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Information on EC 3.4.22.B71 - SENP2 peptidase and Organism(s) Homo sapiens and UniProt Accession Q9HC62
for references in articles please use BRENDA:EC3.4.22.B71preliminary BRENDA-supplied EC number
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3.4.22.B71 SENP2 peptidaseSpecify your search results
Word Map
- 3.4.22.B71
-
sumoylation
- medicine
- atherosclerosis
-
aorta
-
d-flow
-
d-flow-induced
- erk5
-
de-sumoylation
-
p90rsk
-
senps
-
epilepsy
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
The enzyme catalyzes two essential functions in the SUMO pathway: processing of full-length SUMO-1, SUMO-2 and SUMO-3 to their mature forms and deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins. Deconjugates SUMO-2 from mitotic kinase Aurora-B. Deconjugates SUMO-1 from Mdm2, an protein critical for genome integrity in P53-dependent stress response. Cleavage of Gly97-/-His98 bond in the SUMO-1 precursor with release of the propeptide His-Ser-Thr-Val. Cleavage of Gly93-/-Val94 bond in the SUMO-2 precursor with release of the propeptide Val94-Thyr. Cleavage of the Gly92-/-Val93 in the SUMO-3 precursor with release of the propeptide Pro-Glu-Ser-Ser-Leu-Ala-Gly-His-Ser-Phe.
Synonyms
sentrin/sumo-specific protease 2, small ubiquitin-like modifier-specific protease, small ubiquitin-like modifier-specific protease 2, 
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)-Ran GTPase-activating protein 1 conjugate + H2O
SUMO-1 + Ran GTPase-activating protein 1
-
-
-
?
(SUMO-2)-Ran GTPase-activating protein 1 conjugate + H2O
SUMO-2 + Ran GTPase-activating protein 1
-
-
-
?
(SUMO-2/3)-Ran GTPase-activating protein 1 conjugate + H2O
SUMO-2/3 + Ran GTPase-activating protein 1
-
-
-
?
(SUMO-3)-Ran GTPase-activating protein 1 conjugate + H2O
SUMO-3 + Ran GTPase-activating protein 1
-
-
-
?
SUMOylated Smad4 + H2O
?
Smad4 forms complexes with receptor-phosphorylated Smads, and transduces transforming growth factor-beta signals into the nuclei
-
-
?
SUMOylated TBL1/TBLR1 + H2O
?
i.e. transcriptional cofactor transducin beta-like
-
-
?
acetyl-QTGG-7-amino-4-trifluoromethylcoumarin + H2O
acetyl-QTGG + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
SUMO-1 precursor + H2O
SUMO-1 + His-Ser-Thr-Val
-
very low isopeptidase activity with SUMO-1. SENP2 exhibits substantially higher isopeptidase than endopeptidase activity
-
-
?
SUMO-2 precursor + H2O
SUMO-2 + Val-Tyr
-
SENP2 exhibits substantially higher isopeptidase than endopeptidase activity
-
-
?
SUMO-3 precursor + H2O
SUMO-3 + Val-Pro-Glu-Ser-Ser-Leu-Ala-Gly-His-Ser-Phe
-
SENP2 exhibits substantially higher isopeptidase than endopeptidase activity
-
-
?
SUMO-Ran GTPase-activating protein 1 conjugate + H2O
?
-
SENP2 exhibits substantially higher isopeptidase than endopeptidase activity
-
-
?
SUMOylated myocyte-specific enhancer factor-2A + H2O
deSUMOylated myocyte-specific enhancer factor-2A + SUMO
-
deSUMOylation by enzyme SENP2
-
-
?
additional information
?
-
-
nucleoporin Nup153 binds to SENP2 by interacting with the unique N-terminal domain of Nup153 as well as a specific region within the C-terminal FG-rich region. Nup153 is a substrate for SUMOylation, with this modification kept in check by the SUMO protease
-
-
?
SUMO-1 precursor + H2O
SUMO-1 + His-Ser-Thr-Val
50% of SUMO-1 precursor is hydrolyzed after 70 min
-
-
?
SUMO-2 precursor + H2O
SUMO-2 + Val-Tyr
50% of SUMO-2 precursor is hydrolyzed after 15 min
-
-
?
SUMO-3 precursor + H2O
SUMO-3 + Val-Pro-Glu-Ser-Ser-Leu-Ala-Gly-His-Ser-Phe
-
-
-
?
