CATH Classification

Domain Context

CATH Clusters

Superfamily Zinc/RING finger domain, C3HC4 (zinc finger)
Functional Family E3 ubiquitin-protein ligase SHPRH isoform X1

Enzyme Information

Acting on ATP; involved in cellular and subcellular movement.
based on mapping to UniProt Q149N8
RING-type E3 ubiquitin transferase.
based on mapping to UniProt Q149N8
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 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 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 -!- Cf. EC

UniProtKB Entries (1)

Homo sapiens
E3 ubiquitin-protein ligase SHPRH

PDB Structure

PDB 2M85
External Links
Primary Citation
PHD domain from human SHPRH.
Machado, L.E., Pustovalova, Y., Kile, A.C., Pozhidaeva, A., Cimprich, K.A., Almeida, F.C., Bezsonova, I., Korzhnev, D.M.