YEAST:SNF1

Species (Taxon ID)	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s)	SNF1 (synonyms: CAT1, CCR1, GLC2, PAS14)
Protein Name(s)	Carbon catabolite-derepressing protein kinase
External Links
UniProt	P06782
EMBL	M13971 U33050 BK006938
PIR	A26030
RefSeq	NP_010765.3
PDB	2FH9 2QLV 3DAE 3HYH 3MN3 3T4N 3TDH 3TE5
PDBsum	2FH9 2QLV 3DAE 3HYH 3MN3 3T4N 3TDH 3TE5
ProteinModelPortal	P06782
SMR	P06782
BioGrid	32529
DIP	DIP-18N
IntAct	P06782
MINT	MINT-364314
STRING	4932.YDR477W
MaxQB	P06782
PaxDb	P06782
PeptideAtlas	P06782
EnsemblFungi	[example_ID YDR477W]
GeneID	852088
KEGG	sce:YDR477W
CYGD	YDR477w
SGD	S000002885
eggNOG	COG0515
GeneTree	ENSGT00760000118892
HOGENOM	HOG000233016
InParanoid	P06782
KO	K12761
OMA	MSSFSAY
OrthoDB	EOG793BK1
BioCyc	YEAST:G3O-30003-MONOMER
BRENDA	2.7.11.1
Reactome	REACT_209479 REACT_212098 REACT_254023 REACT_260529
EvolutionaryTrace	P06782
NextBio	970409
Proteomes	UP000002311
Genevestigator	P06782
GO	GO:0031588 GO:0005737 GO:0000324 GO:0005641 GO:0031965 GO:0005634 GO:0004679 GO:0005524 GO:0004674 GO:0005975 GO:0007155 GO:0006995 GO:0071940 GO:0001403 GO:0017148 GO:1900436 GO:0045722 GO:0006468 GO:0007124 GO:0006109 GO:0001302 GO:0090606
InterPro	IPR028375 IPR011009 IPR000719 IPR017441 IPR002290 IPR008271 IPR013896
Pfam	PF00069 PF08587
SMART	SM00220
SUPFAM	SSF103243 SSF56112
PROSITE	PS00107 PS50011 PS00108

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0009758	carbohydrate utilization	PMID:7040163^[1]	ECO:0000315			P		Table 4	complete
involved_in	GO:0000132	establishment of mitotic spindle orientation	PMID:29643469^[2]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000001762 SGD:S000006190	P	happens_during:(GO:0000089)	Seeded From UniProt	complete
involved_in	GO:0000132	establishment of mitotic spindle orientation	PMID:29643469^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	happens_during:(GO:0000089)	Seeded From UniProt	complete
part_of	GO:0000144	cellular bud neck septin ring	PMID:29643469^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:16823961^[3]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	PMID:16319894^[4]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:14576278^[5]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	PMID:16319894^[4]	ECO:0007005	high throughput direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:2000222	positive regulation of pseudohyphal growth	PMID:12024013^[6]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000000270,SGD:S000002450	P		Seeded From UniProt	complete
involved_in	GO:2000222	positive regulation of pseudohyphal growth	PMID:16980405^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	PMID:27524664^[8]	ECO:0000314	direct assay evidence used in manual assertion		P	has_direct_input:(UniProtKB:P27705)	Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	PMID:27524664^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_direct_input:(UniProtKB:P27705)	Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:27524664^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:P27705)	Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:27524664^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	has_direct_input:(UniProtKB:P27705)	Seeded From UniProt	complete
involved_in	GO:0016239	positive regulation of macroautophagy	PMID:11486014^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006986	response to unfolded protein	PMID:25730376^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0005086	ARF guanyl-nucleotide exchange factor activity	PMID:26198097^[11]	ECO:0000314	direct assay evidence used in manual assertion		F	has_regulation_target:(UniProtKB:P40994) happens_during:(GO:0042149)	Seeded From UniProt	complete
involved_in	GO:1900436	positive regulation of filamentous growth of a population of unicellular organisms in response to starvation	PMID:22904036^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0071940	fungal-type cell wall assembly	PMID:24486034^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	happens_during:(GO:0033554)	Seeded From UniProt	complete
involved_in	GO:0045722	positive regulation of gluconeogenesis	PMID:8628258^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045722	positive regulation of gluconeogenesis	PMID:9111319^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045722	positive regulation of gluconeogenesis	PMID:8710504^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0090606	single-species surface biofilm formation	PMID:12024013^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0031588	nucleotide-activated protein kinase complex	PMID:9121458^[17]	ECO:0000353	physical interaction evidence used in manual assertion	SGD:S000000829 SGD:S000002830 SGD:S000003083 SGD:S000003176	C		Seeded From UniProt	complete
