BAIT

IPL1

PAC15, aurora kinase, L000000871, YPL209C
Aurora kinase of conserved chromosomal passenger complex; mediates release on mono-oriented kinetochores from microtubules in meiosis I, also release of kinetochores from cluster at SPBs at meiosis exit; helps maintain condensed chromosomes during anaphase, early telophase; required for SPB cohesion and prevention of multipolar spindle formation; Iocalizes to nuclear foci that diffuse upon DNA replication stress; required for inhibition of karyopherin Pse1p upon SAC arrest
Kinome Project (Sc)
Saccharomyces cerevisiae (S288c)
PREY

RRP5

L000003232, YMR229C
RNA binding protein involved in synthesis of both 18S and 5.8S rRNAs; component of both the ribosomal small subunit (SSU) processosome and the 90S preribosome; acts as part of a Mak21p-Noc2p-Rrp5p module that associates with nascent pre-rRNA during transcription and has a role in bigenesis of the large ribosomal subunit; has binding preference for single stranded tracts of U's; relocalizes from nucleolus to nucleus upon DNA replication stress
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

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
IPL1 RRP5
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

High-BioGRID
520598

Curated By

  • BioGRID