases in the hepatopancreas of fish exposed to 8 weeks of overwinter starvation conditions. The expression of isoform AMPKbeta1b significantly increases in the adipose tissue of fish exposed to 1 week of overwinter starvation conditions. The mRNA levels of enzyme isoforms in hepatocytes and adipocytes change significantly with in the first 24 h of exposure to the overwinter starvation conditions
the expression of enzyme isoform AMPKbeta2 significantly increases in the hepatopancreas of fish exposed to 12 weeks of overwinter starvation conditions. The expression of isoform AMPKbeta2 significantly increases in the adipose tissue of fish exposed to 8 weeks of overwinter starvation conditions. The mRNA levels of enzyme isoforms in hepatocytes and adipocytes change significantly with in the first 24 h of exposure to the overwinter starvation conditions
the expression of enzyme isoform AMPKgamma1 significantly increases in the hepatopancreas of fish exposed to 12 weeks of overwinter starvation conditions. The expression of isoform AMPKgamma1 significantly increases in the adipose tissue of fish exposed to 4 weeks of overwinter starvation conditions. The mRNA levels of enzyme isoforms in hepatocytes and adipocytes change significantly with in the first 24 h of exposure to the overwinter starvation conditions
the expression of enzyme isoform AMPKgamma2a significantly increases in the hepatopancreas of fish exposed to 16 weeks of overwinter starvation conditions. The expression of isoform AMPKgamma2a significantly increases in the adipose tissue of fish exposed to 8 weeks of overwinter starvation conditions. The mRNA levels of enzyme isoforms in hepatocytes and adipocytes change significantly with in the first 24 h of exposure to the overwinter starvation conditions
the expression of enzyme isoform AMPKgamma2b significantly increases in the hepatopancreas of fish exposed to 8 weeks of overwinter starvation conditions. The expression of isoform AMPKgamma2b significantly increases in the adipose tissue of fish exposed to 4 weeks of overwinter starvation conditions. The mRNA levels of enzyme isoforms in hepatocytes and adipocytes change significantly with in the first 24 h of exposure to the overwinter starvation conditions
the expression of enzyme isoform AMPKgamma3 significantly increases in the hepatopancreas of fish exposed to 16 weeks of overwinter starvation conditions. The expression of isoform AMPKgamma3 significantly increases in the adipose tissue of fish exposed to 4 weeks of overwinter starvation conditions. The mRNA levels of enzyme isoforms in hepatocytes and adipocytes change significantly with in the first 24 h of exposure to the overwinter starvation conditions
the expression of isoform AMPKalpha1 significantly increases in the hepatopancreas of fish exposed to 1 week of overwinter starvation conditions. The expression enzyme isoform AMPK alpha1 significantly increases in the adipose tissue of fish exposed to 4 weeks of overwinter starvation conditions. The mRNA levels of enzyme isoforms in hepatocytes and adipocytes change significantly with in the first 24 h of exposure to the overwinter starvation conditions
the expression of various enzyme isoform AMPKbeta1a significantly increases in the hepatopancreas of fish exposed to 16 weeks of overwinter starvation conditions. The expression of isoform AMPKbeta1a significantly increases in the adipose tissue of fish exposed to 1 week of overwinter starvation conditions. The mRNA levels of enzyme isoforms in hepatocytes and adipocytes change significantly with in the first 24 h of exposure to the overwinter starvation conditions
the mRNA level of subunit AMPK-alpha is up-regulated in the hepatopancreas and muscle after acute low-salinity stress at 3 psu for 6 h compared with control salinity at 20 psu. After 8-week salinity stress at 3 psu, AMPK-alpha and mRNA level in the hepatopancreas is significantly higher than those of the control at 30 psu. Muscle and hepatopancreas show increases in enzyme protein after 6 h exposure to low salinity, but there are no differences seen after long term acclimation
the mRNA level of subunit AMPK-beta is up-regulated in the hepatopancreas and muscle after acute low-salinity stress at 3 psu for 6 h compared with control salinity at 20 psu. After 8-week salinity stress at 3 psu, AMPK-beta mRNA level in the hepatopancreas is significantly higher than those of the control at 30 psu. Muscle and hepatopancreas show increases in enzyme protein after 6 h exposure to low salinity, but there are no differences seen after long term acclimation
loss of AMPK beta-subunit expression in beta1-/- and beta2-/- mice, leading to a low-bone-mass phenotype
-
loss of AMPK beta-subunit expression in beta1-/- and beta2-/- mice, leading to a low-bone-mass phenotype
-
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
industry
-
AMPK as a molecular target capable of modifying energy substrate utilization may result in the development of new technologies that increase milk production or modify milk composition during periods of increased energy demand
medicine
pharmacology
-
selective AMPK activators are potential therapeutics in type 2 diabetes
additional information
drug development
-
pharmacological activators of AMPK can act as treatments for diabetes and the metabolic syndrome
drug development
-
activating AMPK may have therapeutic potential in treating dry macular degeneration
drug development
-
AMPK is a highly attractive target for the prevention and treatment of type 2 diabetes and other disorders of the metabolic syndrome, and to curb the prevalence and costs of type 2 diabetes
drug development
-
AMPK is a highly attractive target for the prevention and treatment of type 2 diabetes and other disorders of the metabolic syndrome, and to curb the prevalence and costs of type 2 diabetes
drug development
-
AMPK is regarded as one of the most promising targets for new drugs to treat the growing incidence of metabolic diseases such as obesity and type 2 diabetes and cardiovascular disease
drug development
-
AMPK is regarded as one of the most promising targets for new drugs to treat the growing incidence of metabolic diseases such as obesity and type 2 diabetes and cardiovascular disease
drug development
-
AMPK is regarded as one of the most promising targets for new drugs to treat the growing incidence of metabolic diseases such as obesity and type 2 diabetes and cardiovascular disease
drug development
-
AMPK is regarded as one of the most promising targets for new drugs to treat the growing incidence of metabolic diseases such as obesity and type 2 diabetes and cardiovascular disease
drug development
-
AMPK represents an attractive therapeutic target for vascular disease treatment
drug development
-
AMPK represents an attractive therapeutic target for vascular disease treatment
drug development
-
AMPK represents an attractive therapeutic target for vascular disease treatment
drug development
-
targeting SIRT1-AMPK pathway may serve as a new target for the development of new anti HIV-1 agents
drug development
-
the AMPK inhibitor 6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine may serve as a useful molecule in both basic and clinical research on adipogenesis and as a potential lead compound for the treatment of obesity
drug development
-
the glucose-sensitive stimulatory impact of BLX-1002 on beta-cell function associated with AMPK activation may translate into substantial clinical benefits of the drug in the management of type 2 diabetes, by avoidance of hypoglycemia
drug development
-
triterpenoids are potential hypoglycemic components of the plant and the mechanism underlying their action involves AMPK
drug development
AMP-activated protein kinase (AMPK) is a potential target for drug design against metabolic syndrome, obesity and type 2 diabetes
drug development
P54646; O43741; Q9UGI9
AMPK alpha2beta2gamma3 is an attractive target for drug development for diabetes and metabolic syndrome
drug development
design and development of isoform-selective AMPK activators that are likely to be useful for the treatment of cardiovascular and metabolic diseases
medicine
-
compounds that would cause activation of enzyme in skeletal muscle promise to be attractive agents for therapeutic intervention
medicine
-
decreasing the ischaemic-induced activation of AMPK may be a therapeutic approach to treating ischaemic heart disease, AMPK may be an important pharmacological target for improving cardiac efficiency following ischaemia
medicine
-
defects or disuse of the AMPK signaling system would be predicted to result in many of the metabolic perturbations observed in type 2 diabetes mellitus
medicine
-
implication of AMPK in the pathogenesis of chronic intestinal inflammatory conditions, such as inflammatory bowel disease
medicine
-
enzyme inhibition is a viable therapeutic strategy to prevent ischemic brain injury following stroke
medicine
-
the enzyme can be an alternative therapeutic approach to preventing and managing obesity
additional information
AMPK is an earlier indicator of temperature stress in rock crabs than HSP70, especially during the initial response to high temperatures. AMPK activity is a cellular marker that indicates a thermal threshold, called the pejus temperature
additional information
AMPK is an earlier indicator of temperature stress in rock crabs than HSP70, especially during the initial response to high temperatures. AMPK activity is a cellular marker that indicates a thermal threshold, called the pejus temperature
REF.
