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Carbon catabolite-derepressing protein kinase (EC 2.7.11.1) (Sucrose nonfermentating protein 1)

 SNF1_YEAST              Reviewed;         633 AA.
P06782; D6VTA0;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-JAN-1988, sequence version 1.
12-SEP-2018, entry version 207.
RecName: Full=Carbon catabolite-derepressing protein kinase {ECO:0000303|PubMed:3526554};
EC=2.7.11.1 {ECO:0000269|PubMed:15719021, ECO:0000269|PubMed:2557546, ECO:0000269|PubMed:3526554};
AltName: Full=Sucrose nonfermentating protein 1 {ECO:0000303|PubMed:6366512};
Name=SNF1 {ECO:0000303|PubMed:6366512};
Synonyms=CAT1, CCR1 {ECO:0000303|PubMed:1944227}, GLC2, PAS14;
OrderedLocusNames=YDR477W; ORFNames=D8035.20;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=3526554; DOI=10.1126/science.3526554;
Celenza J.L., Carlson M.;
"A yeast gene that is essential for release from glucose repression
encodes a protein kinase.";
Science 233:1175-1180(1986).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
PROTEIN SEQUENCE OF 274-284; 528-539 AND 622-630, AND PHOSPHORYLATION
AT THR-210.
PubMed=7905477;
Mitchelhill K.I., Stapleton D., Gao G., House C., Michell B.,
Katsis F., Witters L.A., Kemp B.E.;
"Mammalian AMP-activated protein kinase shares structural and
functional homology with the catalytic domain of yeast Snf1 protein
kinase.";
J. Biol. Chem. 269:2361-2364(1994).
[5]
IDENTIFICATION, AND FUNCTION.
PubMed=6366512; DOI=10.1128/MCB.4.1.49;
Celenza J.L., Carlson M.;
"Cloning and genetic mapping of SNF1, a gene required for expression
of glucose-repressible genes in Saccharomyces cerevisiae.";
Mol. Cell. Biol. 4:49-53(1984).
[6]
INDUCTION.
PubMed=6366513; DOI=10.1128/MCB.4.1.54;
Celenza J.L., Carlson M.;
"Structure and expression of the SNF1 gene of Saccharomyces
cerevisiae.";
Mol. Cell. Biol. 4:54-60(1984).
[7]
FUNCTION.
PubMed=3049551; DOI=10.1128/jb.170.10.4838-4845.1988;
Bisson L.F.;
"High-affinity glucose transport in Saccharomyces cerevisiae is under
general glucose repression control.";
J. Bacteriol. 170:4838-4845(1988).
[8]
MUTAGENESIS OF LYS-84, CATALYTIC ACTIVITY, INTERACTION WITH SNF4, AND
ACTIVITY REGULATION.
PubMed=2557546; DOI=10.1128/MCB.9.11.5034;
Celenza J.L., Carlson M.;
"Mutational analysis of the Saccharomyces cerevisiae SNF1 protein
kinase and evidence for functional interaction with the SNF4
protein.";
Mol. Cell. Biol. 9:5034-5044(1989).
[9]
INTERACTION WITH SNF4.
PubMed=2481228; DOI=10.1128/MCB.9.11.5045;
Celenza J.L., Eng F.J., Carlson M.;
"Molecular analysis of the SNF4 gene of Saccharomyces cerevisiae:
evidence for physical association of the SNF4 protein with the SNF1
protein kinase.";
Mol. Cell. Biol. 9:5045-5054(1989).
[10]
FUNCTION.
PubMed=1944227; DOI=10.1007/BF00267461;
Denis C.L., Audino D.C.;
"The CCR1 (SNF1) and SCH9 protein kinases act independently of cAMP-
dependent protein kinase and the transcriptional activator ADR1 in
controlling yeast ADH2 expression.";
Mol. Gen. Genet. 229:395-399(1991).
[11]
FUNCTION.
PubMed=8289797; DOI=10.1128/MCB.14.2.1160;
Ulery T.L., Jang S.H., Jaehning J.A.;
"Glucose repression of yeast mitochondrial transcription: kinetics of
derepression and role of nuclear genes.";
Mol. Cell. Biol. 14:1160-1170(1994).
[12]
MUTAGENESIS OF GLY-53 AND THR-210.
PubMed=1468623;
Estruch F., Treitel M.A., Yang X., Carlson M.;
"N-terminal mutations modulate yeast SNF1 protein kinase function.";
Genetics 132:639-650(1992).
