CATH Classification

Domain Context

CATH Clusters

Superfamily Ubiquitin-related
Functional Family Sentrin-specific protease 7

Enzyme Information

3.4.22.68
Ulp1 peptidase.
based on mapping to UniProt Q9BQF6
Hydrolysis of the alpha-linked peptide bond in the sequence Gly- Gly-|-Ala-Thr-Tyr at the C-terminal end of the small ubiquitin-like modifier (SUMO) propeptide, Smt3, leading to the mature form of the protein. A second reaction involves the cleavage of an epsilon-linked peptide bond between the C-terminal glycine of the mature SUMO and the lysine epsilon-amino group of the target protein.
-!- The enzyme from Saccharomyces cerevisiae can also recognize small ubiquitin-like modifier 1 (SUMO-1) from human as a substrate in both SUMO-processing (alpha-linked peptide bonds) and SUMO-deconjugation (epsilon-linked peptide bonds) reactions. -!- Ulp1 has several functions, including an essential role in chromosomal segregation and progression of the cell cycle through the G2/M phase of the cell cycle. -!- Belongs to peptidase family C48.

UniProtKB Entries (1)

Q9BQF6
SENP7_HUMAN
Homo sapiens
Sentrin-specific protease 7

PDB Structure

PDB 3EAY
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structure of the Human SENP7 Catalytic Domain and Poly-SUMO Deconjugation Activities for SENP6 and SENP7.
Lima, C.D., Reverter, D.
J.Biol.Chem.
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