Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(SUMO-1)-mitochondrial fission GTPase DRP1 congugate + H2O
SUMO-1 + mitochondrial fission GTPase DRP1
(SUMO-1)-Ran GTPase-activating protein 1 conjugate + H2O
SUMO-1 + Ran GTPase-activating protein 1
SENP5 more efficiently removes SUMO-2 and SUMO-3 than SUMO-1 from SUMO-modified Ran GTPase-activating protein 1 conjugate
-
-
?
(SUMO-2)-Ran GTPase-activating protein 1 conjugate + H2O
SUMO-2 + Ran GTPase-activating protein 1
SENP5 more efficiently removes SUMO-2 and SUMO-3 than SUMO-1 from SUMO-modified Ran GTPase-activating protein 1 conjugate
-
-
?
(SUMO-3)-Ran GTPase-activating protein 1 conjugate + H2O
SUMO-3 + Ran GTPase-activating protein 1
SENP5 more efficiently removes SUMO-2 and SUMO-3 than SUMO-1 from SUMO-modified Ran GTPase-activating protein 1 conjugate
-
-
?
SUMO-1 precursor + H2O
SUMO-1 + His-Ser-Thr-Val
the catalytic domain of SENP5 shows higher efficiency for processing SUMO-3 over SUMO-1 precursors in vitro
-
-
?
SUMO-3 precursor + H2O
SUMO-3 + Val-Pro-Glu-Ser-Ser-Leu-Ala-Gly-His-Ser-Phe
the catalytic domain of SENP5 shows higher efficiency for processing SUMO-3 over SUMO-1 precursors in vitro
-
-
?
SUMOylated ATRIP + H2O
?
ATRIP i.e regulator of ATR, ATM [ataxia telangiectasia-mutated]- and Rad3-related kinase
-
-
?
SUMOylated dynamin related protein + H2O
dynamin related protein + SUMO
-
-
-
-
?
(SUMO-1)-mitochondrial fission GTPase DRP1 congugate + H2O
SUMO-1 + mitochondrial fission GTPase DRP1
-
-
-
-
?
(SUMO-1)-mitochondrial fission GTPase DRP1 congugate + H2O
SUMO-1 + mitochondrial fission GTPase DRP1
SENP5 catalyzes the cleavage of SUMO1 from a number of mitochondrial substrates. SENP5 is a new regulator of SUMO1 proteolysis from mitochondrial targets, impacting mitochondrial morphology and metabolism
-
-
?
(SUMO-1)-mitochondrial fission GTPase DRP1 congugate + H2O
SUMO-1 + mitochondrial fission GTPase DRP1
SENP5 preferentially deSUMOylates SUMO2 and SUMO3 proteins
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(SUMO-1)-mitochondrial fission GTPase DRP1 congugate + H2O
SUMO-1 + mitochondrial fission GTPase DRP1
SUMOylated dynamin related protein + H2O
dynamin related protein + SUMO
-
-
-
-
?
(SUMO-1)-mitochondrial fission GTPase DRP1 congugate + H2O
SUMO-1 + mitochondrial fission GTPase DRP1
-
-
-
-
?
(SUMO-1)-mitochondrial fission GTPase DRP1 congugate + H2O
SUMO-1 + mitochondrial fission GTPase DRP1
SENP5 catalyzes the cleavage of SUMO1 from a number of mitochondrial substrates. SENP5 is a new regulator of SUMO1 proteolysis from mitochondrial targets, impacting mitochondrial morphology and metabolism
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Breast Neoplasms
SENP5 mediates breast cancer invasion via a TGF?RI SUMOylation cascade.
Breast Neoplasms
The SUMO-specific protease SENP5 controls DNA damage response and promotes tumorigenesis in hepatocellular carcinoma.
Carcinogenesis
The SUMO-specific protease SENP5 controls DNA damage response and promotes tumorigenesis in hepatocellular carcinoma.
Carcinoma
Inhibition of SENP5 suppresses cell growth and promotes apoptosis in osteosarcoma cells.
Carcinoma
Overexpression of SENP5 in oral squamous cell carcinoma and its association with differentiation.
Carcinoma
Sentrin/small ubiquitin-like modifier-specific protease 5 protects oral cancer cells from oxidative stress-induced apoptosis.
Carcinoma
The SUMO-specific protease SENP5 controls DNA damage response and promotes tumorigenesis in hepatocellular carcinoma.
