Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

5'-AMP-activated protein kinase catalytic subunit alpha-1 (AMPK subunit alpha-1) (EC 2.7.11.1) (Acetyl-CoA carboxylase kinase) (ACACA kinase) (EC 2.7.11.27) (Hydroxymethylglutaryl-CoA reductase kinase) (HMGCR kinase) (EC 2.7.11.31) (Tau-protein kinase PRKAA1) (EC 2.7.11.26)

 AAPK1_MOUSE             Reviewed;         559 AA.
Q5EG47;
13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
28-JUL-2009, sequence version 2.
30-AUG-2017, entry version 125.
RecName: Full=5'-AMP-activated protein kinase catalytic subunit alpha-1;
Short=AMPK subunit alpha-1;
EC=2.7.11.1 {ECO:0000250|UniProtKB:P54645};
AltName: Full=Acetyl-CoA carboxylase kinase;
Short=ACACA kinase;
EC=2.7.11.27 {ECO:0000250|UniProtKB:P54645};
AltName: Full=Hydroxymethylglutaryl-CoA reductase kinase;
Short=HMGCR kinase;
EC=2.7.11.31 {ECO:0000250|UniProtKB:P54645};
AltName: Full=Tau-protein kinase PRKAA1;
EC=2.7.11.26;
Name=Prkaa1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 10-559.
STRAIN=C57BL/6N; TISSUE=Muscle;
Xie X., Chen Y.;
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
[3]
ENZYME REGULATION, AND PHOSPHORYLATION AT THR-183.
PubMed=16054095; DOI=10.1016/j.cmet.2005.05.009;
Hawley S.A., Pan D.A., Mustard K.J., Ross L., Bain J., Edelman A.M.,
Frenguelli B.G., Hardie D.G.;
"Calmodulin-dependent protein kinase kinase-beta is an alternative
upstream kinase for AMP-activated protein kinase.";
Cell Metab. 2:9-19(2005).
[4]
FUNCTION IN PHOSPHORYLATION OF LIPE, AND MUTAGENESIS OF ASP-168.
PubMed=15878856; DOI=10.1074/jbc.M414222200;
Daval M., Diot-Dupuy F., Bazin R., Hainault I., Viollet B.,
Vaulont S., Hajduch E., Ferre P., Foufelle F.;
"Anti-lipolytic action of AMP-activated protein kinase in rodent
adipocytes.";
J. Biol. Chem. 280:25250-25257(2005).
[5]
PHOSPHORYLATION AT THR-183, AND ENZYME REGULATION.
PubMed=15980064; DOI=10.1074/jbc.M503824200;
Hurley R.L., Anderson K.A., Franzone J.M., Kemp B.E., Means A.R.,
Witters L.A.;
"The Ca2+/calmodulin-dependent protein kinase kinases are AMP-
activated protein kinase kinases.";
J. Biol. Chem. 280:29060-29066(2005).
[6]
FUNCTION IN PHOSPHORYLATION OF CRTC2.
PubMed=16148943; DOI=10.1038/nature03967;
Koo S.-H., Flechner L., Qi L., Zhang X., Screaton R.A., Jeffries S.,
Hedrick S., Xu W., Boussouar F., Brindle P., Takemori H., Montminy M.;
"The CREB coactivator TORC2 is a key regulator of fasting glucose
metabolism.";
Nature 437:1109-1111(2005).
[7]
FUNCTION IN PHOSPHORYLATION OF CRTC2, AND PHOSPHORYLATION AT THR-183.
PubMed=16308421; DOI=10.1126/science.1120781;
Shaw R.J., Lamia K.A., Vasquez D., Koo S.-H., Bardeesy N.,
Depinho R.A., Montminy M., Cantley L.C.;
"The kinase LKB1 mediates glucose homeostasis in liver and therapeutic
effects of metformin.";
Science 310:1642-1646(2005).
[8]
FUNCTION IN PHOSPHORYLATION OF TBC1D4.
PubMed=16804075; DOI=10.2337/db06-0175;
Treebak J.T., Glund S., Deshmukh A., Klein D.K., Long Y.C.,
Jensen T.E., Jorgensen S.B., Viollet B., Andersson L., Neumann D.,
Wallimann T., Richter E.A., Chibalin A.V., Zierath J.R.,
Wojtaszewski J.F.;
"AMPK-mediated AS160 phosphorylation in skeletal muscle is dependent
on AMPK catalytic and regulatory subunits.";
Diabetes 55:2051-2058(2006).