SUMO-3 precursor + H2O
SUMO-3 + Val-Pro-Glu-Ser-Ser-Leu-Ala-Gly-His-Ser-Phe
50% of SUMO-1 precursor is hydrolyzed after 160 min
-
-
?
poly-SUMO-2/3-Aurora-B conjugate + H2O
?
-
specifically deconjugates SUMO from mitotic kinase Aurora-B. Lys202 on human Aurora-B is preferentially modified by SUMO, and enhancement of SUMOylation in cells facilitates Aurora-B autophosphorylation, which is essential for its activation. Conversely, SENP2-mediated deSUMOylation of Aurora-B down-regulates its autophosphorylation in cells and also impairs its re-activation in Aurora inhibitor VX-680-treated mitotic cells. Poly-SUMO-2 conjugation of Aurora-B occurs during the M phase ofthe cell cycle, and both SUMO-2 and PIAS3 are localized adjacent to Aurora-B in the kinetochores in early mitosis. Aurora-B is a mitotic SUMO substrate and its kinase activity is fine-tuned by the SUMO system
-
-
?
poly-SUMO-2/3-Aurora-B conjugate + H2O
?
-
specifically deconjugates SUMO from mitotic kinase Aurora-B. Lys-202 residue on human Aurora-B is preferentially modified by SUMO
-
-
?
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
poly-SUMO-2/3-Aurora-B conjugate + H2O
?
-
specifically deconjugates SUMO from mitotic kinase Aurora-B. Lys202 on human Aurora-B is preferentially modified by SUMO, and enhancement of SUMOylation in cells facilitates Aurora-B autophosphorylation, which is essential for its activation. Conversely, SENP2-mediated deSUMOylation of Aurora-B down-regulates its autophosphorylation in cells and also impairs its re-activation in Aurora inhibitor VX-680-treated mitotic cells. Poly-SUMO-2 conjugation of Aurora-B occurs during the M phase ofthe cell cycle, and both SUMO-2 and PIAS3 are localized adjacent to Aurora-B in the kinetochores in early mitosis. Aurora-B is a mitotic SUMO substrate and its kinase activity is fine-tuned by the SUMO system
-
-
?
SUMOylated myocyte-specific enhancer factor-2A + H2O
deSUMOylated myocyte-specific enhancer factor-2A + SUMO
-
deSUMOylation by enzyme SENP2
-
-
?
additional information
?
-
-
nucleoporin Nup153 binds to SENP2 by interacting with the unique N-terminal domain of Nup153 as well as a specific region within the C-terminal FG-rich region. Nup153 is a substrate for SUMOylation, with this modification kept in check by the SUMO protease
-
-
?
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00547
(SUMO-1)-Ran GTPase-activating protein 1 conjugate
pH 8.0, 23°C
-
0.033
(SUMO-2/3)-Ran GTPase-activating protein 1 conjugate
pH 8.0, 23°C
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
weak expression, benign breast adenofibroma cell and malignant breast cancer tissue
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
SENP2 shuttles between the nucleus and the cytoplasm. Identification of a bipartite nuclear localization signal and a CRM1-dependent nuclear export signal in the SUMO protease SENP2. Nucleocytoplasmic shuttling is a crucial regulatory mechanism for SENP2 function
SENP2 associates with the nuclear face of nuclear pores. This association requires protein sequences near the N-terminus of SENP2. Association with the pore plays an important negative role in the regulation of SENP2, perhaps by restricting its activity to a subset of the conjugated proteins within the nucleus
the enzyme SENP2 is targeted to kinetochores in mitosis. SENP2 targeting occurs through a mechanism dependent on the Nup107-160 subcomplex of the nuclear pore complex and is modulated through interactions with karyopherin alpha
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
RNA interference SENP2 knockdown produces no detectable phenotypes, while overexpression of SENP2, but not other SUMO-specific isopeptidases, causes a defect in chromosome congression that depends on its precise kinetochore targeting. Isozyme SENP2 overexpression uniquely induces prometaphase arrest
physiological function
evolution
-
SUMO-specific protease 2 (SENP2) is a de-SUMOylation protease family member
malfunction
metabolism
physiological function
additional information
-
SENP2 is a target of SUMO modification and has targeting preference for SUMO paralogues and substrates
physiological function
enzyme SENP2 is an important mediator of precise spatial and temporal control of sumoylation in mitosis required for chromosome segregation
physiological function
SENP2 inhibits nuclear translocation of beta-catenin, which targets the promotor of MMP13 to activate MMP13 to enhance bladder cancer cell metastasis
physiological function