[13]
INTERACTION WITH SIP1; SIP2 AND GAL83.
PubMed=7813428;
Yang X., Jiang R., Carlson M.;
"A family of proteins containing a conserved domain that mediates
interaction with the yeast SNF1 protein kinase complex.";
EMBO J. 13:5878-5886(1994).
[14]
FUNCTION, AND INTERACTION WITH SIP4.
PubMed=8628258; DOI=10.1128/MCB.16.5.1921;
Lesage P., Yang X., Carlson M.;
"Yeast SNF1 protein kinase interacts with SIP4, a C6 zinc cluster
transcriptional activator: a new role for SNF1 in the glucose
response.";
Mol. Cell. Biol. 16:1921-1928(1996).
[15]
INTERACTION WITH SNF4; SIP1; SIP2 AND GAL83.
PubMed=9121458; DOI=10.1128/MCB.17.4.2099;
Jiang R., Carlson M.;
"The Snf1 protein kinase and its activating subunit, Snf4, interact
with distinct domains of the Sip1/Sip2/Gal83 component in the kinase
complex.";
Mol. Cell. Biol. 17:2099-2106(1997).
[16]
PHOSPHORYLATION AT THR-210, AND MUTAGENESIS OF LYS-84 AND THR-210.
PubMed=11486005; DOI=10.1074/jbc.M104418200;
McCartney R.R., Schmidt M.C.;
"Regulation of Snf1 kinase. Activation requires phosphorylation of
threonine 210 by an upstream kinase as well as a distinct step
mediated by the Snf4 subunit.";
J. Biol. Chem. 276:36460-36466(2001).
[17]
PHOSPHORYLATION AT THR-210, AND INTERACTION WITH SAK1.
PubMed=12748292; DOI=10.1128/MCB.23.11.3909-3917.2003;
Nath N., McCartney R.R., Schmidt M.C.;
"Yeast Pak1 kinase associates with and activates Snf1.";
Mol. Cell. Biol. 23:3909-3917(2003).
[18]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[19]
FUNCTION IN PHOSPHORYLATION OF CAT8.
PubMed=15121831; DOI=10.1128/MCB.24.10.4083-4091.2004;
Charbon G., Breunig K.D., Wattiez R., Vandenhaute J., Noel-Georis I.;
"Key role of Ser562/661 in Snf1-dependent regulation of Cat8p in
Saccharomyces cerevisiae and Kluyveromyces lactis.";
Mol. Cell. Biol. 24:4083-4091(2004).
[20]
FUNCTION IN PHOSPHORYLATION OF HISTONE H3, AND IDENTIFICATION IN THE
SNF1 KINASE COMPLEX.
PubMed=15719021; DOI=10.1038/sj.emboj.7600577;
Lo W.-S., Gamache E.R., Henry K.W., Yang D., Pillus L., Berger S.L.;
"Histone H3 phosphorylation can promote TBP recruitment through
distinct promoter-specific mechanisms.";
EMBO J. 24:997-1008(2005).
[21]
INTERACTION WITH CTK1.
PubMed=16182287; DOI=10.1016/j.febslet.2005.08.057;
Van Driessche B., Coddens S., Van Mullem V., Vandenhaute J.;
"Glucose deprivation mediates interaction between CTDK-I and Snf1 in
Saccharomyces cerevisiae.";
FEBS Lett. 579:5318-5324(2005).
[22]
PHOSPHORYLATION, AND INTERACTION WITH SAK1.
PubMed=16847059; DOI=10.1074/jbc.M603811200;
Elbing K., Rubenstein E.M., McCartney R.R., Schmidt M.C.;
"Subunits of the Snf1 kinase heterotrimer show interdependence for
association and activity.";
J. Biol. Chem. 281:26170-26180(2006).
[23]
SUBCELLULAR LOCATION.
PubMed=17237508; DOI=10.1534/genetics.106.068932;
Sarma N.J., Haley T.M., Barbara K.E., Buford T.D., Willis K.A.,
Santangelo G.M.;
"Glucose-responsive regulators of gene expression in Saccharomyces
cerevisiae function at the nuclear periphery via a reverse recruitment
mechanism.";
Genetics 175:1127-1135(2007).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413 AND SER-487, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413 AND SER-632, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[27]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-461, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
[28]
SUMOYLATION AT LYS-549 BY MMS21, AND MUTAGENESIS OF LYS-549.
