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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_HUMAN             Reviewed;         559 AA.
Q13131; A8MTQ6; B2R7E1; O00286; Q5D0E1; Q86VS1; Q9UNQ4;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
28-JUL-2009, sequence version 4.
22-NOV-2017, entry version 193.
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; Synonyms=AMPK1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
LEU-10.
TISSUE=Brain, and Testis;
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]
NUCLEOTIDE SEQUENCE [MRNA] OF 3-559 (ISOFORM 1).
TISSUE=Mammary gland;
Yano K.;
"Nucleotide sequence of cDNA for human AMP-activated protein kinase
alpha-1.";
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-559 (ISOFORM 1).
TISSUE=Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-559 (ISOFORM 1).
TISSUE=Umbilical cord blood;
PubMed=11042152; DOI=10.1101/gr.140200;
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
"Cloning and functional analysis of cDNAs with open reading frames for
300 previously undefined genes expressed in CD34+ hematopoietic
stem/progenitor cells.";
Genome Res. 10:1546-1560(2000).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 36-209 (ISOFORM 1).
TISSUE=Intestine;
Taboada E.N., Hickey D.A.;
Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 303-559 (ISOFORMS 1/2).
TISSUE=Liver;
PubMed=8557660; DOI=10.1074/jbc.271.2.611;
Stapleton D., Mitchelhill K.I., Gao G., Widmer J., Michell B.J.,
Teh T., House C.M., Fernandez C.S., Cox T., Witters L.A., Kemp B.E.;
"Mammalian AMP-activated protein kinase subfamily.";
J. Biol. Chem. 271:611-614(1996).
[8]
DOMAIN AIS.
PubMed=9857077; DOI=10.1074/jbc.273.52.35347;
Crute B.E., Seefeld K., Gamble J., Kemp B.E., Witters L.A.;
"Functional domains of the alpha1 catalytic subunit of the AMP-
activated protein kinase.";
J. Biol. Chem. 273:35347-35354(1998).
[9]
FUNCTION.
PubMed=11554766; DOI=10.1006/bbrc.2001.5627;
Imamura K., Ogura T., Kishimoto A., Kaminishi M., Esumi H.;
"Cell cycle regulation via p53 phosphorylation by a 5'-AMP activated
protein kinase activator, 5-aminoimidazole-4-carboxamide-1-beta-D-
ribofuranoside, in a human hepatocellular carcinoma cell line.";
Biochem. Biophys. Res. Commun. 287:562-567(2001).
[10]
FUNCTION IN PHOSPHORYLATION OF EP300.
PubMed=11518699; DOI=10.1074/jbc.C100316200;
Yang W., Hong Y.H., Shen X.Q., Frankowski C., Camp H.S., Leff T.;
"Regulation of transcription by AMP-activated protein kinase:
phosphorylation of p300 blocks its interaction with nuclear
receptors.";
J. Biol. Chem. 276:38341-38344(2001).
[11]
ENZYME REGULATION.
PubMed=11602624; DOI=10.1172/JCI13505;
Zhou G., Myers R., Li Y., Chen Y., Shen X., Fenyk-Melody J., Wu M.,
Ventre J., Doebber T., Fujii N., Musi N., Hirshman M.F.,
Goodyear L.J., Moller D.E.;
"Role of AMP-activated protein kinase in mechanism of metformin
action.";
J. Clin. Invest. 108:1167-1174(2001).
[12]
FUNCTION IN PHOSPHORYLATION OF CFTR.
PubMed=12519745; DOI=10.1152/ajpcell.00227.2002;
Hallows K.R., Kobinger G.P., Wilson J.M., Witters L.A., Foskett J.K.;
"Physiological modulation of CFTR activity by AMP-activated protein
kinase in polarized T84 cells.";
Am. J. Physiol. 284:C1297-C1308(2003).
[13]
FUNCTION IN PHOSPHORYLATION OF TSC2.
PubMed=14651849; DOI=10.1016/S0092-8674(03)00929-2;
Inoki K., Zhu T., Guan K.L.;
"TSC2 mediates cellular energy response to control cell growth and
survival.";
Cell 115:577-590(2003).
