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-2 (AMPK subunit alpha-2) (EC 2.7.11.1) (Acetyl-CoA carboxylase kinase) (ACACA kinase) (EC 2.7.11.27) (Hydroxymethylglutaryl-CoA reductase kinase) (HMGCR kinase) (EC 2.7.11.31)

 AAPK2_MOUSE             Reviewed;         552 AA.
Q8BRK8; B1ASQ8; Q3UYM4;
28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
28-FEB-2018, entry version 139.
RecName: Full=5'-AMP-activated protein kinase catalytic subunit alpha-2;
Short=AMPK subunit alpha-2;
EC=2.7.11.1 {ECO:0000250|UniProtKB:Q09137};
AltName: Full=Acetyl-CoA carboxylase kinase;
Short=ACACA kinase;
EC=2.7.11.27 {ECO:0000250|UniProtKB:Q09137};
AltName: Full=Hydroxymethylglutaryl-CoA reductase kinase;
Short=HMGCR kinase;
EC=2.7.11.31 {ECO:0000250|UniProtKB:Q09137};
Name=Prkaa2 {ECO:0000312|MGI:MGI:1336173};
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 [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3] {ECO:0000305, ECO:0000312|EMBL:BAC31746.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-552.
STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC31746.1};
TISSUE=Brain cortex {ECO:0000312|EMBL:BAC31746.1}, and
Medulla oblongata {ECO:0000312|EMBL:BAE22188.1};
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15331533; DOI=10.2337/diabetes.53.9.2242;
Villena J.A., Viollet B., Andreelli F., Kahn A., Vaulont S., Sul H.S.;
"Induced adiposity and adipocyte hypertrophy in mice lacking the AMP-
activated protein kinase-alpha2 subunit.";
Diabetes 53:2242-2249(2004).
[5]
FUNCTION IN PHOSPHORYLATION OF GYS1.
PubMed=15561936; DOI=10.2337/diabetes.53.12.3074;
Jorgensen S.B., Nielsen J.N., Birk J.B., Olsen G.S., Viollet B.,
Andreelli F., Schjerling P., Vaulont S., Hardie D.G., Hansen B.F.,
Richter E.A., Wojtaszewski J.F.;
"The alpha2-5'AMP-activated protein kinase is a site 2 glycogen
synthase kinase in skeletal muscle and is responsive to glucose
loading.";
Diabetes 53:3074-3081(2004).
[6]
PHOSPHORYLATION AT THR-172, AND ENZYME REGULATION.
PubMed=15980064; DOI=10.1074/jbc.M503824200;
Hurley R.L., Anderson K.A., Franzone J.M., Kemp B.E., Means A.R.,
Witters L.A.;
"The Ca2+/calmodulin-dependent protein kinase kinases are AMP-
activated protein kinase kinases.";
J. Biol. Chem. 280:29060-29066(2005).
[7]
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).
[8]
FUNCTION IN PHOSPHORYLATION OF CRTC2, AND PHOSPHORYLATION AT THR-172.
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).
[9]
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).
[10]
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).
[11]
FUNCTION IN PHOSPHORYLATION OF PPARGC1A.
PubMed=17609368; DOI=10.1073/pnas.0705070104;
Jager S., Handschin C., St-Pierre J., Spiegelman B.M.;
"AMP-activated protein kinase (AMPK) action in skeletal muscle via
direct phosphorylation of PGC-1alpha.";
Proc. Natl. Acad. Sci. U.S.A. 104:12017-12022(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, AND 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).
[13]
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).
[14]
FUNCTION IN PHOSPHORYLATION OF CRY1.
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-377, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, and
Pancreas;
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, AND MUTAGENESIS OF ASP-157.
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]
FUNCTION IN PHOSPHORYLATION OF HDAC5, AND MUTAGENESIS OF LYS-45.
PubMed=21454484; DOI=10.1074/jbc.M110.199372;
Zhao J.X., Yue W.F., Zhu M.J., Du M.;
"AMP-activated protein kinase regulates beta-catenin transcription via
histone deacetylase 5.";
J. Biol. Chem. 286:16426-16434(2011).
[19]
PHOSPHORYLATION BY ULK1.
