 SWIRM Domain | |
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Class:Chromatin remodeling
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Structure:
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Domain binding and function:
SWIRM is an evolutionarily conserved, eukaryotic domain found in proteins implicated in chromatin remodeling and gene expression. It is composed of approximately 85 amino acids forming a five-helix-bundle, histone-like fold consisting of two helix-turn-helix motifs positioned around a long, central helix. The variation in orientation of the helix-turn-helix motifs relative to one another may account for differences in cellular function across SWIRM domains. The SWIRM domains of human ADA2α and SMARC2 have been shown to bind to both nucleosomal and double-stranded DNA. The SWIRM domain of ADA2α colocalizes with lysine-acetylated histone H3 in the nucleus and enhances access to nucleosomal linker DNA bound to histone H1, thereby potentiating ACF remodeling activity.
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Examples of Proteins:
| SWIRM proteins |
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| ADA2 |  |
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| SMARC2 | |
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| LSD1 | |
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| Swi3 | |
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| Rsc8 | |
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Moira
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Referenced in part on Cell Signaling Technology Website, Reference Section on Protein Domains. We gratefully acknowledge the following contributors:
Piers Nash1, Dan Lin3, Kathleen Binns2, Clark Wells2, Rob Ingham2, Terry Kubiseski2, Bernard Liu1, Matt Smith2,3, Ivan Blasutig2,3, Maria Sierra1, Caesar Lim2,3, Michael Arc1, Jim Fawcett2 and Tony Pawson2,3.
1. Ben May Institute for Cancer Research, The University of Chicago, Chicago, Illinois, 60637, USA
2. Program in Molecular Biology and Cancer, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, M5G 1X5, Canada
3. Department of Molecular and Medical Genetics, University of Toronto, Toronto, Ontario, M5S 1A8, Canada
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