[14]
PHOSPHORYLATION AT THR-183, AND ENZYME REGULATION.
PubMed=14976552; DOI=10.1038/sj.emboj.7600110;
Lizcano J.M., Goeransson O., Toth R., Deak M., Morrice N.A.,
Boudeau J., Hawley S.A., Udd L., Maekelae T.P., Hardie D.G.,
Alessi D.R.;
"LKB1 is a master kinase that activates 13 kinases of the AMPK
subfamily, including MARK/PAR-1.";
EMBO J. 23:833-843(2004).
[15]
PHOSPHORYLATION AT THR-183, AND ENZYME REGULATION.
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).
[16]
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).
[17]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15866171; DOI=10.1016/j.molcel.2005.03.027;
Jones R.G., Plas D.R., Kubek S., Buzzai M., Mu J., Xu Y.,
Birnbaum M.J., Thompson C.B.;
"AMP-activated protein kinase induces a p53-dependent metabolic
checkpoint.";
Mol. Cell 18:283-293(2005).
[18]
INTERACTION WITH FNIP1.
PubMed=17028174; DOI=10.1073/pnas.0603781103;
Baba M., Hong S.-B., Sharma N., Warren M.B., Nickerson M.L.,
Iwamatsu A., Esposito D., Gillette W.K., Hopkins R.F. III,
Hartley J.L., Furihata M., Oishi S., Zhen W., Burke T.R. Jr.,
Linehan W.M., Schmidt L.S., Zbar B.;
"Folliculin encoded by the BHD gene interacts with a binding protein,
FNIP1, and AMPK, and is involved in AMPK and mTOR signaling.";
Proc. Natl. Acad. Sci. U.S.A. 103:15552-15557(2006).
[19]
DOMAIN AIS, AND MUTAGENESIS OF VAL-307.
PubMed=17088252; DOI=10.1074/jbc.M605790200;
Pang T., Xiong B., Li J.Y., Qiu B.Y., Jin G.Z., Shen J.K., Li J.;
"Conserved alpha-helix acts as autoinhibitory sequence in AMP-
activated protein kinase alpha subunits.";
J. Biol. Chem. 282:495-506(2007).
[20]
FUNCTION IN PHOSPHORYLATION OF FOXO3.
PubMed=17711846; DOI=10.1074/jbc.M705325200;
Greer E.L., Oskoui P.R., Banko M.R., Maniar J.M., Gygi M.P.,
Gygi S.P., Brunet A.;
"The energy sensor AMP-activated protein kinase directly regulates the
mammalian FOXO3 transcription factor.";
J. Biol. Chem. 282:30107-30119(2007).
[21]
FUNCTION IN CELL POLARITY.
PubMed=17486097; DOI=10.1038/nature05828;
Lee J.H., Koh H., Kim M., Kim Y., Lee S.Y., Karess R.E., Lee S.H.,
Shong M., Kim J.M., Kim J., Chung J.;
"Energy-dependent regulation of cell structure by AMP-activated
protein kinase.";
Nature 447:1017-1020(2007).
[22]
FUNCTION IN PHOSPHORYLATION OF HDAC5.
PubMed=18184930; DOI=10.2337/db07-0843;
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).
[23]
INTERACTION WITH FNIP2.
PubMed=18403135; DOI=10.1016/j.gene.2008.02.022;
Hasumi H., Baba M., Hong S.-B., Hasumi Y., Huang Y., Yao M.,
Valera V.A., Linehan W.M., Schmidt L.S.;
"Identification and characterization of a novel folliculin-interacting
protein FNIP2.";
Gene 415:60-67(2008).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-382, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[26]
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).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[28]
INTERACTION WITH FNIP2.
PubMed=18663353; DOI=10.1038/onc.2008.261;
Takagi Y., Kobayashi T., Shiono M., Wang L., Piao X., Sun G.,
Zhang D., Abe M., Hagiwara Y., Takahashi K., Hino O.;
"Interaction of folliculin (Birt-Hogg-Dube gene product) with a novel
Fnip1-like (FnipL/Fnip2) protein.";
Oncogene 27:5339-5347(2008).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356; SER-486; THR-490
AND SER-496, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-32 AND SER-467, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-382, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[32]
FUNCTION IN PHOSPHORYLATION OF KLC1.