SENP2 interacts with Smad4 through SENP2 residue 363-400. The same segment is also important for desumoylation of Smad4, and able to relieve sumoylation-mediated TGF-beta repression. The SENP2363-400 segment is critical for TGF-beta-induced cell migration, which is correlated with SENP2363-400 deletion mutant that fails to increase matrix metalloproteinase (MMP)-9 and epithelial-to-mesenchymal transition marker gene expression. The interaction and desumoylation between SENP2 and Smad4 promote cell migration in triple-negative breast cancer cells
physiological function
SENP2 knockdown results in a decrease of E-cadherin and an increase of N-cadherin and fibronectin at both transcript and protein levels. SENP2 overexpression results in deSUMOylation of TGF-betaR I in bladder cancer cells and suppresses TGF-beta signaling and TGF-beta-induced epithelial-mesenchymal transition. SENP2 regulates TGF-beta signaling partly through deSUMOylation of TGFbeta receptor I
malfunction
-
differential localization of nucleoporins upon codepletion of SENP1 and SENP2 in HeLa cells, immunohistochemic analysis, overview
malfunction
-
overexpression of enzyme SENP2 reduces the glucose uptake and lactate production, increasing the cellular ATP levels in MCF-7 cells. The MCF-7 cells overexpressing enzyme SENP2 exhibit decreased expression levels of key glycolytic enzymes and an increased rate of glucose oxidation compared with control MCF-7 cells, indicating inhibited glycolysis but enhanced oxidative mitochondrial respiration. The cells have a reduced amount of phosphorylated AKT
malfunction
-
silencing the expression of enzyme SENP2 significantly induces the expression of MMP13 , forced MMP13 expression is sufficient to restore cell invasion in SENP2 overexpressed T24 bladder cancer cells
malfunction
-
specifically, either RNAi depletion of SENP1/SENP2 or expression of dominantly interfering mutants of these proteins results in increased sumoylation of endogenous Nup153. Catalytically inactive SENP2 maintains specific attributes, although it has enhanced interaction with sumoylated Nup153, overview. Truncated SENP2CD is robustly modified by SUMO2
metabolism
-
SENP2 protein is accumulated in response to activity-dependent stimuli which in turn mediated activity dependent-regulation of MEF2A deSUMOylation
physiological function
-
mitotic kinase Aurora-B is a mitotic SUMO substrate and its kinase activity is fine-tuned by the SUMO system
physiological function
-
enzyme SENP2 represses glycolysis and shifts glucose metabolic strategy, in part through inhibition of AKT phosphorylation, function of SENP2 in regulating glucose metabolism, overview
physiological function
-
SENP2, as well as SENP1, regulates the proper localization of nucleoporins, overview. The enzyme interacts with the nucleoporin Nup153 via a dual interface that includes a bridging interaction with the soluble transport receptor importin beta and a SUMO-mediated mechanism, and also with Nup358 and members of the Nup107-160 complex at distinct regions of SENP2 that can independently direct SENP2 to the nuclear rim. SENP1 and SENP2 are not required for localization of the transmembrane proteins nucleoporin POM121 and inner nuclear envelope protein Sun1 or expansion of the interphase nuclear envelope
physiological function
-
SENP2, but not SENP1, regulates MEF2A deSUMOylation in an activity dependent manner, enzyme SENP2 markedly enhances the transcription of MEF2A through directly deSUMOylation
physiological function
-
SUMO-specific protease 2 suppresses cell migration and invasion through selectively inhibiting the expression of MMP13 in bladder cancer cells, the enzyme has an indispensable role in the regulation of NF-kappaB transcriptional activation and Wnt signaling. The enzyme inhibits bladder cancer cells migration and invasion in vitro
physiological function
-
the SUMO proteases play roles both in processing SUMO during the biogenesis of this peptide moiety and also in reversing SUMO modification on specific targets to control the activities conferred by this posttranslational modification. Specificity of the role for SENP1 and SENP2 in maintaining desumoylation of Nup153
physiological function
-
ectopic expression of SENP2 results in the suppression of proliferation, migration and invasion in osteosarcoma cells, whereas SENP2 knockdown has the opposite effect
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
ubiquitination
SENP2 can be polyubiquitinated in vivo and degraded through proteolysis. Restricting SENP2 in the nucleus by mutations in the nuclear export signal (NES) impairs its polyubiquitination, whereas a cytoplasm-localized SENP2 made by introducing mutations in the nuclear localization signal (NLS) can be efficiently polyubiquitinated, suggesting that SENP2 is ubiquitinated in the cytoplasm
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant chimeric mutant SENP2 C548S-loop1 in complex with SUMO2, X-ray diffraction structure determination and analysis at 2.15 A resolution
