Aliases for BARD1 Gene
External Ids for BARD1 Gene
Previous GeneCards Identifiers for BARD1 Gene
This gene encodes a protein which interacts with the N-terminal region of BRCA1. In addition to its ability to bind BRCA1 in vivo and in vitro, it shares homology with the 2 most conserved regions of BRCA1: the N-terminal RING motif and the C-terminal BRCT domain. The RING motif is a cysteine-rich sequence found in a variety of proteins that regulate cell growth, including the products of tumor suppressor genes and dominant protooncogenes. This protein also contains 3 tandem ankyrin repeats. The BARD1/BRCA1 interaction is disrupted by tumorigenic amino acid substitutions in BRCA1, implying that the formation of a stable complex between these proteins may be an essential aspect of BRCA1 tumor suppression. This protein may be the target of oncogenic mutations in breast or ovarian cancer. Multiple alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Sep 2013]
GeneCards Summary for BARD1 Gene
BARD1 (BRCA1 Associated RING Domain 1) is a Protein Coding gene. Diseases associated with BARD1 include Breast Cancer and Rare Breast Tumor. Among its related pathways are Homologous DNA Pairing and Strand Exchange and DNA damage_ATM/ATR regulation of G1/S checkpoint. Gene Ontology (GO) annotations related to this gene include protein homodimerization activity and protein heterodimerization activity.
UniProtKB/Swiss-Prot Summary for BARD1 Gene
E3 ubiquitin-protein ligase. The BRCA1-BARD1 heterodimer specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Plays a central role in the control of the cell cycle in response to DNA damage. Acts by mediating ubiquitin E3 ligase activity that is required for its tumor suppressor function. Also forms a heterodimer with CSTF1/CSTF-50 to modulate mRNA processing and RNAP II stability by inhibiting pre-mRNA 3' cleavage.