Identification of a RING protein that can interact in vivo with the BRCA1 gene product.
The hereditary breast and ovarian cancer gene, BRCA1, encodes a large polypeptide that contains the cysteine-rich RING motif, a zinc-binding domain found in a variety of regulatory proteins. Here we describe a novel protein that interacts in vivo with the N-terminal region of BRCA1. This BRCA1-associated RING domain (BARD1) protein ... contains an N-terminal RING motif, three tandem ankyrin repeats, and a C-terminal sequence with significant homology to the phylogenetically conserved BRCT domains that lie near the C terminus of BRCA1. The BARD1/BRCA1 interaction is disrupted by BRCA1 missense mutations that segregate with breast cancer susceptibility, indicating that BARD1 may be involved in mediating tumour suppression by BRCA1.
Mesh Terms:
Amino Acid Sequence, Ankyrins, BRCA1 Protein, Binding Sites, Breast Neoplasms, Carrier Proteins, Cell Line, Escherichia coli, Female, Hela Cells, Humans, Molecular Sequence Data, Mutagenesis, Site-Directed, Ovarian Neoplasms, Protein Binding, Recombinant Fusion Proteins, Saccharomyces cerevisiae, Sequence Homology, Amino Acid, Tumor Cells, Cultured, Tumor Suppressor Proteins, Ubiquitin-Protein Ligases
Amino Acid Sequence, Ankyrins, BRCA1 Protein, Binding Sites, Breast Neoplasms, Carrier Proteins, Cell Line, Escherichia coli, Female, Hela Cells, Humans, Molecular Sequence Data, Mutagenesis, Site-Directed, Ovarian Neoplasms, Protein Binding, Recombinant Fusion Proteins, Saccharomyces cerevisiae, Sequence Homology, Amino Acid, Tumor Cells, Cultured, Tumor Suppressor Proteins, Ubiquitin-Protein Ligases
Nat. Genet.
Date: Dec. 01, 1996
PubMed ID: 8944023
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