PubMed=20074060; DOI=10.1042/BST0380205;
McDonald A., Fogarty S., Leclerc I., Hill E.V., Hardie D.G.,
Rutter G.A.;
"Cell-wide analysis of secretory granule dynamics in three dimensions
in living pancreatic beta-cells: evidence against a role for AMPK-
dependent phosphorylation of KLC1 at Ser517/Ser520 in glucose-
stimulated insulin granule movement.";
Biochem. Soc. Trans. 38:205-208(2010).
[33]
FUNCTION.
PubMed=20160076; DOI=10.1073/pnas.0913860107;
Alexander A., Cai S.L., Kim J., Nanez A., Sahin M., MacLean K.H.,
Inoki K., Guan K.L., Shen J., Person M.D., Kusewitt D., Mills G.B.,
Kastan M.B., Walker C.L.;
"ATM signals to TSC2 in the cytoplasm to regulate mTORC1 in response
to ROS.";
Proc. Natl. Acad. Sci. U.S.A. 107:4153-4158(2010).
[34]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[35]
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).
[36]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[37]
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).
[38]
INTERACTION WITH PRKAB1 AND PRKAG1, AND ENZYME REGULATION.
PubMed=21680840; DOI=10.1126/science.1200094;
Oakhill J.S., Steel R., Chen Z.P., Scott J.W., Ling N., Tam S.,
Kemp B.E.;
"AMPK is a direct adenylate charge-regulated protein kinase.";
Science 332:1433-1435(2011).
[39]
REVIEW ON FUNCTION.
PubMed=17307971; DOI=10.1161/01.RES.0000256090.42690.05;
Towler M.C., Hardie D.G.;
"AMP-activated protein kinase in metabolic control and insulin
signaling.";
Circ. Res. 100:328-341(2007).
[40]
REVIEW ON FUNCTION.
PubMed=17712357; DOI=10.1038/nrm2249;
Hardie D.G.;
"AMP-activated/SNF1 protein kinases: conserved guardians of cellular
energy.";
Nat. Rev. Mol. Cell Biol. 8:774-785(2007).
[41]
DEPHOSPHORYLATION.
PubMed=23088624; DOI=10.1042/BJ20121201;
Chida T., Ando M., Matsuki T., Masu Y., Nagaura Y.,
Takano-Yamamoto T., Tamura S., Kobayashi T.;
"N-Myristoylation is essential for protein phosphatases PPM1A and
PPM1B to dephosphorylate their physiological substrates in cells.";
Biochem. J. 449:741-749(2013).
[42]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-32; THR-382; SER-486;
THR-490 AND SER-496, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[43]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-355; SER-496; SER-508;
SER-524 AND SER-527, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[44]
VARIANT [LARGE SCALE ANALYSIS] ARG-16.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- 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:11518699,
ECO:0000269|PubMed:11554766, ECO:0000269|PubMed:12519745,
ECO:0000269|PubMed:14651849, ECO:0000269|PubMed:15866171,
ECO:0000269|PubMed:17486097, ECO:0000269|PubMed:17711846,
ECO:0000269|PubMed:18184930, ECO:0000269|PubMed:18439900,
ECO:0000269|PubMed:20074060, ECO:0000269|PubMed:20160076,
ECO:0000269|PubMed:21205641}.
-!- 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;
-!- 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. AMPK is activated by antihyperglycemic drug
metformin, a drug prescribed to patients with type 2 diabetes: in
vivo, metformin seems to mainly inhibit liver gluconeogenesis.
However, metformin can be used to activate AMPK in muscle and
other cells in culture or ex vivo (PubMed:11602624). 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:11602624,
ECO:0000269|PubMed:14976552, ECO:0000269|PubMed:15980064,
ECO:0000269|PubMed:16054095, ECO:0000269|PubMed:21680840}.
