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CUE Domain
Class:Ubiquitin processes

No ImageThe CUE domain is structurally related to the ubiquitin-binding UBA domain and is comprised of a three-helix bundle. A conserved MFP motif in alpha helix1 and LL motif in alpha helix 3 interact with the conserved hydrophobic patch of ubiquitin. The CUE domain has also been reported to exist as a domain-swapped dimer that makes additional contacts with ubiquitin, and consequently, binds ubiquitin with higher affinity.

Structure Reference:
Kang, R.S et al. (2003) Cell 113(5), 621630.
"CUE domain of the yeast Cue2 protein bound to ubiquitin (red)".

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.
Examples of Proteins:
Vps9 -- mono and polyubiquitin
Cue1-- mono and polyubiquitin
Tollip -- monoubiquitin (polyubiquitin not tested)

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