BAIT

SNF1

CAT1, CCR1, GLC2, HAF3, PAS14, AMP-activated serine/threonine-protein kinase catalytic subunit SNF1, L000001944, YDR477W
AMP-activated serine/threonine protein kinase; found in a complex containing Snf4p and members of the Sip1p/Sip2p/Gal83p family; required for transcription of glucose-repressed genes, thermotolerance, sporulation, and peroxisome biogenesis; involved in regulation of the nucleocytoplasmic shuttling of Hxk2p; regulates filamentous growth in response to starvation; SUMOylation by Mms21p inhibits its function and targets Snf1p for destruction via the Slx5-Slx8 Ubiquitin ligase
Saccharomyces cerevisiae (S288c)
PREY

SCH9

HRM2, KOM1, serine/threonine protein kinase SCH9, L000001810, YHR205W
AGC family protein kinase; functional ortholog of mammalian S6 kinase; phosphorylated by Tor1p and required for TORC1-mediated regulation of ribosome biogenesis, translation initiation, and entry into G0 phase; involved in transactivation of osmostress-responsive genes; regulates G1 progression, cAPK activity and nitrogen activation of the FGM pathway; integrates nutrient signals and stress signals from sphingolipids to regulate lifespan
Saccharomyces cerevisiae (S288c)

Biochemical Activity (Phosphorylation)

An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation.

Publication

Acetylation of yeast AMPK controls intrinsic aging independently of caloric restriction.

Lu JY, Lin YY, Sheu JC, Wu JT, Lee FJ, Chen Y, Lin MI, Chiang FT, Tai TY, Berger SL, Zhao Y, Tsai KS, Zhu H, Chuang LM, Boeke JD

Acetylation of histone and nonhistone proteins is an important posttranslational modification affecting many cellular processes. Here, we report that NuA4 acetylation of Sip2, a regulatory β subunit of the Snf1 complex (yeast AMP-activated protein kinase), decreases as cells age. Sip2 acetylation, controlled by antagonizing NuA4 acetyltransferase and Rpd3 deacetylase, enhances interaction with Snf1, the catalytic subunit of Snf1 complex. Sip2-Snf1 ... [more]

Cell Sep. 16, 2011; 146(6);969-79 [Pubmed: 21906795]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
SNF1 SCH9
Biochemical Activity
Biochemical Activity

An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation.

High-BioGRID
200483
SCH9 SNF1
Negative Genetic
Negative Genetic

Mutations/deletions in separate genes, each of which alone causes a minimal phenotype, but when combined in the same cell results in a more severe fitness defect or lethality under a given condition. This term is reserved for high or low throughput studies with scores.

High-0.25BioGRID
2130221

Curated By

  • BioGRID