An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods.

Publication

Assembly of the WHIP-TRIM14-PPP6C Mitochondrial Complex Promotes RIG-I-Mediated Antiviral Signaling.

Tan P, He L, Cui J, Qian C, Cao X, Lin M, Zhu Q, Li Y, Xing C, Yu X, Wang HY, Wang RF

Mitochondrial antiviral signaling platform protein (MAVS) acts as a central hub for RIG-I receptor proximal signal propagation. However, key components in the assembly of the MAVS mitochondrial platform that promote RIG-I mitochondrial localization and optimal activation are still largely undefined. Employing pooled RNAi and yeast two-hybrid screenings, we report that the mitochondrial adaptor protein tripartite motif (TRIM)14 provides a docking ... [more]

Mol. Cell Oct. 19, 2017; 68(2);293-307.e5 [Pubmed: 29053956]

Throughput

High Throughput

Additional Notes

evidence from proximity label-MS experiment, specifically APEX-2 biotin labeling

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
VIM TRIM14	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.	Luck K (2020)	High	-	BioGRID	2695513

Curated By

BioGRID

Interaction Summary

TRIM14

Gene Ontology Biological Process

Gene Ontology Cellular Component

VIM

Gene Ontology Biological Process

Gene Ontology Molecular Function

double-stranded RNA binding [IDA]glycoprotein binding [IPI]identical protein binding [IPI]protein C-terminus binding [IPI]protein binding [IPI]scaffold protein binding [IPI]structural constituent of cytoskeleton [IDA]