CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.200 | Phosphorylase Kinase; domain 1 |
|
3.30.200.60 | Peptidase C65 Otubain, subdomain 1 |
Domain Context
CATH Clusters
| Superfamily | Peptidase C65 Otubain, subdomain 1 |
| Functional Family | Ubiquitin thioesterase |
Enzyme Information
| 3.4.19.12 |
Ubiquitinyl hydrolase 1.
based on mapping to UniProt Q96FW1
Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
-!- Links to polypeptides smaller than 60 residues are hydrolyzed more readily than those to larger polypeptides. -!- Isoforms exist with quantitatively different specificities among the best known being UCH-L1 and UCH-L3, major proteins of the brain of mammals. -!- Inhibited by ubiquitin aldehyde (in which Gly76 is replaced by aminoacetaldehyde). -!- Belongs to peptidase family C12.
|
| 3.4.19.12 |
Ubiquitinyl hydrolase 1.
based on mapping to UniProt Q9XVR6
Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
-!- Links to polypeptides smaller than 60 residues are hydrolyzed more readily than those to larger polypeptides. -!- Isoforms exist with quantitatively different specificities among the best known being UCH-L1 and UCH-L3, major proteins of the brain of mammals. -!- Inhibited by ubiquitin aldehyde (in which Gly76 is replaced by aminoacetaldehyde). -!- Belongs to peptidase family C12.
|
UniProtKB Entries (2)
| Q9XVR6 |
OTUBL_CAEEL
Caenorhabditis elegans
Ubiquitin thioesterase otubain-like
|
| P61088 |
UBE2N_HUMAN
Homo sapiens
Ubiquitin-conjugating enzyme E2 N
|
PDB Structure
| PDB | 4DHZ |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
The mechanism of OTUB1-mediated inhibition of ubiquitination.
Nature
|