PubMed=21460634; DOI=10.4161/auto.7.7.15451;
Loffler A.S., Alers S., Dieterle A.M., Keppeler H., Franz-Wachtel M.,
Kundu M., Campbell D.G., Wesselborg S., Alessi D.R., Stork B.;
"Ulk1-mediated phosphorylation of AMPK constitutes a negative
regulatory feedback loop.";
Autophagy 7:696-706(2011).
[20]
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).
[21]
FUNCTION IN PHOSPHORYLATION OF ULK1.
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).
[22]
FUNCTION IN PHOSPHORYLATION OF ULK1.
PubMed=21205641; DOI=10.1126/science.1196371;
Egan D.F., Shackelford D.B., Mihaylova M.M., Gelino S., Kohnz R.A.,
Mair W., Vasquez D.S., Joshi A., Gwinn D.M., Taylor R., Asara J.M.,
Fitzpatrick J., Dillin A., Viollet B., Kundu M., Hansen M., Shaw R.J.;
"Phosphorylation of ULK1 (hATG1) by AMP-activated protein kinase
connects energy sensing to mitophagy.";
Science 331:456-461(2011).
[23]
ENZYME REGULATION BY SALICYLATE.
PubMed=22517326; DOI=10.1126/science.1215327;
Hawley S.A., Fullerton M.D., Ross F.A., Schertzer J.D., Chevtzoff C.,
Walker K.J., Peggie M.W., Zibrova D., Green K.A., Mustard K.J.,
Kemp B.E., Sakamoto K., Steinberg G.R., Hardie D.G.;
"The ancient drug salicylate directly activates AMP-activated protein
kinase.";
Science 336:918-922(2012).
[24]
FUNCTION, PHOSPHORYLATION AT THR-172, AND ENZYME REGULATION.
PubMed=23332761; DOI=10.1016/j.cell.2012.12.016;
Kim J., Kim Y.C., Fang C., Russell R.C., Kim J.H., Fan W., Liu R.,
Zhong Q., Guan K.L.;
"Differential regulation of distinct Vps34 complexes by AMPK in
nutrient stress and autophagy.";
Cell 152:290-303(2013).
-!- FUNCTION: Catalytic subunit of AMP-activated protein kinase
(AMPK), an energy sensor protein kinase that plays a key role in
regulating cellular energy metabolism. In response to reduction of
intracellular ATP levels, AMPK activates energy-producing pathways
and inhibits energy-consuming processes: inhibits protein,
carbohydrate and lipid biosynthesis, as well as cell growth and
proliferation. AMPK acts via direct phosphorylation of metabolic
enzymes, and by longer-term effects via phosphorylation of
transcription regulators. Also acts as a regulator of cellular
polarity by remodeling the actin cytoskeleton; probably by
indirectly activating myosin. Regulates lipid synthesis by
phosphorylating and inactivating lipid metabolic enzymes such as
ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and
cholesterol synthesis by phosphorylating acetyl-CoA carboxylase
(ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes,
respectively. Regulates insulin-signaling and glycolysis by
phosphorylating IRS1, PFKFB2 and PFKFB3. Involved in insulin
receptor/INSR internalization (By similarity). AMPK stimulates
glucose uptake in muscle by increasing the translocation of the
glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly
by mediating phosphorylation of TBC1D4/AS160. Regulates
transcription and chromatin structure by phosphorylating
transcription regulators involved in energy metabolism such as
CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP,
EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A. Acts as a key
regulator of glucose homeostasis in liver by phosphorylating
CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the
cytoplasm. In response to stress, phosphorylates 'Ser-36' of
histone H2B (H2BS36ph), leading to promote transcription. Acts as
a key regulator of cell growth and proliferation by
phosphorylating TSC2, RPTOR and ATG1/ULK1: in response to nutrient
limitation, negatively regulates the mTORC1 complex by
phosphorylating RPTOR component of the mTORC1 complex and by
phosphorylating and activating TSC2. In response to nutrient
limitation, promotes autophagy by phosphorylating and activating
