CATH Classification

Domain Context

CATH Clusters

Superfamily Bromodomain-like
Functional Family Transcription intermediary factor 1-alpha

Enzyme Information
RING-type E3 ubiquitin transferase.
based on mapping to UniProt O15164
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
Transcription intermediary factor 1-alpha

PDB Structure

External Links
Primary Citation
Structure-Guided Design of IACS-9571, a Selective High-Affinity Dual TRIM24-BRPF1 Bromodomain Inhibitor.
Palmer, W.S., Poncet-Montange, G., Liu, G., Petrocchi, A., Reyna, N., Subramanian, G., Theroff, J., Yau, A., Kost-Alimova, M., Bardenhagen, J.P., Leo, E., Shepard, H.E., Tieu, T.N., Shi, X., Zhan, Y., Zhao, S., Barton, M.C., Draetta, G., Toniatti, C., Jones, P., Geck Do, M., Andersen, J.N.