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TITLE
JOURNAL
VOL.
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YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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Regulation of liver hydroxymethylglutaryl-CoA reductase by a bicyclic phosphorylation system
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Rattus norvegicus
Ball, K.L.; Dale, S.; Weekes, J.; Hardie, D.G.
Biochemical characterization of two forms of 3-hydroxy-3-methylglutaryl-CoA reductase kinase from cauliflower (Brassica oleracea)
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Carling, D.; Clarke, P.R.; Hardie, D.G.
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Homo sapiens, Rattus norvegicus, Sus scrofa
Beg, Z.H.; Stonik, J.A.; Brewer, H.B.
3-Hydroxy-3-methylglutaryl coenzyme A reductase: regulation of enzymatic activity by phosphorylation and dephosphorylation
Proc. Natl. Acad. Sci. USA
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3678-3682
1978
Rattus norvegicus
Ingebritsen, T.S.; Lee, H.S.; Parker, R.A.; Gibson, D.M.
Reversible modulation of the activities of both liver microsomal hydroxymethylglutaryl coenzyme A reductase and its inactivating enzyme. Evidence for regulation by phosphorylation-dephosphorylation
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81
1268-1277
1978
Rattus norvegicus
Beg, Z.H.; Stonik, J.A.
Reversible inactivation of 3-hydroxy-3-methylglutaryl coenzyme A reductase: reductase kinase and mevalonate kinase are separate enzymes
Biochem. Biophys. Res. Commun.
108
559-566
1982
Rattus norvegicus
Ferrer, A.; Hegardt, F.G.
Phosphorylation of 3-hydroxy-3-methylglutaryl coenzyme A reductase by microsomal 3-hydroxy-3-methylglutaryl coenzyme A reductase kinase
Arch. Biochem. Biophys.
230
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1984
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Harwood, H.J.; Brandt, K.G.; Rodwell, V.W.
Allosteric activation of rat liver cytosolic 3-hydroxy-3-methylglutaryl coenzyme A reductase kinase by nucleoside diphosphates
J. Biol. Chem.
259
2810-2815
1984
Rattus norvegicus
Ferrer, A.; Caelles, C.; Massot, N.; Hegardt, F.G.
Activation of rat liver cytosolic 3-hydroxy-3-methylglutaryl coenzyme A reductase kinase by adenosine 5-monophosphate
Biochem. Biophys. Res. Commun.
132
497-504
1985
Rattus norvegicus
Beg, Z.H.; Stonik, J.A.; Brewer, H.B.
Phosphorylation and modulation of the enzymic activity of native and protease-cleaved purified hepatic 3-hydroxy-3-methylglutaryl-coenzyme A reductase by a calcium/calmodulin-dependent protein kinase
J. Biol. Chem.
262
13228-13240
1987
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Ferrer, A.; Caelles, C.; Massot, N.; Hegardt, F.G.
Allosteric activation of rat liver microsomal [hydroxymethylglutaryl-CoA reductase (NADPH)]kinase by nucleoside phosphates
Biol. Chem. Hoppe-Seyler
368
249-257
1987
Rattus norvegicus
Weekes, J.; Ball, K.L.; Caudwell, F.B.; Hardie, D.G.
Specificity determinants for the AMP-activated protein kinase and its plant homologue analysed using synthetic peptides
FEBS Lett.
334
335-339
1993
Brassica oleracea, Rattus norvegicus
Omkumar, R.V.; Darnay, B.G.; Rodwell, V.W.
Modulation of syrian hamster 3-hydroxy-3-methylglutaryl-CoA reductase activity by phosphorylation. Role of serine 871 [published erratum appears in J Biol Chem 1994 Jun 10;269(23):16518]
J. Biol. Chem.
269
6810-6814
1994
Rattus norvegicus
Henin, N.; Vincent, M.F.; Van den Berghe, G.
Stimulation of rat liver AMP-activated protein kinase by AMP analogues
Biochim. Biophys. Acta
1290
197-203
1996
Rattus norvegicus
Fryer, L.G.; Foufelle, F.; Barnes, K.; Baldwin, S.A.; Woods, A.; Carling, D.
Characterization of the role of the AMP-activated protein kinase in the stimulation of glucose transport in skeletal muscle cells
Biochem. J.
363
167-174
2002
Mus musculus
Park, H.; Kaushik, V.K.; Constant, S.; Prentki, M.; Przybytkowski, E.; Ruderman, N.B.; Saha, A.K.
Coordinate regulation of malonyl-CoA decarboxylase, sn-glycerol-3-phosphate acyltransferase, and acetyl-CoA carboxylase by AMP-activated protein kinase in rat tissues in response to exercise
J. Biol. Chem.
277
32571-32577
2002
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Wang, W.; Fan, J.; Yang, X.; Furer-Galban, S.; Lopez de Silanes, I.; von Kobbe, C.; Guo, J.; Georas, S.N.; Foufelle, F.; Hardie, D.G.; Carling, D.; Gorospe, M.
AMP-activated kinase regulates cytoplasmic HuR
Mol. Cell. Biol.
