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YEAST:SNF1

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Contents

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_010765.1
PDB 2FH9
2QLV
3DAE
3HYH
3MN3
3T4N
3TDH
3TE5
PDBsum 2FH9
2QLV
3DAE
3HYH
3MN3
3T4N
3TDH
3TE5
ProteinModelPortal P06782
SMR P06782
DIP DIP-18N
IntAct P06782
MINT MINT-364314
STRING P06782
PeptideAtlas P06782
EnsemblFungi YDR477W
GeneID 852088
KEGG sce:YDR477W
NMPDR fig|4932.3.peg.1538
CYGD YDR477w
SGD S000002885
eggNOG fuNOG05716
GeneTree EFGT00070000008711
HOGENOM HBG755340
OMA SKIGILP
OrthoDB EOG4Q5CXQ
BRENDA 2.7.11.1
NextBio 970409
ArrayExpress P06782
Genevestigator P06782
GermOnline YDR477W
GO GO:0031588
GO:0000324
GO:0005739
GO:0005641
GO:0031965
GO:0004679
GO:0005524
GO:0005515
GO:0042710
GO:0005975
GO:0007155
GO:0006995
GO:0001403
GO:0017148
GO:0045722
GO:0007124
GO:0001302
GO:0007165
InterPro IPR011009
IPR000719
IPR017441
IPR017442
IPR008271
IPR002290
IPR013896
KO K12761
Pfam PF00069
PF08587
SMART SM00220
SUPFAM SSF56112
PROSITE PS00107
PS50011
PS00108

Annotations

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0000166

nucleotide binding

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0547

F

Seeded From UniProt

GO:0000324

fungal-type vacuole

PMID:11331606[1]

IPI: Inferred from Physical Interaction

C

Seeded From UniProt

GO:0001302

replicative cell aging

PMID:10921902[2]

IGI: Inferred from Genetic Interaction

SGD:S000002830

P

Seeded From UniProt

GO:0001302

replicative cell aging

PMID:10921902[2]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

GO:0001403

invasive growth in response to glucose limitation

PMID:11095711[3]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

GO:0001403

invasive growth in response to glucose limitation

PMID:12556493[4]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

GO:0004672

protein kinase activity

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000719

F

Seeded From UniProt

GO:0004672

protein kinase activity

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR002290

F

Seeded From UniProt

GO:0004674

protein serine/threonine kinase activity

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR008271

F

Seeded From UniProt

GO:0004674

protein serine/threonine kinase activity

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR013896

F

Seeded From UniProt

GO:0004674

protein serine/threonine kinase activity

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0723

F

Seeded From UniProt

GO:0004679

AMP-activated protein kinase activity

PMID:11486005[5]

IMP: Inferred from Mutant Phenotype

F

Seeded From UniProt

GO:0004679

AMP-activated protein kinase activity

PMID:2557546[6]

IDA: Inferred from Direct Assay

F

Seeded From UniProt

GO:0004679

AMP-activated protein kinase activity

PMID:7913470[7]

IMP: Inferred from Mutant Phenotype

F

Seeded From UniProt

GO:0005515

protein binding

PMID:11283351[8]

IPI: Inferred from Physical Interaction

UniProtKB:Q04739

F

Seeded From UniProt

GO:0005515

protein binding

PMID:11805826[9]

IPI: Inferred from Physical Interaction

UniProtKB:P34164

F

Seeded From UniProt

GO:0005515

protein binding

PMID:16260785[10]

IPI: Inferred from Physical Interaction

UniProtKB:P12904

F

Seeded From UniProt

GO:0005515

protein binding

PMID:20489023[11]

IPI: Inferred from Physical Interaction

UniProtKB:P22211

F

Seeded From UniProt

GO:0005515

protein binding

PMID:20489023[11]

IPI: Inferred from Physical Interaction

UniProtKB:Q00684

F

Seeded From UniProt

GO:0005524

ATP binding

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000719

F

Seeded From UniProt

GO:0005524

ATP binding

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR002290

F

Seeded From UniProt

GO:0005524

ATP binding

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR017441

F

Seeded From UniProt

GO:0005524

ATP binding

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0067

F

Seeded From UniProt

GO:0005634

nucleus

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0539

C

Seeded From UniProt

GO:0005634

nucleus

PMID:11331606[1]

IPI: Inferred from Physical Interaction

C

Seeded From UniProt

GO:0005634

nucleus

PMID:17237508[12]

IDA: Inferred from Direct Assay

C

Seeded From UniProt

GO:0005641

nuclear envelope lumen

PMID:17237508[12]

IDA: Inferred from Direct Assay

C

Seeded From UniProt

GO:0005737

cytoplasm

PMID:11331606[1]

IPI: Inferred from Physical Interaction

C

Seeded From UniProt

GO:0005737

cytoplasm

PMID:17237508[12]

