BAIT

PHO85

LDB15, cyclin-dependent serine/threonine-protein kinase PHO85, phoU, L000001431, YPL031C
Cyclin-dependent kinase; has ten cyclin partners; involved in regulating the cellular response to nutrient levels and environmental conditions and progression through the cell cycle
Kinome Project (Sc)
Saccharomyces cerevisiae (S288c)
PREY

ALY1

ART6, YKR021W
Alpha arrestin, substrate of calcineurin; controls nutrient-mediated intracellular sorting of permease Gap1p; interacts with AP-1 subunit Apl4p; dephosphorylation of Aly1p required for the endocytosis of Dip5p; may regulate endocytosis of plasma membrane proteins by recruiting ubiquitin ligase Rsp5p to plasma membrane targets; ALY1 has a paralog, ALY2, that arose from the whole genome duplication
Kinome Project (Sc)
UPS Project
GO Process (4)
GO Function (1)
GO Component (3)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

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
  • complex with PHO80

Curated By

  • BioGRID