BAIT

KKQ8

putative serine/threonine protein kinase KKQ8, L000004097, YKL168C
Putative serine/threonine protein kinase with unknown cellular role; KKQ8 has a paralog, HAL5, that arose from the whole genome duplication
GO Process (0)
GO Function (1)
GO Component (1)

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)
PREY

YKL091C

SFH1, phosphatidylinositol/phosphatidylcholine-binding protein
Putative phosphatidylinositol/phosphatidylcholine transfer protein; possibly involved in lipid metabolism; localizes to the nucleus; contains a CRAL/TRIO domain and binds several lipids in a large-scale study; YKL091C has a paralog, SEC14, that arose from the whole genome duplication
GO Process (0)
GO Function (4)
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