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[1]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
The mouse genome sequencing consortium;
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
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[2]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-552.
STRAIN=C57BL/6J;
TISSUE=Brain cortex, and Medulla oblongata;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[3]
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FUNCTION, AND KNOCKOUT.
PubMed=15331533 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[4]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-500, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1073/pnas.0609836104; PubMed=17242355 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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- FUNCTION: Responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase. It also regulates cholesterol synthesis via phosphorylation and inactivation of hormone-sensitive lipase and hydroxymethylglutaryl-CoA reductase. Appears to act as a metabolic stress-sensing protein kinase switching off biosynthetic pathways when cellular ATP levels are depleted and when 5'-AMP rises in response to fuel limitation and/or hypoxia. This is a catalytic subunit.
- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
- COFACTOR: Magnesium (By similarity).
- ENZYME REGULATION: Binding of AMP results in allosteric activation, inducing phosphorylation on Thr-172 by STK11 in complex with STE20-related adapter-alpha (STRAD alpha) pseudo kinase and CAB39. Also activated by phosphorylation by CAMKK2 triggered by a rise in intracellular calcium ions, without detectable changes in the AMP/ATP ratio (By similarity).
- SUBUNIT: Heterotrimer of a catalytic subunit, a beta and a gamma non-catalytic subunits (By similarity).
- MISCELLANEOUS: Mice lacking Prkaa2 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.
- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily.
- SIMILARITY: Contains 1 protein kinase domain.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 552 AA [This is the length of the unprocessed precursor] |
Molecular weight: 62006 Da [This is the MW of the unprocessed precursor] |
CRC64: 593911EAB3BBFE3F [This is a checksum on the sequence] |
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10 20 30 40 50 60
MAEKQKHDGR VKIGHYVLGD TLGVGTFGKV KIGEHQLTGH KVAVKILNRQ KIRSLDVVGK
70 80 90 100 110 120
IKREIQNLKL FRHPHIIKLY QVISTPTDFF MVMEYVSGGE LFDYICKHGR VEEVEARRLF
130 140 150 160 170 180
QQILSAVDYC HRHMVVHRDL KPENVLLDAQ MNAKIADFGL SNMMSDGEFL RTSCGSPNYA
190 200 210 220 230 240
APEVISGRLY AGPEVDIWSC GVILYALLCG TLPFDDEHVP TLFKKIRGGV FYIPDYLNRS
250 260 270 280 290 300
VATLLMHMLQ VDPLKRATIK DIREHEWFKQ DLPSYLFPED PSYDANVIVD EAVKEVCEKF
310 320 330 340 350 360
ECTESEVMNS LYSGDPQDQL AVAYHLIIDN RRIMNQASEF YLASSPPSGS FMDDSAMHIP
370 380 390 400 410 420
PGLKPHPERM PPLIADSPKA RCPLDALNTT KPKSLAVKKA KWHLGIRSQS KACDIMAEVY
430 440 450 460 470 480
RAMKQLGFEW KVVNAYHLRV RRKNPVTGNY VKMSLQLYLV DSRSYLLDFK SIDDEVVEQR
490 500 510 520 530 540
SGSSTPQRSC SAAGLHRARS SFDSSTAENH SLSGSLTGSL TGSTLSSASP RLGSHTMDFF
550
EMCASLITAL AR
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Q8BRK8 in FASTA format |
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ExPASy Home page
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