22
3425-3436
2002
Homo sapiens
Hopkins, T.A.; Dyck, J.R.B.; Lopaschuk, G.D.
AMP-activated protein kinase regulation of fatty acid oxidation in the ischaemic heart
Biochem. Soc. Trans.
31
207-212
2003
Homo sapiens
Wang, W.; Yang, X.; Lopez de Silanes, I.; Carling, D.; Gorospe, M.
Increased AMP:ATP ratio and AMP-activated protein kinase activity during cellular senescence linked to reduced HuR function
J. Biol. Chem.
278
27016-27023
2003
Homo sapiens
Beg, Z.H.; Stonik, J.A.; Brewer, B.
Characterization and regulation of reductase kinase, a protein kinase that modulates the enzymic activity of 3-hydroxy-3-methylglutaryl-coenzyme A reductase
Proc. Natl. Acad. Sci. USA
76
4375-4379
1979
Rattus norvegicus
Weekes, J.; Hawley, S.A.; Corton, J.; Shugar, D.; Hardie, D.G.
Activation of rat liver AMP-activated protein kinase by kinase kinase in a purified, reconstituted system. Effects of AMP and AMP analogues
Eur. J. Biochem.
219
751-757
1994
Rattus norvegicus
Beg, Z.H.; Stonik, J.A.; Brewer, B.
In vivo modulation of rat liver 3-hydroxy-3-methylglutaryl-coenzyme A reductase, reductase kinase, and reductase kinase kinase by mevalonolactone
Proc. Natl. Acad. Sci. USA
81
7293-7297
1984
Rattus norvegicus
Beg, Z.H.; Stonik, J.A.; Brewer, B.
Human hepatic 3-hydroxy-3-methylglutaryl coenzyme A reductase: evidence for the regulation of enzymic activity by a bicyclic phosphorylation cascade
Biochem. Biophys. Res. Commun.
119
488-498
1984
Homo sapiens
Hawley, S.A.; Selbert, M.A.; Goldstein, E.G.; Edelman, A.M.; Carling, D.; Hardie, D.G.
5'-AMP activates the AMP-activated protein kinase cascade, and Ca2+/calmodulin activates the calmodulin-dependent protein kinase I cascade, via three independent mechanisms
J. Biol. Chem.
270
27186-27191
1995
Rattus norvegicus
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
Rattus norvegicus
Woods, A.; Cheung, P.C.; Smith, F.C.; Davison, M.D.; Scott, J.; Beri, R.K.; Carling, D.
Characterization of AMP-activated protein kinase beta and gamma subunits. Assembly of the heterotrimeric complex in vitro
J. Biol. Chem.
271
10282-10290
1996
Rattus norvegicus
Crute, B.E.; Seefeld, K.; Gamble, J.; Kemp, B.E.; Witters, L.A.
Functional domains of the a1 catalytic subunit of the AMP-activated protein kinase
J. Biol. Chem.
273
35347-35354
1998
Rattus norvegicus
Muoio, D.M.; Seefeld, K.; Witters, L.A.; Coleman, R.A.
AMP-activated kinase reciprocally regulates triacylglycerol synthesis and fatty acid oxidation in liver and muscle: evidence that sn-glycerol-3-phosphate acyltransferase is a novel target
Biochem. J.
338
783-791
1999
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Winder, W.W.; Hardie, D.G.
AMP-activated protein kinase, a metabolic master switch: possible roles in type 2 diabetes
Am. J. Physiol.
277
E1-10
1999
Homo sapiens
Kishi, K.; Yuasa, T.; Minami, A.; Yamada, M.; Hagi, A.; Hayashi, H.; Kemp, B.E.; Witters, L.A.; Ebina, Y.
AMP-activated protein kinase is activated by the stimulations of G(q)-coupled receptors
Biochem. Biophys. Res. Commun.
276
16-22
2000
Cricetulus griseus
Stein, S.C.; Woods, A.; Jones, N.A.; Davison, M.D.; Carling, D.
The regulation of AMP-activated protein kinase by phosphorylation
Biochem. J.
345
437-443
2000
Rattus norvegicus
-
Hamilton, S.R.; Stapleton, D.; O'Donnell, J.B.; Kung, J.T.; Dalal, S.R.; Kemp, B.E.; Witters, L.A.
An activating mutation in the g1 subunit of the AMP-activated protein kinase
FEBS Lett.
500
163-168
2001
Homo sapiens
Musi, N.; Hayashi, T.; Fujii, N.; Hirshman, M.F.; Witters, L.A.; Goodyear, L.J.
AMP-activated protein kinase activity and glucose uptake in rat skeletal muscle
Am. J. Physiol.
280
E677-684
2001
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Warden, S.M.; Richardson, C.; O'Donnell, J.Jr.; Stapleton, D.; Kemp, B.E.; Witters, L.A.
Post-translational modifications of the beta-1 subunit of AMP-activated protein kinase affect enzyme activity and cellular localization
Biochem. J.
354
275-283
2001
Homo sapiens
Morrow, V.A.; Foufelle, F.; Connell, J.M.; Petrie, J.R.; Gould, G.W.; Salt, I.P.
Direct activation of AMP-activated protein kinase stimulates nitric-oxide synthesis in human aortic endothelial cells
J. Biol. Chem.
278
31629-31639
2003
Homo sapiens
Woods, A.; Vertommen, D.; Neumann, D.; Tuerk, 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
Rattus norvegicus
Xing, Y.; Musi, N.; Fujii, N.; Zou, L.; Luptak, I.; Hirshman, M.F.; Goodyear, L.J.; Tian, R.
Glucose metabolism and energy homeostasis in mouse hearts overexpressing dominant negative alpha2 subunit of AMP-activated protein kinase
J. Biol. Chem.
278
28372-28377
2003
Mus musculus
Zang, M.; Zuccollo, A.; Hou, X.; Nagata, D.; Walsh, K.; Herscovitz, H.; Brecher, P.; Ruderman, N.B.; Cohen, R.A.
AMP-activated protein kinase is required for the lipid-lowering effect of metformin in insulin-resistant human HepG2 cells
J. Biol. Chem.
279
47898-47905
2004
Homo sapiens
Samari, H.R.; Moeller, M.T.N.; Holden, L.; Asmyhr, T.; Seglen, P.O.
Stimulation of hepatocytic AMP-activated protein kinase by okadaic acid and other autophygy-suppressive toxins
Biochem. J.
386
237-244
2005
Rattus norvegicus
Crawford, R.M.; Treharne, K.J.; Best, O.G.; Muimo, R.; Riemen, C.E.; Mehta, A
A novel physical and functional association between nucleoside diphosphate kinase A and AMP-activated protein kinase alpha1 in liver and lung
Biochem. J.