-!- 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. {ECO:0000269|PubMed:17028174,
ECO:0000269|PubMed:18403135, ECO:0000269|PubMed:18663353,
ECO:0000269|PubMed:21680840}.
-!- INTERACTION:
Q9NYB9:ABI2; NbExp=3; IntAct=EBI-1181405, EBI-743598;
Q08117:AES; NbExp=3; IntAct=EBI-1181405, EBI-717810;
O14503:BHLHE40; NbExp=3; IntAct=EBI-1181405, EBI-711810;
O14627:CDX4; NbExp=3; IntAct=EBI-1181405, EBI-10181162;
Q13363-2:CTBP1; NbExp=3; IntAct=EBI-1181405, EBI-10171858;
O95073:FSBP; NbExp=3; IntAct=EBI-1181405, EBI-1059030;
Q08379:GOLGA2; NbExp=3; IntAct=EBI-1181405, EBI-618309;
Q6NT76:HMBOX1; NbExp=3; IntAct=EBI-1181405, EBI-2549423;
Q8IX15-3:HOMEZ; NbExp=3; IntAct=EBI-1181405, EBI-10172004;
P08238:HSP90AB1; NbExp=2; IntAct=EBI-1181405, EBI-352572;
Q9UKT9:IKZF3; NbExp=3; IntAct=EBI-1181405, EBI-747204;
Q8NBZ0:INO80E; NbExp=3; IntAct=EBI-1181405, EBI-769401;
Q6A162:KRT40; NbExp=3; IntAct=EBI-1181405, EBI-10171697;
Q96JM7:L3MBTL3; NbExp=3; IntAct=EBI-1181405, EBI-2686809;
Q5JR59:MTUS2; NbExp=3; IntAct=EBI-1181405, EBI-742948;
Q8IXK0:PHC2; NbExp=3; IntAct=EBI-1181405, EBI-713786;
Q96PV4:PNMA5; NbExp=3; IntAct=EBI-1181405, EBI-10171633;
Q9Y478:PRKAB1; NbExp=6; IntAct=EBI-1181405, EBI-719769;
O43741:PRKAB2; NbExp=12; IntAct=EBI-1181405, EBI-1053424;
P54619:PRKAG1; NbExp=10; IntAct=EBI-1181405, EBI-1181439;
Q93062:RBPMS; NbExp=3; IntAct=EBI-1181405, EBI-740322;
Q8HWS3:RFX6; NbExp=3; IntAct=EBI-1181405, EBI-746118;
Q9UFD9:RIMBP3; NbExp=3; IntAct=EBI-1181405, EBI-10182375;
Q9HAT0:ROPN1; NbExp=3; IntAct=EBI-1181405, EBI-1378139;
Q9Y2D8:SSX2IP; NbExp=3; IntAct=EBI-1181405, EBI-2212028;
Q9NVV9:THAP1; NbExp=3; IntAct=EBI-1181405, EBI-741515;
P14373:TRIM27; NbExp=3; IntAct=EBI-1181405, EBI-719493;
Q15654:TRIP6; NbExp=3; IntAct=EBI-1181405, EBI-742327;
Q9Y3Q8:TSC22D4; NbExp=3; IntAct=EBI-1181405, EBI-739485;
Q5T124:UBXN11; NbExp=3; IntAct=EBI-1181405, EBI-746004;
Q9H9H4:VPS37B; NbExp=3; IntAct=EBI-1181405, EBI-4400866;
Q8N1B4:VPS52; NbExp=3; IntAct=EBI-1181405, EBI-2799833;
P46937:YAP1; NbExp=3; IntAct=EBI-1181405, EBI-1044059;
O96006:ZBED1; NbExp=3; IntAct=EBI-1181405, EBI-740037;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15866171}.
Nucleus {ECO:0000269|PubMed:15866171}. Note=In response to stress,
recruited by p53/TP53 to specific promoters.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q13131-1; Sequence=Displayed;
Name=2;
IsoId=Q13131-2; Sequence=VSP_035431;
-!- DOMAIN: The AIS (autoinhibitory sequence) region shows some
sequence similarity with the ubiquitin-associated domains and
represses kinase activity. {ECO:0000269|PubMed:17088252,
ECO:0000269|PubMed:9857077}.
