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Details on Person Ubiquitin E3 ligases confer specificity to ubiquitination by...

Class:IdSummation:982860
_displayNameUbiquitin E3 ligases confer specificity to ubiquitination by...
_timestamp2010-11-01 10:30:58
created[InstanceEdit:982858] Garapati, P V, 2010-10-29
literatureReference[LiteratureReference:982870] RING domain E3 ubiquitin ligases
modified[InstanceEdit:983177] Jupe, S, 2010-10-29
[InstanceEdit:983290] Garapati, P V, 2010-11-01
textUbiquitin E3 ligases confer specificity to ubiquitination by recognizing target substrates and mediating transfer of ubiquitin from an E2 ubiquitin-conjugating enzyme to substrate (Raymond et al. 2009). E3 ligases includes a large, diverse set of proteins characterized by several defining motifs which include a HECT (homologous to E6-associated C-terminus), RING (Really Interesting New Gene) and U-box domains. The E3 ligases can be multisubunit complexes rather than a single polypeptide. Presently three different kinds of E3 complexes have been described called SCF, APC, and VHL. E3 ligases binds to both substrate and an E2 thioesterified with ubiquitin (E2-Ub).
(summation)[Reaction:983157] Interaction of E3 with substrate and E2-Ub complex [Homo sapiens]
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