392
201-209
2005
Homo sapiens, Rattus norvegicus
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
Homo sapiens
Daval, M.; Diot-Dupuy F.; Bazin, R.; Hainault, I.; Viollet, B.; Vaulont, S.; Hajduch, E.; Ferr, P.; Foufelle, F.
Anti-lipolytic action of AMP-activated protein kinase in rodent adipocytes
J. Biol. Chem.
280
25250-25257
2005
Mus musculus, Rattus norvegicus
Mukhtar, M.H.; Payne, V.A.; Arden, C.; Harbottle, A.; Khan, S.; Lange, A.J.; Agius, L.
Inhibition of glucokinase translocation by AMP-activated protein kinase is associated with phosphorylation of both GKRP and 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
Am. J. Physiol. Regul. Integr. Comp. Physiol.
294
R766-R774
2008
Rattus norvegicus
Horman, S.; Morel, N.; Vertommen, D.; Hussain, N.; Neumann, D.; Beauloye, C.; El Najjar, N.; Forcet, C.; Viollet, B.; Walsh, M.P.; Hue, L.; Rider, M.H.
AMP-activated protein kinase phosphorylates and desensitizes smooth muscle myosin light chain kinase
J. Biol. Chem.
283
18505-18512
2008
Mus musculus
Long, Y.C.; Zierath, J.R.
Influence of AMP-activated protein kinase and calcineurin on metabolic networks in skeletal muscle
Am. J. Physiol. Endocrinol. Metab.
295
E545-E552
2008
Mus musculus
Li, X.; Han, Y.; Pang, W.; Li, C.; Xie, X.; Shyy, J.Y.; Zhu, Y.
AMP-activated protein kinase promotes the differentiation of endothelial progenitor cells
Arterioscler. Thromb. Vasc. Biol.
28
1789-1795
2008
Homo sapiens
Viana, R.; Aguado, C.; Esteban, I.; Moreno, D.; Viollet, B.; Knecht, E.; Sanz, P.
Role of AMP-activated protein kinase in autophagy and proteasome function
Biochem. Biophys. Res. Commun.
369
964-968
2008
Homo sapiens
Borger, D.R.; Gavrilescu, L.C.; Bucur, M.C.; Ivan, M.; Decaprio, J.A.
AMP-activated protein kinase is essential for survival in chronic hypoxia
Biochem. Biophys. Res. Commun.
370
230-234
2008
Rattus norvegicus
Garcia-Villafranca, J.; Guillen, A.; Castro, J.
Ethanol consumption impairs regulation of fatty acid metabolism by decreasing the activity of AMP-activated protein kinase in rat liver
Biochimie
90
460-466
2008
Rattus norvegicus
Kim, S.J.; Jung, J.Y.; Kim, H.W.; Park, T.
Anti-obesity effects of Juniperus chinensis extract are associated with increased AMP-activated protein kinase expression and phosphorylation in the visceral adipose tissue of rats
Biol. Pharm. Bull.
31
1415-1421
2008
Rattus norvegicus
Gybina, A.A.; Prohaska, J.R.
Copper deficiency results in AMP-activated protein kinase activation and acetyl-CoA carboxylase phosphorylation in rat cerebellum
Brain Res.
1204
69-76
2008
Rattus norvegicus
Short, J.D.; Houston, K.D.; Dere, R.; Cai, S.L.; Kim, J.; Johnson, C.L.; Broaddus, R.R.; Shen, J.; Miyamoto, S.; Tamanoi, F.; Kwiatkowski, D.; Mills, G.B.; Walker, C.L.
AMP-activated protein kinase signaling results in cytoplasmic sequestration of p27
Cancer Res.
68
6496-6506
2008
Mus musculus
Witczak, C.A.; Sharoff, C.G.; Goodyear, L.J.
AMP-activated protein kinase in skeletal muscle: from structure and localization to its role as a master regulator of cellular metabolism
Cell. Mol. Life Sci.
65
3737-3755
2008
Saccharomyces cerevisiae, Homo sapiens, Rattus norvegicus
McCrimmon, R.J.; Shaw, M.; Fan, X.; Cheng, H.; Ding, Y.; Vella, M.C.; Zhou, L.; McNay, E.C.; Sherwin, R.S.
Key role for AMP-activated protein kinase in the ventromedial hypothalamus in regulating counterregulatory hormone responses to acute hypoglycemia
Diabetes
57
444-450
2008
Rattus norvegicus
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
Homo sapiens
Osler, M.E.; Zierath, J.R.
Adenosine 5-monophosphate-activated protein kinase regulation of fatty acid oxidation in skeletal muscle
Endocrinology
149
935-941
2008
Homo sapiens
Mayer, A.; Denanglaire, S.; Viollet, B.; Leo, O.; Andris, F.
AMP-activated protein kinase regulates lymphocyte responses to metabolic stress but is largely dispensable for immune cell development and function
Eur. J. Immunol.
38
948-956
2008
Mus musculus
Robertson, T.P.; Mustard, K.J.; Lewis, T.H.; Clark, J.H.; Wyatt, C.N.; Blanco, E.A.; Peers, C.; Hardie, D.G.; Evans, A.M.
AMP-activated protein kinase and hypoxic pulmonary vasoconstriction
Eur. J. Pharmacol.
595
39-43
2008
Rattus norvegicus
Beale, E.G.
5-AMP-activated protein kinase signaling in Caenorhabditis elegans
Exp. Biol. Med.
233
12-20
2008
Caenorhabditis elegans
Christ-Crain, M.; Kola, B.; Lolli, F.; Fekete, C.; Seboek, D.; Wittmann, G.; Feltrin, D.; Igreja, S.C.; Ajodha, S.; Harvey-White, J.; Kunos, G.; Mueller, B.; Pralong, F.; Aubert, G.; Arnaldi, G.; Giacchetti, G.; Boscaro, M.; Grossman, A.B.; Korbonits, M.
AMP-activated protein kinase mediates glucocorticoid-induced metabolic changes: a novel mechanism in Cushings syndrome
FASEB J.
22
1672-1683
2008
Homo sapiens, Rattus norvegicus
Summermatter, S.; Mainieri, D.; Russell, A.P.; Seydoux, J.; Montani, J.P.; Buchala, A.; Solinas, G.; Dulloo, A.G.
Thrifty metabolism that favors fat storage after caloric restriction: a role for skeletal muscle phosphatidylinositol-3-kinase activity and AMP-activated protein kinase
FASEB J.
22
774-785
2008
Rattus norvegicus
Hardie, D.G.
Role of AMP-activated protein kinase in the metabolic syndrome and in heart disease
FEBS Lett.