part_of	GO:0031588	nucleotide-activated protein kinase complex	PMID:2481228^[18]	ECO:0000353	physical interaction evidence used in manual assertion	SGD:S000003083	C		Seeded From UniProt	complete
part_of	GO:0031588	nucleotide-activated protein kinase complex	PMID:2481228^[18]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0031588	nucleotide-activated protein kinase complex	PMID:12393914^[19]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0017148	negative regulation of translation	PMID:18955495^[20]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000000735 SGD:S000001905 SGD:S000002691	P		Seeded From UniProt	complete
involved_in	GO:0017148	negative regulation of translation	PMID:18955495^[20]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007155	cell adhesion	PMID:12556493^[21]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:2000222	positive regulation of pseudohyphal growth	PMID:12024013^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006995	cellular response to nitrogen starvation	PMID:12024013^[6]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	PMID:11486005^[22]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:17237508^[23]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005641	nuclear envelope lumen	PMID:17237508^[23]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:17237508^[23]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004679	AMP-activated protein kinase activity	PMID:7913470^[24]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004679	AMP-activated protein kinase activity	PMID:2557546^[25]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004679	AMP-activated protein kinase activity	PMID:11486005^[22]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:7913470^[24]	ECO:0000314	direct assay evidence used in manual assertion		F	happens_during:(GO:0042149)	Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:2557546^[25]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:P06782)	Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:11486005^[22]	ECO:0000314	direct assay evidence used in manual assertion		F	has_input:(UniProtKB:P27705) happens_during:(GO:0042149)	Seeded From UniProt	complete
involved_in	GO:0001403	invasive growth in response to glucose limitation	PMID:11095711^[26]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0001403	invasive growth in response to glucose limitation	PMID:12556493^[21]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0001302	replicative cell aging	PMID:10921902^[27]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000002830	P		Seeded From UniProt	complete
involved_in	GO:0001302	replicative cell aging	PMID:10921902^[27]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0000324	fungal-type vacuole	PMID:11331606^[28]	ECO:0000353	physical interaction evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0035556	intracellular signal transduction	PMID:21873635^[29]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:104754 MGI:MGI:2445031 PANTHER:PTN000678822 UniProtKB:P57059 UniProtKB:Q9H0K1 UniProtKB:Q9IA88	P		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	PMID:21873635^[29]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0023169 FB:FBgn0261278 MGI:MGI:104754 MGI:MGI:1202065 MGI:MGI:1336173 MGI:MGI:1347352 MGI:MGI:1351488 MGI:MGI:1923020 MGI:MGI:2445031 MGI:MGI:3037705 PANTHER:PTN000678822 RGD:1359167 RGD:3387 RGD:620545 RGD:620893 RGD:69407 RGD:69653 SGD:S000000931 SGD:S000001531 SGD:S000001584 SGD:S000002529 SGD:S000002885 SGD:S000004086 SGD:S000005127 TAIR:locus:2094672 UniProtKB:O60285 UniProtKB:P57059 UniProtKB:Q13131 UniProtKB:Q6SA08 UniProtKB:Q8IWQ3 UniProtKB:Q8IY84 UniProtKB:Q8TDC3 UniProtKB:Q9BXA6 UniProtKB:Q9BXA7 UniProtKB:Q9H093 UniProtKB:Q9H0K1 UniProtKB:Q9IA88 UniProtKB:Q9NRH2	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21873635^[29]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:104754 MGI:MGI:106924 MGI:MGI:1347559 MGI:MGI:2145955 MGI:MGI:2445031 PANTHER:PTN000678822 PomBase:SPAC23H4.02 PomBase:SPBC32C12.03c PomBase:SPCC297.03 PomBase:SPCC74.03c RGD:3387 RGD:620893 SGD:S000000601 SGD:S000000931 SGD:S000001124 SGD:S000001651 SGD:S000002885 SGD:S000003820 SGD:S000005127 SGD:S000006062 TAIR:locus:2009812 TAIR:locus:2032075 TAIR:locus:2140104 