The BRCA2 gene is composed of 27 exons and spans approximately 84.2 kb of genomic DNA.

The BRCA2 gene encodes a 11386 bp mRNA transcript. Transcription site is located 227 bp upstream the first ATG of the BRCA2 ORF. The translation start site is located in exon 2.

No pseudogene reported.

Human BRCA2 protein is composed of 3418 amino acids (384 kDa).
The N-terminal part of the BRCA2 protein contains a transcriptional activation domain (aa 18-105).
BRCA2 exon 11 encodes eight conserved motifs termed BRC repeats. Each of these repeats is composed of about 30 residues.
A DNA-binding domain has been located in the C-terminal region of the BRCA2 protein (aa 2478-3185). It is composed of a conserved helical domain and three OB folds.
Two nuclear localization signals (NLS) have been identified in the C-terminal region of BRCA2.

BRCA2 expression is proportional to the rate of cell proliferation. Non-dividing cells do not express BRCA2 while wide expression of BRCA2 was observed in actively dividing tissues, including the epithelium of the breast during puberty and pregnancy.
The BRCA2 expression is regulated during the cell cycle, with highest expression during the S phase of the cell cycle.
Most of the BRCA2 proteins are associated to DSS1. The presence of DSS1 was demonstrated to stabilize the BRCA2 protein.

BRCA2 is a nuclear protein.

BRCA2 has been implicated in maintenance of genomic integrity and in the cellular response to DNA damage. The BRCA2 protein interacts with the RAD51 recombinase to regulate homologous recombination (HR). BRCA2 regulates the intracellular localization of RAD51. It also targets the RAD51 to ssDNA and inhibits dsDNA binding, thus regulating/enhancing DNA strand exchange activity of RAD51. CHEK1 and CHEK2 both phosphorylate the RAD51/BRCA2 complex and regulate the functional association of this complex in response to DNA damage.
BRCA2 is also implicated in cell cycle checkpoints. Following exposure to X-rays or UV light, cells expressing truncated BRCA2 protein exhibit arrest in the G1 and G2/M phases. BRCA2 protein plays a role in mitotic spindle assembly checkpoints through modulation of the level of spindle assembly checkpoint proteins including Aurora A and Aurora B.
A role in regulation of transcription has been attributed to BRCA2. BRCA2 binding to the DSS1 protein appears to be required for proper completion of cell division in yeast.
The BRCA2 protein demonstrated the ability to stimulate transcription. For example, exogenous expression of BRCA2 can stimulate transcription of androgen receptor-regulated genes. This function of BRCA2 is regulated by the binding of the EMSY protein to the region of BRCA2 responsible for transcriptional activation. An excess of EMSY results in silencing of BRCA2-driven transcriptional activation.
BRCA2 localizes to meiotic chromosomes during early meiotic prophase I when homologous chromosomes undergo synapsis. Moreover, BRCA2 interacts with the meiosis-specific recombinase DMC1, thus implicating BRCA2 in meiotic recombination.

BRCA2 homologs have been found in a diverse range of organisms. In addition to zebrafish and C. elegans, homologs exist in diverse eukaryotes, from plants to parasitic organisms.
Low general conservation is found in BRCA2. Higher level of homology is observed for several segments, including transactivation domain, BRC repeats and nuclear localization signals located within C-terminal region.

High risk of breast and ovarian cancer is associated with germline BRCA2 mutations. Cumulative risk of breast cancer in BRCA2 mutation carriers was estimated to 45% by the age of 70 years while ovarian cancer risk in carriers was estimated to 11%. Increased risk of several other cancers are associated with BRCA2 mutations, especially for prostate and pancreatic cancer.

Somatic mutations in BRCA2 are infrequent in sporadic breast cancer. Methylation of the BRCA2 promoter has not been detected in normal tissues nor in breast and ovarian cancers. Loss of heterozygosity at the BRCA2 locus has been frequently found in sporadic breast and ovarian tumors.