582
81-89
2008
Arabidopsis thaliana, Saccharomyces cerevisiae, Caenorhabditis elegans, Dictyostelium discoideum, Drosophila melanogaster, Giardia intestinalis, Homo sapiens, Mus musculus, Physcomitrium patens, Rattus norvegicus, Schizosaccharomyces pombe, Trypanosoma brucei
Caligiuri, A.; Bertolani, C.; Guerra, C.T.; Aleffi, S.; Galastri, S.; Trappoliere, M.; Vizzutti, F.; Gelmini, S.; Laffi, G.; Pinzani, M.; Marra, F.
Adenosine monophosphate-activated protein kinase modulates the activated phenotype of hepatic stellate cells
Hepatology
47
668-676
2008
Homo sapiens
Ronnett, G.V.; Aja, S.
AMP-activated protein kinase in the brain
Int. J. Obes.
32
S42-S48
2008
Rattus norvegicus
Thomson, D.M.; Herway, S.T.; Fillmore, N.; Kim, H.; Brown, J.D.; Barrow, J.R.; Winder, W.W.
AMP-activated protein kinase phosphorylates transcription factors of the CREB family
J. Appl. Physiol.
104
429-438
2008
Mus musculus
Boyle, J.G.; Logan, P.J.; Ewart, M.; Reihill, J.A.; Ritchie, S.A.; Connell, J.M.; Cleland, S.J.; Salt, I.P.
Rosiglitazone stimulates nitric oxide synthesis in human aortic endothelial cells via AMP-activated protein kinase
J. Biol. Chem.
283
11210-11217
2008
Homo sapiens
Cheung, W.D.; Hart, G.W.
AMP-activated protein kinase and p38 MAPK activate O-GlcNAcylation of neuronal proteins during glucose deprivation
J. Biol. Chem.
283
13009-13020
2008
Mus musculus
Lee, H.; Cho, J.S.; Lambacher, N.; Lee, J.; Lee, S.J.; Lee, T.H.; Gartner, A.; Koo, H.S.
The Caenorhabditis elegans AMP-activated protein kinase AAK-2 is phosphorylated by LKB1 and is required for resistance to oxidative stress and for normal motility and foraging behavior
J. Biol. Chem.
283
14988-14993
2008
Caenorhabditis elegans
Riek, U.; Scholz, R.; Konarev, P.; Rufer, A.; Suter, M.; Nazabal, A.; Ringler, P.; Chami, M.; Mueller, S.A.; Neumann, D.; Forstner, M.; Hennig, M.; Zenobi, R.; Engel, A.; Svergun, D.; Schlattner, U.; Wallimann, T.
Structural properties of AMP-activated protein kinase: dimerization, molecular shape, and changes upon ligand binding
J. Biol. Chem.
283
18331-18343
2008
Rattus norvegicus (P54645), Rattus norvegicus (P80385), Rattus norvegicus (P80386), Rattus norvegicus (Q09137)
Cao, C.; Lu, S.; Kivlin, R.; Wallin, B.; Card, E.; Bagdasarian, A.; Tamakloe, T.; Chu, W.M.; Guan, K.L.; Wan, Y.
AMP-activated protein kinase contributes to UV- and H2O2-induced apoptosis in human skin keratinocytes
J. Biol. Chem.
283
28897-28908
2008
Homo sapiens
Miyamoto, T.; Oshiro, N.; Yoshino, K.; Nakashima, A.; Eguchi, S.; Takahashi, M.; Ono, Y.; Kikkawa, U.; Yonezawa, K.
AMP-activated protein kinase phosphorylates Golgi-specific brefeldin A resistance factor 1 at Thr1337 to induce disassembly of Golgi apparatus
J. Biol. Chem.
283
4430-4438
2008
Homo sapiens
Iseli, T.J.; Oakhill, J.S.; Bailey, M.F.; Wee, S.; Walter, M.; van Denderen, B.J.; Castelli, L.A.; Katsis, F.; Witters, L.A.; Stapleton, D.; Macaulay, S.L.; Michell, B.J.; Kemp, B.E.
AMP-activated protein kinase subunit interactions: beta1:gamma1 association requires beta1 Thr-263 and Tyr-267
J. Biol. Chem.
283
4799-4807
2008
Homo sapiens, Rattus norvegicus
Han, J.H.; Ahn, Y.H.; Choi, K.Y.; Hong, S.H.
Involvement of AMP-activated protein kinase and p38 mitogen-activated protein kinase in 8-Cl-cAMP-induced growth inhibition
J. Cell. Physiol.
218
104-112
2009
Homo sapiens
Vadasz, I.; Dada, L.A.; Briva, A.; Trejo, H.E.; Welch, L.C.; Chen, J.; Toth, P.T.; Lecuona, E.; Witters, L.A.; Schumacker, P.T.; Chandel, N.S.; Seeger, W.; Sznajder, J.I.
AMP-activated protein kinase regulates CO2-induced alveolar epithelial dysfunction in rats and human cells by promoting Na,K-ATPase endocytosis
J. Clin. Invest.
118
752-762
2008
Rattus norvegicus
Jibb, L.A.; Richards, J.G.
AMP-activated protein kinase activity during metabolic rate depression in the hypoxic goldfish, Carassius auratus
J. Exp. Biol.
211
3111-3122
2008
Carassius auratus
Zhu, M.J.; Han, B.; Tong, J.; Ma, C.; Kimzey, J.M.; Underwood, K.R.; Xiao, Y.; Hess, B.W.; Ford, S.P.; Nathanielsz, P.W.; Du, M.
AMP-activated protein kinase signalling pathways are down regulated and skeletal muscle development impaired in fetuses of obese, over-nourished sheep
J. Physiol.
586
2651-2664
2008
Ovis aries
eshmukh, A.S.; Treebak, J.T.; Long, Y.C.; Viollet, B.; Wojtaszewski, J.F.; Zierath, J.R.
Role of adenosine 5'-monophosphate-activated protein kinase subunits in skeletal muscle mammalian target of rapamycin signaling
Mol. Endocrinol.
22
1105-1112
2008
Mus musculus
Irrcher, I.; Ljubicic, V.; Kirwan, A.F.; Hood, D.A.
AMP-activated protein kinase-regulated activation of the PGC-1alpha promoter in skeletal muscle cells
PLoS ONE
3
e3614
2008
Homo sapiens
Hegarty, B.D.; Turner, N.; Cooney, G.J.; Kraegen, E.W.
Insulin resistance and fuel homeostasis: the role of AMP-activated protein kinase
Acta Physiol. (Oxf.)
196
129-145
2009
Homo sapiens, Mus musculus, Rattus norvegicus
Oakhill, J.S.; Scott, J.W.; Kemp, B.E.
Structure and function of AMP-activated protein kinase
Acta Physiol. (Oxf.)
