ID SNF1_YEAST Reviewed; 633 AA. AC P06782; D6VTA0; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1988, sequence version 1. DT 30-AUG-2017, entry version 196. DE RecName: Full=Carbon catabolite-derepressing protein kinase {ECO:0000303|PubMed:3526554}; DE EC=2.7.11.1 {ECO:0000269|PubMed:15719021, ECO:0000269|PubMed:2557546, ECO:0000269|PubMed:3526554}; DE AltName: Full=Sucrose nonfermentating protein 1 {ECO:0000303|PubMed:6366512}; GN Name=SNF1 {ECO:0000303|PubMed:6366512}; GN Synonyms=CAT1, CCR1 {ECO:0000303|PubMed:1944227}, GLC2, PAS14; GN OrderedLocusNames=YDR477W; ORFNames=D8035.20; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=3526554; DOI=10.1126/science.3526554; RA Celenza J.L., Carlson M.; RT "A yeast gene that is essential for release from glucose repression RT encodes a protein kinase."; RL Science 233:1175-1180(1986). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169867; RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., RA Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., RA Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., RA Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., RA Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., RA Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., RA Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., RA Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., RA Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., RA Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., RA Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., RA Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., RA Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., RA Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., RA Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., RA Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., RA Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., RA Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., RA Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., RA Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., RA Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., RA Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., RA Waterston R., Albermann K., Hani J., Heumann K., Kleine K., RA Mewes H.-W., Zollner A., Zaccaria P.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."; RL Nature 387:75-78(1997). RN [3] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., RA Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and RT now."; RL G3 (Bethesda) 4:389-398(2014). RN [4] RP PROTEIN SEQUENCE OF 274-284; 528-539 AND 622-630, AND PHOSPHORYLATION RP AT THR-210. RX PubMed=7905477; RA Mitchelhill K.I., Stapleton D., Gao G., House C., Michell B., RA Katsis F., Witters L.A., Kemp B.E.; RT "Mammalian AMP-activated protein kinase shares structural and RT functional homology with the catalytic domain of yeast Snf1 protein RT kinase."; RL J. Biol. Chem. 269:2361-2364(1994). RN [5] RP IDENTIFICATION, AND FUNCTION. RX PubMed=6366512; DOI=10.1128/MCB.4.1.49; RA Celenza J.L., Carlson M.; RT "Cloning and genetic mapping of SNF1, a gene required for expression RT of glucose-repressible genes in Saccharomyces cerevisiae."; RL Mol. Cell. Biol. 4:49-53(1984). RN [6] RP INDUCTION. RX PubMed=6366513; DOI=10.1128/MCB.4.1.54; RA Celenza J.L., Carlson M.; RT "Structure and expression of the SNF1 gene of Saccharomyces RT cerevisiae."; RL Mol. Cell. Biol. 4:54-60(1984). RN [7] RP FUNCTION. RX PubMed=3049551; DOI=10.1128/jb.170.10.4838-4845.1988; RA Bisson L.F.; RT "High-affinity glucose transport in Saccharomyces cerevisiae is under RT general glucose repression control."; RL J. Bacteriol. 