PROSITE documentation PDOC51376DBB domain profile
The following proteins share a number of distinct parts, namely, ankyrin repeats (see <PDOC50088>), a coiled coil, and a stretch of approximately 140 amino acid residues upstream of the ankyrin repeats, which has been called the Dof/BCAP/BANK (DBB) domain [1,2]:
- Drosophila Downstream-of-EGF receptor (Dof), a protein essential for the morphogenesis of both the mesoderm and the tracheae. It has been proposed to mediate the transmission of a signal from an activated receptor to other components of the cell, including the MAP kinase cascade.
- Vertebrate BANK and BCAP proteins that function in B-cell signaling.
These proteins are involved in signaling; however, unlike Dof, BANK and BCAP are not implicated in FGF signaling but appear to have undergone rapid change during the course of evolution to acquire a novel function with the development of the immune system in higher vertebrates.
The DBB domain in both Dof and BCAP is required to mediate self-association in yeast cells, indicating that this domain may have a more general role in mediating protein-protein interactions [1].
The profile we developed covers the entire DBB domain.
Last update:April 2008 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Battersby A. Csiszar A. Leptin M. Wilson R. |
| Title | Isolation of proteins that interact with the signal transduction molecule Dof and identification of a functional domain conserved between Dof and vertebrate BCAP. | |
| Source | J. Mol. Biol. 329:479-493(2003). | |
| PubMed ID | 12767830 |
| 2 | Authors | Wilson R. Battersby A. Csiszar A. Vogelsang E. Leptin M. |
| Title | A functional domain of Dof that is required for fibroblast growth factor signaling. | |
| Source | Mol. Cell. Biol. 24:2263-2276(2004). | |
| PubMed ID | 14993266 |
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