[9]
FUNCTION IN PHOSPHORYLATION OF TBC1D4.
PubMed=16804077; DOI=10.2337/db06-0150;
Kramer H.F., Witczak C.A., Fujii N., Jessen N., Taylor E.B.,
Arnolds D.E., Sakamoto K., Hirshman M.F., Goodyear L.J.;
"Distinct signals regulate AS160 phosphorylation in response to
insulin, AICAR, and contraction in mouse skeletal muscle.";
Diabetes 55:2067-2076(2006).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[11]
UBIQUITINATION.
PubMed=18254724; DOI=10.1042/BJ20080067;
Al-Hakim A.K., Zagorska A., Chapman L., Deak M., Peggie M.,
Alessi D.R.;
"Control of AMPK-related kinases by USP9X and atypical
Lys(29)/Lys(33)-linked polyubiquitin chains.";
Biochem. J. 411:249-260(2008).
[12]
FUNCTION IN PHOSPHORYLATION OF RPTOR.
PubMed=18439900; DOI=10.1016/j.molcel.2008.03.003;
Gwinn D.M., Shackelford D.B., Egan D.F., Mihaylova M.M., Mery A.,
Vasquez D.S., Turk B.E., Shaw R.J.;
"AMPK phosphorylation of raptor mediates a metabolic checkpoint.";
Mol. Cell 30:214-226(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-496, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[14]
FUNCTION IN PHOSPHORYLATION OF CRY1, AND SUBCELLULAR LOCATION.
PubMed=19833968; DOI=10.1126/science.1172156;
Lamia K.A., Sachdeva U.M., DiTacchio L., Williams E.C., Alvarez J.G.,
Egan D.F., Vasquez D.S., Juguilon H., Panda S., Shaw R.J.,
Thompson C.B., Evans R.M.;
"AMPK regulates the circadian clock by cryptochrome phosphorylation
and degradation.";
Science 326:437-440(2009).
[15]
FUNCTION IN PHOSPHORYLATION OF CTNNB1.
PubMed=20361929; DOI=10.1016/j.bbrc.2010.03.161;
Zhao J., Yue W., Zhu M.J., Sreejayan N., Du M.;
"AMP-activated protein kinase (AMPK) cross-talks with canonical Wnt
signaling via phosphorylation of beta-catenin at Ser 552.";
Biochem. Biophys. Res. Commun. 395:146-151(2010).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486 AND THR-490, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Lung, Pancreas, Spleen, and
Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[17]
FUNCTION IN PHOSPHORYLATION OF H2B.
PubMed=20647423; DOI=10.1126/science.1191241;
Bungard D., Fuerth B.J., Zeng P.Y., Faubert B., Maas N.L., Viollet B.,
Carling D., Thompson C.B., Jones R.G., Berger S.L.;
"Signaling kinase AMPK activates stress-promoted transcription via
histone H2B phosphorylation.";
Science 329:1201-1205(2010).
[18]
PHOSPHORYLATION BY ULK1 AND ULK2.
PubMed=21460634; DOI=10.4161/auto.7.7.15451;
Loffler A.S., Alers S., Dieterle A.M., Keppeler H., Franz-Wachtel M.,
Kundu M., Campbell D.G., Wesselborg S., Alessi D.R., Stork B.;
"Ulk1-mediated phosphorylation of AMPK constitutes a negative
regulatory feedback loop.";
Autophagy 7:696-706(2011).
[19]
FUNCTION IN PHOSPHORYLATION OF SREBF1 AND SREBF2, AND ENZYME
REGULATION.
PubMed=21459323; DOI=10.1016/j.cmet.2011.03.009;
Li Y., Xu S., Mihaylova M.M., Zheng B., Hou X., Jiang B., Park O.,
Luo Z., Lefai E., Shyy J.Y., Gao B., Wierzbicki M., Verbeuren T.J.,
Shaw R.J., Cohen R.A., Zang M.;
"AMPK phosphorylates and inhibits SREBP activity to attenuate hepatic
steatosis and atherosclerosis in diet-induced insulin-resistant
mice.";
Cell Metab. 13:376-388(2011).
