Ontology highlight
ABSTRACT:
SUBMITTER: Luders J
PROVIDER: S-EPMC1326417 | biostudies-literature | 2003 Dec
REPOSITORIES: biostudies-literature
Lüders Jens J Pyrowolakis George G Jentsch Stefan S
EMBO reports 20031107 12
Ubiquitin and ubiquitin-like modifiers (UBLs) form covalent complexes with other proteins by isopeptide formation between their carboxyl (C)-termini and epsilon-amino groups of lysine residues of acceptor proteins. A hallmark of UBLs is a protruding C-terminal tail with a terminal glycine residue, which is required for ATP-dependent conjugation. Recently, the highly conserved protein HUB1 (homologous to ubiquitin 1) has been reported to function as a UBL following C-terminal processing. HUB1 exh ...[more]