Senp2 crystallization is performed at 4°C using sitting and hanging drop vapor diffusion methods. X-ray structures of Senp2 catalytic protease domain and of a covalent thiohemiacetal transition-state complex obtained between the Senp2 catalytic domain and SUMO-1 reveales details of the respective protease and substrate surfaces utilized in interactions between these two proteins. Comparative biochemical and structural analysis between Senp2 and the yeast SUMO protease Ulp1 reveales differential abilities to process SUMO-1, SUMO-2, and SUMO-3 in maturation and deconjugation reactions
X-ray structures are determined for a catalytically inert SENP2 protease domain in complex with conjugated RanGAP1-SUMO-1 or RanGAP1-SUMO-2, or in complex with SUMO-2 or SUMO-3 precursors
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F393G/K394G
construction of a chimeric enzyme SENP2 mutant with the insertion of loop1 from SENP6 into its sequence causing mutation of F393G/K394G, loop1 insertion is a determinant for SUMO2/3 activity and specificity, structure of SENP2-loop1 in complex with SUMO2, overview. The mutant reveals the details of an interface exclusive to SENP6/7 and the formation of unique contacts between both proteins, and the mutant shows an increase of the proteolytic activity for diSUMO2 and polySUMO2 substrates. The chimeric insertion mutant used for crystallization studies is also mutated at active site residue, C548S, for a stable complex formation
G545D
slight decrease in SUMO-1 processing activity and SUMO-2 processing activity. Decrease in cleavage of the RanGAP1-SUMO-1 conjugate
G545F
decrease in SUMO-1 processing activitya and SUMO-2 processing activity. Increase in SUMO-3 procesing activity
G545S
decrease in SUMO-1 processing activity, SUMO-2 processing activity and SUMO-3 procesing activity. Decrease in cleavage of the RanGAP1-SUMO-1 conjugate
M497A
increase in SUMO-1 processing activity and SUMO-3 procesing activity. Decrease in cleavage of the RanGAP1-SUMO-1 conjugate. Slight decrease in cleavage of the RanGAP1-SUMO-2/3 conjugate
M497L
decrease in SUMO-1 processing activity, SUMO-2 processing activity and SUMO-3 procesing activity
M497N
slight increase in SUMO-1 processing activity, decrease in SUMO-2 processing activity. Decrease in cleavage of the RanGAP1-SUMO-1 conjugate
M497Q
decrease in SUMO-1 processing activity, SUMO-2 processing activity and SUMO-3 procesing activity. Decrease in cleavage of the RanGAP1-SUMO-1 conjugate. Decrease in cleavage of the RanGAP1-SUMO-2/3 conjugate
R576L/K577M
catalytically inactive SENP2 mutant, unable to regulate TGF-beta signaling
V477A
substitution results in mild effects on processing or deconjugation
R576L/K577M
-
the catalytically inactive enzyme mutant SENP2Cat cannot regulate MMP13
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
catalytic C-terminal domain of human SENP2(364489) expressed in Escherichia coli
recombinant chimeric mutant SENP2 C548S-loop1 in complex with SUMO2 by gel filtration
catalytic domains of SENP2 expressed in Escherichia coli BL21 (DE3) as N-terminal His-tagged proteins
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
the catalytic C-terminal domain of human SENP2(364-489) is expressed from pET28b in Escherichia coli BL21(DE3) codon-plus cells
expression of catalytic domains of SENP2 in Escherichia coli BL21 (DE3) as N-terminal His-tagged proteins
-
gene SP2, recombinant expression of GFP-tagged or untagged SENP2 and the catalytically dead enzyme mutant transiently in HeLa cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
SENP2 expression is significantly downregulated in clinical osteosarcoma tissues compared with adjacent normal samples. Ectopic expression of SENP2 results in the suppression of proliferation, migration and invasion in osteosarcoma cells, whereas SENP2 knockdown has the opposite effect. SENP2 is associated with the proteaxadsome-dependent ubiquitination and degradation of SRY-box-9 (SOX9). SOX9 silencing impairs SENP2-depletion-induced accelerated cell growth and migration
medicine
in bladder cancer cells, SENP2 inhibits MMP13 expression through deSUMOylation of TBL1/TBLR1, which inhibits nuclear translocation of beta-catenin
medicine
SENP2 is frequently downregulated in bladder cancer, especially in metastatic bladder cancer. SENP2 downregulation is associated with more aggressive phenotypes and poor patient outcomes. SENP2 suppresses bladder cancer cell invasion in vitro and tumor metastasis in vivo, acts as a tumor suppressor gene in bladder cancer
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Itahana, Y.; Yeh, E.T.; Zhang, Y.