[20]
FUNCTION IN PHOSPHORYLATION OF ULK1, AND MUTAGENESIS OF ASP-168.
PubMed=21258367; DOI=10.1038/ncb2152;
Kim J., Kundu M., Viollet B., Guan K.L.;
"AMPK and mTOR regulate autophagy through direct phosphorylation of
Ulk1.";
Nat. Cell Biol. 13:132-141(2011).
[21]
FUNCTION IN PHOSPHORYLATION OF ULK1.
PubMed=21205641; DOI=10.1126/science.1196371;
Egan D.F., Shackelford D.B., Mihaylova M.M., Gelino S., Kohnz R.A.,
Mair W., Vasquez D.S., Joshi A., Gwinn D.M., Taylor R., Asara J.M.,
Fitzpatrick J., Dillin A., Viollet B., Kundu M., Hansen M., Shaw R.J.;
"Phosphorylation of ULK1 (hATG1) by AMP-activated protein kinase
connects energy sensing to mitophagy.";
Science 331:456-461(2011).
-!- FUNCTION: Catalytic subunit of AMP-activated protein kinase
(AMPK), an energy sensor protein kinase that plays a key role in
regulating cellular energy metabolism. In response to reduction of
intracellular ATP levels, AMPK activates energy-producing pathways
and inhibits energy-consuming processes: inhibits protein,
carbohydrate and lipid biosynthesis, as well as cell growth and
proliferation. AMPK acts via direct phosphorylation of metabolic
enzymes, and by longer-term effects via phosphorylation of
transcription regulators. Also acts as a regulator of cellular
polarity by remodeling the actin cytoskeleton; probably by
indirectly activating myosin. Regulates lipid synthesis by
phosphorylating and inactivating lipid metabolic enzymes such as
ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and
cholesterol synthesis by phosphorylating acetyl-CoA carboxylase
(ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes,
respectively. Regulates insulin-signaling and glycolysis by
phosphorylating IRS1, PFKFB2 and PFKFB3. AMPK stimulates glucose
uptake in muscle by increasing the translocation of the glucose
transporter SLC2A4/GLUT4 to the plasma membrane, possibly by
mediating phosphorylation of TBC1D4/AS160. Regulates transcription
and chromatin structure by phosphorylating transcription
regulators involved in energy metabolism such as CRTC2/TORC2,
FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A,
p53/TP53, SREBF1, SREBF2 and PPARGC1A. Acts as a key regulator of
glucose homeostasis in liver by phosphorylating CRTC2/TORC2,
leading to CRTC2/TORC2 sequestration in the cytoplasm. In response
to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph),
leading to promote transcription. Acts as a key regulator of cell
growth and proliferation by phosphorylating TSC2, RPTOR and
ATG1/ULK1: in response to nutrient limitation, negatively
regulates the mTORC1 complex by phosphorylating RPTOR component of
the mTORC1 complex and by phosphorylating and activating TSC2. In
response to nutrient limitation, promotes autophagy by
phosphorylating and activating ATG1/ULK1. AMPK also acts as a
regulator of circadian rhythm by mediating phosphorylation of
CRY1, leading to destabilize it. May regulate the Wnt signaling
pathway by phosphorylating CTNNB1, leading to stabilize it. Also
has tau-protein kinase activity: in response to amyloid beta A4
protein (APP) exposure, activated by CAMKK2, leading to
phosphorylation of MAPT/TAU; however the relevance of such data
remains unclear in vivo. Also phosphorylates CFTR, EEF2K, KLC1,
NOS3 and SLC12A1. {ECO:0000269|PubMed:15878856,
ECO:0000269|PubMed:16148943, ECO:0000269|PubMed:16308421,
ECO:0000269|PubMed:16804075, ECO:0000269|PubMed:16804077,
ECO:0000269|PubMed:18439900, ECO:0000269|PubMed:19833968,
ECO:0000269|PubMed:20361929, ECO:0000269|PubMed:20647423,
ECO:0000269|PubMed:21205641, ECO:0000269|PubMed:21258367,
ECO:0000269|PubMed:21459323}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000250|UniProtKB:P54645}.
-!- CATALYTIC ACTIVITY: ATP + [acetyl-CoA carboxylase] = ADP +
[acetyl-CoA carboxylase] phosphate.
{ECO:0000250|UniProtKB:P54645}.
