BARD1 BRCT domains (human, recombinant)

BRCA1-associated RING domain protein 1 (BARD1) is a binding partner of the breast and ovarian tumor suppressor (BRCA1).{25463,25465} BARD1 binding to BRCA1 via the RING and BRCT domains regulates BRCA1 stability, cellular localization, and function.{25465,25460,25467} Heterodimeric BRCA1/BARD1 enhances BRCA1 functions, including the maintenance of genomic stability by participating in DNA repair mechanisms.{25460} Further, BRCA1/BARD1 heterodimers have been shown to have ubiquitin ligase activity.{23643} BARD1 has also been shown to mediate p53-dependent, BRCA1-independent apoptosis.{25459,25464} BARD1 binding to the mRNA polyadenylation factor, cleavage stimulation factor-50, is involved in inhibiting mRNA processing and tumor suppression.{25461,25462} BARD1 contains two BRCA1 C-terminal (BRCT) domains.{25463} BRCT domains are modular units of ~100 amino acids that fold independently and recognize linear phosphoserine or phosphothreonine regions to mediate protein-protein and protein-DNA interactions.{23632,22097} BRCT domains were initially recognized in the C-terminal region of the breast cancer protein BRCA1, as well as the p53 binding protein and the yeast cell cycle checkpoint protein RAD9.{23633} BRCT domains often occur as tandem repeats at the C-terminal end of several proteins that are functionally diverse.{22097} Most BRCT domain-containing proteins participate in DNA-damage checkpoint control or DNA-repair pathways, or both.{23634,23633} Thus, BRCT domain-containing proteins likely participate in the cellular response to DNA damage. This recombinant protein product contains the first and second BRCT domains of BARD1.