PubMed=24108357; DOI=10.1073/pnas.1304839110;
Simpson-Lavy K.J., Johnston M.;
"Sumoylation regulates the SNF1 protein kinase.";
Proc. Natl. Acad. Sci. U.S.A. 110:17432-17437(2013).
[29]
FUNCTION.
PubMed=25730376; DOI=10.1042/BJ20140734;
Ferrer-Dalmau J., Randez-Gil F., Marquina M., Prieto J.A.,
Casamayor A.;
"Protein kinase Snf1 is involved in the proper regulation of the
unfolded protein response in Saccharomyces cerevisiae.";
Biochem. J. 468:33-47(2015).
[30]
DOMAIN, MUTAGENESIS OF GLY-357 AND LEU-367, FUNCTION, AND SUBCELLULAR
LOCATION.
PubMed=25869125; DOI=10.1074/jbc.M115.647032;
Jiao R., Postnikoff S., Harkness T.A., Arnason T.G.;
"The SNF1 kinase ubiquitin-associated domain restrains its activation,
activity, and the yeast life span.";
J. Biol. Chem. 290:15393-15404(2015).
[31]
FUNCTION, AND INTERACTION WITH CYR1.
PubMed=26309257; DOI=10.1074/jbc.M115.658005;
Nicastro R., Tripodi F., Gaggini M., Castoldi A., Reghellin V.,
Nonnis S., Tedeschi G., Coccetti P.;
"Snf1 phosphorylates adenylate cyclase and negatively regulates
protein kinase A-dependent transcription in Saccharomyces
cerevisiae.";
J. Biol. Chem. 290:24715-24726(2015).
[32]
FUNCTION.
PubMed=25428989; DOI=10.1091/mbc.E14-06-1088;
DeMille D., Badal B.D., Evans J.B., Mathis A.D., Anderson J.F.,
Grose J.H.;
"PAS kinase is activated by direct SNF1-dependent phosphorylation and
mediates inhibition of TORC1 through the phosphorylation and
activation of Pbp1.";
Mol. Biol. Cell 26:569-582(2015).
[33]
FUNCTION.
PubMed=26667037; DOI=10.1128/MCB.00436-15;
Braun K.A., Dombek K.M., Young E.T.;
"Snf1-dependent transcription confers glucose-induced decay upon the
mRNA product.";
Mol. Cell. Biol. 36:628-644(2015).
[34]
FUNCTION, AND PHOSPHORYLATION AT THR-210.
PubMed=26394309; DOI=10.1371/journal.pgen.1005491;
Mizuno T., Masuda Y., Irie K.;
"The Saccharomyces cerevisiae AMPK, Snf1, negatively regulates the
Hog1 MAPK pathway in ER stress response.";
PLoS Genet. 11:E1005491-E1005491(2015).
[35]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 41-315, AND DOMAIN.
PubMed=16236260; DOI=10.1016/j.bbrc.2005.09.181;
Rudolph M.J., Amodeo G.A., Bai Y., Tong L.;
"Crystal structure of the protein kinase domain of yeast AMP-activated
protein kinase Snf1.";
Biochem. Biophys. Res. Commun. 337:1224-1228(2005).
[36]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 46-319, AND DOMAIN.
PubMed=16531232; DOI=10.1016/j.str.2005.12.008;
Nayak V., Zhao K., Wyce A., Schwartz M.F., Lo W.S., Berger S.L.,
Marmorstein R.;
"Structure and dimerization of the kinase domain from yeast Snf1, a
member of the Snf1/AMPK protein family.";
Structure 14:477-485(2006).
[37]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 460-630 IN COMPLEX WITH SNF4
AND SIP2, DOMAIN, AND ACTIVITY REGULATION.
PubMed=17851534; DOI=10.1038/nature06127;
Amodeo G.A., Rudolph M.J., Tong L.;
"Crystal structure of the heterotrimer core of Saccharomyces
cerevisiae AMPK homologue SNF1.";
Nature 449:492-495(2007).
[38]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 41-315, DOMAIN, AND
PHOSPHORYLATION AT THR-210.
PubMed=19474788; DOI=10.1038/nature08075;
Chen L., Jiao Z.H., Zheng L.S., Zhang Y.Y., Xie S.T., Wang Z.X.,
Wu J.W.;
"Structural insight into the autoinhibition mechanism of AMP-activated
protein kinase.";
Nature 459:1146-1149(2009).