-!- CATALYTIC ACTIVITY: ATP + [hydroxymethylglutaryl-CoA reductase
(NADPH)] = ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
phosphate. {ECO:0000250|UniProtKB:P54645}.
-!- CATALYTIC ACTIVITY: ATP + [tau protein] = ADP + [tau protein]
phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- ENZYME REGULATION: Activated by phosphorylation on Thr-183.
Binding of AMP to non-catalytic gamma subunit (PRKAG1, PRKAG2 or
PRKAG3) results in allosteric activation, inducing phosphorylation
on Thr-183. AMP-binding to gamma subunit also sustains activity by
preventing dephosphorylation of Thr-183. ADP also stimulates Thr-
183 phosphorylation, without stimulating already phosphorylated
AMPK. ATP promotes dephosphorylation of Thr-183, rendering the
enzyme inactive. Under physiological conditions AMPK mainly exists
in its inactive form in complex with ATP, which is much more
abundant than AMP. Selectively inhibited by compound C (6-[4-(2-
Piperidin-1-yl-ethoxy)-phenyl)]-3-pyridin-4-yl-pyyrazolo[1,5-a]
pyrimidine. Activated by resveratrol, a natural polyphenol present
in red wine, and S17834, a synthetic polyphenol.
{ECO:0000269|PubMed:15980064, ECO:0000269|PubMed:16054095,
ECO:0000269|PubMed:21459323}.
-!- SUBUNIT: AMPK is a heterotrimer of an alpha catalytic subunit
(PRKAA1 or PRKAA2), a beta (PRKAB1 or PRKAB2) and a gamma non-
catalytic subunits (PRKAG1, PRKAG2 or PRKAG3). Interacts with
FNIP1 and FNIP2.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000269|PubMed:19833968}. Note=In response to stress,
recruited by p53/TP53 to specific promoters.
-!- DOMAIN: The AIS (autoinhibitory sequence) region shows some
sequence similarity with the ubiquitin-associated domains and
represses kinase activity. {ECO:0000250}.
-!- PTM: Phosphorylated at Thr-183 by STK11/LKB1 in complex with
STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Also
phosphorylated at Thr-183 by CAMKK2; triggered by a rise in
intracellular calcium ions, without detectable changes in the
AMP/ATP ratio. CAMKK1 can also phosphorylate Thr-183, but at a
much lower level. Dephosphorylated by protein phosphatase 2A and
2C (PP2A and PP2C). Phosphorylated by ULK1 and ULK2; leading to
negatively regulate AMPK activity and suggesting the existence of
a regulatory feedback loop between ULK1, ULK2 and AMPK.
Dephosphorylated by PPM1A and PPM1B (By similarity).
{ECO:0000250}.
-!- PTM: Ubiquitinated. {ECO:0000269|PubMed:18254724}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. SNF1 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AC131919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC135079; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AY885266; AAW79567.1; -; mRNA.
CCDS; CCDS49574.1; -.
RefSeq; NP_001013385.3; NM_001013367.3.
UniGene; Mm.207004; -.
PDB; 5UFU; X-ray; 3.45 A; A=11-559.
PDBsum; 5UFU; -.
ProteinModelPortal; Q5EG47; -.
SMR; Q5EG47; -.
BioGrid; 222923; 32.
DIP; DIP-47622N; -.
IntAct; Q5EG47; 27.
STRING; 10090.ENSMUSP00000063166; -.
ChEMBL; CHEMBL1075161; -.
iPTMnet; Q5EG47; -.
PhosphoSitePlus; Q5EG47; -.
SwissPalm; Q5EG47; -.
EPD; Q5EG47; -.
MaxQB; Q5EG47; -.
PaxDb; Q5EG47; -.
PRIDE; Q5EG47; -.
Ensembl; ENSMUST00000051186; ENSMUSP00000063166; ENSMUSG00000050697.
GeneID; 105787; -.
KEGG; mmu:105787; -.
UCSC; uc007vct.1; mouse.
CTD; 5562; -.
MGI; MGI:2145955; Prkaa1.
eggNOG; KOG0586; Eukaryota.
eggNOG; ENOG410XNQ0; LUCA.
GeneTree; ENSGT00790000122947; -.
HOGENOM; HOG000233016; -.
HOVERGEN; HBG050432; -.
