| Description | Ubiquitin-fold proteins are an important class of eukaryotic post-translational modifiers [ , ]. They are generally short proteins (less than 200 amino acids) which contain the core β-grasp fold (also known as the ubiquitin fold) and a C-terminal extension which enables their attachment to other proteins through the terminal carboxyl group. Protein-conjugated ubiquitins have been implicated an a wide variety of cellular process including proteolysis, DNA repair, transcription and autophagy Some ubiquitin-like proteins are not conjugated to proteins, but are instead anchored to the cell membrane by attachment to phospholipids or isoprenes. The functions of these membrane-associated proteins are not generally well understood. In the case of isoprene attachemnet, the prenyl group may also play a role in enhancing protein-protein interactions.This entry represents a group of membrane-associated ubiquitin-fold proteins found in plants and animals [ ]. In Arabidopsis, membrane-anchored ubiquitin-fold (MUB) proteins recruit and dock specific E2s to the plasma membrane. They appear to interact noncovalently with an E2 surface opposite the active site that forms a covalent linkage with Ub []. The animal homologues of MUBs, also known as UBL3, have also been identified as ubiquitin-like proteins []. | Name | Membrane-anchored ubiquitin-fold protein |
| Short Name | MUB | Type | Family |
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