BAIT

IKS1

protein kinase IKS1, L000004209, YJL057C
Protein kinase of unknown cellular role; putative serine/threonine kinase; expression is induced during mild heat stress; deletion mutants are hypersensitive to copper sulphate and resistant to sorbate; interacts with an N-terminal fragment of Sst2p
GO Process (1)
GO Function (1)
GO Component (0)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Saccharomyces cerevisiae (S288c)
PREY

RTR1

YER139C
CTD phosphatase; dephosphorylates S5-P in the C-terminal domain of Rpo21p; has a cysteine-rich motif required for function and conserved in eukaryotes; shuttles between the nucleus and cytoplasm; RTR1 has a paralog, RTR2, that arose from the whole genome duplication
GO Process (2)
GO Function (1)
GO Component (2)

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