CATH Classification

Domain Context

CATH Clusters

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

Enzyme Information

3.6.4.-
Acting on ATP; involved in cellular and subcellular movement.
based on mapping to UniProt Q149N8
2.3.2.27
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.
-!- 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)

Q149N8
SHPRH_HUMAN
Homo sapiens
E3 ubiquitin-protein ligase SHPRH

PDB Structure

PDB 2M85
External Links
Method SOLUTION NMR
Organism
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.
J.Biomol.Nmr