ATG1/ULK1. AMPK also acts as a regulator of circadian rhythm by
mediating phosphorylation of CRY1, leading to destabilize it. May
regulate the Wnt signaling pathway by phosphorylating CTNNB1,
leading to stabilize it. Also phosphorylates CFTR, EEF2K, KLC1,
NOS3 and SLC12A1. Plays an important role in the differential
regulation of pro-autophagy (composed of PIK3C3, BECN1, PIK3R4 and
UVRAG or ATG14) and non-autophagy (composed of PIK3C3, BECN1 and
PIK3R4) complexes, in response to glucose starvation. Can inhibit
the non-autophagy complex by phosphorylating PIK3C3 and can
activate the pro-autophagy complex by phosphorylating BECN1
(PubMed:23332761). {ECO:0000250|UniProtKB:P54646,
ECO:0000269|PubMed:15331533, ECO:0000269|PubMed:15561936,
ECO:0000269|PubMed:16148943, ECO:0000269|PubMed:16308421,
ECO:0000269|PubMed:16804075, ECO:0000269|PubMed:16804077,
ECO:0000269|PubMed:17609368, 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:21454484,
ECO:0000269|PubMed:21459323, ECO:0000269|PubMed:23332761}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000250|UniProtKB:Q09137}.
-!- CATALYTIC ACTIVITY: ATP + [acetyl-CoA carboxylase] = ADP +
[acetyl-CoA carboxylase] phosphate.
{ECO:0000250|UniProtKB:Q09137}.
-!- CATALYTIC ACTIVITY: ATP + [hydroxymethylglutaryl-CoA reductase
(NADPH)] = ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)]
phosphate. {ECO:0000250|UniProtKB:Q09137}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:Q13131};
-!- ENZYME REGULATION: Activated by phosphorylation on Thr-172.
Binding of AMP to non-catalytic gamma subunit (PRKAG1, PRKAG2 or
PRKAG3) results in allosteric activation, inducing phosphorylation
on Thr-172. AMP-binding to gamma subunit also sustains activity by
preventing dephosphorylation of Thr-172. ADP also stimulates Thr-
172 phosphorylation, without stimulating already phosphorylated
AMPK. ATP promotes dephosphorylation of Thr-172, rendering the
enzyme inactive. Under physiological conditions AMPK mainly exists
in its inactive form in complex with ATP, which is much more
abundant than AMP. Selectively inhibited by compound C (6-[4-(2-
Piperidin-1-yl-ethoxy)-phenyl)]-3-pyridin-4-yl-pyyrazolo[1,5-a]
pyrimidine. Activated by resveratrol, a natural polyphenol present
in red wine, and S17834, a synthetic polyphenol.
Salicylate/aspirin directly activates kinase activity, primarily
by inhibiting Thr-172 dephosphorylation.
{ECO:0000269|PubMed:15980064, ECO:0000269|PubMed:21459323,
ECO:0000269|PubMed:22517326, ECO:0000269|PubMed:23332761}.
-!- 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 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus. 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: Ubiquitinated. {ECO:0000250}.
-!- PTM: Phosphorylated at Thr-172 by STK11/LKB1 in complex with
STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Also
phosphorylated at Thr-172 by CAMKK2; triggered by a rise in
intracellular calcium ions, without detectable changes in the
AMP/ATP ratio. CAMKK1 can also phosphorylate Thr-172, but at much
lower level. Dephosphorylated by protein phosphatase 2A and 2C
(PP2A and PP2C). Phosphorylated by ULK1; leading to negatively
regulate AMPK activity and suggesting the existence of a
regulatory feedback loop between ULK1 and AMPK. Dephosphorylated
by PPM1A and PPM1B at Thr-172 (mediated by STK11/LKB1) (By
similarity). {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice develop obesity when animals are fed a
high-fat diet, as a result of an enhanced lipid accumulation in
pre-existing adipocytes but not in other tissues.
{ECO:0000269|PubMed:15331533}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. SNF1 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AL627307; CAM18832.1; -; Genomic_DNA.
