BAIT

SLT2

BYC2, LYT2, MPK1, SLK2, mitogen-activated serine/threonine-protein kinase SLT2, L000001919, YHR030C
Serine/threonine MAP kinase; involved in regulating maintenance of cell wall integrity, cell cycle progression, and nuclear mRNA retention in heat shock; required for mitophagy and pexophagy; affects recruitment of mitochondria to phagophore assembly site (PAS); plays a role in adaptive response of cells to cold; regulated by the PKC1-mediated signaling pathway; SLT2 has a paralog, KDX1, that arose from the whole genome duplication
Saccharomyces cerevisiae (S288c)
PREY

RPA34

CST21, DNA-directed RNA polymerase I subunit RPA34, A34.5, L000004132, L000003000, S000029123, YJL148W
RNA polymerase I subunit A34.5; essential for nucleolar assembly and for high polymerase loading rate; nucleolar localization depends on Rpa49p
Saccharomyces cerevisiae (S288c)

Reconstituted Complex

An interaction is detected between purified proteins in vitro.

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