CATH Domain 1fbvA04
|1.20.930||Transcription Elongation Factor S-II; Chain A|
|1.20.930.20||Adaptor protein Cbl, N-terminal domain|
|Superfamily||Adaptor protein Cbl, N-terminal domain|
|Functional Family||E3 ubiquitin-protein ligase CBL|
RING-type E3 ubiquitin transferase.
based on mapping to UniProt P22681
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)- ubiquitinyl-[acceptor protein]-L-lysine.
-!- RING E3 ubiquitin transferases serve as mediators bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme (EC 220.127.116.11) and an acceptor protein together to enable the direct transfer of ubiquitin through the formation of an isopeptide bond between the C-terminal glycine residue of ubiquitin and the epsilon-amino group of an L-lysine residue of the acceptor protein. -!- Unlike EC 18.104.22.168 the RING-E3 domain does not form a catalytic thioester intermediate with ubiquitin. -!- Many members of the RING-type E3 ubiquitin transferase family are not able to bind a substrate directly, and form a complex with a cullin scaffold protein and a substrate recognition module (the complexes are named CRL for Cullin-RING-Ligase). -!- In these complexes, the RING-type E3 ubiquitin transferase provides an additional function, mediating the transfer of a NEDD8 protein from a dedicated E2 carrier to the cullin protein (see EC 22.214.171.124). -!- Cf. EC 126.96.36.199.
UniProtKB Entries (1)
Tyrosine-protein kinase ZAP-70
Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases.