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Information on EC 3.4.22.B72 - SENP3 peptidase and Organism(s) Mus musculus and UniProt Accession Q9EP97
for references in articles please use BRENDA:EC3.4.22.B72preliminary BRENDA-supplied EC number
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3.4.22.B72 SENP3 peptidaseSpecify your search results
Word Map
- 3.4.22.B72
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desumoylation
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senps
- isopeptidase
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deconjugation
- nucleoplasm
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de-conjugating
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dynamin-related
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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.
Synonyms
senp3, sumo-specific protease 3, sumo-specific proteases 3, sumo2/3-specific protease, sumo-2/3-specific protease, sentrin-specific protease 3, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SENP3
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
additional information
?
-
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SUMO-2/3-conjugated targets are more successfully deconjugated by SENP3 than SUMO-1-containing species
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?
additional information
?
-
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enzyme SENP3 deconjugates SUMO2/3 from protein substrates
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-
?
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
additional information
?
-
-
SUMO-2/3-conjugated targets are more successfully deconjugated by SENP3 than SUMO-1-containing species
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?
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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dynamic changes in SENP3 expression in the cerebral cortex and in its cellular localization in traumatic brain injury compared to normal, overview
additional information
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immunohistochemical and expression anaysis of the enzyme in brain tissues, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
SENP3 is predominantly expressed in the nucleus of Sertoli and spermatocyte cells in adult mouse testis
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
evolution
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the enzyme is a member of the small ubiquitin-like modifier-specific protease family
physiological function
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the enzyme SENP3 is critical for maintaining the level of SUMOylated and un-SUMOylated substrates required for normal physiology because of its isopeptidase activity, whereby it cleaves the isopeptide bond between SUMO and substrate proteins, as a result, SENP3 may weaken the neuroprotective effect of SUMO-2/3
physiological function
knockdown of SENP3 compromises tight junctions in Sertoli cells by destructing the permeability function with a concomitant decline in trans-epithelial electrical resistance in primary Sertoli cells. SENP3 knockdown disrupts F-actin architecture in Sertoli cells through intervening Rac1/CDC42-N-WASP-Arp2/3 signaling pathway and Profilin-1 abundance
physiological function
SENP3 is a pivotal regulator of regulatory T cells (Treg cells) that functions by controlling the SUMOylation and nuclear localization of transcription factor BACH2. Treg cell-specific deletion of Senp3 results in T cell activation, autoimmune symptoms and enhanced antitumor T cell responses. SENP3-mediated BACH2 deSUMOylation prevents the nuclear export of BACH2, thereby repressing the genes associated with CD4+ T effector cell differentiation and stabilizing Treg cell-specific gene signatures. SENP3 accumulation triggered by reactive oxygen species is involved in Treg cell-mediated tumor immunosuppression
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). POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
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
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Senp3 is destabilized in an nucleophosmin-dependent manner by a process involving sequential p19Arf-induced Senp3 phosphorylation, ubiquitination and proteasomal degradation
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
traumatic brain injury upregulates the enzyme expression in the brain, especially in the neurons and astrocytes
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kuo, M.L.; den Besten, W.; Thomas, M.C.; Sherr, C.J.
Arf-induced turnover of the nucleolar nucleophosmin-associated SUMO-2/3 protease Senp3
Cell Cycle
7
3378-3387
2008
Mus musculus (Q9EP97), Mus musculus
Yu, Z.; Li, H.; Yan, H.Y.; Yang, Y.Q.; Zhang, D.D.; Huang, L.T.; Xie, G.B.; Liu, M.; Tohti, M.; Hang, C.H.
Expression and cell distribution of SENP3 in brain tissue after traumatic brain injury in mice: a pilot study
Cell. Mol. Neurobiol.
35
733-740
2015
Mus musculus, Mus musculus ICR
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 (Q9EP97), Mus musculus
Yu, X.; Lao, Y.; Teng, X.L.; Li, S.; Zhou, Y.; Wang, F.; Guo, X.; Deng, S.; Chang, Y.; Wu, X.; Liu, Z.; Chen, L.; Lu, L.M.; Cheng, J.; Li, B.; Su, B.; Jiang, J.; Li, H.B.; Huang, C.; Yi, J.; Zou, Q.
SENP3 maintains the stability and function of regulatory T cells via BACH2 deSUMOylation
Nat. Commun.
9
3157
2018
Mus musculus (Q9EP97)
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