196
3-14
2009
Saccharomyces cerevisiae, Homo sapiens, Mus musculus, Rattus norvegicus, Schizosaccharomyces pombe, Sus scrofa
McBride, A.; Hardie, D.G.
AMP-activated protein kinase--a sensor of glycogen as well as AMP and ATP?
Acta Physiol. (Oxf.)
196
99-113
2009
Homo sapiens, Mus musculus, Rattus norvegicus
Zhang, F.; Dey, D.; Braenstroem, R.; Forsberg, L.; Lu, M.; Zhang, Q.; Sjoeholm, A.
BLX-1002, a novel thiazolidinedione with no PPAR affinity, stimulates AMP-activated protein kinase activity, raises cytosolic Ca2+, and enhances glucose-stimulated insulin secretion in a PI3K-dependent manner
Am. J. Physiol. Cell Physiol.
296
C346-C354
2009
Mus musculus
McFadden, J.W.; Corl, B.A.
Activation of AMP-activated protein kinase (AMPK) inhibits fatty acid synthesis in bovine mammary epithelial cells
Biochem. Biophys. Res. Commun.
390
388-393
2009
Bos taurus
Choi, J.S.; Park, C.; Jeong, J.W.
AMP-activated protein kinase is activated in Parkinsons disease models mediated by 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine
Biochem. Biophys. Res. Commun.
391
147-151
2010
Homo sapiens, Mus musculus
Gao, Y.; Zhou, Y.; Xu, A.; Wu, D.
Effects of an AMP-activated protein kinase inhibitor, compound C, on adipogenic differentiation of 3T3-L1 cells
Biol. Pharm. Bull.
31
1716-1722
2008
Mus musculus
Vazquez-Martin, A.; Oliveras-Ferraros, C.; Menendez, J.A.
The active form of the metabolic sensor: AMP-activated protein kinase (AMPK) directly binds the mitotic apparatus and travels from centrosomes to the spindle midzone during mitosis and cytokinesis
Cell Cycle
8
2385-2398
2009
Homo sapiens
Gundewar, S.; Calvert, J.W.; Jha, S.; Toedt-Pingel, I.; Ji, S.Y.; Nunez, D.; Ramachandran, A.; Anaya-Cisneros, M.; Tian, R.; Lefer, D.J.
Activation of AMP-activated protein kinase by metformin improves left ventricular function and survival in heart failure
Circ. Res.
104
403-411
2009
Mus musculus, Mus musculus C57/BL6J
Zou, M.H.; Wu, Y.
AMP-activated protein kinase activation as a strategy for protecting vascular endothelial function
Clin. Exp. Pharmacol. Physiol.
35
535-545
2008
Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces sp.
Li, C.; Keaney, J.F.
AMP-activated protein kinase: a stress-responsive kinase with implications for cardiovascular disease
Curr. Opin. Pharmacol.
10
111-115
2010
Saccharomyces cerevisiae, Canis lupus familiaris, Homo sapiens, Mus musculus, Rattus norvegicus
Kelly, M.; Gauthier, M.S.; Saha, A.K.; Ruderman, N.B.
Activation of AMP-activated protein kinase by interleukin-6 in rat skeletal muscle: association with changes in cAMP, energy state, and endogenous fuel mobilization
Diabetes
58
1953-1960
2009
Rattus norvegicus
Beck Jorgensen, S.; ONeill, H.M.; Hewitt, K.; Kemp, B.E.; Steinberg, G.R.
Reduced AMP-activated protein kinase activity in mouse skeletal muscle does not exacerbate the development of insulin resistance with obesity
Diabetologia
52
2395-2404
2009
Mus musculus
Foeller, M.; Sopjani, M.; Koka, S.; Gu, S.; Mahmud, H.; Wang, K.; Floride, E.; Schleicher, E.; Schulz, E.; Muenzel, T.; Lang, F.
Regulation of erythrocyte survival by AMP-activated protein kinase
FASEB J.
23
1072-1080
2009
Homo sapiens, Mus musculus
Setsuie, R.; Suzuki, M.; Kabuta, T.; Fujita, H.; Miura, S.; Ichihara, N.; Yamada, D.; Wang, Y.L.; Ezaki, O.; Suzuki, Y.; Wada, K.
Ubiquitin C-terminal hydrolase-L3-knockout mice are resistant to diet-induced obesity and show increased activation of AMP-activated protein kinase in skeletal muscle
FASEB J.
23
4148-4157
2009
Mus musculus
Quinn, J.M.; Tam, S.; Sims, N.A.; Saleh, H.; McGregor, N.E.; Poulton, I.J.; Scott, J.W.; Gillespie, M.T.; Kemp, B.E.; van Denderen, B.J.
Germline deletion of AMP-activated protein kinase beta subunits reduces bone mass without altering osteoclast differentiation or function
FASEB J.
24
275-285
2010
Mus musculus, Mus musculus C57/BL6J
Cheng, H.L.; Huang, H.K.; Chang, C.I.; Tsai, C.P.; Chou, C.H.
A cell-based screening identifies compounds from the stem of Momordica charantia that overcome insulin resistance and activate AMP-activated protein kinase
J. Agric. Food Chem.
56
6835-6843
2008
Mus musculus
Choi, H.C.; Song, P.; Xie, Z.; Wu, Y.; Xu, J.; Zhang, M.; Dong, Y.; Wang, S.; Lau, K.; Zou, M.H.
Reactive nitrogen species is required for the activation of the AMP-activated protein kinase by statin in vivo
J. Biol. Chem.
283
20186-20197
2008
Bos taurus, Homo sapiens, Mus musculus, Mus musculus C57/BL6J
Chan, A.Y.; Dolinsky, V.W.; Soltys, C.L.; Viollet, B.; Baksh, S.; Light, P.E.; Dyck, J.R.
Resveratrol inhibits cardiac hypertrophy via AMP-activated protein kinase and Akt
J. Biol. Chem.
283
24194-24201
2008
Mus musculus, Rattus norvegicus
Garcia-Roves, P.M.; Osler, M.E.; Holmstroem, M.H.; Zierath, J.R.
Gain-of-function R225Q mutation in AMP-activated protein kinase gamma3 subunit increases mitochondrial biogenesis in glycolytic skeletal muscle
J. Biol. Chem.
283
35724-35734
2008
Mus musculus
Qin, S.; De Vries, G.W.
alpha2 But not alpha1 AMP-activated protein kinase mediates oxidative stress-induced inhibition of retinal pigment epithelium cell phagocytosis of photoreceptor outer segments
J. Biol. Chem.
283
6744-6751
2008
Homo sapiens
Scharl, M.; Paul, G.; Barrett, K.E.; McCole, D.F.
