 |
|
| PROSITE documentation PDOC00127 |
Ubiquitin carboxyl-terminal hydrolases family 1 cysteine active site
Description:
Ubiquitin carboxyl-terminal hydrolases (EC 3.4.19.12) (UCH) (deubiquitinating
enzymes) [1,2] are thiol proteases that recognize and hydrolyze the peptide
bond at the C-terminal glycine of ubiquitin. These enzymes are involved in the
processing of poly-ubiquitin precursors as well as that of ubiquinated
proteins.
There are two distinct families of UCH. The first class consist of enzymes of
about 25 Kd and is currently represented by:
- Mammalian isozymes L1, L3 and L5.
- Yeast YUH1.
- Drosophila Uch.
One of the active site residues of class-I UCH [3] is a cysteine. We derived
a signature pattern from the region around that residue.
Note:
These proteins belong to family C12 in the classification of peptidases
[4,E1].
Last update:
December 2001 / Text revised.
Technical section:
PROSITE method (with tools and information) covered by this documentation:
| UCH_1, PS00140; Ubiquitin carboxyl-terminal hydrolase family 1 cysteine active-site (PATTERN) |
| Consensus pattern: |
Q-x(3)-N-[SA]-C-G-x(3)-[LIVM](2)-H-[SA]-[LIVM]-[SA]
C is the active site residue |
| Sequences known to belong to this class detected by the pattern: |
ALL |
| Other sequence(s) detected in Swiss-Prot: |
NONE. |
|
|
|
| Matching PDB structures:
1CMX 1UCH 1XD3 2ETL ... [ALL] |
References:
| 1 |
Authors | Jentsch S., Seufert W., Hauser H.-P. |
| Title | Genetic analysis of the ubiquitin system. |
| Source | Biochim. Biophys. Acta 1089:127-139(1991). |
| PubMed ID | 1647207 |
| 2 |
Authors | D'andrea A., Pellman D. |
| Source | Crit. Rev. Biochem. Mol. Biol. 33:337-352(1998). |
| 3 |
Authors | Johnston S.C., Larsen C.N., Cook W.J., Wilkinson K.D., Hill C.P. |
| Title | Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 A resolution. |
| Source | EMBO J. 16:3787-3796(1997). |
| PubMed ID | 9233788 |
| DOI | 10.1093/emboj/16.13.3787 |
| 4 |
Authors | Rawlings N.D., Barrett A.J. |
| Title | Families of cysteine peptidases. |
| Source | Methods Enzymol. 244:461-486(1994). |
| PubMed ID | 7845226 |
Copyright:
PROSITE is copyright. It is produced by the Swiss Institute of
Bioinformatics (SIB). There are no restrictions on its use by non-profit
institutions as long as its content is in no way modified. Usage by and
for commercial entities requires a license agreement. For information
about the licensing scheme send an email to license@isb-sib.ch or
see: http://www.expasy.org/prosite/prosite_license.htm.
Miscellaneous:
View entry in original PROSITE document format
View entry in raw text format (no links)