Home | Contact

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.

These proteins belong to family C12 in the classification of peptidases [4,E1].

December 2001 / Text revised.

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.

• Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00140 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00140 • Scan Swiss-Prot/TrEMBL entries against PS00140 • view ligand binding statistics

Matching PDB structures: 1CMX 1UCH 1XD3 2ETL ... [ALL]

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
Source	http://www.uniprot.org/docs/peptidas

PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. 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

Prosite License or see: prosite_license.html.


View entry in original PROSITE document format
View entry in raw text format (no links)

SIB Swiss Institute of Bioinformatics | Disclaimer