AMP-activated protein kinase mediates the interferon-gamma-induced decrease in intestinal epithelial barrier function
J. Biol. Chem.
284
27952-27963
2009
Homo sapiens
Meares, G.P.; Hughes, K.J.; Jaimes, K.F.; Salvatori, A.S.; Rhodes, C.J.; Corbett, J.A.
AMP-activated protein kinase attenuates nitric oxide-induced beta-cell death
J. Biol. Chem.
285
3191-3200
2010
Rattus norvegicus
Frederich, M.; ORourke, M.R.; Furey, N.B.; Jost, J.A.
AMP-activated protein kinase (AMPK) in the rock crab, Cancer irroratus: an early indicator of temperature stress
J. Exp. Biol.
212
722-730
2009
Cancer irroratus (B8Y8L1), Cancer irroratus (B8Y8L2)
Bendayan, M.; Londono, I.; Kemp, B.E.; Hardie, G.D.; Ruderman, N.; Prentki, M.
Association of AMP-activated protein kinase subunits with glycogen particles as revealed in situ by immunoelectron microscopy
J. Histochem. Cytochem.
57
963-971
2009
Rattus norvegicus
Kola, B.
Role of AMP-activated protein kinase in the control of appetite
J. Neuroendocrinol.
20
942-951
2008
Homo sapiens, Mus musculus, Rattus norvegicus
Gusarova, G.A.; Dada, L.A.; Kelly, A.M.; Brodie, C.; Witters, L.A.; Chandel, N.S.; Sznajder, J.I.
Alpha1-AMP-activated protein kinase regulates hypoxia-induced Na,K-ATPase endocytosis via direct phosphorylation of protein kinase C zeta
Mol. Cell. Biol.
29
3455-3464
2009
Homo sapiens
Hien, T.T.; Kim, H.G.; Han, E.H.; Kang, K.W.; Jeong, H.G.
Molecular mechanism of suppression of MDR1 by puerarin from Pueraria lobata via NF-kappaB pathway and cAMP-responsive element transcriptional activity-dependent up-regulation of AMP-activated protein kinase in breast cancer MCF-7/adr cells
Mol. Nutr. Food Res.
54
918-928
2010
Homo sapiens
Chen, L.; Jiao, Z.H.; Zheng, L.S.; Zhang, Y.Y.; Xie, S.T.; Wang, Z.X.; Wu, J.W.
Structural insight into the autoinhibition mechanism of AMP-activated protein kinase
Nature
459
1146-1149
2009
Saccharomyces cerevisiae, Rattus norvegicus, Schizosaccharomyces pombe
Spasic, M.R.; Callaerts, P.; Norga, K.K.
AMP-activated protein kinase (AMPK) molecular crossroad for metabolic control and survival of neurons
Neuroscientist
15
309-316
2009
Saccharomyces cerevisiae, Homo sapiens, Mus musculus, Rattus norvegicus
Sidani, S.; Kopic, S.; Socrates, T.; Kirchhoff, P.; Foeller, M.; Murek, M.; Capasso, A.; Geibel, J.P.
AMP-activated protein kinase: a physiological off switch for murine gastric acid secretion
Pflugers Arch.
459
39-46
2009
Mus musculus
Khanal, P.; Oh, W.K.; Thuong, P.T.; Cho, S.D.; Choi, H.S.
24-hydroxyursolic acid from the leaves of the Diospyros kaki (Persimmon) induces apoptosis by activation of AMP-activated protein kinase
Planta Med.
76
689-693
2010
Homo sapiens
Zhang, H.S.; Wu, M.R.
SIRT1 regulates Tat-induced HIV-1 transactivation through activating AMP-activated protein kinase
Virus Res.
146
51-57
2009
Homo sapiens
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. Sect. D
67
480-487
2011
Homo sapiens (P54646)
Wang, Y.; Viollet, B.; Terkeltaub, R.; Liu-Bryan, R.
AMP-activated protein kinase suppresses urate crystal-induced inflammation and transduces colchicine effects in macrophages
Ann. Rheum. Dis.
75
286-294
2016
Mus musculus (Q5EG47), Mus musculus C57BL/6/129 (Q5EG47)
Thali, R.F.; Tuerk, R.D.; Scholz, R.; Yoho-Auchli, Y.; Brunisholz, R.A.; Neumann, D.
Novel candidate substrates of AMP-activated protein kinase identified in red blood cell lysates
Biochem. Biophys. Res. Commun.
398
296-301
2010
Homo sapiens (Q13131)
Sano, S.; Sakagami, R.; Sekiguchi, M.; Hidaka, M.
Stabilization of MAPO1 by specific binding with folliculin and AMP-activated protein kinase in O6-methylguanine-induced apoptosis
Biochem. Biophys. Res. Commun.
430
810-815
2013
Homo sapiens (Q13131)
Mobbs, J.I.; Koay, A.; Di Paolo, A.; Bieri, M.; Petrie, E.J.; Gorman, M.A.; Doughty, L.; Parker, M.W.; Stapleton, D.I.; Griffin, M.D.; Gooley, P.R.
Determinants of oligosaccharide specificity of the carbohydrate-binding modules of AMP-activated protein kinase
Biochem. J.
468
245-257
2015
Rattus norvegicus (P80386), Rattus norvegicus (Q9QZH4)
Rajamohan, F.; Reyes, A.R.; Frisbie, R.K.; Hoth, L.R.; Sahasrabudhe, P.; Magyar, R.; Landro, J.A.; Withka, J.M.; Caspers, N.L.; Calabrese, M.F.; Ward, J.; Kurumbail, R.G.
Probing the enzyme kinetics, allosteric modulation and activation of alpha1- and alpha2-subunit-containing AMP-activated protein kinase (AMPK) heterotrimeric complexes by pharmacological and physiological activators
Biochem. J.
473
581-592
2016
Homo sapiens (Q13131 AND P54646)
Guevelou, E.; Huvet, A.; Galindo-Sanchez, C.E.; Milan, M.; Quillien, V.; Daniel, J.Y.; Quere, C.; Boudry, P.; Corporeau, C.
Sex-specific regulation of AMP-activated protein kinase (AMPK) in the Pacific oyster Crassostrea gigas
Biol. Reprod.
89
100
2013
Crassostrea gigas (J7H7T6), Crassostrea gigas (K1R1Z4), Crassostrea gigas (T1R3F6)
Chandrashekarappa, D.G.; McCartney, R.R.; ODonnell, A.F.; Schmidt, M.C.
The beta subunit of yeast AMP-activated protein kinase directs substrate specificity in response to alkaline stress
Cell. Signal.
