show all | hide all No of entries

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.B72
preliminary 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 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.B72 SENP3 peptidase
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Mus musculus
UNIPROT: Q9EP97
Word Map
The taxonomic range for the selected organisms is: Mus musculus
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SENP3
SUMO-specific proteases 3
244
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
SUMOylated transcription factor BACH2 + H2O
?
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
SUMO-2/3-conjugated targets are more successfully deconjugated by SENP3 than SUMO-1-containing species
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
spatial and temporal expression patterns of SENP3, overview
Manually annotated by BRENDA team
-
dynamic changes in SENP3 expression in the cerebral cortex and in its cellular localization in traumatic brain injury compared to normal, overview
Manually annotated by BRENDA team
additional information
-
immunohistochemical and expression anaysis of the enzyme in brain tissues, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
evolution
-
the enzyme is a member of the small ubiquitin-like modifier-specific protease family
physiological function
-
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SENP3_MOUSE
568
0
64403
Swiss-Prot
-
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
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
SENP3 quantitative real-time PCR expression analysis
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
traumatic brain injury upregulates the enzyme expression in the brain, especially in the neurons and astrocytes
-
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
Wu, D.; Huang, C.J.; Khan, F.A.; Jiao, X.F.; Liu, X.M.; Pandupuspitasari, N.S.; Brohi, R.D.; Huo, L.J.
SENP3 grants tight junction integrity and cytoskeleton architecture in mouse Sertoli cells
Oncotarget
8
58430-58442
2017
Mus musculus (Q9EP97), Mus musculus
Manually annotated by BRENDA team
Select items on the left to see more content.