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 27-MAR-2024, entry version 238. 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; Saccharomycetes; OC 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 encodes RT 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., Paulin L., RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., RA Wilson R., 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., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [4] RP PROTEIN SEQUENCE OF 274-284; 528-539 AND 622-630, AND PHOSPHORYLATION AT RP THR-210. RX PubMed=7905477; DOI=10.1016/s0021-9258(17)41951-x; RA Mitchelhill K.I., Stapleton D., Gao G., House C., Michell B., Katsis F., RA Witters L.A., Kemp B.E.; RT "Mammalian AMP-activated protein kinase shares structural and functional RT homology with the catalytic domain of yeast Snf1 protein kinase."; RL J. Biol. Chem. 269:2361-2364(1994). RN [5] RP IDENTIFICATION, AND FUNCTION. RX PubMed=6366512; DOI=10.1128/mcb.4.1.49-53.1984; RA Celenza J.L., Carlson M.; RT "Cloning and genetic mapping of SNF1, a gene required for expression of RT 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.4.1.54-60.1984; RA Celenza J.L., Carlson M.; RT "Structure and expression of the SNF1 gene of Saccharomyces 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 ACTIVITY REGULATION. RX PubMed=2557546; DOI=10.1128/mcb.9.11.5034-5044.1989; RA Celenza J.L., Carlson M.; RT "Mutational analysis of the Saccharomyces cerevisiae SNF1 protein kinase RT and evidence for functional interaction with the SNF4 protein."; RL Mol. Cell. Biol. 9:5034-5044(1989). RN [9] RP INTERACTION WITH SNF4. RX PubMed=2481228; DOI=10.1128/mcb.9.11.5045-5054.1989; RA Celenza J.L., Eng F.J., Carlson M.; RT "Molecular analysis of the SNF4 gene of Saccharomyces cerevisiae: evidence RT for physical association of the SNF4 protein with the SNF1 protein RT 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.14.2.1160-1170.1994; 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; DOI=10.1093/genetics/132.3.639; 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; DOI=10.1002/j.1460-2075.1994.tb06933.x; 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 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 with RT distinct domains of the Sip1/Sip2/Gal83 component in the kinase 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 mediated by RT 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., Dephoure N., RA 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 SNF1 RP 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 distinct RT 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 BY RP 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 phosphoproteome RT 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 insights RT into evolution."; RL Science 325:1682-1686(2009). RN [27] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-461, AND IDENTIFICATION BY RP 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., Casamayor A.; RT "Protein kinase Snf1 is involved in the proper regulation of the unfolded RT 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., Nonnis S., RA Tedeschi G., Coccetti P.; RT "Snf1 phosphorylates adenylate cyclase and negatively regulates protein RT kinase A-dependent transcription in Saccharomyces 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., Grose J.H.; RT "PAS kinase is activated by direct SNF1-dependent phosphorylation and RT mediates inhibition of TORC1 through the phosphorylation and activation of RT 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 mRNA RT 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 Hog1 RT 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 member RT 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 AND RP SIP2, DOMAIN, AND ACTIVITY 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 cerevisiae RT 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., 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 AT RP 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., Haire L.F., RA Ogrodowicz R., Martin S.R., Schmidt M.C., Gamblin S.J., Carling D.; RT "ADP regulates SNF1, the Saccharomyces cerevisiae homolog of AMP-activated RT protein kinase."; RL Cell Metab. 14:707-714(2011). CC -!