CATH Classification

Domain Context

CATH Clusters

Superfamily Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Functional Family E3 ubiquitin-protein ligase UHRF1

Enzyme Information

2.3.2.27
RING-type E3 ubiquitin transferase.
based on mapping to UniProt Q96T88
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)

Q96T88
UHRF1_HUMAN
Homo sapiens
E3 ubiquitin-protein ligase UHRF1

PDB Structure

PDB 2FAZ
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Ubiquitin-Like Domain of Human Nuclear Zinc Finger Protein NP95
Walker, J.R., Wybenga-Groot, L., Doherty, R.S., Finerty Jr., P.J., Newman, E., Mackenzie, F.M., Weigelt, J., Sundstrom, M., Arrowsmith, C., Edwards, A., Bochkarev, A., Dhe-Paganon, S.
To be Published