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

Phenotypic and Interaction Profiling of the Human Phosphatases Identifies Diverse Mitotic Regulators.

St-Denis N, Gupta GD, Lin ZY, Gonzalez-Badillo B, Veri AO, Knight JD, Rajendran D, Couzens AL, Currie KW, Tkach JM, Cheung SW, Pelletier L, Gingras AC

Reversible phosphorylation is a fundamental regulatory mechanism, intricately coordinated by kinases and phosphatases, two classes of enzymes widely disrupted in human disease. To better understand the functions of the relatively understudied phosphatases, we have used complementary affinity purification and proximity-based interaction proteomics approaches to generate a physical interactome for 140 human proteins harboring phosphatase catalytic domains. We identified 1,335 high-confidence ... [more]

Cell Rep Nov. 22, 2016; 17(9);2488-2501 [Pubmed: 27880917]

Throughput

High Throughput

Additional Notes

BioID

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
PTPRA EXOC3	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.	Yadav L (2020)	High	-	BioGRID	-

Curated By

BioGRID

Interaction Summary

PTPRA

Gene Ontology Biological Process

Gene Ontology Molecular Function

protein binding [IPI]protein tyrosine phosphatase activity [TAS]transmembrane receptor protein tyrosine phosphatase activity [TAS]

Gene Ontology Cellular Component

EXOC3

Gene Ontology Biological Process

Gene Ontology Molecular Function

SNARE binding [IBA]protein binding [IPI]