BAIT

PRR2

serine/threonine protein kinase PRR2, YDL214C

Serine/threonine protein kinase; inhibits pheromone induced signalling downstream of MAPK, possibly at the level of the Ste12p transcription factor; mutant has increased aneuploidy tolerance; PRR2 has a paralog, NPR1, that arose from the whole genome duplication

Kinome Project (Sc)

GO Process (3)

GO Function (2)

GO Component (0)

Gene Ontology Biological Process

negative regulation of conjugation with cellular fusion [IGI, IMP]

negative regulation of transcription from RNA polymerase II promoter by pheromones [IGI, IMP]

protein phosphorylation [IDA]

Gene Ontology Molecular Function

protein kinase activity [IDA]
protein serine/threonine kinase activity [ISS]

SGD Alliance of Genome Resources Entrez Gene RefSeq UniprotKB

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

integral component of membrane [ISM]

SGD Alliance of Genome Resources Entrez Gene RefSeq UniprotKB

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

Interaction Summary