CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.533 | Death Domain, Fas |
|
1.10.533.10 | Death Domain, Fas |
Domain Context
CATH Clusters
| Superfamily | Death Domain, Fas |
| Functional Family | Baculoviral IAP repeat-containing 2 |
Enzyme Information
| 2.3.2.27 |
RING-type E3 ubiquitin transferase.
based on mapping to UniProt Q13490
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.
-!- The RING domain of E3 ubiquitin transferase serves as a mediator bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme and the 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 an the epsilon-amino group of an L-lysine residue of the acceptor protein. -!- The RING-E3 domain does not form a catalytic thioester intermediate with ubiquitin (unlike the HECT domain, EC 2.3.2.26). -!- RING-type ubiquitin transferases may occur as single-chain enzymes but also in dimeric forms or in multi-subunit assemblies. -!- Formerly EC 6.3.2.19 and EC 6.3.2.21.
|
UniProtKB Entries (1)
| Q13490 |
BIRC2_HUMAN
Homo sapiens
Baculoviral IAP repeat-containing protein 2
|
PDB Structure
| PDB | 2L9M |
| External Links | |
| Method | SOLUTION NMR |
| Organism | |
| Primary Citation |
CARD-mediated autoinhibition of cIAP1's E3 ligase activity suppresses cell proliferation and migration.
Mol.Cell
|
