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

Proteomic analysis of SRm160-containing complexes reveals a conserved association with cohesin.

McCracken S, Longman D, Marcon E, Moens P, Downey M, Nickerson JA, Jessberger R, Wilde A, Caceres JF, Emili A, Blencowe BJ

In this study, we describe a rapid immunoaffinity purification procedure for gel-free tandem mass spectrometry-based analysis of endogenous protein complexes and apply it to the characterization of complexes containing the SRm160 (serine/arginine repeat-related nuclear matrix protein of 160 kDa) splicing coactivator. In addition to promoting splicing, SRm160 stimulates 3'-end processing via its N-terminal PWI nucleic acid-binding domain and is found ... [more]

J. Biol. Chem. Dec. 23, 2005; 280(51);42227-36 [Pubmed: 16159877]

Throughput

Low Throughput

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
DNAJC8 SRRM1	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.	Piette BL (2021)	High	4.24	BioGRID	2940096

Curated By

BioGRID

Interaction Summary

SRRM1

Gene Ontology Biological Process

Gene Ontology Molecular Function

poly(A) RNA binding [IDA]

Gene Ontology Cellular Component

DNAJC8