BAIT

PHO80

AGS3, TUP7, VAC5, phoR, L000001426, YOL001W
Cyclin; interacts with cyclin-dependent kinase Pho85p; regulates the response to nutrient levels and environmental conditions, including the response to phosphate limitation and stress-dependent calcium signaling
Kinome Project (Sc)
Saccharomyces cerevisiae (S288c)
PREY

PDR1

AMY1, ANT1, BOR2, CYH3, NRA2, SMR2, TIL1, TPE1, TPE3, drug-responsive transcription factor PDR1, L000002984, L000003503, L000001361, YGL013C
Transcription factor that regulates the pleiotropic drug response; zinc cluster protein that is a master regulator involved in recruiting other zinc cluster proteins to pleiotropic drug response elements (PDREs) to fine tune the regulation of multidrug resistance genes; relocalizes to the cytosol in response to hypoxia; PDR1 has a paralog, PDR3, that arose from the whole genome duplication
Saccharomyces cerevisiae (S288c)

Dosage Lethality

A genetic interaction is inferred when over expression or increased dosage of one gene causes lethality in a strain that is mutated or deleted for another gene.

Publication

Functional Analysis of Kinases and Transcription Factors in Saccharomyces cerevisiae Using an Integrated Overexpression Library.

Youn JY, Friesen H, Nguyen Ba AN, Liang W, Messier V, Cox MJ, Moses AM, Andrews B

Kinases and transcription factors (TFs) are key modulators of important signaling pathways and their activities underlie the proper function of many basic cellular processes such as cell division, differentiation and development. Changes in kinase and TF dosage are often associated with disease, yet a systematic assessment of the cellular phenotypes caused by the combined perturbation of kinases and TFs has ... [more]

G3 (Bethesda) Jan. 25, 2017; 0(0); [Pubmed: 28122947]

Throughput

  • High Throughput

Ontology Terms

  • phenotype: inviable (APO:0000112)

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
PHO80 PDR1
PCA
PCA

A Protein-Fragment Complementation Assay (PCA) is a protein-protein interaction assay in which a bait protein is expressed as fusion to one of the either N- or C- terminal peptide fragments of a reporter protein and prey protein is expressed as fusion to the complementary N- or C- terminal fragment of the same reporter protein. Interaction of bait and prey proteins bring together complementary fragments, which can then fold into an active reporter, e.g. the split-ubiquitin assay.

Low-BioGRID
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Curated By

  • BioGRID