Ontology highlight
ABSTRACT:
SUBMITTER: Wu PY
PROVIDER: S-EPMC204484 | biostudies-literature | 2003 Oct
REPOSITORIES: biostudies-literature
Wu Pei-Ying PY Hanlon Mary M Eddins Michael M Tsui Colleen C Rogers Richard S RS Jensen Jane P JP Matunis Michael J MJ Weissman Allan M AM Wolberger Cynthia C Pickart Cecile M CM
The EMBO journal 20031001 19
Ubiquitin (Ub) regulates diverse functions in eukaryotes through its attachment to other proteins. The defining step in this protein modification pathway is the attack of a substrate lysine residue on Ub bound through its C-terminus to the active site cysteine residue of a Ub-conjugating enzyme (E2) or certain Ub ligases (E3s). So far, these E2 and E3 cysteine residues are the only enzyme groups known to participate in the catalysis of conjugation. Here we show that a strictly conserved E2 aspar ...[more]