BAIT

TPK1

PKA1, SRA3, cAMP-dependent protein kinase catalytic subunit TPK1, L000002045, YJL164C
cAMP-dependent protein kinase catalytic subunit; promotes vegetative growth in response to nutrients via the Ras-cAMP signaling pathway; inhibited by regulatory subunit Bcy1p in the absence of cAMP; phosphorylates and inhibits Whi3p to promote G1/S phase passage; partially redundant with Tpk2p and Tpk3p; phosphorylates pre-Tom40p, which impairs its import into mitochondria under non-respiratory conditions; TPK1 has a paralog, TPK3, that arose from the whole genome duplication
Kinome Project (Sc)
GO Process (3)
GO Function (2)
GO Component (3)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)
PREY

VHS2

YIL135C
Regulator of septin dynamics; involved in the regulation of septin dynamics at bud neck after mitotic entry, likely by stabilizing septin structure; regulated at post-translational level by cell cycle dependent phosphorylation; likely phosphorylated by Cdc28p and dephosphorylated by Cdc14p before cytokinesis; high-copy suppressor of synthetic lethality of sis2 sit4 double mutant; VHS2 has a paralog, MLF3, that arose from the whole genome duplication
GO Process (1)
GO Function (0)
GO Component (1)

Gene Ontology Biological Process

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

Curated By

  • BioGRID