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

Interaction proteomics identify NEURL4 and the HECT E3 ligase HERC2 as novel modulators of centrosome architecture.

Al-Hakim AK, Bashkurov M, Gingras AC, Durocher D, Pelletier L

Centrosomes are composed of a centriole pair surrounded by an intricate proteinaceous matrix referred to as pericentriolar material. Although the mechanisms underpinning the control of centriole duplication are now well understood, we know relatively little about the control of centrosome size and shape. Here we used interaction proteomics to identify the E3 ligase HERC2 and the neuralized homologue NEURL4 as ... [more]

Mol. Cell Proteomics Jun. 01, 2012; 11(6);M111.014233 [Pubmed: 22261722]

Throughput

High Throughput

Additional Notes

table 1, S1.

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
HERC2 SRGAP2	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.	Saez I (2018)	High	-	BioGRID	2526160

Curated By

BioGRID

Interaction Summary

HERC2

Gene Ontology Biological Process

Gene Ontology Molecular Function

SUMO binding [IDA]guanyl-nucleotide exchange factor activity [NAS]protein binding [IPI]ubiquitin protein ligase binding [IPI]ubiquitin-protein transferase activity [IDA]

Gene Ontology Cellular Component

SRGAP2

Gene Ontology Biological Process

Gene Ontology Molecular Function

Rac GTPase activator activity [IDA, IMP]Rac GTPase binding [IDA]protein binding [IPI]protein homodimerization activity [IDA]