- FUNCTION: Serine/threonine protein kinase essential for release from CC glucose repression (PubMed:3526554, PubMed:6366512, PubMed:3049551, CC PubMed:1944227, PubMed:8289797, PubMed:8628258, PubMed:25869125). CC Catalytic subunit of the AMP-activated protein kinase complex also CC known as the SNF1 kinase complex (Snf1c), a central regulator of CC cellular energy homeostasis, which, in response to a fall in CC intracellular ATP levels, activates energy-producing pathways and CC inhibits energy-consuming processes (PubMed:8289797, PubMed:26667037). CC The complex phosphorylates histone H3 to form H3S10ph, which promotes CC H3K14ac formation, leading to transcriptional activation through TBP CC recruitment to the promoters (PubMed:15719021). The complex also CC negatively regulates the HOG1 MAPK pathway in ER stress response CC including 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 activates CC PBS1, leading to the inhibition of the TORC1 signaling pathway CC (PubMed:25428989). SNF1 also interacts and phosphorylates adenylate CC cyclase CYR1 and negatively regulates the protein kinase A signaling CC pathway (PubMed:26309257). Also phosphorylates and regulates the CC 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: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CC Evidence={ECO:0000269|PubMed:15719021, ECO:0000269|PubMed:2557546, CC ECO:0000269|PubMed:3526554}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:15719021, CC ECO:0000269|PubMed:2557546, ECO:0000269|PubMed:3526554}; CC -!- ACTIVITY 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 also CC known as the SNF1 kinase complex (Snf1c), a heterotrimeric complex CC composed of an alpha subunit (SNF1), a regulatory subunit beta (GAL83 CC and substoichiometric alternate beta subunits SIP1 and SIP2), and a CC regulatory subunit gamma (SNF4) (PubMed:2557546, PubMed:2481228, CC PubMed:7813428, PubMed:9121458, PubMed:15719021, PubMed:17851534). CC Interacts with the transcriptional activator SIP4 (PubMed:8628258). CC Interacts with SAK1 (PubMed:12748292, PubMed:16847059). Interacts with CC CTK1 (PubMed:16182287): Interacts with adenylate cyclase CYR1 CC (PubMed:26309257). {ECO:0000269|PubMed:12748292, CC ECO:0000269|PubMed:15719021, ECO:0000269|PubMed:16182287, CC ECO:0000269|PubMed:16847059, ECO:0000269|PubMed:17851534, CC ECO:0000269|PubMed:2481228, ECO:0000269|PubMed:2557546, CC ECO:0000269|PubMed:26309257, ECO:0000269|PubMed:7813428, CC ECO:0000269|PubMed:8628258, ECO:0000269|PubMed:9121458}. CC -!- INTERACTION: CC P06782; Q00684: CDC14; NbExp=2; IntAct=EBI-17516, EBI-4192; CC P06782; Q04739: GAL83; NbExp=5; IntAct=EBI-17516, EBI-7244; CC P06782; P22211: NPR1; NbExp=2; IntAct=EBI-17516, EBI-12207; CC P06782; Q00816: REG1; NbExp=7; IntAct=EBI-17516, EBI-8270; CC P06782; P38232: REG2; NbExp=3; IntAct=EBI-17516, EBI-14921; CC P06782; P34164: SIP2; NbExp=11; IntAct=EBI-17516, EBI-17187; CC P06782; P06782: SNF1; NbExp=6; IntAct=EBI-17516, EBI-17516; CC P06782; P12904: SNF4; NbExp=22; IntAct=EBI-17516, EBI-17537; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25869125}. Nucleus CC {ECO:0000269|PubMed:25869125}. Nucleus membrane CC {ECO:0000269|PubMed:17237508}; Peripheral membrane protein CC {ECO:0000269|PubMed:17237508}. Note=Nuclear translocation occurs under CC nitrogen and glucose starvation conditions (PubMed:25869125). CC {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 domain CC (AID) inhibits kinase activity of the protein kinase domain (KD) CC (PubMed:19474788, PubMed:20823513). The AID is sequestered by SNF4 CC within the AMP-activated protein kinase complex which might correspond CC 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 AID CC dampens kinase activation, probably by restraining SNF1-SNF4 CC associations (PubMed:25869125). Moreover, the UBA domain influences CC life span in a FKH1- and FKH2-dependent mechanism (PubMed:25869125). CC {ECO:0000269|PubMed:25869125}. CC -!- PTM: Phosphorylation at Thr-210 in response to glucose limitation leads CC to activation of kinase activity (PubMed:11486005, PubMed:12748292). CC ADP, but not AMP, protects the enzyme from dephosphorylation at Thr-210 CC by GLC7 (PubMed:22019086). {ECO:0000269|PubMed:12748292, CC ECO:0000269|PubMed:22019086}. CC -!- PTM: Sumoylation by the SUMO (E3) ligase MMS21 leads to inhibition by CC interaction of SUMO attached to Lys-549 with a SUMO-interacting CC sequence motif located near the active site of SNF1, and by targeting CC SNF1 for glucose-induced destruction via the SLX5-SLX8 (SUMO-directed) CC ubiquitin ligase (PubMed:24108357). {ECO:0000269|PubMed:24108357}. CC -!