-!- PTM: Ubiquitinated. {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. {ECO:0000269|PubMed:14976552,
ECO:0000269|PubMed:15980064, ECO:0000269|PubMed:16054095,
ECO:0000269|PubMed:21460634}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. SNF1 subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA64850.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAD43027.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAH37303.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAA36547.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAG35788.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AC008810; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC048980; AAH48980.1; -; mRNA.
EMBL; AB022017; BAA36547.1; ALT_INIT; mRNA.
EMBL; AK312947; BAG35788.1; ALT_INIT; mRNA.
EMBL; BC037303; AAH37303.1; ALT_INIT; mRNA.
EMBL; AF100763; AAD43027.1; ALT_INIT; mRNA.
EMBL; U22456; AAA64850.1; ALT_INIT; mRNA.
EMBL; Y12856; CAA73361.1; -; mRNA.
CCDS; CCDS3932.2; -. [Q13131-1]
CCDS; CCDS3933.2; -. [Q13131-2]
PIR; G01743; G01743.
RefSeq; NP_006242.5; NM_006251.5. [Q13131-1]
RefSeq; NP_996790.3; NM_206907.3. [Q13131-2]
UniGene; Hs.43322; -.
PDB; 4RED; X-ray; 2.95 A; A/B=22-362.
PDB; 4RER; X-ray; 4.05 A; A=20-559.
PDB; 4REW; X-ray; 4.58 A; A=20-559.
PDB; 5EZV; X-ray; 2.99 A; A/C=359-401.
PDBsum; 4RED; -.
PDBsum; 4RER; -.
PDBsum; 4REW; -.
PDBsum; 5EZV; -.
ProteinModelPortal; Q13131; -.
SMR; Q13131; -.
BioGrid; 111549; 156.
CORUM; Q13131; -.
DIP; DIP-39973N; -.
IntAct; Q13131; 104.
MINT; MINT-6771251; -.
STRING; 9606.ENSP00000346148; -.
BindingDB; Q13131; -.
ChEMBL; CHEMBL4045; -.
DrugBank; DB00945; Acetylsalicylic acid.
DrugBank; DB00131; Adenosine monophosphate.
DrugBank; DB00171; Adenosine triphosphate.
DrugBank; DB00914; Phenformin.
GuidetoPHARMACOLOGY; 1541; -.
iPTMnet; Q13131; -.
PhosphoSitePlus; Q13131; -.
BioMuta; PRKAA1; -.
DMDM; 254763436; -.
EPD; Q13131; -.
MaxQB; Q13131; -.
PaxDb; Q13131; -.
PeptideAtlas; Q13131; -.
PRIDE; Q13131; -.
DNASU; 5562; -.
Ensembl; ENST00000354209; ENSP00000346148; ENSG00000132356. [Q13131-2]
Ensembl; ENST00000397128; ENSP00000380317; ENSG00000132356. [Q13131-1]
GeneID; 5562; -.
KEGG; hsa:5562; -.
UCSC; uc003jmb.4; human. [Q13131-1]
CTD; 5562; -.
DisGeNET; 5562; -.
EuPathDB; HostDB:ENSG00000132356.11; -.
GeneCards; PRKAA1; -.
H-InvDB; HIX0004832; -.
HGNC; HGNC:9376; PRKAA1.
HPA; CAB005050; -.
HPA; HPA035409; -.
HPA; HPA064946; -.
MIM; 602739; gene.
neXtProt; NX_Q13131; -.
OpenTargets; ENSG00000132356; -.
PharmGKB; PA33744; -.
eggNOG; KOG0586; Eukaryota.
eggNOG; ENOG410XNQ0; LUCA.
GeneTree; ENSGT00900000140875; -.
HOGENOM; HOG000233016; -.
HOVERGEN; HBG050432; -.
KO; K07198; -.
OMA; QGVRRAK; -.
OrthoDB; EOG091G03TG; -.
PhylomeDB; Q13131; -.
TreeFam; TF314032; -.
