Colligins are collagen-binding proteins localized to the endoplasmic reticulum that belong to the superfamily of serine protease inhibitors and play a role in collagen biosynthesis. Previously, we cloned the human colligin-2 gene (CBP2) and mapped it to chromosome 11q13.15. To further characterize the CBP2 gene, we have determined its genomic structure and the 5'-flanking sequence. The CBP2 gene spanned approximately 11 kb of genomic DNA and consisted of five exons. The promoter sequence of the human gene showed significant homology to that of its murine counterpart, which contained several regulatory sequences including heat-shock and retinoic acid-responsive elements. These findings suggest colligin may function as a collagen-specific molecular chaperon and play a role in the process of retinoic acid-induced differentiation.