BAIT

CMK2

calmodulin-dependent protein kinase CMK2, L000000367, YOL016C
Calmodulin-dependent protein kinase; may play a role in stress response, many CA++/calmodulan dependent phosphorylation substrates demonstrated in vitro, amino acid sequence similar to mammalian Cam Kinase II; CMK2 has a paralog, CMK1, that arose from the whole genome duplication
GO Process (2)
GO Function (2)
GO Component (1)

Gene Ontology Biological Process

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)
PREY

DBR1

PRP26, L000000495, YKL149C
RNA lariat debranching enzyme; catalyzes debranching of lariat introns formed during pre-mRNA splicing; required for efficient Ty1 transposition; knockdown of human homolog Dbr1 rescues toxicity of RNA-binding proteins TDP-43 and FUS which are implicated in amyotrophic lateral sclerosis (ALS), suggests potential therapeutic target for ALS and related TDP-43 proteinopathies
GO Process (5)
GO Function (1)
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