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- **************************************************************
- * Ubiquitin carboxyl-terminal hydrolases family 2 signatures *
- **************************************************************
-
- Ubiquitin carboxyl-terminal hydrolases (EC 3.1.2.15) (UCH) (deubiquitinating
- enzymes) [1] 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 second class [2] consist of large
- proteins (800 to 200 residues) and is currently represented by:
-
- - Yeast UBP1, UBP2, UBP3 and UBP4 (DOA4/SSV7).
- - Yeast hypothetical protein YKR098c.
- - Human tre-2.
- - Mouse Unp.
- - Drosophila fat facets protein (gene faf).
- - Caenorhabditis elegans hypothetical protein R10E11.3.
-
- These proteins only share two regions of similarity. The first region contains
- a conserved cysteine which is probably implicated in the catalytic mechanism.
- The second region contains two conserved histidines residues, one of which is
- also probably implicated in the catalytic mechanism. We have developed
- signature pattern for both conserved regions.
-
- -Consensus pattern: [LIVMFY]-x(3)-[AGC]-[NA]-x-C-[FY]-[LIVMC]-[NS]-[SC]-x-
- [LIVM]-Q
- [C is the putative active site residue]
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: NONE.
-
- -Consensus pattern: Y-x-L-x-[SAG]-[LIVMT]-x(2)-H-x-G-x(4,5)-G-H-Y
- [The two H's are putative active site residues]
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: dog apomucin.
-
- -Last update: June 1994 / First entry.
-
- [ 1] Jentsch S., Seufert W., Hauser H.-P.
- Biochim. Biophys. Acta 1089:127-139(1991).
- [ 2] Papa F.R., Hochstrasser M.
- Nature 366:313-319(1993).
-