BAIT

TPK3

cAMP-dependent protein kinase catalytic subunit TPK3, L000002327, YKL166C
cAMP-dependent protein kinase catalytic subunit; promotes vegetative growth in response to nutrients via the Ras-cAMP signaling pathway; partially redundant with Tpk1p and Tpk2p; localizes to P-bodies during stationary phase; TPK3 has a paralog, TPK1, 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

APN1

DNA-(apurinic or apyrimidinic site) lyase APN1, L000000096, YKL114C
Major apurinic/apyrimidinic endonuclease; 3'-repair diesterase; involved in repair of DNA damage by oxidation and alkylating agents; also functions as a 3'-5' exonuclease to repair 7,8-dihydro-8-oxodeoxyguanosine; genetically interacts with NTG1 to maintain mitochondrial genome integrity
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

Curated By

  • BioGRID