|Family type peptidase||C98.001 - USPL1 peptidase (Homo sapiens), MEROPS Accession MER0407721 (peptidase unit: 229-499)|
|Content of family||Family C98 contains isopeptidases that release SUMO from conjugated proteins|
Identifier created: MEROPS 9.8 (17 December 2012)|
The human USPL1 ('ubiquitin-specific protease-like 1', C98.001) has been characterized as a desumoylating enzyme (Schulz et al., 2012). Families C48 and C98 also contain peptidases that release SUMO from conjugated proteins (Hickey et al., 2012).
|Active site residues||C236 H456 D472 |
|Active site||The catalytic triad Cys236, His456 and Asp472 has been identified by sequence comparison with members of family C19 (Schulz et al., 2012). Mutagenesis of Trp229 and Trp237 residues in human USPL1 has implicated these residues in substrate binding because mutants failed to bind or cleave SUMO conjugates (Schulz et al., 2012).|
|Activities and specificities||Besides acting as an isopeptidase, USPL1 also acts as a normal peptidase being able to release SUMO from its precursor (Schulz et al., 2012). USLP1 does not bind or cleave ubiquitin conjugates (Schulz et al., 2012).|
|Molecular structure||No tertiary structure has yet been solved for any member of family C98. The family is, however, believed to be distantly related to family C19 and hence is a member of clan CA. Surprisingly, the three families of deSUMOlatying peptidases are members of three different clans despite being the same catalytic type.|