170:4838-4845(1988). RN [8] RP MUTAGENESIS OF LYS-84, CATALYTIC ACTIVITY, INTERACTION WITH SNF4, AND RP ENZYME REGULATION. RX PubMed=2557546; DOI=10.1128/MCB.9.11.5034; RA Celenza J.L., Carlson M.; RT "Mutational analysis of the Saccharomyces cerevisiae SNF1 protein RT kinase and evidence for functional interaction with the SNF4 RT protein."; RL Mol. Cell. Biol. 9:5034-5044(1989). RN [9] RP INTERACTION WITH SNF4. RX PubMed=2481228; DOI=10.1128/MCB.9.11.5045; RA Celenza J.L., Eng F.J., Carlson M.; RT "Molecular analysis of the SNF4 gene of Saccharomyces cerevisiae: RT evidence for physical association of the SNF4 protein with the SNF1 RT protein kinase."; RL Mol. Cell. Biol. 9:5045-5054(1989). RN [10] RP FUNCTION. RX PubMed=1944227; DOI=10.1007/BF00267461; RA Denis C.L., Audino D.C.; RT "The CCR1 (SNF1) and SCH9 protein kinases act independently of cAMP- RT dependent protein kinase and the transcriptional activator ADR1 in RT controlling yeast ADH2 expression."; RL Mol. Gen. Genet. 229:395-399(1991). RN [11] RP FUNCTION. RX PubMed=8289797; DOI=10.1128/MCB.14.2.1160; RA Ulery T.L., Jang S.H., Jaehning J.A.; RT "Glucose repression of yeast mitochondrial transcription: kinetics of RT derepression and role of nuclear genes."; RL Mol. Cell. Biol. 14:1160-1170(1994). RN [12] RP MUTAGENESIS OF GLY-53 AND THR-210. RX PubMed=1468623; RA Estruch F., Treitel M.A., Yang X., Carlson M.; RT "N-terminal mutations modulate yeast SNF1 protein kinase function."; RL Genetics 132:639-650(1992). RN [13] RP INTERACTION WITH SIP1; SIP2 AND GAL83. RX PubMed=7813428; RA Yang X., Jiang R., Carlson M.; RT "A family of proteins containing a conserved domain that mediates RT interaction with the yeast SNF1 protein kinase complex."; RL EMBO J. 13:5878-5886(1994). RN [14] RP FUNCTION, AND INTERACTION WITH SIP4. RX PubMed=8628258; DOI=10.1128/MCB.16.5.1921; RA Lesage P., Yang X., Carlson M.; RT "Yeast SNF1 protein kinase interacts with SIP4, a C6 zinc cluster RT transcriptional activator: a new role for SNF1 in the glucose RT response."; RL Mol. Cell. Biol. 16:1921-1928(1996). RN [15] RP INTERACTION WITH SNF4; SIP1; SIP2 AND GAL83. RX PubMed=9121458; DOI=10.1128/MCB.17.4.2099; RA Jiang R., Carlson M.; RT "The Snf1 protein kinase and its activating subunit, Snf4, interact RT with distinct domains of the Sip1/Sip2/Gal83 component in the kinase RT complex."; RL Mol. Cell. Biol. 17:2099-2106(1997). RN [16] RP PHOSPHORYLATION AT THR-210, AND MUTAGENESIS OF LYS-84 AND THR-210. RX PubMed=11486005; DOI=10.1074/jbc.M104418200; RA McCartney R.R., Schmidt M.C.; RT "Regulation of Snf1 kinase. Activation requires phosphorylation of RT threonine 210 by an upstream kinase as well as a distinct step RT mediated by the Snf4 subunit."; RL J. Biol. Chem. 276:36460-36466(2001). RN [17] RP PHOSPHORYLATION AT THR-210, AND INTERACTION WITH SAK1. RX PubMed=12748292; DOI=10.1128/MCB.23.11.3909-3917.2003; RA Nath N., McCartney R.R., Schmidt M.C.; RT "Yeast Pak1 kinase associates with and activates Snf1."; RL Mol. Cell. Biol. 23:3909-3917(2003). RN [18] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [19] RP FUNCTION IN PHOSPHORYLATION OF CAT8. RX PubMed=15121831; DOI=10.1128/MCB.24.10.4083-4091.2004; RA Charbon G., Breunig K.D., Wattiez R., Vandenhaute J., Noel-Georis I.; RT "Key role of Ser562/661 in Snf1-dependent regulation of Cat8p in RT Saccharomyces cerevisiae and Kluyveromyces lactis."; RL Mol. Cell. Biol. 24:4083-4091(2004). RN [20] RP FUNCTION IN PHOSPHORYLATION OF HISTONE H3, AND IDENTIFICATION IN THE RP SNF1 KINASE COMPLEX. RX PubMed=15719021; DOI=10.1038/sj.emboj.7600577; RA Lo W.