BAIT

EPN1

Epsin 1
GO Process (5)
GO Function (1)
GO Component (2)
Rattus norvegicus

Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Publication

A role for epsin N-terminal homology/AP180 N-terminal homology (ENTH/ANTH) domains in tubulin binding.

Hussain NK, Yamabhai M, Bhakar AL, Metzler M, Ferguson SS, Hayden MR, McPherson PS, Kay BK

The epsin N-terminal homology (ENTH) domain is a protein module of approximately 150 amino acids found at the N terminus of a variety of proteins identified in yeast, plants, nematode, frog, and mammals. ENTH domains comprise multiple alpha-helices folded upon each other to form a compact globular structure that has been implicated in interactions with lipids and proteins. In characterizing ... [more]

J. Biol. Chem. Aug. 01, 2003; 278(31);28823-30 [Pubmed: 12750376]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
TUBA1A EPN1
Affinity Capture-Western
Affinity Capture-Western

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 identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.

Low-BioGRID
-

Curated By

  • BioGRID