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[1]
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NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6N;
TISSUE=Muscle;
Xie X.,
Chen Y.;
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
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[2]
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ENZYME REGULATION, AND PHOSPHORYLATION AT THR-172.
DOI=10.1016/j.cmet.2005.05.009; PubMed=16054095 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[3]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-497, 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 (By similarity).
- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
- COFACTOR: Magnesium.
- 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.
- SUBUNIT: Heterotrimer of an alpha catalytic subunit, a beta and a gamma non-catalytic subunits. Interacts with FNIP1 and FNIP2 (By similarity).
- 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: 548 AA [This is the length of the unprocessed precursor] |
Molecular weight: 62556 Da [This is the MW of the unprocessed precursor] |
CRC64: FCC0D4C20FFF44D1 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MAEKQKHDGR VKIGHYILGD TLGVGTFGKV KVGKHELTGH KVAVKILNRQ KIRSLDVVGK
70 80 90 100 110 120
IRREIQNLKL FRHPHIIKLY QVISTPSDIF MVMEYVSGGE LFDYICKNGR LDEKESRRLF
130 140 150 160 170 180
QQILSGVDYC HRHMVVHRDL KPENVLLDAH MNAKIADFGL SNMMSDGEFL RTSCGSPNYA
190 200 210 220 230 240
APEVISGRLY AGPEVDIWSS GVILYALLCG TLPFDDDHVP TLFKKICDGI FYTPQYLNPS
250 260 270 280 290 300
VISLLKHMLQ VDPMKRAAIK DIREHEWFKQ DLPKYLFPED PSYSSTMIDD EALKEVCEKF
310 320 330 340 350 360
ECSEEEVLSC LYNRNHQDPL AVAYHLIIDN RRIMNEAKDF YLATSPPDSF LDDHHLTRPH
370 380 390 400 410 420
PERVPFLVAE TPRARHTLDE LNPQKSKHQG VRKAKWHLGI RSQSRPNDIM AEVCRAIKQL
430 440 450 460 470 480
DYEWKVVNPY YLRVRRKNPV TSTFSKMSLQ LYQVDSRTYL LDFRSIDDEI TEAKSGTATP
490 500 510 520 530 540
QRSGSISNYR SCQRSDSDAE AQGKPSDVSL TSSVTSLDSS PVDVAPRPGS HTIEFFEMCA
NLIKILAQ
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Q5EG47 in FASTA format |
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