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| PROSITE documentation PDOC00127 [for PROSITE entry PS00140] |
Ubiquitin carboxyl-terminal hydrolases family 1 cysteine active site
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.
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PROSITE method (with tools and information) covered by this documentation:
| 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 |
| E1 | Title | https://www.uniprot.org/docs/peptidas |
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