BAIT

PHO88

L000003995, YBR106W
Probable membrane protein; involved in phosphate transport; role in the maturation of secretory proteins; pho88 pho86 double null mutant exhibits enhanced synthesis of repressible acid phosphatase at high inorganic phosphate concentrations
GO Process (2)
GO Function (0)
GO Component (2)

Gene Ontology Biological Process

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)
PREY

OLE1

MDM2, stearoyl-CoA 9-desaturase, L000001052, L000001297, YGL055W
Delta(9) fatty acid desaturase; required for monounsaturated fatty acid synthesis and for normal distribution of mitochondria
GO Process (1)
GO Function (2)
GO Component (2)
Saccharomyces cerevisiae (S288c)

Negative Genetic

Mutations/deletions in separate genes, each of which alone causes a minimal phenotype, but when combined in the same cell results in a more severe fitness defect or lethality under a given condition. This term is reserved for high or low throughput studies with scores.

Publication

Exploration of the function and organization of the yeast early secretory pathway through an epistatic miniarray profile.

Schuldiner M, Collins SR, Thompson NJ, Denic V, Bhamidipati A, Punna T, Ihmels J, Andrews B, Boone C, Greenblatt JF, Weissman JS, Krogan NJ

We present a strategy for generating and analyzing comprehensive genetic-interaction maps, termed E-MAPs (epistatic miniarray profiles), comprising quantitative measures of aggravating or alleviating interactions between gene pairs. Crucial to the interpretation of E-MAPs is their high-density nature made possible by focusing on logically connected gene subsets and including essential genes. Described here is the analysis of an E-MAP of genes ... [more]

Cell Nov. 04, 2005; 123(3);507-19 [Pubmed: 16269340]

Quantitative Score

  • -4.2205 [SGA Score]

Throughput

  • High Throughput

Ontology Terms

  • phenotype: colony size (APO:0000063)

Additional Notes

  • An Epistatic MiniArray Profile (E-MAP) analysis was used to quantitatively score genetic interactions based on fitness defects estimated from the colony size of double versus single mutants. Genetic interactions were considered significant if they had an S score > 2.5 for positive interactions (suppression) and S score < -2.5 for negative interactions (synthetic sick/lethality).

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
PHO88 OLE1
Affinity Capture-MS
Affinity Capture-MS

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.

High-BioGRID
-
PHO88 OLE1
Affinity Capture-MS
Affinity Capture-MS

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.

High2BioGRID
3604054
OLE1 PHO88
Negative Genetic
Negative Genetic

Mutations/deletions in separate genes, each of which alone causes a minimal phenotype, but when combined in the same cell results in a more severe fitness defect or lethality under a given condition. This term is reserved for high or low throughput studies with scores.

High-4.2205BioGRID
209585
OLE1 PHO88
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.

High-BioGRID
433821
PHO88 OLE1
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.

High-BioGRID
-

Curated By

  • BioGRID