Carcinoma, Hepatocellular
The SUMO-specific protease SENP5 controls DNA damage response and promotes tumorigenesis in hepatocellular carcinoma.
Cardiomyopathies
SENP5, a SUMO isopeptidase, induces apoptosis and cardiomyopathy.
Cardiomyopathy, Dilated
SUMOylation in cardiac disorders - a review.
Epilepsy
SUMO proteases SENP3 and SENP5 spatiotemporally regulate the kinase activity of Aurora A.
Glioblastoma
SUMOylation Regulator-Related Molecules Can Be Used as Prognostic Biomarkers for Glioblastoma.
Heart Failure
SUMOylation in cardiac disorders - a review.
Muscular Diseases
SENP5, a SUMO isopeptidase, induces apoptosis and cardiomyopathy.
Neoplasms
The SUMO-specific protease SENP5 controls DNA damage response and promotes tumorigenesis in hepatocellular carcinoma.
Osteosarcoma
Inhibition of SENP5 suppresses cell growth and promotes apoptosis in osteosarcoma cells.
Osteosarcoma
The SUMO-specific protease SENP5 controls DNA damage response and promotes tumorigenesis in hepatocellular carcinoma.
Squamous Cell Carcinoma of Head and Neck
Inhibition of SENP5 suppresses cell growth and promotes apoptosis in osteosarcoma cells.
Squamous Cell Carcinoma of Head and Neck
Overexpression of SENP5 in oral squamous cell carcinoma and its association with differentiation.
Squamous Cell Carcinoma of Head and Neck
Sentrin/small ubiquitin-like modifier-specific protease 5 protects oral cancer cells from oxidative stress-induced apoptosis.
Squamous Cell Carcinoma of Head and Neck
The SUMO-specific protease SENP5 controls DNA damage response and promotes tumorigenesis in hepatocellular carcinoma.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
SENP5 expression is chiefly detected in the cytoplasm of tumor cells and in the cytoplasm and/or nucleus of normal epithelium cells
brenda
-
-
brenda
Senp5 is localized to presynaptic terminals, postsynaptic spines, and mitochondria in axon terminals
brenda
-
-
brenda
-
brenda
-
in interphase, SenP5 resides primarily within the nucleoli, in addition to a cytosolic pool. Relocalization of SenP5 from the nucleoli to the mitochondrial surface at G2/M transition prior to nuclear envelope breakdown
brenda
-
in interphase, SenP5 resides primarily within the nucleoli, in addition to a cytosolic pool. Relocalization of SenP5 from the nucleoli to the mitochondrial surface at G2/M transition prior to nuclear envelope breakdown. Transition of SenP5 to the mitochondria plays an important role in mitochondrial fragmentation during mitosis
brenda
Senp5 is localized to presynaptic terminals, postsynaptic spines, and mitochondria in axon terminals
brenda
-
in interphase, SenP5 resides primarily within the nucleoli, in addition to a cytosolic pool. Relocalization of SenP5 from the nucleoli to the mitochondrial surface at G2/M transition prior to nuclear envelope breakdown
brenda
localize predominantly to the nucleolus
brenda
-
SENP5 expression is chiefly detected in the cytoplasm of tumor cells and in the cytoplasm and/or nucleus of normal epithelium cells
brenda
-
SENP5 localizes within the granular component of the nucleolus, a subnucleolar compartment that contains B23/nucleophosmin
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
metabolism
-
SUMO conjugation is a dynamic posttranslational modification that can be readily reversed by the activity of sentrin-specific proteases (SENPs). Elevated expression of SENP5 in the failing human hearts, development of cardiomyopathy, overview
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
malfunction
silencing of SENP5 results in a fragmented and altered morphology
malfunction
-
H2O2 alone enhances mitochondrial network formation, whereas the combination of H2O2 and enzyme SENP5 silencing leads to mitochondrial fragmentation in the CAL-27 cells
malfunction
-
SENP5 enzyme overexpression leads to cardiac dysfunction, accompanied by decreased cardiomyocyte proliferation and elevated apoptosis, overview. Transgenic SENP5-hearts, that are larger than wild-type, unveil a decrease in SUMO attachment to dynamin related protein (Drp1), a factor critical for mitochondrial fission, phenotype, overview
