CATH Classification

Domain Context

CATH Clusters

Superfamily Zinc/RING finger domain, C3HC4 (zinc finger)
Functional Family E3 ubiquitin-protein ligase RNF125 isoform X2

Enzyme Information

2.3.2.27
RING-type E3 ubiquitin transferase.
based on mapping to UniProt Q96EQ8
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 2.3.2.23) 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 2.3.2.26 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 2.3.2.32). -!- Cf. EC 2.3.2.31.

UniProtKB Entries (1)

Q96EQ8
RN125_HUMAN
Homo sapiens
E3 ubiquitin-protein ligase RNF125

PDB Structure

PDB 5DKA
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
A C2HC zinc finger is essential for the RING-E2 interaction of the ubiquitin ligase RNF125.
Bijlmakers, M.J., Teixeira, J.M., Boer, R., Mayzel, M., Puig-Sarries, P., Karlsson, G., Coll, M., Pons, M., Crosas, B.
Sci Rep