Any feedback?
Information on EC 3.4.22.B73 - SENP5 peptidase and Organism(s) Homo sapiens
for references in articles please use BRENDA:EC3.4.22.B73preliminary BRENDA-supplied EC number
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.4.22.B73 SENP5 peptidaseSpecify your search results
Word Map
- 3.4.22.B73
-
senps
-
desumoylation
-
deconjugation
- isopeptidase
-
mitosis
-
fission
- nucleolus
-
regulator-related
- medicine
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
SENP5 more efficiently removes SUMO-2 and SUMO-3 than SUMO-1 from SUMO-modified target such as Ran GTPase-activating protein 1. Catalyzes desumoylation of mitochondrial fission GTPase DRP1.
Synonyms
senp5, sumo-specific protease 5, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(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
-
-
?
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
B23/nucleophosmin
-
B23/nucleophosmin physically interacts with SENP3 and SENP5 and regulates their abundance. It thus plays a critical role in controlling the profile of SUMO conjugates within nucleoli through SENP3 and SENP5
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
significant increase in the level of enzyme SENP5 in human idiopathic failing hearts
-
the SENP5 expression status is associated with differentiation of oral squamous cell carcinoma and not with any other clinicopathological parameters
-
enzyme SENP5 overexpression occurs in 31 OSCC tissue specimens
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
SENP5 expression is chiefly detected in the cytoplasm of tumor cells and in the cytoplasm and/or nucleus of normal epithelium cells
-
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
-
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
-
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
-
SENP5 expression is chiefly detected in the cytoplasm of tumor cells and in the cytoplasm and/or nucleus of normal epithelium cells
-
SENP5 localizes within the granular component of the nucleolus, a subnucleolar compartment that contains B23/nucleophosmin
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
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
physiological function
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 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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C713S
no isopeptidase activity, no desumoylation of (SUMO-1)-Ran GTPase-activating protein 1 conjugate
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
transgenic overexpression of SENP5 in murine cardiomyocytes, overexpression of SENP5 leads to cardiac dysfunction, accompanied by decreased cardiomyocyte proliferation and elevated apoptosis
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
the SENP5 expression status is associated with differentiation of oral squamous cell carcinoma and not with any other clinicopathological parameters. No detected correlation between SENP5 expression and the degree of epithelial dysplasia in the paracarcinoma epithelium. No expression difference between primary tumors and lymph node metastatic lesions. SENP5 expression is not associated with lymph node metastasis and cumulative survival
medicine
Senp5 is significantly repressed in clinical acute myeloid leukemia when compared to healthy neutrophil samples
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
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)
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
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
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
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
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
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)
EXTERNAL LINKS (specific for EC-Number 3.4.22.B73)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