EMBL; AL929466; CAM18832.1; JOINED; Genomic_DNA.
EMBL; AL929466; CAM24127.1; -; Genomic_DNA.
EMBL; AL627307; CAM24127.1; JOINED; Genomic_DNA.
EMBL; BC138565; AAI38566.1; -; mRNA.
EMBL; BC138566; AAI38567.1; -; mRNA.
EMBL; AK044030; BAC31746.1; -; mRNA.
EMBL; AK134573; BAE22188.1; -; mRNA.
CCDS; CCDS18416.1; -.
RefSeq; NP_835279.2; NM_178143.2.
UniGene; Mm.48638; -.
ProteinModelPortal; Q8BRK8; -.
SMR; Q8BRK8; -.
BioGrid; 223817; 2.
IntAct; Q8BRK8; 2.
STRING; 10090.ENSMUSP00000030243; -.
ChEMBL; CHEMBL1255154; -.
iPTMnet; Q8BRK8; -.
PhosphoSitePlus; Q8BRK8; -.
MaxQB; Q8BRK8; -.
PaxDb; Q8BRK8; -.
PeptideAtlas; Q8BRK8; -.
PRIDE; Q8BRK8; -.
Ensembl; ENSMUST00000030243; ENSMUSP00000030243; ENSMUSG00000028518.
GeneID; 108079; -.
KEGG; mmu:108079; -.
UCSC; uc008tyd.2; mouse.
CTD; 5563; -.
MGI; MGI:1336173; Prkaa2.
eggNOG; KOG0586; Eukaryota.
eggNOG; ENOG410XNQ0; LUCA.
GeneTree; ENSGT00900000140868; -.
HOGENOM; HOG000233016; -.
HOVERGEN; HBG050432; -.
InParanoid; Q8BRK8; -.
KO; K07198; -.
OMA; RWHFGIR; -.
OrthoDB; EOG091G03TG; -.
TreeFam; TF314032; -.
Reactome; R-MMU-1632852; Macroautophagy.
Reactome; R-MMU-163680; AMPK inhibits chREBP transcriptional activation activity.
Reactome; R-MMU-200425; Import of palmitoyl-CoA into the mitochondrial matrix.
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.
ChiTaRS; Prkaa2; mouse.
PRO; PR:Q8BRK8; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000028518; -.
Genevisible; Q8BRK8; MM.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0016607; C:nuclear speck; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0031588; C:nucleotide-activated protein kinase complex; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IDA:MGI.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IMP:UniProtKB.
GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; ISO:MGI.
GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO; GO:0035690; P:cellular response to drug; IMP:MGI.
GO; GO:0042149; P:cellular response to glucose starvation; IDA:UniProtKB.
GO; GO:0031669; P:cellular response to nutrient levels; IDA:UniProtKB.
GO; GO:0071380; P:cellular response to prostaglandin E stimulus; IGI:MGI.
GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0055089; P:fatty acid homeostasis; ISS:UniProtKB.
GO; GO:0042593; P:glucose homeostasis; IMP:UniProtKB.
GO; GO:0008610; P:lipid biosynthetic process; IDA:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0032007; P:negative regulation of TOR signaling; IMP:UniProtKB.
GO; GO:0010508; P:positive regulation of autophagy; IMP:UniProtKB.
GO; GO:0045821; P:positive regulation of glycolytic process; ISS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
GO; GO:2000505; P:regulation of energy homeostasis; ISS:UniProtKB.
GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
GO; GO:0016241; P:regulation of macroautophagy; IDA:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0014850; P:response to muscle activity; IMP:MGI.
GO; GO:0006950; P:response to stress; 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_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF16579; AdenylateSensor; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF103243; SSF103243; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
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 1 552 5'-AMP-activated protein kinase catalytic
subunit alpha-2.
/FTId=PRO_0000262957.
DOMAIN 16 268 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 22 30 ATP. {ECO:0000250|UniProtKB:P28523,
ECO:0000255|PROSITE-ProRule:PRU00159}.
REGION 291 376 AIS. {ECO:0000250}.