BRENDA; 2.7.11.1; 2681.
Reactome; R-HSA-1632852; Macroautophagy.
Reactome; R-HSA-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
SignaLink; Q13131; -.
SIGNOR; Q13131; -.
ChiTaRS; PRKAA1; human.
GeneWiki; Protein_kinase,_AMP-activated,_alpha_1; -.
GenomeRNAi; 5562; -.
PRO; PR:Q13131; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000132356; -.
CleanEx; HS_PRKAA1; -.
ExpressionAtlas; Q13131; baseline and differential.
Genevisible; Q13131; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005622; C:intracellular; IMP:ParkinsonsUK-UCL.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0031588; C:nucleotide-activated protein kinase complex; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS: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:0004691; F:cAMP-dependent protein kinase activity; NAS:UniProtKB.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0035174; F:histone serine kinase activity; ISS: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; IDA:UniProtKB.
GO; GO:0050321; F:tau-protein kinase activity; IEA:UniProtKB-EC.
GO; GO:0000187; P:activation of MAPK activity; NAS:UniProtKB.
GO; GO:0061762; P:CAMKK-AMPK signaling cascade; IMP:ParkinsonsUK-UCL.
GO; GO:0007050; P:cell cycle arrest; TAS:Reactome.
GO; GO:0071361; P:cellular response to ethanol; IEA:Ensembl.
GO; GO:0042149; P:cellular response to glucose starvation; ISS: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; ISS:UniProtKB.
GO; GO:0071417; P:cellular response to organonitrogen compound; IEA:Ensembl.
GO; GO:0071380; P:cellular response to prostaglandin E stimulus; IEA:Ensembl.
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; IEA:Ensembl.
GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
GO; GO:0006006; P:glucose metabolic process; IEA:Ensembl.
GO; GO:0008610; P:lipid biosynthetic process; ISS:UniProtKB.
GO; GO:0016236; P:macroautophagy; TAS:Reactome.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
GO; GO:2001274; P:negative regulation of glucose import in response to insulin stimulus; IEA:Ensembl.
GO; GO:0046318; P:negative regulation of glucosylceramide biosynthetic process; NAS:UniProtKB.
GO; GO:0050995; P:negative regulation of lipid catabolic process; ISS:UniProtKB.
GO; GO:0032007; P:negative regulation of TOR signaling; ISS:UniProtKB.
GO; GO:0010508; P:positive regulation of autophagy; IDA:ParkinsonsUK-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:0045542; P:positive regulation of cholesterol biosynthetic process; NAS:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
GO; GO:0045821; P:positive regulation of glycolytic process; ISS:UniProtKB.
GO; GO:0048643; P:positive regulation of skeletal muscle tissue development; IEA:Ensembl.
GO; GO:0051291; P:protein heterooligomerization; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
GO; GO:2000505; P:regulation of energy homeostasis; ISS:UniProtKB.
GO; GO:0016241; P:regulation of macroautophagy; TAS:Reactome.
GO; GO:0033135; P:regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
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; IEA:Ensembl.
GO; GO:0010332; P:response to gamma radiation; ISS:UniProtKB.
GO; GO:0001666; P:response to hypoxia; NAS:UniProtKB.
GO; GO:0009411; P:response to UV; IEA:Ensembl.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
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;
3D-structure; Alternative splicing; 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; Polymorphism;
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_0000085589.
DOMAIN 27 279 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 33 41 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 302 381 AIS.
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:0000244|PubMed:19369195,
ECO:0000244|PubMed:23186163}.
MOD_RES 183 183 Phosphothreonine; by LKB1 and CaMKK2.
{ECO:0000250|UniProtKB:Q5EG47}.
MOD_RES 269 269 Phosphothreonine.
{ECO:0000250|UniProtKB:P54645}.
MOD_RES 355 355 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 356 356 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 360 360 Phosphoserine; by ULK1. {ECO:0000250}.
MOD_RES 368 368 Phosphothreonine; by ULK1. {ECO:0000250}.
MOD_RES 382 382 Phosphothreonine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 397 397 Phosphoserine; by ULK1.
