Table 1.
Biological properties and structural information of SENP isoforms.
| SENP isoform | Specificity | Subcellular localization | Enzymatic activity | Amino acid residues | Structural information |
|---|---|---|---|---|---|
| SENP1 | SUMO-1/2/3 | Nucleoplasm | Precursor processing, isopeptidase | 643 Catalytic domain (419–643) |
Apo (2IYC, 2XPH, 2XRE, 2CKG) With SUMO-1 (2IY1, 2G4D) With SUMO-2 (2IYD, 2CKH) With SUMO-1 and substrate RanGAP1 (2IY0) |
| SENP2 | SUMO-1/2/3 | Nuclear pore | Precursor processing, isopeptidase | 589 Catalytic domain (365–589) |
Apo (1TH0) With SUMO-1 (1TGZ) With preSUMO-2 (2IO0, 3ZO5) With preSUMO-3 (2IO1) With SUMO-1 and substrate RanGAP1 (2IO2) With SUMO-2 and substrate RanGAP1 (2IO3) |
| SENP3 | SUMO-2/3 | Nucleolus | Isopeptidase | 574 Catalytic domain (353–574) |
Not available |
| SENP5 | SUMO-2/3 | Nucleolus | Precursor processing, isopeptidase | 755 Catalytic domain (567–755) |
Not available |
| SENP6 | SUMO-2/3 | Nucleoplasm | Isopeptidase | 1112 Catalytic domain (637–1112) |
Not available |
| SENP7 | SUMO-2/3 | Nucleoplasm | Isopeptidase | 984 Catalytic domain (662–984) |
Apo (3EAY) |