BAIT

YCK2

serine/threonine protein kinase YCK2, L000002501, YNL154C
Palmitoylated plasma membrane-bound casein kinase I (CK1) isoform; shares redundant functions with Yck1p in morphogenesis, proper septin assembly, endocytic trafficking, and glucose sensing; stabilized by Sod1p binding in the presence of glucose and oxygen, causing glucose repression of respiratory metabolism; YCK2 has a paralog, YCK1, that arose from the whole genome duplication
Kinome Project (Sc)
GO Process (4)
GO Function (2)
GO Component (3)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

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