BAIT

KSP1

putative serine/threonine protein kinase KSP1, L000000921, YHR082C
Serine/threonine protein kinase; associates with TORC1 and likely involved in TOR signaling cascades; negative regulator of autophagy; nuclear translocation required for haploid filamentous growth; regulates filamentous growth induced nuclear translocation of Bcy1p, Fus3p, and Sks1p; overproduction causes allele-specific suppression of prp20-10; protein abundance increases in response to DNA replication stress
Kinome Project (Sc)
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