CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.10 | Roll |
|
3.10.20 | Ubiquitin-like (UB roll) |
|
3.10.20.90 | Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 |
Domain Context
CATH Clusters
| Superfamily | Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 |
| Functional Family | deubiquitinating protein VCIP135 isoform X1 |
Enzyme Information
| 3.4.19.12 |
Ubiquitinyl hydrolase 1.
based on mapping to UniProt Q8CF97
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)
| Q8CF97 |
VCIP1_RAT
Rattus norvegicus
Deubiquitinating protein VCIP135
|
PDB Structure
| PDB | 2MX2 |
| External Links | |
| Method | SOLUTION NMR |
| Organism | |
| Primary Citation |
Structure and interaction mode of the UBX-L domain of VCIP135 determined by solution NMR spectroscopy
To be Published
|