BRD7, a novel NPC-related gene, was isolated through cDNA representational difference analysis (RDA). The studies showed that wild-type BRD7 interacted with H3 peptide acetylated at Lys14, while the bromodomain deleted mutant lost this ability. Bromodomain is an evolutionally conserved domain which forms a bundle of four a-helices(α_z, α_A, α_B, α_C) and two loops (ZA loop，BC loop). Alignment of the amino acid sequence of BRD7 protein with known structure of proteins in PDB (protein database), it was considered that Bromodomain of BRD7 has the same characteristic. Based on results of bio-informatics, mutants of Bromodomain were constructed. The peptide binding assays was performed to detect the binding of mutants with acetylated histone H3. The results indicated that two loops (ZA loop，BC loop) were essential for Bromodomain binding to acetylated histone H3, while two loops(ZA loop，BC loop) could influence the sub-cellular location of BRD7 through indirect immunofluorescence. At last, it was found that the CBP(CREB binding protein) is a novel interaction protein of BRD7. The CBP not only has histone acetyltransferases (HATs) to acetylate lysines on N-terminal tails of histones but also plays a key role as co-activator for a wide variety of transcription factors.