-S., Gamache E.R., Henry K.W., Yang D., Pillus L., Berger S.L.; RT "Histone H3 phosphorylation can promote TBP recruitment through RT distinct promoter-specific mechanisms."; RL EMBO J. 24:997-1008(2005). RN [21] RP INTERACTION WITH CTK1. RX PubMed=16182287; DOI=10.1016/j.febslet.2005.08.057; RA Van Driessche B., Coddens S., Van Mullem V., Vandenhaute J.; RT "Glucose deprivation mediates interaction between CTDK-I and Snf1 in RT Saccharomyces cerevisiae."; RL FEBS Lett. 579:5318-5324(2005). RN [22] RP PHOSPHORYLATION, AND INTERACTION WITH SAK1. RX PubMed=16847059; DOI=10.1074/jbc.M603811200; RA Elbing K., Rubenstein E.M., McCartney R.R., Schmidt M.C.; RT "Subunits of the Snf1 kinase heterotrimer show interdependence for RT association and activity."; RL J. Biol. Chem. 281:26170-26180(2006). RN [23] RP SUBCELLULAR LOCATION. RX PubMed=17237508; DOI=10.1534/genetics.106.068932; RA Sarma N.J., Haley T.M., Barbara K.E., Buford T.D., Willis K.A., RA Santangelo G.M.; RT "Glucose-responsive regulators of gene expression in Saccharomyces RT cerevisiae function at the nuclear periphery via a reverse recruitment RT mechanism."; RL Genetics 175:1127-1135(2007). RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=ADR376; RX PubMed=17330950; DOI=10.1021/pr060559j; RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., RA Elias J.E., Gygi S.P.; RT "Large-scale phosphorylation analysis of alpha-factor-arrested RT Saccharomyces cerevisiae."; RL J. Proteome Res. 6:1190-1197(2007). RN [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413 AND SER-487, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth RT phosphoproteome analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413 AND SER-632, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19779198; DOI=10.1126/science.1172867; RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.; RT "Global analysis of Cdk1 substrate phosphorylation sites provides RT insights into evolution."; RL Science 325:1682-1686(2009). RN [27] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-461, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22106047; DOI=10.1002/pmic.201100166; RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.; RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae."; RL Proteomics 12:236-240(2012). RN [28] RP SUMOYLATION AT LYS-549 BY MMS21, AND MUTAGENESIS OF LYS-549. RX PubMed=24108357; DOI=10.1073/pnas.1304839110; RA Simpson-Lavy K.J., Johnston M.; RT "Sumoylation regulates the SNF1 protein kinase."; RL Proc. Natl. Acad. Sci. U.S.A. 110:17432-17437(2013). RN [29] RP FUNCTION. RX PubMed=25730376; DOI=10.1042/BJ20140734; RA Ferrer-Dalmau J., Randez-Gil F., Marquina M., Prieto J.A., RA Casamayor A.; RT "Protein kinase Snf1 is involved in the proper regulation of the RT unfolded protein response in Saccharomyces cerevisiae."; RL Biochem. J. 468:33-47(2015). RN [30] RP DOMAIN, MUTAGENESIS OF GLY-357 AND LEU-367, FUNCTION, AND SUBCELLULAR RP LOCATION. RX PubMed=25869125; DOI=10.1074/jbc.M115.647032; RA Jiao R., Postnikoff S., Harkness T.A., Arnason T.G.; RT "The SNF1 kinase ubiquitin-associated domain restrains its activation, RT activity, and the yeast life span."; RL J. Biol. Chem. 290:15393-15404(2015). RN [31] RP FUNCTION, AND INTERACTION WITH CYR1. RX PubMed=26309257; DOI=10.1074/jbc.M115.658005; RA Nicastro R., Tripodi F., Gaggini M., Castoldi A., Reghellin V., RA Nonnis S., Tedeschi G., Coccetti P.; RT "Snf1 