BAIT

KIN28

TFIIH complex serine/threonine-protein kinase subunit KIN28, L000000905, YDL108W
Serine/threonine protein kinase, subunit of transcription factor TFIIH; involved in transcription initiation at RNA polymerase II promoters; phosphorylates Ser5 residue of the PolII C-terminal domain (CTD) at gene promoters; relocalizes to the cytosol in response to hypoxia
Saccharomyces cerevisiae (S288c)
PREY

RPP2B

RPL45, YPA1, ribosomal protein P2B, YP2beta, P2B, L45, L000001736, YDR382W
Ribosomal protein P2 beta; a component of the ribosomal stalk, which is involved in the interaction between translational elongation factors and the ribosome; free (non-ribosomal) P2 stimulates the phosphorylation of the eIF2 alpha subunit (Sui2p) by Gcn2p; regulates the accumulation of P1 (Rpp1Ap and Rpp1Bp) in the cytoplasm
GO Process (2)
GO Function (2)
GO Component (1)
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