The Pawson Lab - UEV Domain

Class:Ubiquitin processes

Structure:
“The UEV domain of TSG101 bound to ubiquitin (red)”

Structure Reference:
Sundquist, WI. et al. (2004) Molecular Cell. 13(6): 783-9. PDB: 1S1Q.

Domain binding and function:
The UEV (Ubiquitin E2 variant) domain is ubiquitin binding domain of ~145 amino acids. The structure of the UEV domain contains a characteristic α/β fold similar to the canonical E2 enzyme but has an additional N-terminal helix and lacks the two C-terminal helices. Found in TSG101/Vps23 proteins, the UEV interacts with a ubiquitin molecule and is essential for the trafficking of a number of ubiquitylated cargoes to MVBs. Furthermore, the UEV domain can bind to Pro-Thr/Ser-Ala-Pro peptide ligands, a fact exploited by viruses such as HIV. Thus, the TSG101 UEV domain binds to the PTAP tetrapeptide motif in the viral Gag protein that is involved in viral budding.

Examples of Proteins:

UEV proteins		Binding Partner
TSG101		Ubiquitin
		Pro-Thr/Ser-Ala-Pro

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 Smith^2,3, Ivan Blasutig^2,3, Maria Sierra¹, Caesar Lim^2,3, Michael Arc¹, Jim Fawcett² and Tony Pawson^2,3.
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