phosphorylates adenylate cyclase and negatively regulates RT protein kinase A-dependent transcription in Saccharomyces RT cerevisiae."; RL J. Biol. Chem. 290:24715-24726(2015). RN [32] RP FUNCTION. RX PubMed=25428989; DOI=10.1091/mbc.E14-06-1088; RA DeMille D., Badal B.D., Evans J.B., Mathis A.D., Anderson J.F., RA Grose J.H.; RT "PAS kinase is activated by direct SNF1-dependent phosphorylation and RT mediates inhibition of TORC1 through the phosphorylation and RT activation of Pbp1."; RL Mol. Biol. Cell 26:569-582(2015). RN [33] RP FUNCTION. RX PubMed=26667037; DOI=10.1128/MCB.00436-15; RA Braun K.A., Dombek K.M., Young E.T.; RT "Snf1-dependent transcription confers glucose-induced decay upon the RT mRNA product."; RL Mol. Cell. Biol. 36:628-644(2015). RN [34] RP FUNCTION, AND PHOSPHORYLATION AT THR-210. RX PubMed=26394309; DOI=10.1371/journal.pgen.1005491; RA Mizuno T., Masuda Y., Irie K.; RT "The Saccharomyces cerevisiae AMPK, Snf1, negatively regulates the RT Hog1 MAPK pathway in ER stress response."; RL PLoS Genet. 11:E1005491-E1005491(2015). RN [35] RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 41-315, AND DOMAIN. RX PubMed=16236260; DOI=10.1016/j.bbrc.2005.09.181; RA Rudolph M.J., Amodeo G.A., Bai Y., Tong L.; RT "Crystal structure of the protein kinase domain of yeast AMP-activated RT protein kinase Snf1."; RL Biochem. Biophys. Res. Commun. 337:1224-1228(2005). RN [36] RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 46-319, AND DOMAIN. RX PubMed=16531232; DOI=10.1016/j.str.2005.12.008; RA Nayak V., Zhao K., Wyce A., Schwartz M.F., Lo W.S., Berger S.L., RA Marmorstein R.; RT "Structure and dimerization of the kinase domain from yeast Snf1, a RT member of the Snf1/AMPK protein family."; RL Structure 14:477-485(2006). RN [37] RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 460-630 IN COMPLEX WITH SNF4 RP AND SIP2, DOMAIN, AND ENZYME REGULATION. RX PubMed=17851534; DOI=10.1038/nature06127; RA Amodeo G.A., Rudolph M.J., Tong L.; RT "Crystal structure of the heterotrimer core of Saccharomyces RT cerevisiae AMPK homologue SNF1."; RL Nature 449:492-495(2007). RN [38] RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 41-315, DOMAIN, AND RP PHOSPHORYLATION AT THR-210. RX PubMed=19474788; DOI=10.1038/nature08075; RA Chen L., Jiao Z.H., Zheng L.S., Zhang Y.Y., Xie S.T., Wang Z.X., RA Wu J.W.; RT "Structural insight into the autoinhibition mechanism of AMP-activated RT protein kinase."; RL Nature 459:1146-1149(2009). RN [39] RP X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 50-320, AND DOMAIN. RX PubMed=20823513; DOI=10.1107/S1744309110028265; RA Rudolph M.J., Amodeo G.A., Tong L.; RT "An inhibited conformation for the protein kinase domain of the RT Saccharomyces cerevisiae AMPK homolog Snf1."; RL Acta Crystallogr. F 66:999-1002(2010). RN [40] RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 457-633, AND PHOSPHORYLATION RP AT THR-210. RX PubMed=22019086; DOI=10.1016/j.cmet.2011.09.009; RA Mayer F.V., Heath R., Underwood E., Sanders M.J., Carmena D., RA McCartney R.R., Leiper F.C., Xiao B., Jing C., Walker P.A., RA Haire L.F., Ogrodowicz R., Martin S.R., Schmidt M.C., Gamblin S.J., RA Carling D.; RT "ADP regulates SNF1, the Saccharomyces cerevisiae homolog of AMP- RT activated protein kinase."; RL Cell Metab. 14:707-714(2011). CC -!