BAIT

NPR1

serine/threonine protein kinase NPR1, L000001273, YNL183C
Protein kinase; stabilizes several plasma membrane amino acid transporters by antagonizing their ubiquitin-mediated degradation; phosphorylates Aly2p; negatively regulates Ldb19p-mediated endocytosis through phosphorylation of Ldb19p, which prevents its association with the plasma membrane; Npr1p activity is negatively regulated via phosphorylation by the TOR complex; NPR1 has a paralog, PRR2, that arose from the whole genome duplication
Kinome Project (Sc)
Saccharomyces cerevisiae (S288c)
PREY

YAR1

L000002496, YPL239W
Ankyrin-repeat containing, nucleocytoplasmic shuttling chaperone; prevents aggregation of Rps3p in the cytoplasm, associates with free Rps3p in the cytoplasm and delivers it to the 90S in the nucleus; required for 40S ribosomal subunit export, biogenesis and adaptation to osmotic and oxidative stress; expression repressed by heat shock
GO Process (5)
GO Function (1)
GO Component (2)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)

Reconstituted Complex

An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.

Publication

Diverse protein kinase interactions identified by protein microarrays reveal novel connections between cellular processes.

Fasolo J, Sboner A, Sun MG, Yu H, Chen R, Sharon D, Kim PM, Gerstein M, Snyder M

Protein kinases are key regulators of cellular processes. In spite of considerable effort, a full understanding of the pathways they participate in remains elusive. We globally investigated the proteins that interact with the majority of yeast protein kinases using protein microarrays. Eighty-five kinases were purified and used to probe yeast proteome microarrays. One-thousand-twenty-three interactions were identified, and the vast majority ... [more]

Genes Dev. Apr. 01, 2011; 25(7);767-78 [Pubmed: 21460040]

Throughput

  • High Throughput

Additional Notes

  • High Throughput: Proteome microarrays were used to identify proteins that interact with protein kinases.

Curated By

  • BioGRID