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.

Publication

Proteome survey reveals modularity of the yeast cell machinery.

Gavin AC, Aloy P, Grandi P, Krause R, Boesche M, Marzioch M, Rau C, Jensen LJ, Bastuck S, Duempelfeld B, Edelmann A, Heurtier MA, Hoffman V, Hoefert C, Klein K, Hudak M, Michon AM, Schelder M, Schirle M, Remor M, Rudi T, Hooper S, Bauer A, Bouwmeester T, Casari G, Drewes G, Neubauer G, Rick JM, Kuster B, Bork P, Russell RB, Superti-Furga G

Protein complexes are key molecular entities that integrate multiple gene products to perform cellular functions. Here we report the first genome-wide screen for complexes in an organism, budding yeast, using affinity purification and mass spectrometry. Through systematic tagging of open reading frames (ORFs), the majority of complexes were purified several times, suggesting screen saturation. The richness of the data set ... [more]

Nature Mar. 30, 2006; 440(7084);631-6 [Pubmed: 16429126]

Throughput

High Throughput

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
UTP15 UTP9	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.	Gavin AC (2006)	High	-	BioGRID	-
UTP9 UTP15	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.	Grandi P (2002)	High	-	BioGRID	-
UTP15 UTP9	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.	Grandi P (2002)	High	-	BioGRID	-
UTP9 UTP15	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.	Krogan NJ (2004)	High	-	BioGRID	-
UTP9 UTP15	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.	Krogan NJ (2006)	High	-	BioGRID	-
UTP9 UTP15	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.	Michaelis AC (2023)	High	10	BioGRID	3595386
UTP15 UTP9	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.	Poell G (2014)	Low	-	BioGRID	2822348
UTP15 UTP9	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.	Costanzo M (2016)	High	-0.3704	BioGRID	1946934
UTP9 UTP15	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.	Costanzo M (2016)	High	-0.2425	BioGRID	1937118
UTP9 UTP15	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.	Tarassov K (2008)	High	-	BioGRID	-
UTP9 UTP15	Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.	Freed EF (2010)	Low	-	BioGRID	-

Curated By

BioGRID

Interaction Summary

UTP9

Gene Ontology Biological Process

Gene Ontology Molecular Function

snoRNA binding [IPI]

Gene Ontology Cellular Component

UTP15