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

Mapping the MOB proteins' proximity network reveals a unique interaction between human MOB3C and the RNase P complex.

Elkholi IE, Boulais J, Thibault MP, Phan HD, Robert A, Lai LB, Faubert D, Smith MJ, Gopalan V, Cote JF

Distinct functions mediated by members of the monopolar spindle-one-binder (MOB) family of proteins remain elusive beyond the evolutionarily conserved and well-established roles of MOB1 (MOB1A/B) in regulating tissue homeostasis within the Hippo pathway. Since MOB proteins are adaptors, understanding how they engage in protein-protein interactions, and help assemble complexes is essential to define the full scope of their biological functions. ... [more]

J Biol Chem Aug. 01, 2023; ();105123 [Pubmed: 37536630]

Throughput

High Throughput

Additional Notes

BFDR less than or equal to 0.01
BioID
Experiment performed in HEK293 cells
Experiment performed in Hela cells

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
MOB3C POP4	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.	Elkholi IE (2023)	High	-	BioGRID	-

Curated By

BioGRID

Interaction Summary

MOB3C

POP4

Gene Ontology Biological Process

Gene Ontology Molecular Function

RNA binding [TAS]protein binding [IPI]ribonuclease MRP activity [IBA]ribonuclease P RNA binding [IBA]ribonuclease P activity [IBA]

Gene Ontology Cellular Component

Proximity Label-MS