PROSITE documentation PDOC51376
DBB 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.


Technical section

PROSITE method (with tools and information) covered by this documentation:

DBB, PS51376; DBB domain profile  (MATRIX)


1AuthorsBattersby A. Csiszar A. Leptin M. Wilson R.
TitleIsolation of proteins that interact with the signal transduction molecule Dof and identification of a functional domain conserved between Dof and vertebrate BCAP.
SourceJ. Mol. Biol. 329:479-493(2003).
PubMed ID12767830

2AuthorsWilson R. Battersby A. Csiszar A. Vogelsang E. Leptin M.
TitleA functional domain of Dof that is required for fibroblast growth factor signaling.
SourceMol. Cell. Biol. 24:2263-2276(2004).
PubMed ID14993266

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