- FUNCTION: Serine/threonine protein kinase essential for release CC from glucose repression (PubMed:3526554, PubMed:6366512, CC PubMed:3049551, PubMed:1944227, PubMed:8289797, PubMed:8628258, CC PubMed:25869125). Catalytic subunit of the AMP-activated protein CC kinase complex also known as the SNF1 kinase complex (Snf1c), a CC central regulator of cellular energy homeostasis, which, in CC response to a fall in intracellular ATP levels, activates energy- CC producing pathways and inhibits energy-consuming processes CC (PubMed:8289797, PubMed:26667037). The complex phosphorylates CC histone H3 to form H3S10ph, which promotes H3K14ac formation, CC leading to transcriptional activation through TBP recruitment to CC the promoters (PubMed:15719021). The complex also negatively CC regulates the HOG1 MAPK pathway in ER stress response including CC unfolded protein response (UPR) (PubMed:25730376, CC PubMed:26394309). Under nutrient/energy depletion, the complex CC phosphorylates and activates PAS kinase PSK1 which in turn CC activates PBS1, leading to the inhibition of the TORC1 signaling CC pathway (PubMed:25428989). SNF1 also interacts and phosphorylates CC adenylate cyclase CYR1 and negatively regulates the protein kinase CC A signaling pathway (PubMed:26309257). Also phosphorylates and CC regulates the transcriptional activator CAT8 (PubMed:15121831). CC {ECO:0000269|PubMed:15121831, ECO:0000269|PubMed:15719021, CC ECO:0000269|PubMed:1944227, ECO:0000269|PubMed:25428989, CC ECO:0000269|PubMed:25730376, ECO:0000269|PubMed:25869125, CC ECO:0000269|PubMed:26309257, ECO:0000269|PubMed:26394309, CC ECO:0000269|PubMed:26667037, ECO:0000269|PubMed:3049551, CC ECO:0000269|PubMed:3526554, ECO:0000269|PubMed:6366512, CC ECO:0000269|PubMed:8289797, ECO:0000269|PubMed:8628258}. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC {ECO:0000269|PubMed:15719021, ECO:0000269|PubMed:2557546, CC ECO:0000269|PubMed:3526554}. CC -!- ENZYME REGULATION: The kinase activity is positively regulated by CC SNF4 via sequestration of the SNF1 auto-inhibitory domain (AID) CC (PubMed:2557546, PubMed:17851534). {ECO:0000269|PubMed:17851534, CC ECO:0000269|PubMed:2557546}. CC -!- SUBUNIT: Component of the AMP-activated protein kinase complex CC also known as the SNF1 kinase complex (Snf1c), an heterotrimeric CC complex composed of an alpha subunit (SNF1), a regulatory subunit CC beta (GAL83 and substoichiometric alternate beta subunits SIP1 and CC SIP2), and a regulatory subunit gamma (SNF4) (PubMed:2557546, CC PubMed:2481228, PubMed:7813428, PubMed:9121458, PubMed:15719021, CC PubMed:17851534). Inrteracts with the transcriptional activator CC SIP4 (PubMed:8628258). Interacts with SAK1 (PubMed:12748292, CC PubMed:16847059). Interacts with CTK1 (PubMed:16182287): Interacts CC with adenylate cyclase CYR1 (PubMed:26309257). CC {ECO:0000269|PubMed:12748292, ECO:0000269|PubMed:15719021, CC ECO:0000269|PubMed:16182287, ECO:0000269|PubMed:16847059, CC ECO:0000269|PubMed:17851534, ECO:0000269|PubMed:2481228, CC ECO:0000269|PubMed:2557546, ECO:0000269|PubMed:26309257, CC ECO:0000269|PubMed:7813428, ECO:0000269|PubMed:8628258, CC ECO:0000269|PubMed:9121458}. CC -!- INTERACTION: CC Q00684:CDC14; NbExp=2; IntAct=EBI-17516, EBI-4192; CC Q04739:GAL83; NbExp=5; IntAct=EBI-17516, EBI-7244; CC P22211:NPR1; NbExp=2; IntAct=EBI-17516, EBI-12207; CC Q00816:REG1; NbExp=3; IntAct=EBI-17516, EBI-8270; CC P34164:SIP2; NbExp=9; IntAct=EBI-17516, EBI-17187; CC P12904:SNF4; NbExp=17; IntAct=EBI-17516, EBI-17537; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25869125}. CC Nucleus {ECO:0000269|PubMed:25869125}. Nucleus membrane CC {ECO:0000269|PubMed:17237508}; Peripheral membrane protein CC {ECO:0000269|PubMed:17237508}. Note=Nuclear translocation occurs CC under nitrogen and glucose starvation conditions CC (PubMed:25869125). {ECO:0000269|PubMed:25869125}. CC -!