BAIT

ARX1

YDR101C
Nuclear export factor for the ribosomal pre-60S subunit; shuttling factor which directly binds FG rich nucleoporins and facilities translocation through the nuclear pore complex; interacts directly with Alb1p; responsible for Tif6p recycling defects in the absence of Rei1; associated with the ribosomal export complex
GO Process (1)
GO Function (0)
GO Component (6)

Gene Ontology Biological Process

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)
PREY

RPL30

ribosomal 60S subunit protein L30, L30e, rp73, YL38, L32, L30, L000001726, YGL030W
Ribosomal 60S subunit protein L30; involved in pre-rRNA processing in the nucleolus; autoregulates splicing of its transcript; homologous to mammalian ribosomal protein L30, no bacterial homolog
Saccharomyces cerevisiae (S288c)

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.

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

Curated By

  • BioGRID