CATH Classification

Domain Context

CATH Clusters

Superfamily 1.20.58.2190
Functional Family E3 ubiquitin-protein ligase RNF31

Enzyme Information

2.3.2.31
RBR-type E3 ubiquitin transferase.
based on mapping to UniProt Q96EP0
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.
-!- RBR-type E3 ubiquitin transferases have two RING fingers separated by an internal motif (IBR, for In Between RING). -!- The enzyme interacts with the CRL (Cullin-RING ubiquitin Ligase) complexes formed by certain RING-type E3 ubiquitin transferase (see EC 2.3.2.27), which include a neddylated cullin scaffold protein and a substrate recognition module. -!- The RING1 domain binds an EC 2.3.2.23, and transfers the ubiquitin that is bound to it to an internal cysteine residue in the RING2 domain, followed by the transfer of the ubiquitin from RING2 to the substrate. -!- Once the substrate has been ubiquitinated by the RBR-type ligase, it can be ubiqutylated further using ubiquitin carried directly on E2 enzymes, in a reaction catalyzed by EC 2.3.2.27. -!- Activity of the RBR-type enzyme is dependent on neddylation of the cullin protein in the CRL complex. -!- Cf. EC 2.3.2.26, EC 2.3.2.27, and EC 2.3.2.32.

UniProtKB Entries (1)

Q96EP0
RNF31_HUMAN
Homo sapiens
E3 ubiquitin-protein ligase RNF31

PDB Structure

PDB 4P0A
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Binding of OTULIN to the PUB domain of HOIP controls NF-kappa B signaling.
Schaeffer, V., Akutsu, M., Olma, M.H., Gomes, L.C., Kawasaki, M., Dikic, I.
Mol.Cell