BAIT

EF2

CG2238, Dmel\CG2238, EF-2, EF-2b, EF2b, anon-EST:Liang-1.44, chr2L:21668915..21669164, clone 1.44, eEF2, Dmel_CG2238
Elongation factor 2
GO Process (4)
GO Function (1)
GO Component (4)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Drosophila melanogaster
PREY

RPL5

CG17489, Dmel\CG17489, E-2d, L5, M(2)40B, Rp L5, dRPL5, yip6, Dmel_CG17489
Ribosomal protein L5
GO Process (2)
GO Function (4)
GO Component (2)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Drosophila melanogaster

Co-fractionation

Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex.

Publication

Structures of the human and Drosophila 80S ribosome.

Anger AM, Armache JP, Berninghausen O, Habeck M, Subklewe M, Wilson DN, Beckmann R

Protein synthesis in all cells is carried out by macromolecular machines called ribosomes. Although the structures of prokaryotic, yeast and protist ribosomes have been determined, the more complex molecular architecture of metazoan 80S ribosomes has so far remained elusive. Here we present structures of Drosophila melanogaster and Homo sapiens 80S ribosomes in complex with the translation factor eEF2, E-site transfer ... [more]

Nature May. 02, 2013; 497(7447);80-5 [Pubmed: 23636399]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
RPL5 EF2
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.

High-BioGRID
-

Curated By