InParanoid; Q5EG47; -.
KO; K07198; -.
OMA; QGVRRAK; -.
OrthoDB; EOG091G03TG; -.
PhylomeDB; Q5EG47; -.
TreeFam; TF314032; -.
Reactome; R-MMU-1632852; Macroautophagy.
Reactome; R-MMU-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
Reactome; R-MMU-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
PRO; PR:Q5EG47; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000050697; -.
Genevisible; Q5EG47; MM.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005622; C:intracellular; ISO:MGI.
GO; GO:0016607; C:nuclear speck; ISO:MGI.
GO; GO:0031588; C:nucleotide-activated protein kinase complex; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0050405; F:[acetyl-CoA carboxylase] kinase activity; IEA:UniProtKB-EC.
GO; GO:0047322; F:[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase activity; IEA:UniProtKB-EC.
GO; GO:0004679; F:AMP-activated protein kinase activity; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0035174; F:histone serine kinase activity; IDA:UniProtKB.
GO; GO:0019900; F:kinase binding; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
GO; GO:0004672; F:protein kinase activity; ISO:MGI.
GO; GO:0050321; F:tau-protein kinase activity; IEA:UniProtKB-EC.
GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO; GO:0061762; P:CAMKK-AMPK signaling cascade; ISO:MGI.
GO; GO:0071361; P:cellular response to ethanol; IEA:Ensembl.
GO; GO:0042149; P:cellular response to glucose starvation; IDA:UniProtKB.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:0031669; P:cellular response to nutrient levels; IDA:UniProtKB.
GO; GO:0071417; P:cellular response to organonitrogen compound; IEA:Ensembl.
GO; GO:0071380; P:cellular response to prostaglandin E stimulus; IGI:MGI.
GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0009631; P:cold acclimation; IEA:Ensembl.
GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0055089; P:fatty acid homeostasis; ISS:UniProtKB.
GO; GO:0019395; P:fatty acid oxidation; IMP:MGI.
GO; GO:0042593; P:glucose homeostasis; IMP:UniProtKB.
GO; GO:0006006; P:glucose metabolic process; IMP:MGI.
GO; GO:0008610; P:lipid biosynthetic process; IDA:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:2001274; P:negative regulation of glucose import in response to insulin stimulus; IEA:Ensembl.
GO; GO:0050995; P:negative regulation of lipid catabolic process; IDA:UniProtKB.
GO; GO:0032007; P:negative regulation of TOR signaling; IMP:UniProtKB.
GO; GO:0010508; P:positive regulation of autophagy; IMP:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
GO; GO:0045821; P:positive regulation of glycolytic process; ISS:UniProtKB.
GO; GO:0048643; P:positive regulation of skeletal muscle tissue development; IMP:MGI.
GO; GO:0051291; P:protein heterooligomerization; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
GO; GO:2000505; P:regulation of energy homeostasis; ISS:UniProtKB.
GO; GO:0033135; P:regulation of peptidyl-serine phosphorylation; IMP:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0060627; P:regulation of vesicle-mediated transport; IEA:Ensembl.
GO; GO:0014823; P:response to activity; IEA:Ensembl.
GO; GO:0031000; P:response to caffeine; IEA:Ensembl.
GO; GO:1901563; P:response to camptothecin; IMP:UniProtKB.
GO; GO:0010332; P:response to gamma radiation; IMP:UniProtKB.
GO; GO:0042542; P:response to hydrogen peroxide; IMP:UniProtKB.
GO; GO:0009411; P:response to UV; IMP:UniProtKB.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
InterPro; IPR032270; AMPK_C.
InterPro; IPR028375; KA1/Ssp2_C.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF16579; AdenylateSensor; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF103243; SSF103243; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Autophagy; Biological rhythms;
Cholesterol biosynthesis; Cholesterol metabolism; Chromatin regulator;
Complete proteome; Cytoplasm; Fatty acid biosynthesis;
Fatty acid metabolism; Kinase; Lipid biosynthesis; Lipid metabolism;
Magnesium; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Serine/threonine-protein kinase;
Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
Sterol metabolism; Transcription; Transcription regulation;
Transferase; Ubl conjugation; Wnt signaling pathway.
CHAIN 1 559 5'-AMP-activated protein kinase catalytic
subunit alpha-1.
