|PROSITE documentation PDOC00163 [for PROSITE entry PS50127]|
Ubiquitin-conjugating enzymes (EC 220.127.116.11) (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:
April 2006 / Pattern revised.
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).|
|2||Authors||Jentsch S. Seufert W. Hauser H.-P.|
|Title||Genetic analysis of the ubiquitin system.|
|Source||Biochim. Biophys. Acta 1089:127-139(1991).|
|Title||The ubiquitin pathway for protein degradation.|
|Source||Trends Biochem. Sci. 16:265-268(1991).|