Protein Variants | Comment | Organism |
---|---|---|
C713S | no isopeptidase activity, no desumoylation of (SUMO-1)-Ran GTPase-activating protein 1 conjugate | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
nucleolus | localize predominantly to the nucleolus | Homo sapiens | 5730 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q96HI0 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(SUMO-1)-Ran GTPase-activating protein 1 conjugate + H2O | SENP5 more efficiently removes SUMO-2 and SUMO-3 than SUMO-1 from SUMO-modified Ran GTPase-activating protein 1 conjugate | Homo sapiens | SUMO-1 + Ran GTPase-activating protein 1 | - |
? | |
(SUMO-2)-Ran GTPase-activating protein 1 conjugate + H2O | SENP5 more efficiently removes SUMO-2 and SUMO-3 than SUMO-1 from SUMO-modified Ran GTPase-activating protein 1 conjugate | Homo sapiens | SUMO-2 + Ran GTPase-activating protein 1 | - |
? | |
(SUMO-3)-Ran GTPase-activating protein 1 conjugate + H2O | SENP5 more efficiently removes SUMO-2 and SUMO-3 than SUMO-1 from SUMO-modified Ran GTPase-activating protein 1 conjugate | Homo sapiens | SUMO-3 + Ran GTPase-activating protein 1 | - |
? | |
SUMO-1 precursor + H2O | the catalytic domain of SENP5 shows higher efficiency for processing SUMO-3 over SUMO-1 precursors in vitro | Homo sapiens | SUMO-1 + His-Ser-Thr-Val | - |
? | |
SUMO-3 precursor + H2O | the catalytic domain of SENP5 shows higher efficiency for processing SUMO-3 over SUMO-1 precursors in vitro | Homo sapiens | SUMO-3 + Val-Pro-Glu-Ser-Ser-Leu-Ala-Gly-His-Ser-Phe | - |
? |
General Information | Comment | Organism |
---|---|---|
malfunction | knockdown of SENP5 leads to an increase in cells with more than one nucleus or aberrant nuclear structure consistent with defects in mitosis and cytokinesis | Homo sapiens |
physiological function | SENP5 is required for cell division. SENP5 has nonredundant functions in vivo, likely due to distinct substrate specificities in SUMO maturation and deconjugation that are regulated by both the catalytic and noncatalytic domains of the enzyme | Homo sapiens |