BAIT

KIN82

FPK2, putative serine/threonine protein kinase KIN82, L000000906, YCR091W
Putative serine/threonine protein kinase; implicated in the regulation of phospholipid asymmetry through the activation of phospholipid translocases (flippases); involved in the phosphorylation of upstream inhibitory kinase Ypk1p along with Fpk1p; has a redundant role in the cellular response to mating pheromone; KIN82 has a paralog, FPK1, that arose from the whole genome duplication
Kinome Project (Sc)
GO Process (3)
GO Function (1)
GO Component (0)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Saccharomyces cerevisiae (S288c)
PREY

PRM7

YDL038C, pheromone-regulated protein PRM7, YDL039C
Pheromone-regulated protein; predicted to have one transmembrane segment; promoter contains Gcn4p binding elements
GO Process (0)
GO Function (0)
GO Component (1)

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

  • Low Throughput

Curated By

  • BioGRID