PROSITE documentation PDOC51029
MADF domain profile


The myb/SANT-like domain in Adf-1 (MADF) is a ~80-amino-acid module that directs sequence specific DNA binding to a site consisting of multiple trinucleotide repeats. The MADF domain is found in one or more copies in eukaryotic and viral proteins and is often associated with the BESS domain (see <PDOC51031>) [1,2,3].

It is likely that the MADF domain is more closely related to the myb/SANT domain than it is to other HTH domains [1,2,3].

Some proteins known to contain a MADF domain are listed below:

  • Drosophila Adf-1, a transcription factor first identified on the basis of its interaction with the alcohol dehydrogenase promoter but that binds the promoters of a diverse group of genes [1].
  • Drosophila Dorsal-interacting protein 3 (Dip3). It functions both as an activator to bind DNA in a sequence specific manner and a coactivator to stimulate synergistic activation by Dorsal and Twist [2].
  • Drosophila Stonewall (Stwl), a putative transcription factor required for maintenance of female germline stem cells as well as oocyte differentiation.

The profile we developed covers the entire MADF domain.

Last update:

October 2004 / First entry.


Technical section

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

MADF, PS51029; MADF domain profile  (MATRIX)


1AuthorsEngland B.P. Admon A. Tjian R.
TitleCloning of Drosophila transcription factor Adf-1 reveals homology to Myb oncoproteins.
SourceProc. Natl. Acad. Sci. U.S.A. 89:683-687(1992).
PubMed ID1731341

2AuthorsCutler G. Perry K.M. Tjian R.
TitleAdf-1 is a nonmodular transcription factor that contains a TAF-binding Myb-like motif.
SourceMol. Cell. Biol. 18:2252-2261(1998).
PubMed ID9528796

3AuthorsBhaskar V. Courey A.J.
TitleThe MADF-BESS domain factor Dip3 potentiates synergistic activation by Dorsal and Twist.
SourceGene 299:173-184(2002).
PubMed ID12459265

PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.


View entry in original PROSITE document format
View entry in raw text format (no links)