CATH Classification
| Level | CATH Code | Description | 
|---|---|---|
|   | 3 | Alpha Beta | 
|   | 3.90 | Alpha-Beta Complex | 
|   | 3.90.70 | Cathepsin B; Chain A | 
|   | 3.90.70.10 | Cysteine proteinases | 
Domain Context
CATH Clusters
| Superfamily | Cysteine proteinases | 
| Functional Family | Putative ubiquitin carboxyl-terminal hydrolase CYLD | 
Enzyme Information
| 3.4.19.12 | Ubiquitinyl hydrolase 1. based on mapping to UniProt Q9NQC7 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 (1)
| Q9NQC7 | CYLD_HUMAN Homo sapiens Ubiquitin carboxyl-terminal hydrolase CYLD | 
PDB Structure
| PDB | 2VHF | 
| External Links | |
| Method | X-RAY DIFFRACTION | 
| Organism | |
| Primary Citation | The Structure of the Cyld Usp Domain Explains its Specificity for Lys63-Linked Polyubiquitin and Reveals a B-Box Module Mol.Cell.Biol. | 
