BAIT

SPS1

putative serine/threonine protein kinase SPS1, L000002024, YDR523C
Putative protein serine/threonine kinase; expressed at the end of meiosis and localized to the prospore membrane; required for correct localization of enzymes involved in spore wall synthesis
GO Process (3)
GO Function (2)
GO Component (3)
Saccharomyces cerevisiae (S288c)
PREY

DOM34

ribosome dissociation factor DOM34, L000000517, YNL001W
Protein that facilitates ribosomal subunit dissociation; Dom34-Hbs1 complex and Rli1p have roles in dissociating inactive ribosomes to facilitate translation restart, particularly ribosomes stalled in 3' UTRs; required for RNA cleavage in no-go decay, but reports conflict on endonuclease activity; Pelota ortholog; protein abundance increases in response to DNA replication stress; DOM34 has a paralog, YCL001W-B, that arose from the whole genome duplication
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