- INDUCTION: Expression of the SNF1 gene itself is not glucose CC repressible (PubMed:6366513). {ECO:0000269|PubMed:6366513}. CC -!- DOMAIN: The regulatory domain (RS) also called auto-inhibitory CC domain (AID) inhibits kinase activity of the protein kinase domain CC (KD) (PubMed:19474788, PubMed:20823513). The AID is sequestered by CC SNF4 within the AMP-activated protein kinase complex which might CC correspond to the activated SNF1 form (PubMed:17851534). CC {ECO:0000269|PubMed:17851534, ECO:0000269|PubMed:19474788, CC ECO:0000269|PubMed:20823513}. CC -!- DOMAIN: The ubiquitin-associated domain (UBA) localized within the CC AID dampens kinase activation, probably by restraining SNF1-SNF4 CC associations (PubMed:25869125). Moreover, the UBA domain CC influences life span in a FKH1- and FKH2-dependent mechanism CC (PubMed:25869125). {ECO:0000269|PubMed:25869125}. CC -!- PTM: Phosphorylation at Thr-210 in response to glucose limitation CC leads to activation of kinase activity (PubMed:11486005, CC PubMed:12748292). ADP, but not AMP, protects the enzyme from CC dephosphorylation at Thr-210 by GLC7 (PubMed:22019086). CC {ECO:0000269|PubMed:12748292, ECO:0000269|PubMed:22019086}. CC -!- PTM: Sumoylation by the SUMO (E3) ligase MMS21 leads to inhibition CC by interaction of SUMO attached to Lys-549 with a SUMO-interacting CC sequence motif located near the active site of SNF1, and by CC targeting SNF1 for glucose-induced destruction via the SLX5-SLX8 CC (SUMO-directed) ubiquitin ligase (PubMed:24108357). CC {ECO:0000269|PubMed:24108357}. CC -!- MISCELLANEOUS: Present with 589 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK CC Ser/Thr protein kinase family. SNF1 subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M13971; AAA35058.1; -; Genomic_DNA. DR EMBL; U33050; AAB64904.1; -; Genomic_DNA. DR EMBL; BK006938; DAA12310.1; -; Genomic_DNA. DR PIR; A26030; A26030. DR RefSeq; NP_010765.3; NM_001180785.3. DR PDB; 2FH9; X-ray; 2.80 A; A=46-319. DR PDB; 2QLV; X-ray; 2.60 A; A/D=460-630. DR PDB; 3DAE; X-ray; 2.90 A; A/B=41-315. DR PDB; 3HYH; X-ray; 2.20 A; A/B=41-315. DR PDB; 3MN3; X-ray; 2.38 A; A=50-320. DR PDB; 3T4N; X-ray; 2.30 A; A=457-633. DR PDB; 3TDH; X-ray; 2.30 A; A=457-633. DR PDB; 3TE5; X-ray; 2.50 A; A=457-633. DR PDBsum; 2FH9; -. DR PDBsum; 2QLV; -. DR PDBsum; 3DAE; -. DR PDBsum; 3HYH; -. DR PDBsum; 3MN3; -. DR PDBsum; 3T4N; -. DR PDBsum; 3TDH; -. DR PDBsum; 3TE5; -. DR ProteinModelPortal; P06782; -. DR SMR; P06782; -. DR BioGrid; 32529; 797. DR DIP; DIP-18N; -. DR IntAct; P06782; 26. DR MINT; MINT-364314; -. DR STRING; 4932.YDR477W; -. DR iPTMnet; P06782; -. DR MaxQB; P06782; -. DR PRIDE; P06782; -. DR EnsemblFungi; YDR477W; YDR477W; YDR477W. DR GeneID; 852088; -. DR KEGG; sce:YDR477W; -. DR EuPathDB; FungiDB:YDR477W; -. DR SGD; S000002885; SNF1. DR GeneTree; ENSGT00790000122947; -. DR HOGENOM; HOG000233016; -. DR InParanoid; P06782; -. DR KO; K12761; -. DR OMA; RWHFGIR; -. DR OrthoDB; EOG092C0QJU; -. DR BioCyc; YEAST:G3O-30003-MONOMER; -. DR BRENDA; 2.7.11.1; 984. DR Reactome; R-SCE-163680; AMPK inhibits chREBP transcriptional activation activity. DR Reactome; R-SCE-165158; Activation of AKT2. DR Reactome; R-SCE-199418; Negative regulation of the PI3K/AKT network. DR Reactome; R-SCE-200425; Import of palmitoyl-CoA into the mitochondrial matrix. DR Reactome; R-SCE-380972; Energy dependent regulation of mTOR by LKB1-AMPK. DR EvolutionaryTrace; P06782; -. DR PRO; PR:P06782; -. DR Proteomes; UP000002311; Chromosome IV. DR GO; GO:0005737; C:cytoplasm; IDA:SGD. DR GO; GO:0000324; C:fungal-type vacuole; IPI:SGD. DR GO; GO:0005641; C:nuclear envelope lumen; IDA:SGD. DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell. DR GO; GO:0031588; C:nucleotide-activated protein kinase complex; IDA:SGD. DR GO; GO:0005634; C:nucleus; IDA:SGD. DR GO; GO:0004679; F:AMP-activated protein kinase activity; IMP:SGD. DR GO; GO:0005086; F:ARF guanyl-nucleotide exchange factor activity; IDA:SGD. