BAIT

CDC15

LYT1, serine/threonine protein kinase CDC15, L000000255, YAR019C
Protein kinase of the Mitotic Exit Network; localized to the spindle pole bodies at late anaphase; promotes mitotic exit by directly switching on the kinase activity of Dbf2p; required for spindle disassembly after meiosis II; relocalizes to the cytoplasm upon DNA replication stress
GO Process (4)
GO Function (1)
GO Component (3)
Saccharomyces cerevisiae (S288c)
PREY

RIM11

GSK3, MDS1, serine/threonine protein kinase RIM11, L000001056, YMR139W
Protein kinase; required for signal transduction during entry into meiosis; promotes the formation of the Ime1p-Ume6p complex by phosphorylating Ime1p and Ume6p; shares similarity with mammalian glycogen synthase kinase 3-beta; protein abundance increases in response to DNA replication stress; RIM11 has a paralog, MRK1, that arose from the whole genome duplication
GO Process (5)
GO Function (2)
GO Component (1)
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