/FTId=PRO_0000085590.
DOMAIN 27 279 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 33 41 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 302 381 AIS. {ECO:0000250}.
ACT_SITE 150 150 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 56 56 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 32 32 Phosphothreonine.
{ECO:0000250|UniProtKB:Q13131}.
MOD_RES 183 183 Phosphothreonine; by LKB1 and CaMKK2.
{ECO:0000269|PubMed:15980064,
ECO:0000269|PubMed:16054095,
ECO:0000269|PubMed:16308421}.
MOD_RES 355 355 Phosphothreonine.
{ECO:0000250|UniProtKB:Q13131}.
MOD_RES 356 356 Phosphoserine.
{ECO:0000250|UniProtKB:Q13131}.
MOD_RES 360 360 Phosphoserine; by ULK1. {ECO:0000250}.
MOD_RES 368 368 Phosphothreonine; by ULK1. {ECO:0000250}.
MOD_RES 382 382 Phosphothreonine.
{ECO:0000250|UniProtKB:Q13131}.
MOD_RES 397 397 Phosphoserine; by ULK1.
{ECO:0000250|UniProtKB:P54645}.
MOD_RES 467 467 Phosphoserine.
{ECO:0000250|UniProtKB:Q13131}.
MOD_RES 486 486 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 488 488 Phosphothreonine; by ULK1. {ECO:0000250}.
MOD_RES 490 490 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 496 496 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 508 508 Phosphoserine.
{ECO:0000250|UniProtKB:Q13131}.
MOD_RES 524 524 Phosphoserine.
{ECO:0000250|UniProtKB:Q13131}.
MOD_RES 527 527 Phosphoserine.
{ECO:0000250|UniProtKB:Q13131}.
MUTAGEN 168 168 D->A: Loss of kinase activity.
{ECO:0000269|PubMed:15878856,
ECO:0000269|PubMed:21258367}.
CONFLICT 11 12 Missing (in Ref. 2; AAW79567).
{ECO:0000305}.
STRAND 27 35 {ECO:0000244|PDB:5UFU}.
STRAND 37 46 {ECO:0000244|PDB:5UFU}.
TURN 47 49 {ECO:0000244|PDB:5UFU}.
STRAND 52 59 {ECO:0000244|PDB:5UFU}.
HELIX 60 65 {ECO:0000244|PDB:5UFU}.
HELIX 69 81 {ECO:0000244|PDB:5UFU}.
STRAND 90 95 {ECO:0000244|PDB:5UFU}.
STRAND 97 105 {ECO:0000244|PDB:5UFU}.
STRAND 108 111 {ECO:0000244|PDB:5UFU}.
HELIX 112 118 {ECO:0000244|PDB:5UFU}.
HELIX 124 142 {ECO:0000244|PDB:5UFU}.
TURN 143 145 {ECO:0000244|PDB:5UFU}.
TURN 153 155 {ECO:0000244|PDB:5UFU}.
STRAND 156 158 {ECO:0000244|PDB:5UFU}.
STRAND 164 166 {ECO:0000244|PDB:5UFU}.
TURN 188 190 {ECO:0000244|PDB:5UFU}.
HELIX 193 196 {ECO:0000244|PDB:5UFU}.
HELIX 204 220 {ECO:0000244|PDB:5UFU}.
HELIX 230 238 {ECO:0000244|PDB:5UFU}.
HELIX 250 259 {ECO:0000244|PDB:5UFU}.
TURN 264 266 {ECO:0000244|PDB:5UFU}.
HELIX 270 274 {ECO:0000244|PDB:5UFU}.
HELIX 277 280 {ECO:0000244|PDB:5UFU}.
STRAND 407 411 {ECO:0000244|PDB:5UFU}.
HELIX 417 430 {ECO:0000244|PDB:5UFU}.
STRAND 437 439 {ECO:0000244|PDB:5UFU}.
STRAND 442 448 {ECO:0000244|PDB:5UFU}.
TURN 450 452 {ECO:0000244|PDB:5UFU}.
STRAND 455 464 {ECO:0000244|PDB:5UFU}.
STRAND 466 468 {ECO:0000244|PDB:5UFU}.
STRAND 470 477 {ECO:0000244|PDB:5UFU}.
HELIX 542 554 {ECO:0000244|PDB:5UFU}.
