CATH Classification

Domain Context

CATH Clusters

Superfamily Apoptosis, Tumor Necrosis Factor Receptor Associated Protein 2; Chain A
Functional Family TNF receptor-associated factor 6

Enzyme Information

2.3.2.27
RING-type E3 ubiquitin transferase.
based on mapping to UniProt Q12933
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)

Q12933
TRAF2_HUMAN
Homo sapiens
TNF receptor-associated factor 2

PDB Structure

PDB 1D0A
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
The structural basis for the recognition of diverse receptor sequences by TRAF2.
Ye, H., Park, Y.C., Kreishman, M., Kieff, E., Wu, H.
Mol.Cell