Top Module Empty

Bookmark Us

Print E-mail
UIM Domain
Class:Ubiquitin processes

No ImageThe UIM domain consists of a single alpha helix with hydrophobic residues within the helix interacting with the conserved Leu8-Ile44-Val70 hydrophobic patch of ubiquitin. Acidic residues within the UIM also contribute to binding through interaction with basic residues in ubiquitin.

Structure Reference:
Swanson, KA. et al., (2003) EMBO J. 22(18): 4597-4606. The UIM domain of Vps27 bound to ubiquitin (red). PDB: 1Q0W.

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

< Prev   Next >
© 2016 The Pawson Lab
Joomla! is Free Software released under the GNU/GPL License.