Nucleocytoplasmic shuttling modulates activity and ubiquitination-dependent turnover of SUMO-specific protease 2
Mol. Cell. Biol.
26
4675-4689
2006
Homo sapiens (Q9HC62)
Reverter, D.; Lima, C.D.
Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates
Nat. Struct. Mol. Biol.
13
1060-1068
2006
Homo sapiens (Q9HC62)
Ban, R.; Nishida, T.; Urano, T.
Mitotic kinase Aurora-B is regulated by SUMO-2/3 conjugation/deconjugation during mitosis
Genes Cells
16
652-669
2011
Homo sapiens
Hang, J.; Dasso, M.
Association of the human SUMO-1 protease SENP2 with the nuclear pore
J. Biol. Chem.
277
19961-19966
2002
Homo sapiens (Q9HC62)
Mikolajczyk, J.; Drag, M.; Bekes, M.; Cao, J.T.; Ronai, Z.; Salvesen, G.S.
Small ubiquitin-related modifier (SUMO)-specific proteases: profiling the specificities and activities of human SENPs
J. Biol. Chem.
282
26217-26224
2007
Homo sapiens
Reverter, D.; Lima, C.D.
A basis for SUMO protease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex
Structure
12
1519-1531
2004
Homo sapiens (Q9HC62)
Tan, M.Y.; Mu, X.Y.; Liu, B.; Wang, Y.; Bao, E.D.; Qiu, J.X.; Fan, Y.
SUMO-specific protease 2 suppresses cell migration and invasion through inhibiting the expression of MMP13 in bladder cancer cells
Cell. Physiol. Biochem.
32
542-548
2013
Homo sapiens
Cubenas-Potts, C.; Goeres, J.D.; Matunis, M.J.
SENP1 and SENP2 affect spatial and temporal control of sumoylation in mitosis
Mol. Biol. Cell
24
3483-3495
2013
Homo sapiens (Q9HC62)
Chow, K.H.; Elgort, S.; Dasso, M.; Powers, M.A.; Ullman, K.S.
The SUMO proteases SENP1 and SENP2 play a critical role in nucleoporin homeostasis and nuclear pore complex function
Mol. Biol. Cell
25
160-168
2014
Homo sapiens
Lu, H.; Liu, B.; You, S.; Chen, L.; Dongmei, Q.; Gu, M.; Lu, Y.; Chen, Y.; Zhang, F.; Yu, B.
SENP2 regulates MEF2A de-SUMOylation in an activity dependent manner
Mol. Biol. Rep.
40
2485-2490
2013
Homo sapiens
Chow, K.H.; Elgort, S.; Dasso, M.; Ullman, K.S.
Two distinct sites in Nup153 mediate interaction with the SUMO proteases SENP1 and SENP2
Nucleus
3
349-358
2012
Homo sapiens
Tang, S.; Huang, G.; Tong, X.; Xu, L.; Cai, R.; Li, J.; Zhou, X.; Song, S.; Huang, C.; Cheng, J.
Role of SUMO-specific protease 2 in reprogramming cellular glucose metabolism
PLoS ONE
8
e63965
2013
Homo sapiens, Mus musculus
Alegre, K.O.; Reverter, D.
Structural insights into the SENP6 loop1 structure in complex with SUMO2
Protein Sci.
23
433-441
2014
Homo sapiens (Q9HC62)
Pei, H.; Chen, L.; Liao, Q.M.; Wang, K.J.; Chen, S.G.; Liu, Z.J.; Zhang, Z.C.
SUMO-specific protease 2 (SENP2) functions as a tumor suppressor in osteosarcoma via SOX9 degradation
Exp. Ther. Med.
16
5359-5365
2018
Homo sapiens
Tan, M.; Zhang, D.; Zhang, E.; Xu, D.; Liu, Z.; Qiu, J.; Fan, Y.; Shen, B.
SENP2 suppresses epithelial-mesenchymal transition of bladder cancer cells through deSUMOylation of TGF-betaRI
Mol. Carcinog.
56
2332-2341
2017
Homo sapiens (Q9HC62)
Tan, M.; Gong, H.; Wang, J.; Tao, L.; Xu, D.; Bao, E.; Liu, Z.; Qiu, J.
SENP2 regulates MMP13 expression in a bladder cancer cell line through SUMOylation of TBL1/TBLR1
Sci. Rep.
5
13996
2015
Homo sapiens (Q9HC62)
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