SEQUENCE 559 AA; 63929 MW; 08632503663D395B CRC64;
MRRLSSWRKM ATAEKQKHDG RVKIGHYILG DTLGVGTFGK VKVGKHELTG HKVAVKILNR
QKIRSLDVVG KIRREIQNLK LFRHPHIIKL YQVISTPSDI FMVMEYVSGG ELFDYICKNG
RLDEKESRRL FQQILSGVDY CHRHMVVHRD LKPENVLLDA HMNAKIADFG LSNMMSDGEF
LRTSCGSPNY AAPEVISGRL YAGPEVDIWS SGVILYALLC GTLPFDDDHV PTLFKKICDG
IFYTPQYLNP SVISLLKHML QVDPMKRAAI KDIREHEWFK QDLPKYLFPE DPSYSSTMID
DEALKEVCEK FECSEEEVLS CLYNRNHQDP LAVAYHLIID NRRIMNEAKD FYLATSPPDS
FLDDHHLTRP HPERVPFLVA ETPRARHTLD ELNPQKSKHQ GVRKAKWHLG IRSQSRPNDI
MAEVCRAIKQ LDYEWKVVNP YYLRVRRKNP VTSTFSKMSL QLYQVDSRTY LLDFRSIDDE
ITEAKSGTAT PQRSGSISNY RSCQRSDSDA EAQGKPSDVS LTSSVTSLDS SPVDVAPRPG
SHTIEFFEMC ANLIKILAQ


Related products :

Catalog number Product name Quantity
30-953 PRKAA1 belongs to the ser_thr protein kinase family. It is the catalytic subunit of the 5'-prime-AMP-activated protein kinase (AMPK). AMPK is a cellular energy sensor conserved in all eukaryotic cells 0.05 mg
EIAAB24784 GCK family kinase MiNK,Map4k6,MAPK_ERK kinase kinase kinase 6,MEK kinase kinase 6,MEKKK 6,Mink,Mink1,Misshapen_NIK-related kinase,Misshapen-like kinase 1,Mitogen-activated protein kinase kinase kinase
EIAAB24783 GCK family kinase MiNK,Map4k6,MAPK_ERK kinase kinase kinase 6,MEK kinase kinase 6,MEKKK 6,Mink,Mink1,Misshapen_NIK-related kinase,Misshapen-like kinase 1,Mitogen-activated protein kinase kinase kinase
EIAAB25239 C-JUN N-terminal kinase kinase 1,Dual specificity mitogen-activated protein kinase kinase 4,JNK kinase 1,JNK-activating kinase 1,JNKK 1,Jnkk1,MAP kinase kinase 4,Map2k4,MAPK_ERK kinase 4,MAPKK 4,MEK 4
EIAAB25244 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,JNK kinase 2,JNK-activating kinase 2,JNKK 2,MAP kinase kinase 7,Map2k7,MAPK_ERK kinase 7,MAPKK 7,MEK 7,Mkk7,
EIAAB25245 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,JNK kinase 2,JNK-activating kinase 2,JNKK 2,MAP kinase kinase 7,Map2k7,MAPK_ERK kinase 7,MAPKK 7,MEK 7,Rat,R
EIAAB31333 Homo sapiens,Human,PAK1,PAK-1,PKN,PKN1,PRK1,PRKCL1,Protease-activated kinase 1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein kinase PKN-alpha,Protein-kinase C-related kinase 1,Serine_threo
EIAAB25246 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,Homo sapiens,Human,JNK kinase 2,JNK-activating kinase 2,JNKK 2,JNKK2,MAP kinase kinase 7,MAP2K7,MAPK_ERK kin
U0739h CLIA CDK5,CDKN5,Cell division protein kinase 5,Cyclin-dependent kinase 5,Homo sapiens,Human,Serine_threonine-protein kinase PSSALRE,Tau protein kinase II catalytic subunit,TPKII catalytic subunit 96T
E0739h ELISA CDK5,CDKN5,Cell division protein kinase 5,Cyclin-dependent kinase 5,Homo sapiens,Human,Serine_threonine-protein kinase PSSALRE,Tau protein kinase II catalytic subunit,TPKII catalytic subunit 96T
E0739r ELISA Cdk5,Cdkn5,Cell division protein kinase 5,Cyclin-dependent kinase 5,Rat,Rattus norvegicus,Serine_threonine-protein kinase PSSALRE,Tau protein kinase II catalytic subunit,TPKII catalytic subunit 96T
