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

A conserved acetylation switch enables pharmacological control of tubby-like protein stability.

Kerek EM, Yoon KH, Luo SY, Chen J, Valencia R, Julien O, Waskiewicz AJ, Hubbard BP

Tubby-like proteins (TULPs) are characterized by a conserved C-terminal domain that binds phosphoinositides. Collectively, mammalian TULP1-4 proteins play essential roles in intracellular transport, cell differentiation, signaling, and motility. Yet, little is known about how the function of these proteins is regulated in cells. Here, we present the protein-protein interaction network of TULP3, a protein that is responsible for the trafficking ... [more]

J Biol Chem Nov. 13, 2020; (); [Pubmed: 33187986]

Throughput

Low Throughput

Curated By

BioGRID

Interaction Summary

TULP3

Gene Ontology Biological Process

Gene Ontology Molecular Function

enzyme binding [IPI]phosphatidylinositol binding [IDA]phosphatidylinositol-4,5-bisphosphate binding [NAS]protein binding [IPI]protein complex binding [IDA]

Gene Ontology Cellular Component

AAMP