Information on EC 3.4.22.B72 - SENP3 peptidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.22.B72
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
SENP3 peptidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
The enzyme catalyzes the desumoylation of SUMO2 or SUMO3-modified target proteins, but has only weak activity against SUMO1 conjugates. SENP2 catalyzes deconjugation of SUMO2 from nucleophosmin 1.
show the reaction diagram
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(SUMO-2)-nucleophosmin 1 conjugate + H2O
SUMO-2 + nucleophosmin 1
show the reaction diagram
(SUMO-2)-p300 protein + H2O
(SUMO-2) + p300 protein
show the reaction diagram
(SUMO-2/3)-promyelocytic leukemia protein + H2O
SUMO-2/3 + promyelocytic leukemia protein
show the reaction diagram
(SUMO-3)-hypoxia-inducible factor-1alpha protein + H2O
SUMO-3 + hypoxia-inducible factor-1alpha protein
show the reaction diagram
SENP3 can remove SUMO3, but not SUMO1 from hypoxia-inducible factor-1alpha protein
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(SUMO2)-Borealin protein + H2O
SUMO2 + Borealin protein
show the reaction diagram
SUMOylated FOXC2 + H2O
FOXC2 + SUMO
show the reaction diagram
SUMOylated GTPase Drp1 + H2O
GTPase Drp1 + SUMO
show the reaction diagram
SUMOylated RbBP5 + H2O
RbBP5 + SUMO
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(SUMO-2)-nucleophosmin 1 conjugate + H2O
SUMO-2 + nucleophosmin 1
show the reaction diagram
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SENP3 as an essential factor for ribosome biogenesis. It is suggested that deconjugation of SUMO2 from nucleophosmin 1 (NPM1) by SENP3 is critically involved in 28S rRNA maturation
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(SUMO-2)-p300 protein + H2O
(SUMO-2) + p300 protein
show the reaction diagram
Q9H4L4
removing SUMO2/3 from p300 enhances its binding to HIF-1alpha. SENP3 is a redox sensor that regulates hypoxia-inducible factor-1alpha transcriptional activity under oxidative stress through the de-SUMOylation of p300
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(SUMO-2/3)-promyelocytic leukemia protein + H2O
SUMO-2/3 + promyelocytic leukemia protein
show the reaction diagram
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SENP3 appears to be a key mediator in mild oxidative stress-induced cell proliferation via regulation of the SUMOylation status of promyelocytic leukemia protein. SENP3-mediated de-conjugation of SUMO2/3 from PML is responsible for accelerated cell proliferation and decreased promyelocytic leukemia bodies under mild oxidative stress
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(SUMO2)-Borealin protein + H2O
SUMO2 + Borealin protein
show the reaction diagram
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Borealin is dynamically modified by SUMO2/3 during mitosis
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SUMOylated FOXC2 + H2O
FOXC2 + SUMO
show the reaction diagram
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deSUMOylation by enzyme SENP3
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SUMOylated GTPase Drp1 + H2O
GTPase Drp1 + SUMO
show the reaction diagram
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the substrate is a key target for SENP3-mediated deSUMOylation
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SUMOylated RbBP5 + H2O
RbBP5 + SUMO
show the reaction diagram
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deSUMOylation by enzyme SENP3, the protein is part of SET1/MLL complexes
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additional information
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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PERK activation is required for decreased SENP3 activity, overexpression of HA-tagged PERK causes loss of Flag-tagged SENP3 activity in HEK293 cells via a mechanism dependent on PERK kinase activity, which is blocked by overexpression of the PERK inhibitor p58IPK
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
B23/nucleophosmin
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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
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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the enzyme accumulates in a variety of cancers
Manually annotated by BRENDA team
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SENP3 is over-accumulated in a variety of primary human cancers including colon adenocarcinoma. SENP3-mediated de-SUMO2/3 of promyelocytic leukemia might contribute to the development or progression of human cancers
Manually annotated by BRENDA team
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correlation between SENP3 expression and gastric cancer metastasis
Manually annotated by BRENDA team
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immunohistochemical evaluation of SENP3 in patients and oral epithelial tissue adjacent to tumor, overview
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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weak expression in cytoplasm
Manually annotated by BRENDA team
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
the p19Arf protein triggers the sequential phosphorylation, polyubiquitination and rapid proteasomal degradation of Senp3, and this ability of p19Arf to accelerate Senp3 turnover also depends on the presence of nucleophosmin
polyubiquitination
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
SENP3 is continuously degraded through the ubiquitin proteasome pathway under basal condition. Reactive oxygen species inhibit this degradation
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Senp3 is destabilized in an nucleophosmin-dependent manner by a process involving sequential p19Arf-induced Senp3 phosphorylation, ubiquitination and proteasomal degradation
SENP3 is maintained at a low basal level under non-stress condition due to heat shock protein 90 (Hsp90)-independent Hsc70-interacting protein (CHIP)-mediated ubiquitination. Upon mild oxidative stress, SENP3 undergoes thiol modification, which recruits Hsp90. Hsp90/SENP3 association protects SENP3 from CHIP-mediated ubiquitination and subsequent degradation. This effect of Hsp90 requires the presence of CHIP
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
co-expression of Flag-tagged SENP3 with HA-tagged endoplasmic reticulum kinase PERK in HEK293 cells. Overexpression of HA-PERK causes loss of Flag-SENP3 in HEK293 cells, which is blocked by overexpression of the PERK inhibitor p58IPK
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SENP3 quantitative real-time PCR expression analysis
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
correlation between the clinicopathological features and SENP3 expression, overview
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expression of SUMO2/3-specific protease, SENP3 increases after treatment with 50 mM H2O2, and this increase occurs in a dose-dependent manner
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low doses of hydrogen peroxide induce an increase of the SENP3 protein; SENP3 is over-accumulated in a variety of primary human cancers including colon adenocarcinoma
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the enzyme is significantly upregulated in subarachnoid hemorrhage, the expression of SENP3 is increased in the brain cortex, in neurons, rather than astrocytes nor microglia
traumatic brain injury upregulates the enzyme expression in the brain, especially in the neurons and astrocytes
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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generation of HEK293T-sh-SENP3 stable cells