{ECO:0000305|PubMed:21460634}.
MOD_RES 467 467 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 486 486 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 488 488 Phosphothreonine; by ULK1.
{ECO:0000305|PubMed:21460634}.
MOD_RES 490 490 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 496 496 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 508 508 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 524 524 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 527 527 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
VAR_SEQ 121 121 R -> RKSDVPGVVKTGSTKE (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_035431.
VARIANT 10 10 M -> L (in dbSNP:rs17855679).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_058401.
VARIANT 16 16 Q -> R (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035622.
MUTAGEN 307 307 V->G,Q: Activates the kinase activity.
{ECO:0000269|PubMed:17088252}.
CONFLICT 5 5 S -> C (in Ref. 4; BAG35788).
{ECO:0000305}.
CONFLICT 9 9 K -> S (in Ref. 5; AAD43027).
{ECO:0000305}.
CONFLICT 37 37 T -> A (in Ref. 6; AAA64850).
{ECO:0000305}.
CONFLICT 202 202 A -> V (in Ref. 6; AAA64850).
{ECO:0000305}.
CONFLICT 208 208 I -> L (in Ref. 6; AAA64850).
{ECO:0000305}.
CONFLICT 269 269 T -> S (in Ref. 3; BAA36547).
{ECO:0000305}.
STRAND 27 35 {ECO:0000244|PDB:4RED}.
STRAND 40 49 {ECO:0000244|PDB:4RED}.
STRAND 52 59 {ECO:0000244|PDB:4RED}.
HELIX 60 66 {ECO:0000244|PDB:4RED}.
STRAND 68 70 {ECO:0000244|PDB:4RED}.
HELIX 71 77 {ECO:0000244|PDB:4RED}.
STRAND 90 95 {ECO:0000244|PDB:4RED}.
STRAND 97 105 {ECO:0000244|PDB:4RED}.
HELIX 112 118 {ECO:0000244|PDB:4RED}.
HELIX 124 144 {ECO:0000244|PDB:4RED}.
HELIX 153 155 {ECO:0000244|PDB:4RED}.
STRAND 156 158 {ECO:0000244|PDB:4RED}.
STRAND 164 167 {ECO:0000244|PDB:4RED}.
STRAND 169 171 {ECO:0000244|PDB:4RED}.
HELIX 193 196 {ECO:0000244|PDB:4RED}.
HELIX 204 220 {ECO:0000244|PDB:4RED}.
STRAND 227 229 {ECO:0000244|PDB:4RED}.
HELIX 231 233 {ECO:0000244|PDB:4RED}.
HELIX 250 259 {ECO:0000244|PDB:4RED}.
HELIX 264 266 {ECO:0000244|PDB:4RED}.
HELIX 270 274 {ECO:0000244|PDB:4RED}.
HELIX 277 280 {ECO:0000244|PDB:4RED}.
TURN 296 298 {ECO:0000244|PDB:4RED}.
HELIX 301 310 {ECO:0000244|PDB:4RED}.
HELIX 315 323 {ECO:0000244|PDB:4RED}.
HELIX 330 340 {ECO:0000244|PDB:4RED}.
TURN 347 351 {ECO:0000244|PDB:4RED}.
HELIX 372 374 {ECO:0000244|PDB:5EZV}.
SEQUENCE 559 AA; 64009 MW; ABAE71FBF912947A 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 QVDPMKRATI KDIREHEWFK QDLPKYLFPE DPSYSSTMID
DEALKEVCEK FECSEEEVLS CLYNRNHQDP LAVAYHLIID NRRIMNEAKD FYLATSPPDS
FLDDHHLTRP HPERVPFLVA ETPRARHTLD ELNPQKSKHQ GVRKAKWHLG IRSQSRPNDI
MAEVCRAIKQ LDYEWKVVNP YYLRVRRKNP VTSTYSKMSL QLYQVDSRTY LLDFRSIDDE
ITEAKSGTAT PQRSGSVSNY RSCQRSDSDA EAQGKSSEVS LTSSVTSLDS SPVDLTPRPG
SHTIEFFEMC ANLIKILAQ


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