BAIT

RCK1

putative serine/threonine protein kinase RCK1, L000001592, YGL158W
Protein kinase involved in the response to oxidative stress; identified as suppressor of S. pombe cell cycle checkpoint mutations; RCK1 has a paralog, RCK2, that arose from the whole genome duplication
GO Process (2)
GO Function (2)
GO Component (0)
Saccharomyces cerevisiae (S288c)
PREY

UBP10

DOT4, L000004391, L000004588, YNL186W
Ubiquitin-specific protease, deubiquitinates Ub-protein moieties; interacts with proteins that function in rRNA production and ribosome biogenesis; stabilizes Rpa190p, the largest subunit of RNAP I, by mediating its deubiquitination; controls PCNA deubiquitylation; may regulate silencing by acting on Sir4p; involved in posttranscriptionally regulating Gap1p and possibly other transporters; localized to the nucleolus; human USP36 is a functional analog of Ubp10p
GO Process (3)
GO Function (1)
GO Component (2)

Gene Ontology Molecular Function

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

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
RCK1 UBP10
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

High-BioGRID
521200

Curated By

  • BioGRID