[39]
X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 50-320, AND DOMAIN.
PubMed=20823513; DOI=10.1107/S1744309110028265;
Rudolph M.J., Amodeo G.A., Tong L.;
"An inhibited conformation for the protein kinase domain of the
Saccharomyces cerevisiae AMPK homolog Snf1.";
Acta Crystallogr. F 66:999-1002(2010).
[40]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 457-633, AND PHOSPHORYLATION
AT THR-210.
PubMed=22019086; DOI=10.1016/j.cmet.2011.09.009;
Mayer F.V., Heath R., Underwood E., Sanders M.J., Carmena D.,
McCartney R.R., Leiper F.C., Xiao B., Jing C., Walker P.A.,
Haire L.F., Ogrodowicz R., Martin S.R., Schmidt M.C., Gamblin S.J.,
Carling D.;
"ADP regulates SNF1, the Saccharomyces cerevisiae homolog of AMP-
activated protein kinase.";
Cell Metab. 14:707-714(2011).
-!- FUNCTION: Serine/threonine protein kinase essential for release
from glucose repression (PubMed:3526554, PubMed:6366512,
PubMed:3049551, PubMed:1944227, PubMed:8289797, PubMed:8628258,
PubMed:25869125). Catalytic subunit of the AMP-activated protein
kinase complex also known as the SNF1 kinase complex (Snf1c), a
central regulator of cellular energy homeostasis, which, in
response to a fall in intracellular ATP levels, activates energy-
producing pathways and inhibits energy-consuming processes
(PubMed:8289797, PubMed:26667037). The complex phosphorylates
histone H3 to form H3S10ph, which promotes H3K14ac formation,
leading to transcriptional activation through TBP recruitment to
the promoters (PubMed:15719021). The complex also negatively
regulates the HOG1 MAPK pathway in ER stress response including
unfolded protein response (UPR) (PubMed:25730376,
PubMed:26394309). Under nutrient/energy depletion, the complex
phosphorylates and activates PAS kinase PSK1 which in turn
activates PBS1, leading to the inhibition of the TORC1 signaling
pathway (PubMed:25428989). SNF1 also interacts and phosphorylates
adenylate cyclase CYR1 and negatively regulates the protein kinase
A signaling pathway (PubMed:26309257). Also phosphorylates and
regulates the transcriptional activator CAT8 (PubMed:15121831).
{ECO:0000269|PubMed:15121831, ECO:0000269|PubMed:15719021,
ECO:0000269|PubMed:1944227, ECO:0000269|PubMed:25428989,
ECO:0000269|PubMed:25730376, ECO:0000269|PubMed:25869125,
ECO:0000269|PubMed:26309257, ECO:0000269|PubMed:26394309,
ECO:0000269|PubMed:26667037, ECO:0000269|PubMed:3049551,
ECO:0000269|PubMed:3526554, ECO:0000269|PubMed:6366512,
ECO:0000269|PubMed:8289797, ECO:0000269|PubMed:8628258}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:15719021, ECO:0000269|PubMed:2557546,
ECO:0000269|PubMed:3526554}.
-!- ACTIVITY REGULATION: The kinase activity is positively regulated
by SNF4 via sequestration of the SNF1 auto-inhibitory domain (AID)
(PubMed:2557546, PubMed:17851534). {ECO:0000269|PubMed:17851534,
ECO:0000269|PubMed:2557546}.
-!- SUBUNIT: Component of the AMP-activated protein kinase complex
also known as the SNF1 kinase complex (Snf1c), an heterotrimeric
complex composed of an alpha subunit (SNF1), a regulatory subunit
beta (GAL83 and substoichiometric alternate beta subunits SIP1 and
SIP2), and a regulatory subunit gamma (SNF4) (PubMed:2557546,
PubMed:2481228, PubMed:7813428, PubMed:9121458, PubMed:15719021,
PubMed:17851534). Inrteracts with the transcriptional activator
SIP4 (PubMed:8628258). Interacts with SAK1 (PubMed:12748292,
PubMed:16847059). Interacts with CTK1 (PubMed:16182287): Interacts
with adenylate cyclase CYR1 (PubMed:26309257).
{ECO:0000269|PubMed:12748292, ECO:0000269|PubMed:15719021,
ECO:0000269|PubMed:16182287, ECO:0000269|PubMed:16847059,
ECO:0000269|PubMed:17851534, ECO:0000269|PubMed:2481228,
ECO:0000269|PubMed:2557546, ECO:0000269|PubMed:26309257,
ECO:0000269|PubMed:7813428, ECO:0000269|PubMed:8628258,
ECO:0000269|PubMed:9121458}.
