BAIT

SSK2

mitogen-activated protein kinase kinase kinase SSK2, L000002826, YNR031C
MAP kinase kinase kinase of HOG1 mitogen-activated signaling pathway; interacts with Ssk1p, leading to autophosphorylation and activation of Ssk2p which phosphorylates Pbs2p; also mediates actin cytoskeleton recovery from osmotic stress; a HOG-independent function of Ssk2p mediates the calcium-sensitive phenotype of the ptp2 msg5 double disruptant; SSK2 has a paralog, SSK22, that arose from the whole genome duplication
Saccharomyces cerevisiae (S288c)
PREY

BUD27

URI1, S000007647, YFL023W
Unconventional prefoldin protein involved in translation initiation; required for correct assembly of RNAP I, II, and III in an Rpb5p-dependent manner; shuttles between nucleus and cytoplasm; mutants have inappropriate expression of nutrient sensitive genes due to translational derepression of Gcn4p transcription factor; diploid mutants show random budding; ortholog of human URI/RMP
GO Process (4)
GO Function (0)
GO Component (2)
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