- MISCELLANEOUS: Present with 589 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr CC 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 AlphaFoldDB; P06782; -. DR SMR; P06782; -. DR BioGRID; 32529; 863. DR ComplexPortal; CPX-231; Snf1 protein kinase complex variant GAL83. DR ComplexPortal; CPX-232; Snf1 protein kinase complex variant SIP1. DR ComplexPortal; CPX-2800; Snf1 protein kinase complex variant SIP2. DR DIP; DIP-18N; -. DR IntAct; P06782; 55. DR MINT; P06782; -. DR STRING; 4932.YDR477W; -. DR iPTMnet; P06782; -. DR MaxQB; P06782; -. DR PaxDb; 4932-YDR477W; -. DR PeptideAtlas; P06782; -. DR EnsemblFungi; YDR477W_mRNA; YDR477W; YDR477W. DR GeneID; 852088; -. DR KEGG; sce:YDR477W; -. DR AGR; SGD:S000002885; -. DR SGD; S000002885; SNF1. DR VEuPathDB; FungiDB:YDR477W; -. DR eggNOG; KOG0583; Eukaryota. DR GeneTree; ENSGT00940000167424; -. DR HOGENOM; CLU_000288_59_3_1; -. DR InParanoid; P06782; -. DR OMA; SKTKWHF; -. DR OrthoDB; 5475340at2759; -. DR BioCyc; YEAST:G3O-30003-MONOMER; -. DR BRENDA; 2.7.11.1; 984. DR Reactome; R-SCE-1632852; Macroautophagy. DR Reactome; R-SCE-163680; AMPK inhibits chREBP transcriptional activation activity. DR Reactome; R-SCE-200425; Carnitine metabolism. DR Reactome; R-SCE-380972; Energy dependent regulation of mTOR by LKB1-AMPK. DR BioGRID-ORCS; 852088; 6 hits in 13 CRISPR screens. DR EvolutionaryTrace; P06782; -. DR PRO; PR:P06782; -. DR Proteomes; UP000002311; Chromosome IV. DR RNAct; P06782; Protein. DR GO; GO:0000144; C:cellular bud neck septin ring; IDA:SGD. DR GO; GO:0005737; C:cytoplasm; IDA:SGD. DR GO; GO:0005739; C:mitochondrion; HDA: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:0005774; C:vacuolar membrane; IDA:SGD. DR GO; GO:0004679; F:AMP-activated protein kinase activity; IMP:SGD. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:SGD. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0140677; F:molecular function activator activity; EXP:DisProt. DR GO; GO:0004672; F:protein kinase activity; HDA:SGD. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. 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:0000132; P:establishment of mitotic spindle orientation; IMP:SGD. DR GO; GO:0030447; P:filamentous growth; IMP:ComplexPortal. 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:0017148; P:negative regulation of translation; IMP:SGD. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. 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:2000222; P:positive regulation of pseudohyphal growth; IMP:SGD. DR GO; GO:1904547; P:regulation of cellular response to glucose starvation; EXP:ComplexPortal. DR GO; GO:2000217; P:regulation of invasive growth in response to glucose limitation; IMP:ComplexPortal. DR GO; GO:0034976; P:response to endoplasmic reticulum stress; 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; cd12122; AMPKA_C; 1. DR CDD; cd14079; STKc_AMPK_alpha; 1. DR CDD; cd14334; UBA_SNF1_fungi; 1. DR DisProt; DP02769; -. DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1. DR Gene3D; 3.30.310.80; Kinase associated domain 1, KA1; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR032270; AMPK_C. DR InterPro; IPR028375; KA1/Ssp2_C. DR InterPro; IPR011009; Kinase-like_dom_sf. 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 PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1. DR PANTHER; PTHR24346:SF82; SERINE_THREONINE-PROTEIN KINASE MARK-A-RELATED; 1. 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; KA1-like; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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; Cytoplasm; KW Direct protein sequencing; Isopeptide bond; Kinase; Membrane; KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; KW Serine/threonine-protein kinase; Transferase; Ubl conjugation. FT CHAIN 1..633 FT /note="Carbon catabolite-derepressing protein kinase" FT /id="PRO_0000086670" FT DOMAIN 55..306 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000269|PubMed:16236260, ECO:0000269|PubMed:16531232" FT DOMAIN 348..389 FT /note="UBA" FT /evidence="ECO:0000269|PubMed:25869125" FT REGION 1..46 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 313..392 FT /note="Auto-inhibitory domain (AID)" FT /evidence="ECO:0000269|PubMed:17851534, FT ECO:0000269|PubMed:19474788" FT REGION 317..345 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 409..434 