 UIM Domain | |
|
| Class:Ubiquitin processes | |
|
Structure:
| |
|
Domain binding and function:
The ubiquitin-interacting motif (UIM) was first described as a region of sequence homology to the ubiquitin binding S5a subunit of the 26S proteasome. The motif is found in a number of proteins involved in endocytosis and protein trafficking and can bind monoubiquitin as well as polyubiquitin chains. It has been suggested that UIM binding to monoubiquitylated substrates limits polyubiquitin chain assembly by blocking subsequent ubiquitin attachment to Lys48 of ubiquitin. Interestingly, several UIM domain-containing proteins are themselves ubiquitylated in UIM domain-dependent manner.
| |
|
Examples of Proteins:
| UIM proteins |
|
Binding Partner |
| HRS |  |
mono- and polyubiquitin |
| Epsin | |
mono- and polyubiquitin |
| Eps15 | |
mono- and polyubiquitin |
| S5A | |
polyubiquitin |
| STAM | |
mono- and polyubiquitin |
| |
|
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
| |
|
