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| PROSITE documentation PDOC00163 [for PROSITE entry PS00183] |
Ubiquitin-conjugating enzymes signature and profile
Ubiquitin-conjugating enzymes (EC 2.3.2.23) (UBC or E2 enzymes) [1,2,3] catalyze the covalent attachment of ubiquitin to target proteins. An activated ubiquitin moiety is transferred from an ubiquitin-activating enzyme (E1) to E2 which later ligates ubiquitin directly to substrate proteins with or without the assistance of 'N-end' recognizing proteins (E3).
In most species there are many forms of UBC (at least 9 in yeast) which are implicated in diverse cellular functions.
A cysteine residue is required for ubiquitin-thiolester formation. There is a single conserved cysteine in UBC's and the region around that residue is conserved in the sequence of known UBC isozymes. We have used that region as a signature pattern. We also developed a profile that spans the complete catalytical domain.
Expert(s) to contact by email: Last update:April 2006 / Pattern revised.
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PROSITE methods (with tools and information) covered by this documentation:
| 1 | Authors | Jentsch S. Seufert W. Sommer T. Reins H.-A. |
| Title | Ubiquitin-conjugating enzymes: novel regulators of eukaryotic cells. | |
| Source | Trends Biochem. Sci. 15:195-198(1990). | |
| PubMed ID | 2193438 |
| 2 | Authors | Jentsch S. Seufert W. Hauser H.-P. |
| Title | Genetic analysis of the ubiquitin system. | |
| Source | Biochim. Biophys. Acta 1089:127-139(1991). | |
| PubMed ID | 1647207 |
| 3 | Authors | Hershko A. |
| Title | The ubiquitin pathway for protein degradation. | |
| Source | Trends Biochem. Sci. 16:265-268(1991). | |
| PubMed ID | 1656558 |
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