IDA: Inferred from Direct Assay

C

Seeded From UniProt

GO:0005739

mitochondrion

PMID:14576278[13]

IDA: Inferred from Direct Assay

C

Seeded From UniProt

GO:0005739

mitochondrion

PMID:16823961[14]

IDA: Inferred from Direct Assay

C

Seeded From UniProt

GO:0005975

carbohydrate metabolic process

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0119

P

Seeded From UniProt

GO:0006109

regulation of carbohydrate metabolic process

PMID:12167649[15]

IGI: Inferred from Genetic Interaction

P

Seeded From UniProt

GO:0006468

protein phosphorylation

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000719

P

Seeded From UniProt

GO:0006468

protein phosphorylation

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR002290

P

Seeded From UniProt

GO:0006468

protein phosphorylation

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR008271

P

Seeded From UniProt

GO:0006468

protein phosphorylation

PMID:11486005[5]

IDA: Inferred from Direct Assay

P

Seeded From UniProt

GO:0006995

cellular response to nitrogen starvation

PMID:12024013[16]

IDA: Inferred from Direct Assay

P

Seeded From UniProt

GO:0007124

pseudohyphal growth

PMID:12024013[16]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

GO:0007155

cell adhesion

PMID:12556493[4]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

GO:0007165

signal transduction

PMID:10322167[17]

TAS: Traceable Author Statement

P

Seeded From UniProt

GO:0016020

membrane

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0472

C

Seeded From UniProt

GO:0016301

kinase activity

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0418

F

Seeded From UniProt

GO:0016310

phosphorylation

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0418

P

Seeded From UniProt

GO:0016740

transferase activity

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0808

F

Seeded From UniProt

GO:0016772

transferase activity, transferring phosphorus-containing groups

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR011009

F

Seeded From UniProt

GO:0017148

negative regulation of translation

PMID:18955495[18]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

GO:0031588

AMP-activated protein kinase complex

PMID:12393914[19]

IDA: Inferred from Direct Assay

C

Seeded From UniProt

GO:0031588

AMP-activated protein kinase complex

PMID:2481228[20]

IDA: Inferred from Direct Assay

C

Seeded From UniProt

GO:0031588

AMP-activated protein kinase complex

PMID:2481228[20]

IPI: Inferred from Physical Interaction

SGD:S000003083

C

Seeded From UniProt

GO:0031965

nuclear membrane

GO_REF:0000023

IEA: Inferred from Electronic Annotation

SP_SL:SL-0182

C

Seeded From UniProt

GO:0042710

biofilm formation

PMID:12024013[16]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

GO:0045722

positive regulation of gluconeogenesis

PMID:8628258[21]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

GO:0045722

positive regulation of gluconeogenesis

PMID:8710504[22]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

GO:0045722

positive regulation of gluconeogenesis

PMID:9111319[23]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

GO:0009758

carbohydrate utilization

PMID:7040163[24]

IMP: Inferred from Mutant Phenotype

P

Table 4

complete

Notes

References

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

  1. 1.0 1.1 1.2 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
  2. 2.0 2.1 Ashrafi K et al. (2000) Sip2p and its partner snf1p kinase affect aging in S. cerevisiae. Genes Dev 14: 1872-85 PubMed GONUTS page
  3. 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
  4. 4.0 4.1 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
  5. 5.0 5.1 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
  6. 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
  7. 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
  8. Ito T et al. (2001) A comprehensive two-hybrid analysis to explore the yeast protein interactome. Proc Natl Acad Sci U S A 98: 4569-74 PubMed GONUTS page
  9. Gavin AC et al. (2002) Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature 415: 141-7 PubMed GONUTS page
  10. Metz J et al. (2006) The yeast Arr4p ATPase binds the chloride transporter Gef1p when copper is available in the cytosol. J Biol Chem 281: 410-7 PubMed GONUTS page
  11. 11.0 11.1 Breitkreutz A et al. (2010) A global protein kinase and phosphatase interaction network in yeast. Science 328: 1043-6 PubMed GONUTS page
  12. 12.0 12.1 12.2 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
  13. Sickmann A et al. (2003) The proteome of Saccharomyces cerevisiae mitochondria. Proc Natl Acad Sci U S A 100: 13207-12 PubMed GONUTS page
  14. 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
  15. Young ET et al. (2002) Snf1 protein kinase regulates Adr1 binding to chromatin but not transcription activation. J Biol Chem 277: 38095-103 PubMed GONUTS page
  16. 16.0 16.1 16.2 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
  17. Carlson M (1999) Glucose repression in yeast. Curr Opin Microbiol 2: 202-7 PubMed GONUTS page
  18. 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
  19. 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. 20.0 20.1 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
  21. 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
  22. 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
  23. 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
  24. Carlson M et al. (1981) Mutants of yeast defective in sucrose utilization. Genetics 98: 25-40 PubMed GONUTS page
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