-!- INTERACTION:
Self; NbExp=6; IntAct=EBI-17516, EBI-17516;
Q00684:CDC14; NbExp=2; IntAct=EBI-17516, EBI-4192;
Q04739:GAL83; NbExp=5; IntAct=EBI-17516, EBI-7244;
P22211:NPR1; NbExp=2; IntAct=EBI-17516, EBI-12207;
Q00816:REG1; NbExp=7; IntAct=EBI-17516, EBI-8270;
P38232:REG2; NbExp=3; IntAct=EBI-17516, EBI-14921;
P34164:SIP2; NbExp=11; IntAct=EBI-17516, EBI-17187;
P12904:SNF4; NbExp=21; IntAct=EBI-17516, EBI-17537;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25869125}.
Nucleus {ECO:0000269|PubMed:25869125}. Nucleus membrane
{ECO:0000269|PubMed:17237508}; Peripheral membrane protein
{ECO:0000269|PubMed:17237508}. Note=Nuclear translocation occurs
under nitrogen and glucose starvation conditions
(PubMed:25869125). {ECO:0000269|PubMed:25869125}.
-!- INDUCTION: Expression of the SNF1 gene itself is not glucose
repressible (PubMed:6366513). {ECO:0000269|PubMed:6366513}.
-!- DOMAIN: The regulatory domain (RS) also called auto-inhibitory
domain (AID) inhibits kinase activity of the protein kinase domain
(KD) (PubMed:19474788, PubMed:20823513). The AID is sequestered by
SNF4 within the AMP-activated protein kinase complex which might
correspond to the activated SNF1 form (PubMed:17851534).
{ECO:0000269|PubMed:17851534, ECO:0000269|PubMed:19474788,
ECO:0000269|PubMed:20823513}.
-!- DOMAIN: The ubiquitin-associated domain (UBA) localized within the
AID dampens kinase activation, probably by restraining SNF1-SNF4
associations (PubMed:25869125). Moreover, the UBA domain
influences life span in a FKH1- and FKH2-dependent mechanism
(PubMed:25869125). {ECO:0000269|PubMed:25869125}.
-!- PTM: Phosphorylation at Thr-210 in response to glucose limitation
leads to activation of kinase activity (PubMed:11486005,
PubMed:12748292). ADP, but not AMP, protects the enzyme from
dephosphorylation at Thr-210 by GLC7 (PubMed:22019086).
{ECO:0000269|PubMed:12748292, ECO:0000269|PubMed:22019086}.
-!- PTM: Sumoylation by the SUMO (E3) ligase MMS21 leads to inhibition
by interaction of SUMO attached to Lys-549 with a SUMO-interacting
sequence motif located near the active site of SNF1, and by
targeting SNF1 for glucose-induced destruction via the SLX5-SLX8
(SUMO-directed) ubiquitin ligase (PubMed:24108357).
{ECO:0000269|PubMed:24108357}.
-!- MISCELLANEOUS: Present with 589 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. SNF1 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M13971; AAA35058.1; -; Genomic_DNA.
EMBL; U33050; AAB64904.1; -; Genomic_DNA.
EMBL; BK006938; DAA12310.1; -; Genomic_DNA.
PIR; A26030; A26030.
RefSeq; NP_010765.3; NM_001180785.3.
PDB; 2FH9; X-ray; 2.80 A; A=46-319.
PDB; 2QLV; X-ray; 2.60 A; A/D=460-630.
PDB; 3DAE; X-ray; 2.90 A; A/B=41-315.
PDB; 3HYH; X-ray; 2.20 A; A/B=41-315.
PDB; 3MN3; X-ray; 2.38 A; A=50-320.
PDB; 3T4N; X-ray; 2.30 A; A=457-633.
PDB; 3TDH; X-ray; 2.30 A; A=457-633.
PDB; 3TE5; X-ray; 2.50 A; A=457-633.
PDBsum; 2FH9; -.
PDBsum; 2QLV; -.
PDBsum; 3DAE; -.
PDBsum; 3HYH; -.
PDBsum; 3MN3; -.
PDBsum; 3T4N; -.
PDBsum; 3TDH; -.
PDBsum; 3TE5; -.
