EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
3.4.22.B74 | di-SUMO-2 + H2O |
- |
Homo sapiens |
2 SUMO-2 |
- |
? |
3.4.22.B74 | di-SUMO-3 + H2O |
- |
Homo sapiens |
2 SUMO-3 |
- |
? |
3.4.22.B74 | poly-SUMO-2 + H2O |
- |
Homo sapiens |
? |
- |
? |
3.4.22.B74 | poly-SUMO-3 + H2O |
- |
Homo sapiens |
? |
- |
? |
3.4.22.B74 | SUMO-1 precursor + H2O |
- |
Homo sapiens |
SUMO-1 + His-Ser-Thr-Val |
- |
? |
3.4.22.B74 | SUMO-modified promyelocytic leukemia protein + H2O |
- |
Homo sapiens |
SUMO + promyelocytic leukemia protein |
- |
? |
3.4.22.B74 | more |
although SUMO-2/3 chains are the preferred substrate, SENP6 is also capable of cleaving mixed chains of SUMO-1 and SUMO-2/3 |
Homo sapiens |
? |
- |
? |
3.4.22.B74 | SUMOylated TRIM28 + H2O |
i.e. tripartite motif-containing 28, also called KAP1 or TIF1beta |
Mus musculus |
? |
- |
? |
3.4.22.B74 | more |
isozyme SENP6 shows isoform specificity for SUMO2/3 over SUMO1 |
Homo sapiens |
? |
- |
? |
3.4.22.B74 | (SUMO-3)-Ran GTPase-activating protein 1 conjugate + H2O |
SENP6 and SENP7 prefer SUMO2 or SUMO3 in deconjugation reactions with rates comparable with those catalyzed by SENP2. In contrast to SENP2, SENP6 and SENP7 are less able to deconjugate SUMO1-RanGAP1, and products are only detected at enzyme concentrations 100 x higher than that observed for reactions containing SENP2 |
Homo sapiens |
SUMO-3 + Ran GTPase-activating protein 1 |
- |
? |