CATH Classification

Domain Context

CATH Clusters

Superfamily Zinc/RING finger domain, C3HC4 (zinc finger)
Functional Family E3 ubiquitin-protein ligase BRE1B

Enzyme Information

2.3.2.27
RING-type E3 ubiquitin transferase.
based on mapping to UniProt Q5VTR2
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)

Q5VTR2
BRE1A_HUMAN
Homo sapiens
E3 ubiquitin-protein ligase BRE1A

PDB Structure

PDB 5TRB
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structure and Function of the RING Domains of RNF20 and RNF40, Dimeric E3 Ligases that Monoubiquitylate Histone H2B.
Foglizzo, M., Middleton, A.J., Day, C.L.
J.Mol.Biol.