ProteinModelPortal; P06782; -.
SMR; P06782; -.
BioGrid; 32529; 832.
ComplexPortal; CPX-231; Snf1 protein kinase complex variant GAL83.
ComplexPortal; CPX-232; Snf1 protein kinase complex variant SIP1.
ComplexPortal; CPX-2800; Snf1 protein kinase complex variant SIP2.
DIP; DIP-18N; -.
IntAct; P06782; 56.
MINT; P06782; -.
STRING; 4932.YDR477W; -.
iPTMnet; P06782; -.
MaxQB; P06782; -.
PaxDb; P06782; -.
PRIDE; P06782; -.
EnsemblFungi; YDR477W; YDR477W; YDR477W.
GeneID; 852088; -.
KEGG; sce:YDR477W; -.
EuPathDB; FungiDB:YDR477W; -.
SGD; S000002885; SNF1.
GeneTree; ENSGT00900000140868; -.
HOGENOM; HOG000233016; -.
InParanoid; P06782; -.
KO; K12761; -.
OMA; RWHFGIR; -.
OrthoDB; EOG092C0QJU; -.
BioCyc; YEAST:G3O-30003-MONOMER; -.
BRENDA; 2.7.11.1; 984.
Reactome; R-SCE-163680; AMPK inhibits chREBP transcriptional activation activity.
Reactome; R-SCE-165158; Activation of AKT2.
Reactome; R-SCE-199418; Negative regulation of the PI3K/AKT network.
Reactome; R-SCE-200425; Import of palmitoyl-CoA into the mitochondrial matrix.
Reactome; R-SCE-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
EvolutionaryTrace; P06782; -.
PRO; PR:P06782; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0000144; C:cellular bud neck septin ring; IDA:SGD.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0000324; C:fungal-type vacuole; IPI:SGD.
GO; GO:0005641; C:nuclear envelope lumen; IDA:SGD.
GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0031588; C:nucleotide-activated protein kinase complex; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0004679; F:AMP-activated protein kinase activity; IMP:SGD.
GO; GO:0005086; F:ARF guanyl-nucleotide exchange factor activity; IDA:SGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:SGD.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
GO; GO:0007155; P:cell adhesion; IMP:SGD.
GO; GO:0006995; P:cellular response to nitrogen starvation; IDA:SGD.
GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:SGD.
GO; GO:0071940; P:fungal-type cell wall assembly; IMP:SGD.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0001403; P:invasive growth in response to glucose limitation; IMP:SGD.
GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
GO; GO:0017148; P:negative regulation of translation; IMP:SGD.
GO; GO:1900436; P:positive regulation of filamentous growth of a population of unicellular organisms in response to starvation; IMP:SGD.
GO; GO:0045722; P:positive regulation of gluconeogenesis; IMP:SGD.
GO; GO:0016239; P:positive regulation of macroautophagy; IMP:SGD.
GO; GO:2000222; P:positive regulation of pseudohyphal growth; IMP:SGD.
GO; GO:0006468; P:protein phosphorylation; IDA:SGD.
GO; GO:0001302; P:replicative cell aging; IMP:SGD.
GO; GO:0006986; P:response to unfolded protein; IMP:SGD.
GO; GO:0090606; P:single-species surface biofilm formation; IMP:SGD.
CDD; cd14334; UBA_SNF1_fungi; 1.
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.
InterPro; IPR013896; SNF1_UBA.
Pfam; PF16579; AdenylateSensor; 1.
Pfam; PF00069; Pkinase; 1.
Pfam; PF08587; UBA_2; 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; ATP-binding; Carbohydrate metabolism; Complete proteome;
Cytoplasm; Direct protein sequencing; Isopeptide bond; Kinase;
Membrane; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Serine/threonine-protein kinase; Transferase;
Ubl conjugation.
CHAIN 1 633 Carbon catabolite-derepressing protein
kinase.
/FTId=PRO_0000086670.
DOMAIN 55 306 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159,
ECO:0000269|PubMed:16236260,
ECO:0000269|PubMed:16531232}.
DOMAIN 348 389 UBA. {ECO:0000269|PubMed:25869125}.
NP_BIND 61 69 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 313 392 Auto-inhibitory domain (AID).
{ECO:0000269|PubMed:17851534,
ECO:0000269|PubMed:19474788}.
COMPBIAS 18 32 Poly-His.
ACT_SITE 177 177 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 84 84 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 210 210 Phosphothreonine; by autocatalysis.
