CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.1900 | c-terminal domain of poly(a) binding protein |
|
1.10.1900.10 | c-terminal domain of poly(a) binding protein |
Domain Context
CATH Clusters
| Superfamily | c-terminal domain of poly(a) binding protein |
| Functional Family | E3 ubiquitin-protein ligase UBR5 isoform X1 |
Enzyme Information
| 2.3.2.26 |
HECT-type E3 ubiquitin transferase.
based on mapping to UniProt Q62671
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.
-!- In the first step the enzyme transfers ubiquitin from the E2 ubiquitin-conjugating enzyme (EC 2.3.2.23) to a cysteine residue in its HECT domain (which is located in the C-terminal region), forming a thioester bond. -!- In a subsequent step the enzyme transfers the ubiquitin to an acceptor protein, resulting in 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. -!- Cf. EC 2.3.2.27 and EC 2.3.2.31.
|
UniProtKB Entries (2)
| Q62671 |
UBR5_RAT
Rattus norvegicus
E3 ubiquitin-protein ligase UBR5
|
| Q9H074 |
PAIP1_HUMAN
Homo sapiens
Polyadenylate-binding protein-interacting protein 1
|
PDB Structure
| PDB | 3NTW |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
The MLLE domain of the ubiquitin ligase UBR5 binds to its catalytic domain to regulate substrate binding.
J. Biol. Chem.
|