TAIR:locus:2174999 UniProtKB:O14757 UniProtKB:O60285 UniProtKB:P57059 UniProtKB:Q39192 UniProtKB:Q57YE4 UniProtKB:Q7XQP4 UniProtKB:Q8I3C7 UniProtKB:Q8IWQ3 UniProtKB:Q8TDC3 UniProtKB:Q940H6 UniProtKB:Q9IA88 WB:WBGene00002210 WB:WBGene00003919 WB:WBGene00020142 WB:WBGene00021012	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21873635^[29]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0023169 FB:FBgn0261278 MGI:MGI:104754 MGI:MGI:1202065 MGI:MGI:1336173 MGI:MGI:2145955 MGI:MGI:2445031 PANTHER:PTN000678822 PomBase:SPAC23H4.02 PomBase:SPBC19C2.05 PomBase:SPCC74.03c RGD:69407 RGD:69653 SGD:S000001124 SGD:S000002885 SGD:S000003820 SGD:S000005947 TAIR:locus:2009812 TAIR:locus:2032075 TAIR:locus:2140104 TAIR:locus:2159597 TAIR:locus:2160559 TAIR:locus:2174999 UniProtKB:O14757 UniProtKB:O60285 UniProtKB:P43291 UniProtKB:P57059 UniProtKB:Q39192 UniProtKB:Q5N942 UniProtKB:Q7XQP4 UniProtKB:Q8TDC3 UniProtKB:Q940H6 WB:WBGene00002210	C		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:21873635^[29]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0025625 MGI:MGI:104754 MGI:MGI:106924 MGI:MGI:1336173 MGI:MGI:1347559 MGI:MGI:1923020 MGI:MGI:2445031 MGI:MGI:2685946 PANTHER:PTN000678822 PomBase:SPAC57A10.02 PomBase:SPAC644.06c PomBase:SPBC19C2.05 PomBase:SPBC4F6.06 PomBase:SPCC1020.10 PomBase:SPCC297.03 PomBase:SPCC74.03c RGD:1359167 RGD:1563268 RGD:1566256 RGD:3387 RGD:620893 RGD:69407 RGD:69653 SGD:S000000931 SGD:S000001531 SGD:S000001584 SGD:S000002529 SGD:S000002885 SGD:S000004086 SGD:S000005127 SGD:S000005759 TAIR:locus:2009812 TAIR:locus:2094672 TAIR:locus:2102132 UniProtKB:O14757 UniProtKB:O60285 UniProtKB:P57059 UniProtKB:Q14680 UniProtKB:Q6SA08 UniProtKB:Q8IWQ3 UniProtKB:Q8IY84 UniProtKB:Q8TDC3 UniProtKB:Q96PF2 UniProtKB:Q9BXA6 UniProtKB:Q9BXA7 UniProtKB:Q9H093 UniProtKB:Q9H0K1 UniProtKB:Q9IA88 UniProtKB:Q9NRH2 UniProtKB:Q9STV4 WB:WBGene00003919	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:19474788^[30]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P06782	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:16531232^[31]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P06782	F		Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719 InterPro:IPR008271	F		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR013896	F		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719 InterPro:IPR017441	F		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719 InterPro:IPR008271	P		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0723	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F		Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F		Seeded From UniProt	complete
enables	GO:0016301	kinase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0418	F		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C		Seeded From UniProt	complete
involved_in	GO:0016310	phosphorylation	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0418	P		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C		Seeded From UniProt	complete
involved_in	GO:0005975	carbohydrate metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0119	P		Seeded From UniProt	complete
part_of	GO:0031965	nuclear membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0182	C		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Carlson, M et al. (1981) Mutants of yeast defective in sucrose utilization. Genetics 98 25-40 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 Tripodi, F et al. (2018) Snf1/AMPK is involved in the mitotic spindle alignment in Saccharomyces cerevisiae. Sci Rep 8 5853 PubMed GONUTS page
↑ Reinders, J et al. (2006) Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics. J. Proteome Res. 5 1543-54 PubMed GONUTS page
↑ ^4.0 ^4.1 Ptacek, J et al. (2005) Global analysis of protein phosphorylation in yeast. Nature 438 679-84 PubMed GONUTS page
↑ Sickmann, A et al. (2003) The proteome of Saccharomyces cerevisiae mitochondria. Proc. Natl. Acad. Sci. U.S.A. 100 13207-12 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 ^6.3 Kuchin, S et al. (2002) Snf1 protein kinase and the repressors Nrg1 and Nrg2 regulate FLO11, haploid invasive growth, and diploid pseudohyphal differentiation. Mol. Cell. Biol. 22 3994-4000 PubMed GONUTS page
↑ Orlova, M et al. (2006) Nitrogen availability and TOR regulate the Snf1 protein kinase in Saccharomyces cerevisiae. Eukaryotic Cell 5 1831-7 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 ^8.3 McCartney, RR et al. (2016) Activation and inhibition of Snf1 kinase activity by phosphorylation within the activation loop. Biochim. Biophys. Acta 1864 1518-28 PubMed GONUTS page