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..15 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 16..33 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 318..341 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 409..424 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 177 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 61..69 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 84 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 210 FT /note="Phosphothreonine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:11486005, FT ECO:0000269|PubMed:12748292, ECO:0000269|PubMed:22019086, FT ECO:0000269|PubMed:26394309, ECO:0000269|PubMed:7905477" FT MOD_RES 413 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198" FT MOD_RES 487 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 632 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT CROSSLNK 461 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0007744|PubMed:22106047" FT CROSSLNK 549 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000269|PubMed:24108357" FT MUTAGEN 53 FT /note="G->R: Exhibits greater activity than wild-type SNFl FT in an immune complex assay where other associated molecules FT are present, but exhibits the same activity in a protein FT blot assay." FT /evidence="ECO:0000269|PubMed:1468623" FT MUTAGEN 84 FT /note="K->R: Inactivates the kinase activity without FT affecting protein levels." FT /evidence="ECO:0000269|PubMed:11486005, FT ECO:0000269|PubMed:2557546" FT MUTAGEN 210 FT /note="T->A: Inactivates the kinase activity without FT affecting protein levels." FT /evidence="ECO:0000269|PubMed:11486005, FT ECO:0000269|PubMed:1468623" FT MUTAGEN 357 FT /note="G->A: Alters kinase activation and biological FT activity, including enhanced allosteric subunit FT associations and increased oxidative stress resistance and FT life span; when associated with I-367." FT /evidence="ECO:0000269|PubMed:25869125" FT MUTAGEN 367 FT /note="L->I: Alters kinase activation and biological FT activity, including enhanced allosteric subunit FT associations and increased oxidative stress resistance and FT life span; when associated with A-357." FT /evidence="ECO:0000269|PubMed:25869125" FT MUTAGEN 549 FT /note="K->R: Decreases sumoylation of SNF1." FT /evidence="ECO:0000269|PubMed:24108357" FT STRAND 56..62 FT /evidence="ECO:0007829|PDB:3HYH" FT HELIX 64..66 FT /evidence="ECO:0007829|PDB:3MN3" FT STRAND 69..73 FT /evidence="ECO:0007829|PDB:3HYH" FT TURN 75..77 FT /evidence="ECO:0007829|PDB:3HYH" FT STRAND 80..87 FT /evidence="ECO:0007829|PDB:3HYH" FT HELIX 88..91 FT /evidence="ECO:0007829|PDB:3DAE" FT HELIX 97..109 FT /evidence="ECO:0007829|PDB:3HYH" FT STRAND 118..123 FT /evidence="ECO:0007829|PDB:3HYH" FT STRAND 125..133 FT /evidence="ECO:0007829|PDB:3HYH" FT HELIX 139..145 FT /evidence="ECO:0007829|PDB:3HYH" FT HELIX 151..170 FT /evidence="ECO:0007829|PDB:3HYH" FT TURN 180..182 FT /evidence="ECO:0007829|PDB:3HYH" FT STRAND 183..185 FT /evidence="ECO:0007829|PDB:3HYH" FT STRAND 191..193 FT /evidence="ECO:0007829|PDB:3HYH" FT TURN 207..209 FT /evidence="ECO:0007829|PDB:3MN3" FT HELIX 215..217 FT /evidence="ECO:0007829|PDB:3MN3" FT HELIX 220..223 FT /evidence="ECO:0007829|PDB:3HYH" FT STRAND 224..227 FT /evidence="ECO:0007829|PDB:3HYH" FT HELIX 232..247 FT /evidence="ECO:0007829|PDB:3HYH" FT HELIX 257..266 FT /evidence="ECO:0007829|PDB:3HYH" FT HELIX 277..286 FT /evidence="ECO:0007829|PDB:3HYH" FT HELIX 291..293 FT /evidence="ECO:0007829|PDB:3HYH" FT HELIX 297..302 FT /evidence="ECO:0007829|PDB:3HYH" FT HELIX 304..307 FT /evidence="ECO:0007829|PDB:3HYH" FT HELIX 312..314 FT /evidence="ECO:0007829|PDB:3HYH" FT TURN 317..319 FT /evidence="ECO:0007829|PDB:3MN3" FT HELIX 471..473 FT /evidence="ECO:0007829|PDB:3T4N" FT HELIX 475..485 FT /evidence="ECO:0007829|PDB:3T4N" FT HELIX 489..492 FT /evidence="ECO:0007829|PDB:3T4N" FT STRAND 506..511 FT /evidence="ECO:0007829|PDB:3T4N" FT HELIX 515..529 FT /evidence="ECO:0007829|PDB:3T4N" FT STRAND 532..534 FT /evidence="ECO:0007829|PDB:3T4N" FT HELIX 538..540 FT /evidence="ECO:0007829|PDB:3T4N" FT STRAND 543..548 FT /evidence="ECO:0007829|PDB:3T4N" FT STRAND 565..576 FT /evidence="ECO:0007829|PDB:3T4N" FT STRAND 579..590 FT /evidence="ECO:0007829|PDB:3T4N" FT HELIX 607..610 FT /evidence="ECO:0007829|PDB:2QLV" FT HELIX 613..628 FT /evidence="ECO:0007829|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 //