physiological function
SENP5 is a regulator of SUMO1 proteolysis from mitochondrial targets. SENP5 is required to maintain normal mitochondrial morphology and to control intracellular levels of reactive oxygen species. SENP5 expression affects the mitochondrial morphology by increasing the number of cells with elongated tubules
physiological function
-
SENP5 is essential in mitosis and/or cytokinesis
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
physiological function
-
enzyme SENP5 protects the oral squamous cell carcinoma cells from oxidative stress-induced apoptosis. Cell with higher enzyme content show a higher resistance to H2O2, overview
physiological function
-
SUMO isopeptidase SENP5 induces apoptosis and cardiomyopathy, which represents a major health issue and is a leading cause of heart failure. Significant increase in the level of enzyme SEN,P5 in human idiopathic failing hearts
physiological function
Senp5 is overexpressed in hepatocellular carcinoma samples and required for hepatocellular carcinoma cells proliferation both in vitro and in vivo. SENP5-depleted Hep-G2 cells exhibit hypersensitivity to IR and etoposide treatment with defective checkpoint activation including decreased activation of ATM and Rad3-related kinases ATR and phosphorylation of ATR targets. Senp5 interacts with ATR regulator ATRIP and promotes ATRIP deSUMOylation
physiological function
Senp5 is significantly repressed in clinical acute myeloid leukemia when compared to healthy neutrophil samples. SENP5 expression is induced during neutrophil differentiation of acute myeloid leukemia cells, and knocking down SENP5 results in significantly attenuated neutrophil differentiation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Zunino, R.; Schauss, A.; Rippstein, P.; Andrade-Navarro, M.; McBride, H.M.
The SUMO protease SENP5 is required to maintain mitochondrial morphology and function
J. Cell Sci.
120
1178-1188
2007
Homo sapiens (Q96HI0)
brenda
Di Bacco, A.; Ouyang, J.; Lee, H.Y.; Catic, A.; Ploegh, H.; Gill, G.
The SUMO-specific protease SENP5 is required for cell division
Mol. Cell. Biol.
26
4489-4498
2006
Homo sapiens (Q96HI0)
brenda
Zunino, R.; Braschi, E.; Xu, L.; McBride, H.M.
Translocation of SenP5 from the nucleoli to the mitochondria modulates DRP1-dependent fission during mitosis
J. Biol. Chem.
284
17783-17795
2009
Homo sapiens
brenda
Yun, C.; Wang, Y.; Mukhopadhyay, D.; Backlund, P.; Kolli, N.; Yergey, A.; Wilkinson, K.D.; Dasso, M.
Nucleolar protein B23/nucleophosmin regulates the vertebrate SUMO pathway through SENP3 and SENP5 proteases
J. Cell Biol.
183
589-595
2008
Homo sapiens
brenda
Ding, X.; Sun, J.; Wang, L.; Li, G.; Shen, Y.; Zhou, X.; Chen, W.
Overexpression of SENP5 in oral squamous cell carcinoma and its association with differentiation
Oncol. Rep.
20
1041-1045
2008
Homo sapiens
brenda
Kim, E.Y.; Zhang, Y.; Beketaev, I.; Segura, A.M.; Yu, W.; Xi, Y.; Chang, J.; Wang, J.
SENP5, a SUMO isopeptidase, induces apoptosis and cardiomyopathy
J. Mol. Cell. Cardiol.
78
154-164
2015
Homo sapiens
brenda
Cheng, Y.; Guo, X.; Gong, Y.; Ding, X.; Yu, Y.
Sentrin/small ubiquitin-like modifier-specific protease5 protects oral cancer cells from oxidative stress-induced apoptosis
Mol. Med. Rep.
12
2009-2014
2015
Homo sapiens
brenda
Jin, Z.L.; Pei, H.; Xu, Y.H.; Yu, J.; Deng, T.
The SUMO-specific protease SENP5 controls DNA damage response and promotes tumorigenesis in hepatocellular carcinoma
Eur. Rev. Med. Pharmacol. Sci.
20
3566-3573
2016
Homo sapiens (Q96HI0)
brenda
Akiyama, H.; Nakadate, K.; Sakakibara, S.I.
Synaptic localization of the SUMOylation-regulating protease SENP5 in the adult mouse brain
J. Comp. Neurol.
526
990-1005
2018
Mus musculus (Q6NXL6), Mus musculus
brenda
Federzoni, E.A.; Gloor, S.; Jin, J.; Shan-Krauer, D.; Fey, M.F.; Torbett, B.E.; Tschan, M.P.
Linking the SUMO protease SENP5 to neutrophil differentiation of AML cells
Leuk. Res. Rep.
4
32-35
2015
Homo sapiens (Q96HI0)
brenda