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.

Publication

A protein interaction map of Drosophila melanogaster.

Giot L, Bader JS, Brouwer C, Chaudhuri A, Kuang B, Li Y, Hao YL, Ooi CE, Godwin B, Vitols E, Vijayadamodar G, Pochart P, Machineni H, Welsh M, Kong Y, Zerhusen B, Malcolm R, Varrone Z, Collis A, Minto M, Burgess S, McDaniel L, Stimpson E, Spriggs F, Williams J, Neurath K, Ioime N, Agee M, Voss E, Furtak K, Renzulli R, Aanensen N, Carrolla S, Bickelhaupt E, Lazovatsky Y, DaSilva A, Zhong J, Stanyon CA, Finley RL, White KP, Braverman M, Jarvie T, Gold S, Leach M, Knight J, Shimkets RA, McKenna MP, Chant J, Rothberg JM

Drosophila melanogaster is a proven model system for many aspects of human biology. Here we present a two-hybrid-based protein-interaction map of the fly proteome. A total of 10,623 predicted transcripts were isolated and screened against standard and normalized complementary DNA libraries to produce a draft map of 7048 proteins and 20,405 interactions. A computational method of rating two-hybrid interaction confidence ... [more]

Science Dec. 05, 2003; 302(5651);1727-36 [Pubmed: 14605208]

Throughput

High Throughput

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
TRSN TRAX	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.	Guruharsha KG (2011)	High	-	BioGRID	-
TRSN TRAX	Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.	Mo X (2018)	Low	-	FlyBase	-
TRSN TRAX	Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.	Tian Y (2011)	Low	-	FlyBase	-
TRSN TRAX	Co-fractionation 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.	Liu Y (2009)	Low	-	FlyBase	-
TRSN TRAX	Co-fractionation 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.	Tian Y (2011)	Low	-	FlyBase	-
TRSN TRAX	Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro.	Mo X (2018)	Low	-	FlyBase	-
TRSN TRAX	Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro.	Tian Y (2011)	Low	-	FlyBase	-

Curated By

BioGRID

Interaction Summary

TRSN

Gene Ontology Biological Process

Gene Ontology Molecular Function

DNA binding [ISS]endoribonuclease activity [IDA]

Gene Ontology Cellular Component

TRAX