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:SGD. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR GO; GO:0007155; P:cell adhesion; IMP:SGD. DR GO; GO:0006995; P:cellular response to nitrogen starvation; IDA:SGD. DR GO; GO:0071940; P:fungal-type cell wall assembly; IMP:SGD. DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central. DR GO; GO:0001403; P:invasive growth in response to glucose limitation; IMP:SGD. DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central. DR GO; GO:0017148; P:negative regulation of translation; IMP:SGD. DR GO; GO:1900436; P:positive regulation of filamentous growth of a population of unicellular organisms in response to starvation; IMP:SGD. DR GO; GO:0045722; P:positive regulation of gluconeogenesis; IMP:SGD. DR GO; GO:0016239; P:positive regulation of macroautophagy; IMP:SGD. DR GO; GO:0006468; P:protein phosphorylation; IDA:SGD. DR GO; GO:0007124; P:pseudohyphal growth; IMP:SGD. DR GO; GO:0001302; P:replicative cell aging; IMP:SGD. DR GO; GO:0006986; P:response to unfolded protein; IMP:SGD. DR GO; GO:0090606; P:single-species surface biofilm formation; IMP:SGD. DR CDD; cd14334; UBA_SNF1_fungi; 1. DR InterPro; IPR032270; AMPK_C. DR InterPro; IPR028375; KA1/Ssp2_C. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR InterPro; IPR013896; SNF1_UBA. DR Pfam; PF16579; AdenylateSensor; 1. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF08587; UBA_2; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF103243; SSF103243; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Carbohydrate metabolism; Complete proteome; KW Cytoplasm; Direct protein sequencing; Isopeptide bond; Kinase; KW Membrane; Nucleotide-binding; Nucleus; Phosphoprotein; KW Reference proteome; Serine/threonine-protein kinase; Transferase; KW Ubl conjugation. FT CHAIN 1 633 Carbon catabolite-derepressing protein FT kinase. FT /FTId=PRO_0000086670. FT DOMAIN 55 306 Protein kinase. {ECO:0000255|PROSITE- FT ProRule:PRU00159, FT ECO:0000269|PubMed:16236260, FT ECO:0000269|PubMed:16531232}. FT DOMAIN 348 389 UBA. {ECO:0000269|PubMed:25869125}. FT NP_BIND 61 69 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT REGION 313 392 Auto-inhibitory domain (AID). FT {ECO:0000269|PubMed:17851534, FT ECO:0000269|PubMed:19474788}. FT COMPBIAS 18 32 Poly-His. FT ACT_SITE 177 177 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU00159, ECO:0000255|PROSITE- FT ProRule:PRU10027}. FT BINDING 84 84 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT MOD_RES 210 210 Phosphothreonine; by autocatalysis. FT {ECO:0000269|PubMed:11486005, FT ECO:0000269|PubMed:12748292, FT ECO:0000269|PubMed:22019086, FT ECO:0000269|PubMed:26394309, FT ECO:0000269|PubMed:7905477}. FT MOD_RES 413 413 Phosphoserine. FT {ECO:0000244|PubMed:17330950, FT ECO:0000244|PubMed:18407956, FT ECO:0000244|PubMed:19779198}. FT MOD_RES 487 487 Phosphoserine. FT {ECO:0000244|PubMed:18407956}. FT MOD_RES 632 632 Phosphoserine. FT {ECO:0000244|PubMed:19779198}. FT CROSSLNK 461 461 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT {ECO:0000244|PubMed:22106047}. FT CROSSLNK 549 