Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
PROSITE documentation PDOC51029MADF domain profile
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PURL: https://purl.expasy.org/prosite/documentation/PDOC51029
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.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | England B.P. Admon A. Tjian R. |
| Title | Cloning of Drosophila transcription factor Adf-1 reveals homology to Myb oncoproteins. | |
| Source | Proc. Natl. Acad. Sci. U.S.A. 89:683-687(1992). | |
| PubMed ID | 1731341 |
| 2 | Authors | Cutler G. Perry K.M. Tjian R. |
| Title | Adf-1 is a nonmodular transcription factor that contains a TAF-binding Myb-like motif. | |
| Source | Mol. Cell. Biol. 18:2252-2261(1998). | |
| PubMed ID | 9528796 |
| 3 | Authors | Bhaskar V. Courey A.J. |
| Title | The MADF-BESS domain factor Dip3 potentiates synergistic activation by Dorsal and Twist. | |
| Source | Gene 299:173-184(2002). | |
| PubMed ID | 12459265 |
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