ACT_SITE 139 139 Proton acceptor.
{ECO:0000250|UniProtKB:P28523,
ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10027}.
BINDING 45 45 ATP.
MOD_RES 172 172 Phosphothreonine; by LKB1 and CaMKK2.
{ECO:0000269|PubMed:15980064,
ECO:0000269|PubMed:16308421,
ECO:0000269|PubMed:23332761}.
MOD_RES 258 258 Phosphothreonine.
{ECO:0000250|UniProtKB:Q09137}.
MOD_RES 377 377 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 491 491 Phosphoserine.
{ECO:0000250|UniProtKB:Q09137}.
MUTAGEN 45 45 K->A: Loss of kinase activity.
{ECO:0000269|PubMed:21454484}.
MUTAGEN 157 157 D->A: Loss of kinase activity.
{ECO:0000269|PubMed:20647423}.
CONFLICT 15 15 H -> D (in Ref. 3; BAE22188).
{ECO:0000305}.
CONFLICT 289 289 D -> V (in Ref. 3; BAC31746).
{ECO:0000305}.
CONFLICT 380 380 A -> E (in Ref. 3; BAE22188).
{ECO:0000305}.
CONFLICT 502 502 F -> Y (in Ref. 3; BAE22188).
{ECO:0000305}.
CONFLICT 506 506 T -> K (in Ref. 3; BAE22188).
{ECO:0000305}.
SEQUENCE 552 AA; 62022 MW; 020B11E2685BFE39 CRC64;
MAEKQKHDGR VKIGHYVLGD TLGVGTFGKV KIGEHQLTGH KVAVKILNRQ KIRSLDVVGK
IKREIQNLKL FRHPHIIKLY QVISTPTDFF MVMEYVSGGE LFDYICKHGR VEEVEARRLF
QQILSAVDYC HRHMVVHRDL KPENVLLDAQ MNAKIADFGL SNMMSDGEFL RTSCGSPNYA
APEVISGRLY AGPEVDIWSC GVILYALLCG TLPFDDEHVP TLFKKIRGGV FYIPDYLNRS
VATLLMHMLQ VDPLKRATIK DIREHEWFKQ DLPSYLFPED PSYDANVIDD EAVKEVCEKF
ECTESEVMNS LYSGDPQDQL AVAYHLIIDN RRIMNQASEF YLASSPPSGS FMDDSAMHIP
PGLKPHPERM PPLIADSPKA RCPLDALNTT KPKSLAVKKA KWHLGIRSQS KACDIMAEVY
RAMKQLGFEW KVVNAYHLRV RRKNPVTGNY VKMSLQLYLV DSRSYLLDFK SIDDEVVEQR
SGSSTPQRSC SAAGLHRARS SFDSSTAENH SLSGSLTGSL TGSTLSSASP RLGSHTMDFF
EMCASLITAL AR


Related products :

Catalog number Product name Quantity
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
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,
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
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
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
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
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
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
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
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
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
EIAAB29519 Homo sapiens,Human,Phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunit alpha,Phosphoinositide 3-kinase-C2-alpha,PI3K-C2-alpha,PIK3C2A,PtdIns-3-kinase C2 subunit alpha
EIAAB29518 Cpk,Cpk-m,Mouse,Mus musculus,p170,Phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunit alpha,Phosphoinositide 3-kinase-C2-alpha,PI3K-C2-alpha,Pik3c2a,PtdIns-3-kinase C2 subunit alpha
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
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
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
18-783-75638 RABBIT ANTI CaMKII - CALCIUM_CALMODULIN-DEPENDENT KINASE II; EC 2.7.11.17; CaM-kinase II alpha chain; CaM kinase II subunit alpha; CaMK-II subunit alpha Polyclonal 0.05 mg
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
18-783-75678 RABBIT ANTI Cdk5 (C-TERMINAL) - EC 2.7.11.22; Cyclin-dependent kinase 5; Tau protein kinase II catalytic subunit; TPKII catalytic subunit; Serine_threonine-protein kinase PSSALRE Polyclonal 0.05 ml
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


 

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