BAIT

KNS1

serine/threonine protein kinase KNS1, L124, L000000910, YLL019C
Protein kinase involved in negative regulation of PolIII transcription; effector kinase of the TOR signaling pathway and phosphorylates Rpc53p to regulate ribosome and tRNA biosynthesis; member of the LAMMER family of protein kinases, which are serine/threonine kinases also capable of phosphorylating tyrosine residues; capable of autophosphorylation
Kinome Project (Sc)
Saccharomyces cerevisiae (S288c)
PREY

ATG1

APG1, AUT3, CVT10, serine/threonine protein kinase ATG1, L000003955, S000028502, L000004761, YGL180W
Protein serine/threonine kinase; required for vesicle formation in autophagy and the cytoplasm-to-vacuole targeting (Cvt) pathway; structurally required for phagophore assembly site formation; during autophagy forms a complex with Atg13p and Atg17p; essential for cell cycle progression from G2/M to G1 under nitrogen starvation
Kinome Project (Sc)
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

Global analysis of protein phosphorylation in yeast.

Ptacek J, Devgan G, Michaud G, Zhu H, Zhu X, Fasolo J, Guo H, Jona G, Breitkreutz A, Sopko R, McCartney RR, Schmidt MC, Rachidi N, Lee SJ, Mah AS, Meng L, Stark MJ, Stern DF, De Virgilio C, Tyers M, Andrews B, Gerstein M, Schweitzer B, Predki PF, Snyder M

Protein phosphorylation is estimated to affect 30% of the proteome and is a major regulatory mechanism that controls many basic cellular processes. Until recently, our biochemical understanding of protein phosphorylation on a global scale has been extremely limited; only one half of the yeast kinases have known in vivo substrates and the phosphorylating kinase is known for less than 160 ... [more]

Nature Dec. 01, 2005; 438(7068);679-84 [Pubmed: 16319894]

Throughput

  • High Throughput

Additional Notes

  • 32P incorporation on protein chip

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
KNS1 ATG1
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-0.1567BioGRID
2148144

Curated By

  • BioGRID