U0739r CLIA Cdk5,Cdkn5,Cell division protein kinase 5,Cyclin-dependent kinase 5,Rat,Rattus norvegicus,Serine_threonine-protein kinase PSSALRE,Tau protein kinase II catalytic subunit,TPKII catalytic subunit 96T
EIAAB25240 c-Jun N-terminal kinase kinase 1,Dual specificity mitogen-activated protein kinase kinase 4,Homo sapiens,Human,JNK-activating kinase 1,JNKK,JNKK1,MAP kinase kinase 4,MAP2K4,MAPK_ERK kinase 4,MAPKK 4,M
EIAAB24970 Leucine zipper- and sterile alpha motif kinase ZAK,Mitogen-activated protein kinase kinase kinase MLT,Mixed lineage kinase-related kinase,MLK-like mitogen-activated protein triple kinase,MLK-related k
E1358m ELISA kit Apoptosis signal-regulating kinase 1,Ask1,ASK-1,Map3k5,MAPK_ERK kinase kinase 5,MEK kinase 5,MEKK 5,Mekk5,Mitogen-activated protein kinase kinase kinase 5,Mouse,Mus musculus 96T
U1358m CLIA Apoptosis signal-regulating kinase 1,Ask1,ASK-1,Map3k5,MAPK_ERK kinase kinase 5,MEK kinase 5,MEKK 5,Mekk5,Mitogen-activated protein kinase kinase kinase 5,Mouse,Mus musculus 96T
E1358m ELISA Apoptosis signal-regulating kinase 1,Ask1,ASK-1,Map3k5,MAPK_ERK kinase kinase 5,MEK kinase 5,MEKK 5,Mekk5,Mitogen-activated protein kinase kinase kinase 5,Mouse,Mus musculus 96T
E0739r ELISA kit Cdk5,Cdkn5,Cell division protein kinase 5,Cyclin-dependent kinase 5,Rat,Rattus norvegicus,Serine_threonine-protein kinase PSSALRE,Tau protein kinase II catalytic subunit,TPKII catalytic sub 96T
U0739m CLIA Cdk5,Cdkn5,Cell division protein kinase 5,CR6 protein kinase,CRK6,Crk6,Cyclin-dependent kinase 5,Mouse,Mus musculus,Serine_threonine-protein kinase PSSALRE,Tau protein kinase II catalytic subunit 96T
E0739h ELISA kit CDK5,CDKN5,Cell division protein kinase 5,Cyclin-dependent kinase 5,Homo sapiens,Human,Serine_threonine-protein kinase PSSALRE,Tau protein kinase II catalytic subunit,TPKII catalytic subuni 96T
E1358h ELISA kit Apoptosis signal-regulating kinase 1,ASK1,ASK-1,Homo sapiens,Human,MAP3K5,MAPK_ERK kinase kinase 5,MAPKKK5,MEK kinase 5,MEKK 5,MEKK5,Mitogen-activated protein kinase kinase kinase 5 96T
U1358h CLIA Apoptosis signal-regulating kinase 1,ASK1,ASK-1,Homo sapiens,Human,MAP3K5,MAPK_ERK kinase kinase 5,MAPKKK5,MEK kinase 5,MEKK 5,MEKK5,Mitogen-activated protein kinase kinase kinase 5 96T
E1358h ELISA Apoptosis signal-regulating kinase 1,ASK1,ASK-1,Homo sapiens,Human,MAP3K5,MAPK_ERK kinase kinase 5,MAPKKK5,MEK kinase 5,MEKK 5,MEKK5,Mitogen-activated protein kinase kinase kinase 5 96T
18-662-20092 Dual specificity mitogen-activated protein kinase kinase 1 - EC 2.7.12.2; MAP kinase kinase 1; MAPKK 1; ERK activator kinase 1; MAPK_ERK kinase 1; MEK1 Polyclonal 0.1 ml
18-662-20091 Dual specificity mitogen-activated protein kinase kinase 1 - EC 2.7.12.2; MAP kinase kinase 1; MAPKK 1; ERK activator kinase 1; MAPK_ERK kinase 1; MEK1 Polyclonal 0.1 ml


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur