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

CHD3 and CHD4 form distinct NuRD complexes with different yet overlapping functionality.

Hoffmeister H, Fuchs A, Erdel F, Pinz S, Groebner-Ferreira R, Bruckmann A, Deutzmann R, Schwartz U, Maldonado R, Huber C, Dendorfer AS, Rippe K, Laengst G

CHD3 and CHD4 (Chromodomain Helicase DNA binding protein), two highly similar representatives of the Mi-2 subfamily of SF2 helicases, are coexpressed in many cell lines and tissues and have been reported to act as the motor subunit of the NuRD complex (nucleosome remodeling and deacetylase activities). Besides CHD proteins, NuRD contains several repressors like HDAC1/2, MTA2/3 and MBD2/3, arguing for ... [more]

Nucleic Acids Res. Oct. 13, 2017; 45(18);10534-10554 [Pubmed: 28977666]

Throughput

High Throughput

Additional Notes

nuclear extract

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
LMNA CHD3	Co-localization Co-localization Interaction inferred from two proteins that co-localize in the cell by indirect immunofluorescence only when in addition, if one gene is deleted, the other protein becomes mis-localized. Also includes co-dependent association of proteins with promoter DNA in chromatin immunoprecipitation experiments.	Serebryannyy LA (2019)	High	-	BioGRID	2788370

Curated By

BioGRID

Interaction Summary

CHD3

Gene Ontology Biological Process

Gene Ontology Molecular Function

ATP-dependent DNA helicase activity [TAS]helicase activity [NAS]poly(A) RNA binding [IDA]protein binding [IPI]zinc ion binding [NAS]

Gene Ontology Cellular Component

LMNA

Gene Ontology Biological Process

Gene Ontology Molecular Function

protein binding [IPI]structural molecule activity [TAS]