3.4.22.B72: SENP3 peptidase
This is an abbreviated version!
For detailed information about SENP3 peptidase, go to the full flat file.
Word Map on EC 3.4.22.B72
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3.4.22.B72
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sumoylation
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senps
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deconjugation
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isopeptidase
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de-sumoylation
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ranbp2
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de-conjugating
- 3.4.22.B72
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sumoylation
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senps
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deconjugation
- isopeptidase
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de-sumoylation
- ranbp2
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de-conjugating
Reaction
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, sentrin-specific protease 3, small ubiquitin-like modifier-specific protease 3, SUMO-2/3-specific protease, SUMO-specific isopeptidase, SUMO-specific protease 3, SUMO-specific proteases 3, SUMO2/3-specific protease
ECTree
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General Information
General Information on EC 3.4.22.B72 - SENP3 peptidase
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evolution
malfunction
metabolism
physiological function
additional information
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the enzyme is a member of the small ubiquitin-like modifier-specific protease family
evolution
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the enzyme is a member of the SUMO-specific protease family
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evolution
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the enzyme is a member of the small ubiquitin-like modifier-specific protease family
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depletion of SENP3 by short interfering RNA interferes with nucleolar ribosomal RNA processing and inhibits the conversion of the 32S rRNA species to the 28S form, thus phenocopying the processing defect observed on depletion of nucleophosmin 1 (NPM1)
malfunction
upon depletion of SENP3 the amount of Borealin-SUMO2/3 conjugates is significantly increased
malfunction
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downregulation of SENP3 increases Drp1 SUMO-2/3ylation and decreases its mitochondrial association, which reduces Drp1-dependent cytochrome c release via reduced mitochondrial fission and fragmentation. Depletion of enzyme SENP3 prolongs GTPase Drp1 SUMOylation, which suppresses Drp1-mediated cytochrome c release and caspase-mediated cell death. SENP3 levels recover following reoxygenation after oxygen/glucose deprivation allowing deSUMOylation of Drp1, which facilitates Drp1 localization at mitochondria and promotes fragmentation and cytochrome c release. RNAi knockdown of SENP3 protects cells from reoxygenation-induced cell death via a mechanism that requires Drp1 SUMOylation
malfunction
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expression of mesenchymal marker genes and cell migration ability are enhanced in SENP3-overexpressing gastric cancer cells and attenuated in SENP3-knockdown cells
malfunction
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in the absence of SENP3, the association of menin and Ash2L with the DLX3 geneis impaired, leading to decreased H3K4 methylation and reduced recruitment of active RNA polymerase II
metabolism
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molecular mechanisms of SUMOylation in the cellular response to oxygen/glucose deprivation, overview
SENP3 appears to be a key mediator in mild oxidative stress-induced cell proliferation via regulation of the SUMOylation status of promyelocytic leukemia protein
physiological function
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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
physiological function
SENP3 is a redox sensor that regulates hypoxia-inducible factor-1alpha transcriptional activity under oxidative stress through the de-SUMOylation of p300
physiological function
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enzyme SENP3 may play an important role in the development of oral squamous cell carcinoma under oxidative stress
physiological function
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enzyme SENP3-mediated deSUMOylation of dynamin-related protein 1 promotes cell death following ischaemia
physiological function
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SUMO-specific isopeptidase SENP3 regulates MLL1/MLL2 methyltransferase complexes and controls osteogenic differentiation of and DLX3 and RUNX2 expression in human dental follicle stem cells. SUMO-specific isopeptidase SENP3 controls H3K4 methylation by regulating histone-modifying SET1/MLL complexes. SET1/MLL complexes are composed of a histone methyltransferase and the regulatory components WDR5, RbBP5, Ash2L, and DPY-30. MLL1/MLL2 complexes contain menin as additional component and are particularly important for the activationof HOX genes
physiological function
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the enzyme potentiates the transcriptional activity of FOXC2 through deSUMOylation, in favor of the induction of specific mesenchymal gene expression in gastric cancer metastasis. And the enzyme upregulates the transcription of N-cadherin through deSUMOlyation of FOXC2
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
hepatic SENP3 is upregulated in a nonalcoholic fatty liver disease model in vivo and after loading hepatocytes with free fatty acids in vitro. SENP3 gene silencing is associated in vitro with amelioration of lipid accumulation and overexpression with enhancement of lipid accumulation
physiological function
hepatic SENP3 is upregulated in nonalcoholic fatty liver disease patients and after loading hepatocytes with free fatty acids in vitro. SENP3 gene silencing is associated in vitro with amelioration of lipid accumulation and overexpression with enhancement of lipid accumulation. Among SENP3 related genes in nonalcoholic fatty liver disease, apoe, a2m and tnfrsf11b are regulated by SENP3 with free fatty acid stimulation
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
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
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additional information
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the SUMO-2/3-specific protease SENP3 is degraded during oxygen/glucose deprivation, proteolysis of SENP3 requires PERK kinase activity, in vitro modeling of ischaemia, via a pathway involving the unfolded protein response kinase PERK and the lysosomal enzyme cathepsin B, overview. SENP3 degradation does not involve ubiquitination