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

BRCA1 interacts with acetyl-CoA carboxylase through its tandem of BRCT domains.

Magnard C, Bachelier R, Vincent A, Jaquinod M, Kieffer S, Lenoir GM, Venezia ND

Germ-line alterations in BRCA1 are associated with an increased susceptibility to breast and ovarian cancer. BRCA1 is a 220-kDa protein that contains a tandem of two BRCA1 C-Terminal (BRCT) domains. Among missense and nonsense BRCA1 mutations responsible for family breast cancer, some are located into the BRCT tandem of BRCA1 coding sequence. In an attempt to understand how BRCT is ... [more]

Oncogene Oct. 03, 2002; 21(44);6729-39 [Pubmed: 12360400]

Throughput

Low Throughput

Additional Notes

residues 1583-1812 bait;Interaction is completely abolished by five distinct germline BRCA1 deleterious mutations affecting the BRCT tandem of BRCA1

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
BRCA1 ACACA	Affinity Capture-Western Affinity Capture-Western 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 identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.	Jackson KC (2014)	Low	-	BioGRID	-
BRCA1 ACACA	Affinity Capture-Western Affinity Capture-Western 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 identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.	Magnard C (2002)	Low	-	BioGRID	244831
ACACA BRCA1	Affinity Capture-Western Affinity Capture-Western 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 identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.	Moreau K (2006)	Low	-	BioGRID	-
BRCA1 ACACA	Affinity Capture-Western Affinity Capture-Western 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 identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.	Ray H (2009)	Low	-	BioGRID	-
BRCA1 ACACA	Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.	Hunkeler M (2018)	Low	-	BioGRID	2572394
ACACA BRCA1	Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.	Shen Y (2008)	Low	-	BioGRID	717568
BRCA1 ACACA	Protein-peptide Protein-peptide An interaction is detected between a protein and a peptide derived from an interaction partner. This includes phage display experiments.	Petitalot A (2019)	Low	-	BioGRID	2660710
BRCA1 ACACA	Protein-peptide Protein-peptide An interaction is detected between a protein and a peptide derived from an interaction partner. This includes phage display experiments.	Shen Y (2008)	Low	-	BioGRID	717569
BRCA1 ACACA	Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro.	Moreau K (2006)	Low	-	BioGRID	-
BRCA1 ACACA	Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro.	Ray H (2006)	Low	-	BioGRID	-
ACACA BRCA1	Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro.	Ray H (2006)	Low	-	BioGRID	-

Curated By

BioGRID

Interaction Summary

BRCA1

Gene Ontology Biological Process

Gene Ontology Molecular Function

DNA binding [TAS]RNA binding [IDA]androgen receptor binding [NAS]enzyme binding [IPI]protein binding [IPI]transcription coactivator activity [NAS]transcription regulatory region DNA binding [IDA]tubulin binding [NAS]ubiquitin protein ligase binding [IPI]ubiquitin-protein transferase activity [IDA]

Gene Ontology Cellular Component

ACACA