↑ Wang, Z et al. (2001) Antagonistic controls of autophagy and glycogen accumulation by Snf1p, the yeast homolog of AMP-activated protein kinase, and the cyclin-dependent kinase Pho85p. Mol. Cell. Biol. 21 5742-52 PubMed GONUTS page
↑ Ferrer-Dalmau, J et al. (2015) Protein kinase Snf1 is involved in the proper regulation of the unfolded protein response in Saccharomyces cerevisiae. Biochem. J. 468 33-47 PubMed GONUTS page
↑ Hsu, JW et al. (2015) Snf1/AMP-activated protein kinase activates Arf3p to promote invasive yeast growth via a non-canonical GEF domain. Nat Commun 6 7840 PubMed GONUTS page
↑ Karunanithi, S & Cullen, PJ (2012) The filamentous growth MAPK Pathway Responds to Glucose Starvation Through the Mig1/2 transcriptional repressors in Saccharomyces cerevisiae. Genetics 192 869-87 PubMed GONUTS page
↑ Backhaus, K et al. (2013) Mutations in SNF1 complex genes affect yeast cell wall strength. Eur. J. Cell Biol. 92 383-95 PubMed GONUTS page
↑ Lesage, P et al. (1996) 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 1921-8 PubMed GONUTS page
↑ Randez-Gil, F et al. (1997) Glucose derepression of gluconeogenic enzymes in Saccharomyces cerevisiae correlates with phosphorylation of the gene activator Cat8p. Mol. Cell. Biol. 17 2502-10 PubMed GONUTS page
↑ Rahner, A et al. (1996) Dual influence of the yeast Cat1p (Snf1p) protein kinase on carbon source-dependent transcriptional activation of gluconeogenic genes by the regulatory gene CAT8. Nucleic Acids Res. 24 2331-7 PubMed GONUTS page
↑ Jiang, R & Carlson, M (1997) 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 2099-106 PubMed GONUTS page
↑ ^18.0 ^18.1 Celenza, JL et al. (1989) 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 5045-54 PubMed GONUTS page
↑ Nath, N et al. (2002) Purification and characterization of Snf1 kinase complexes containing a defined Beta subunit composition. J. Biol. Chem. 277 50403-8 PubMed GONUTS page
↑ ^20.0 ^20.1 Shirra, MK et al. (2008) A chemical genomics study identifies Snf1 as a repressor of GCN4 translation. J. Biol. Chem. 283 35889-98 PubMed GONUTS page
↑ ^21.0 ^21.1 Vyas, VK et al. (2003) Snf1 kinases with different beta-subunit isoforms play distinct roles in regulating haploid invasive growth. Mol. Cell. Biol. 23 1341-8 PubMed GONUTS page
↑ ^22.0 ^22.1 ^22.2 McCartney, RR & Schmidt, MC (2001) 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 36460-6 PubMed GONUTS page
↑ ^23.0 ^23.1 ^23.2 Sarma, NJ et al. (2007) Glucose-responsive regulators of gene expression in Saccharomyces cerevisiae function at the nuclear periphery via a reverse recruitment mechanism. Genetics 175 1127-35 PubMed GONUTS page
↑ ^24.0 ^24.1 Woods, A et al. (1994) Yeast SNF1 is functionally related to mammalian AMP-activated protein kinase and regulates acetyl-CoA carboxylase in vivo. J. Biol. Chem. 269 19509-15 PubMed GONUTS page
↑ ^25.0 ^25.1 Celenza, JL & Carlson, M (1989) Mutational analysis of the Saccharomyces cerevisiae SNF1 protein kinase and evidence for functional interaction with the SNF4 protein. Mol. Cell. Biol. 9 5034-44 PubMed GONUTS page
↑ Cullen, PJ & Sprague, GF Jr (2000) Glucose depletion causes haploid invasive growth in yeast. Proc. Natl. Acad. Sci. U.S.A. 97 13619-24 PubMed GONUTS page
↑ ^27.0 ^27.1 Ashrafi, K et al. (2000) Sip2p and its partner snf1p kinase affect aging in S. cerevisiae. Genes Dev. 14 1872-85 PubMed GONUTS page
↑ Vincent, O et al. (2001) Subcellular localization of the Snf1 kinase is regulated by specific beta subunits and a novel glucose signaling mechanism. Genes Dev. 15 1104-14 PubMed GONUTS page
↑ ^29.0 ^29.1 ^29.2 ^29.3 ^29.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Chen, L et al. (2009) Structural insight into the autoinhibition mechanism of AMP-activated protein kinase. Nature 459 1146-9 PubMed GONUTS page
↑ Nayak, V et al. (2006) Structure and dimerization of the kinase domain from yeast Snf1, a member of the Snf1/AMPK protein family. Structure 14 477-85 PubMed GONUTS page

[PMID:7040163-1] Carlson, M et al. (1981) Mutants of yeast defective in sucrose utilization. Genetics 98 25-40 PubMed GONUTS page

[PMID:29643469-2] 2.0 ^2.1 ^2.2 Tripodi, F et al. (2018) Snf1/AMPK is involved in the mitotic spindle alignment in Saccharomyces cerevisiae. Sci Rep 8 5853 PubMed GONUTS page

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YEAST:SNF1

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