Abstract
Ubiquitin-like proteins (UBLs) are posttranslational modifiers with a structurally conserved β-grasp fold. These sequence-wise unrelated proteins share similar modification mechanism with ubiquitin and regulate every facet of eukaryote life. With rapidly advancing proteomic techniques, it is now possible to systemically decode UBL modification on protein functions. In this article, we first cover basic biochemical principles of UBL cycling. Then, a brief review of biological implications on several well-characterized UBLs (small ubiquitin-like modifiers (SUMOs), neural precursor cell expressed, developmentally down regulated 8 (NEDD8), interferon-induced 15-kDa protein (Isg15), Atg8, Atg12, and Fat10) is provided.
| Original language | English |
|---|---|
| Title of host publication | Encyclopedia of Biological Chemistry |
| Subtitle of host publication | Second Edition |
| Publisher | Elsevier Inc. |
| Pages | 467-472 |
| Number of pages | 6 |
| ISBN (Electronic) | 9780123786319 |
| ISBN (Print) | 9780123786302 |
| DOIs | |
| Publication status | Published - Feb 15 2013 |
| Externally published | Yes |
Keywords
- ATG12
- ATG8
- Cullins
- FAT10
- Interferon-induced 15-kDa protein (ISG15)
- Neural precursor cell expressed, developmentally down regulated 8 (NEDD8)
- Small ubiquitin-like modifier (SUMO)
- Ubiquitin-like proteins (UBL)
- UBL-binding domain
ASJC Scopus subject areas
- General Biochemistry,Genetics and Molecular Biology