 CUE Domain | |
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| Class:Ubiquitin processes | |
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Structure:
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Domain binding and function:
The CUE domain was first identified as a ubiquitin-binding motif from a yeast two-hybrid screen that could interact with monoubiquitin. The CUE domain is moderately conserved consisting of 40 amino acids and is structurally related to the ubiquitin-binding UBA domain. Both domains are comprised of a three-helix bundle with a conserved hydrophobic path and both domains interact with ubiquitin analogously. The CUE domain is found in proteins with diverse functions including degradation of misfolded proteins in the endoplasmic reticulum and protein sorting. CUE domains, like UIMs, recognize both mono and polyubiquitin as well as in facilitating intramolecular monoubiquitination.
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Examples of Proteins:
Vps9 -- mono and polyubiquitin
Cue1-- mono and polyubiquitin
Tollip -- monoubiquitin (polyubiquitin not tested)
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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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