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

The Ciliopathy Protein CC2D2A Associates with NINL and Functions in RAB8-MICAL3-Regulated Vesicle Trafficking.

Bachmann-Gagescu R, Dona M, Hetterschijt L, Tonnaer E, Peters T, de Vrieze E, Mans DA, van Beersum SE, Phelps IG, Arts HH, Keunen JE, Ueffing M, Roepman R, Boldt K, Doherty D, Moens CB, Neuhauss SC, Kremer H, van Wijk E

Ciliopathies are a group of human disorders caused by dysfunction of primary cilia, ubiquitous microtubule-based organelles involved in transduction of extra-cellular signals to the cell. This function requires the concentration of receptors and channels in the ciliary membrane, which is achieved by complex trafficking mechanisms, in part controlled by the small GTPase RAB8, and by sorting at the transition zone ... [more]

PLoS Genet Oct. 01, 2015; 11(10);e1005575 [Pubmed: 26485645]

Throughput

High Throughput

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
NINL DYNC1LI1	Proximity Label-MS Proximity Label-MS 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.	Gupta GD (2015)	High	-	BioGRID	1432867
NINL DYNC1LI1	Proximity Label-MS Proximity Label-MS 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.	Redwine WB (2017)	High	-	BioGRID	-

Curated By

BioGRID

Interaction Summary

NINL

Gene Ontology Biological Process

Gene Ontology Cellular Component

DYNC1LI1