Ubiquitin-conjugating enzymes (EC 6.3.2.19) (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.
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