RCA1,also named as RNF53,plays a central role in DNA repair by facilitating cellular response to DNA repair. It is required for appropriate cell cycle arrests after ionizing irradiation in both the S-phase and the G2 phase of the cell cycle. The BRCA1-BARD1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair,ubiquitination and transcriptional regulation to maintain genomic stability. BRCA1 acts by mediating ubiquitin E3 ligase activity that is required for its tumor suppressor function. It is involved in transcriptional regulation of P21 in response to DNA damage. BRCA1 is required for FANCD2 targeting to sites of DNA damage. It may function as a transcriptional regulator. BRCA1 inhibits lipid synthesis by binding to inactive phosphorylated ACACA and preventing its dephosphorylation. The antibody is specific to BRCA1. BRCA1 appears to produce multiple splice variants. BRCA1 is a nuclear protein with a molecular mass of 220 kDa. The present study describes the isolation and expression of two cDNAs of BRCA1,including a splice variant designated BRCA1D672-4095. BRCA1D672-4095 is generated by exclusion of exon 11 by in-frame splicing and produces a 97 kDa protein. In contrast to BRCA1,BRCA1D672-4095 localizes to the cytoplasm.
Inherited mutations in BRCA1 and this gene, BRCA2, confer increased lifetime risk of developing breast or ovarian cancer. Both BRCA1 and BRCA2 are involved in maintenance of genome stability, specifically the homologous recombination pathway for double-strand DNA repair. The BRCA2 protein contains several copies of a 70 aa motif called the BRC motif, and these motifs mediate binding to the RAD51 recombinase which functions in DNA repair. BRCA2 is considered a tumor suppressor gene, as tumors with BRCA2 mutations generally exhibit loss of heterozygosity (LOH) of the wild-type allele.
Bromodomain-containing protein 4 (BRD4) is a member of the BET class chromatin reader proteins that bind acetylated histones and play a key role in transcriptional regulation and transmission of epigenetic memory. Remains associated with acetylated chromatin throughout the entire cell cycle and provides epigenetic memory for postmitotic G1 gene transcription by preserving acetylated chromatin status and maintaining high-order chromatin structure. BRD bromodomains serve as recognition motifs for acetylated lysine residues on histones, while the NET domain may function by promoting phosphorylation of the C-terminal domain (CTD) of RNA Polymerase II. Some specific inhibitors of BRD4 that prevent binding to acetylated histones by binding Asn-140 and Asn-433 are promising therapeutic molecules for the treatment of leukemias. BRD4 is a potential therapeutic target in many diseases including breast cancer, AML, multiple myeloma, colon cancer and others.
Bridging Integrator 2 (BIN2) is a cytoplasmic protein. BIN2 contains one BAR domain and Interacts with BIN1. BIN2 is highly expressed in some hematopoietic tissues, including peripheral blood, thymus, colon and placenta. BIN2 is an Arabidopsis GSK3-like kinase that negatively regulates brassinosteroid (BR) signaling. Genetic studies show that BIN2 is inhibited in response to BR perception at the cell surface to relieve its inhibitory effects on downstream targets.
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