549 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO). FT {ECO:0000269|PubMed:24108357}. FT MUTAGEN 53 53 G->R: Exhibits greater activity than FT wild-type SNFl in an immune complex assay FT where other associated molecules are FT present, but exhibits the same activity FT in a protein blot assay. FT {ECO:0000269|PubMed:1468623}. FT MUTAGEN 84 84 K->R: Inactivates the kinase activity FT without affecting protein levels. FT {ECO:0000269|PubMed:11486005, FT ECO:0000269|PubMed:2557546}. FT MUTAGEN 210 210 T->A: Inactivates the kinase activity FT without affecting protein levels. FT {ECO:0000269|PubMed:11486005, FT ECO:0000269|PubMed:1468623}. FT MUTAGEN 357 357 G->A: Alters kinase activation and FT biological activity, including enhanced FT allosteric subunit associations and FT increased oxidative stress resistance and FT life span; when associated with I-367. FT {ECO:0000269|PubMed:25869125}. FT MUTAGEN 367 367 L->I: Alters kinase activation and FT biological activity, including enhanced FT allosteric subunit associations and FT increased oxidative stress resistance and FT life span; when associated with A-357. FT {ECO:0000269|PubMed:25869125}. FT MUTAGEN 549 549 K->R: Decreases sumoylation of SNF1. FT {ECO:0000269|PubMed:24108357}. FT STRAND 56 62 {ECO:0000244|PDB:3HYH}. FT HELIX 64 66 {ECO:0000244|PDB:3MN3}. FT STRAND 69 73 {ECO:0000244|PDB:3HYH}. FT TURN 75 77 {ECO:0000244|PDB:3HYH}. FT STRAND 80 87 {ECO:0000244|PDB:3HYH}. FT HELIX 88 91 {ECO:0000244|PDB:3DAE}. FT HELIX 97 109 {ECO:0000244|PDB:3HYH}. FT STRAND 118 123 {ECO:0000244|PDB:3HYH}. FT STRAND 125 133 {ECO:0000244|PDB:3HYH}. FT HELIX 139 145 {ECO:0000244|PDB:3HYH}. FT HELIX 151 170 {ECO:0000244|PDB:3HYH}. FT TURN 180 182 {ECO:0000244|PDB:3HYH}. FT STRAND 183 185 {ECO:0000244|PDB:3HYH}. FT STRAND 191 193 {ECO:0000244|PDB:3HYH}. FT TURN 207 209 {ECO:0000244|PDB:3MN3}. FT HELIX 215 217 {ECO:0000244|PDB:3MN3}. FT HELIX 220 223 {ECO:0000244|PDB:3HYH}. FT STRAND 224 227 {ECO:0000244|PDB:3HYH}. FT HELIX 232 247 {ECO:0000244|PDB:3HYH}. FT HELIX 257 266 {ECO:0000244|PDB:3HYH}. FT HELIX 277 286 {ECO:0000244|PDB:3HYH}. FT HELIX 291 293 {ECO:0000244|PDB:3HYH}. FT HELIX 297 302 {ECO:0000244|PDB:3HYH}. FT HELIX 304 307 {ECO:0000244|PDB:3HYH}. FT HELIX 312 314 {ECO:0000244|PDB:3HYH}. FT TURN 317 319 {ECO:0000244|PDB:3MN3}. FT HELIX 471 473 {ECO:0000244|PDB:3T4N}. FT HELIX 475 485 {ECO:0000244|PDB:3T4N}. FT HELIX 489 492 {ECO:0000244|PDB:3T4N}. FT STRAND 506 511 {ECO:0000244|PDB:3T4N}. FT HELIX 515 529 {ECO:0000244|PDB:3T4N}. FT STRAND 532 534 {ECO:0000244|PDB:3T4N}. FT HELIX 538 540 {ECO:0000244|PDB:3T4N}. FT STRAND 543 548 {ECO:0000244|PDB:3T4N}. FT STRAND 565 576 {ECO:0000244|PDB:3T4N}. FT STRAND 579 590 {ECO:0000244|PDB:3T4N}. FT HELIX 607 610 {ECO:0000244|PDB:2QLV}. FT HELIX 613 628 {ECO:0000244|PDB:3T4N}. SQ SEQUENCE 633 AA; 72045 MW; F5C63565C986C4E3 CRC64; MSSNNNTNTA PANANSSHHH HHHHHHHHHH GHGGSNSTLN NPKSSLADGA HIGNYQIVKT LGEGSFGKVK LAYHTTTGQK VALKIINKKV LAKSDMQGRI EREISYLRLL RHPHIIKLYD VIKSKDEIIM VIEYAGNELF DYIVQRDKMS EQEARRFFQQ IISAVEYCHR HKIVHRDLKP ENLLLDEHLN VKIADFGLSN IMTDGNFLKT SCGSPNYAAP EVISGKLYAG PEVDVWSCGV ILYVMLCRRL PFDDESIPVL FKNISNGVYT LPKFLSPGAA GLIKRMLIVN PLNRISIHEI MQDDWFKVDL PEYLLPPDLK PHPEEENENN DSKKDGSSPD NDEIDDNLVN ILSSTMGYEK DEIYESLESS EDTPAFNEIR DAYMLIKENK SLIKDMKANK SVSDELDTFL SQSPPTFQQQ SKSHQKSQVD HETAKQHARR MASAITQQRT YHQSPFMDQY KEEDSTVSIL PTSLPQIHRA NMLAQGSPAA SKISPLVTKK SKTRWHFGIR SRSYPLDVMG EIYIALKNLG AEWAKPSEED LWTIKLRWKY DIGNKTNTNE KIPDLMKMVI QLFQIETNNY LVDFKFDGWE SSYGDDTTVS NISEDEMSTF SAYPFLHLTT KLIMELAVNS QSN //