28
1881-1893
2016
Saccharomyces cerevisiae (P32578), Saccharomyces cerevisiae (P34164), Saccharomyces cerevisiae (Q04739), Saccharomyces cerevisiae, Saccharomyces cerevisiae S228C (P32578), Saccharomyces cerevisiae S228C (P34164), Saccharomyces cerevisiae S228C (Q04739)
Yu, D.; Peng, Y.; Ayaz-Guner, S.; Gregorich, Z.R.; Ge, Y.
Comprehensive characterization of AMP-activated protein kinase catalytic domain by top-down mass spectrometry
J. Am. Soc. Mass Spectrom.
27
220-232
2016
Homo sapiens (Q13131)
Alesutan, I.; Foeller, M.; Sopjani, M.; Dermaku-Sopjani, M.; Zelenak, C.; Froehlich, H.; Velic, A.; Fraser, S.; Kemp, B.E.; Seebohm, G.; Voelkl, H.; Lang, F.
Inhibition of the heterotetrameric K+ channel KCNQ1/KCNE1 by the AMP-activated protein kinase
Mol. Membr. Biol.
28
79-89
2011
Homo sapiens (Q13131 AND Q9Y478 AND P54619)
Peng, C.; Head-Gordon, T.
The dynamical mechanism of auto-inhibition of AMP-activated protein kinase
PLoS Comput. Biol.
7
e1002082
2011
Schizosaccharomyces pombe
Rajamohan, F.; Harris, M.S.; Frisbie, R.K.; Hoth, L.R.; Geoghegan, K.F.; Valentine, J.J.; Reyes, A.R.; Landro, J.A.; Qiu, X.; Kurumbail, R.G.
Escherichia coli expression, purification and characterization of functional full-length recombinant alpha2beta2gamma3 heterotrimeric complex of human AMP-activated protein kinase
Protein Expr. Purif.
73
189-197
2010
Homo sapiens (P54646 AND O43741 AND Q9UGI9)
Lanaspa, M.A.; Epperson, L.E.; Li, N.; Cicerchi, C.; Garcia, G.E.; Roncal-Jimenez, C.A.; Trostel, J.; Jain, S.; Mant, C.T.; Rivard, C.J.; Ishimoto, T.; Shimada, M.; Sanchez-Lozada, L.G.; Nakagawa, T.; Jani, A.; Stenvinkel, P.; Martin, S.L.; Johnson, R.J.
Opposing activity changes in AMP deaminase and AMP-activated protein kinase in the hibernating ground squirrel
PLoS ONE
10
e0123509
2015
Ictidomys tridecemlineatus
Eom, J.W.; Kim, T.Y.; Seo, B.R.; Park, H.; Koh, J.Y.; Kim, Y.H.
Identifying new AMP-activated protein kinase inhibitors that protect against ischemic brain injury
ACS Chem. Neurosci.
10
2345-2354
2019
Mus musculus
Noor, H.B.; Mou, N.A.; Salem, L.; Shimul, M.F.A.; Biswas, S.; Akther, R.; Khan, S.; Raihan, S.; Mohib, M.M.; Sagor, M.A.T.
Anti-inflammatory property of AMP-activated protein kinase
Antiinflamm. Antiallergy Agents Med. Chem.
19
2-41
2020
Mus musculus
Wu, W.; Sun, J.; Ji, H.; Yu, H.; Zhou, J.
AMP-activated protein kinase in the grass carp Ctenopharyngodon idellus Molecular characterization, tissue distribution and mRNA expression in response to overwinter starvation stress
Comp. Biochem. Physiol. B
246-247
110457
2020
Ctenopharyngodon idella (A0A514YC25), Ctenopharyngodon idella (A0A515J4H7), Ctenopharyngodon idella (A0A515J4I2), Ctenopharyngodon idella (A0A515J4I4), Ctenopharyngodon idella (A0A515J4J0), Ctenopharyngodon idella (A0A515J4J2), Ctenopharyngodon idella (A0A515J4J3), Ctenopharyngodon idella (A0A515J4V2), Ctenopharyngodon idella (A0A515J4V7), Ctenopharyngodon idella
Xu, C.; Li, E.; Xu, Z.; Wang, S.; Chen, K.; Wang, X.; Li, T.; Qin, J.; Chen, L.
Molecular characterization and expression of AMP-activated protein kinase in response to low-salinity stress in the Pacific white shrimp Litopenaeus vannamei
Comp. Biochem. Physiol. B Biochem. Mol. Biol.
198
79-90
2016
Penaeus vannamei (A0A0F6RAR3), Penaeus vannamei (A0A0F6TML3), Penaeus vannamei (A0A0F6TN48)
Matheson, C.J.; Casalvieri, K.A.; Backos, D.S.; Minhajuddin, M.; Jordan, C.T.; Reigan, P.
Substituted oxindol-3-ylidenes as AMP-activated protein kinase (AMPK) inhibitors
Eur. J. Med. Chem.
197
112316
2020
Homo sapiens (P54646), Homo sapiens (Q13131)
Chen, M.; Liu, J.; Yang, L.; Ling, W.
AMP-activated protein kinase regulates lipid metabolism and the fibrotic phenotype of hepatic stellate cells through inhibition of autophagy
FEBS Open Bio
7
811-820
2017
Homo sapiens
Gao, F.; Qian, Y.J.; Chen, F.H.; Zhu, H.B.
Comparative analysis of stimulation and binding characteristics of adenosine analogs to AMP-activated protein kinase
J. Asian Nat. Prod. Res.
21
916-927
2019
Rattus norvegicus
Han, J.S.; Sung, J.H.; Lee, S.K.
Inhibition of cholesterol synthesis in HepG2 cells by GINST-decreasing HMG-CoA reductase expression via AMP-activated protein kinase
J. Food Sci.
82
2700-2705
2017
Homo sapiens
Singh, S.; Singh, P.K.; Suhail, H.; Arumugaswami, V.; Pellett, P.E.; Giri, S.; Kumar, A.
Adenosine monophosphate-activated protein kinase restricts Zika virus replication in endothelial cells by potentiating innate antiviral responses and inhibiting glycolysis
J. Immunol.
204
1810-1824
2020
Homo sapiens
Moral-Sanz, J.; Mahmoud, A.; Ross, F.; Eldstrom, J.; Fedida, D.; Hardie, D.; Evans, A.
AMP-activated protein kinase inhibits Kv1.5 channel currents of pulmonary arterial myocytes in response to hypoxia and inhibition of mitochondrial oxidative phosphorylation
J. Physiol.
594
4901-4915
2016
Rattus norvegicus
Hermann, R.; Mestre Cordero, V.; Fernandez Pazos, M.; Reznik, F.; Velez, D.; Savino, E.; Marina Prendes, M.; Varela, A.
Differential effects of AMP-activated protein kinase in isolated rat atria subjected to simulated ischemia-reperfusion depending on the energetic substrates available
Pflugers Arch.
470
367-383
2018
Rattus norvegicus
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