{ECO:0000269|PubMed:11486005,
ECO:0000269|PubMed:12748292,
ECO:0000269|PubMed:22019086,
ECO:0000269|PubMed:26394309,
ECO:0000269|PubMed:7905477}.
MOD_RES 413 413 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 487 487 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 632 632 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
CROSSLNK 461 461 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CROSSLNK 549 549 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:24108357}.
MUTAGEN 53 53 G->R: Exhibits greater activity than
wild-type SNFl in an immune complex assay
where other associated molecules are
present, but exhibits the same activity
in a protein blot assay.
{ECO:0000269|PubMed:1468623}.
MUTAGEN 84 84 K->R: Inactivates the kinase activity
without affecting protein levels.
{ECO:0000269|PubMed:11486005,
ECO:0000269|PubMed:2557546}.
MUTAGEN 210 210 T->A: Inactivates the kinase activity
without affecting protein levels.
{ECO:0000269|PubMed:11486005,
ECO:0000269|PubMed:1468623}.
MUTAGEN 357 357 G->A: Alters kinase activation and
biological activity, including enhanced
allosteric subunit associations and
increased oxidative stress resistance and
life span; when associated with I-367.
{ECO:0000269|PubMed:25869125}.
MUTAGEN 367 367 L->I: Alters kinase activation and
biological activity, including enhanced
allosteric subunit associations and
increased oxidative stress resistance and
life span; when associated with A-357.
{ECO:0000269|PubMed:25869125}.
MUTAGEN 549 549 K->R: Decreases sumoylation of SNF1.
{ECO:0000269|PubMed:24108357}.
STRAND 56 62 {ECO:0000244|PDB:3HYH}.
HELIX 64 66 {ECO:0000244|PDB:3MN3}.
STRAND 69 73 {ECO:0000244|PDB:3HYH}.
TURN 75 77 {ECO:0000244|PDB:3HYH}.
STRAND 80 87 {ECO:0000244|PDB:3HYH}.
HELIX 88 91 {ECO:0000244|PDB:3DAE}.
HELIX 97 109 {ECO:0000244|PDB:3HYH}.
STRAND 118 123 {ECO:0000244|PDB:3HYH}.
STRAND 125 133 {ECO:0000244|PDB:3HYH}.
HELIX 139 145 {ECO:0000244|PDB:3HYH}.
HELIX 151 170 {ECO:0000244|PDB:3HYH}.
TURN 180 182 {ECO:0000244|PDB:3HYH}.
STRAND 183 185 {ECO:0000244|PDB:3HYH}.
STRAND 191 193 {ECO:0000244|PDB:3HYH}.
TURN 207 209 {ECO:0000244|PDB:3MN3}.
HELIX 215 217 {ECO:0000244|PDB:3MN3}.
HELIX 220 223 {ECO:0000244|PDB:3HYH}.
STRAND 224 227 {ECO:0000244|PDB:3HYH}.
HELIX 232 247 {ECO:0000244|PDB:3HYH}.
HELIX 257 266 {ECO:0000244|PDB:3HYH}.
HELIX 277 286 {ECO:0000244|PDB:3HYH}.
HELIX 291 293 {ECO:0000244|PDB:3HYH}.
HELIX 297 302 {ECO:0000244|PDB:3HYH}.
HELIX 304 307 {ECO:0000244|PDB:3HYH}.
HELIX 312 314 {ECO:0000244|PDB:3HYH}.
TURN 317 319 {ECO:0000244|PDB:3MN3}.
HELIX 471 473 {ECO:0000244|PDB:3T4N}.
HELIX 475 485 {ECO:0000244|PDB:3T4N}.
HELIX 489 492 {ECO:0000244|PDB:3T4N}.
STRAND 506 511 {ECO:0000244|PDB:3T4N}.
HELIX 515 529 {ECO:0000244|PDB:3T4N}.
STRAND 532 534 {ECO:0000244|PDB:3T4N}.
HELIX 538 540 {ECO:0000244|PDB:3T4N}.
STRAND 543 548 {ECO:0000244|PDB:3T4N}.
STRAND 565 576 {ECO:0000244|PDB:3T4N}.
STRAND 579 590 {ECO:0000244|PDB:3T4N}.
HELIX 607 610 {ECO:0000244|PDB:2QLV}.
HELIX 613 628 {ECO:0000244|PDB:3T4N}.
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


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