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Information on EC 3.4.22.B74 - SENP6 peptidase
for references in articles please use BRENDA:EC3.4.22.B74
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Please check here for current data: EC unknown
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preliminary BRENDA-supplied EC number
EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.22 Cysteine endopeptidases
3.4.22.B74 SENP6 peptidase
The enzyme appears in viruses and cellular organisms
- 3.4.22.B74
- leukemia
- sumo3
-
sumoylation
-
circadian
-
promyelocytic
-
ubiquitin-related
-
heterodimeric
- clock
-
sumo-specific
-
rhythmic
Reaction Schemes
showThe 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. 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. The enzyme catalyzes the desumoylation of SUMO-modified promyelocytic leukemia protein. SENP6 prefers the LRGG-/- sequence versus the QTGG-/- sequence. SENP6 is essential for inner kinetochore assembly.
Synonyms
susp1, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SENP6
sentrin/SUMO-specific protease 6
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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. 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. The enzyme catalyzes the desumoylation of SUMO-modified promyelocytic leukemia protein. SENP6 prefers the LRGG-/- sequence versus the QTGG-/- sequence. SENP6 is essential for inner kinetochore assembly.
-
-
-
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(polySUMO-2/3)-BRCA1-BARD1 + H2O
hypoSUMOylated-BRCA1-BARD1 + SUMO-2/3
Substrates: SENP6 deconjugates SUMO2/3 polymers
Products: -
Products: -
?
(SUMO-1)-beta-galactosidase conjugate + H2O
SUMO-1 + beta-galactosidase
Substrates: SUSP1 expressed in Escherichia coli cells efficiently releases SUMO-1 from SUMO-1-beta-galactosidase fusion but not from other ubiquitin-like protein fusions, including Smt3-beta-galactosidase
Products: -
Products: -
?
(SUMO-3)-Ran GTPase-activating protein 1 conjugate + H2O
SUMO-3 + Ran GTPase-activating protein 1
Substrates: SENP6 and SENP7 prefer SUMO2 or SUMO3 in deconjugation reactions with rates comparable with those catalyzed by SENP2. In contrast to SENP2, SENP6 and SENP7 are less able to deconjugate SUMO1-RanGAP1, and products are only detected at enzyme concentrations 100 x higher than that observed for reactions containing SENP2
Products: -
Products: -
?
53BP1 + H2O
hypoSUMOylated-53BP1 + SUMO-2/3
Substrates: SENP6 deconjugates SUMO2/3 polymers
Products: -
Products: -
?
acetyl-LRGG-7-amido-4-trifluoromethylcoumarin + H2O
acetyl-LRGG + 7-amino-4-trifluoromethylcoumarin
-
Substrates: SENP6 prefers the LRGG sequence, residues typical of Nedd8 or ubiquitin in the P3 and P4 positions
Products: -
Products: -
?
acetyl-QTGG-7-amido-4-trifluoromethylcoumarin + H2O
acetyl-QTGG + 7-amino-4-trifluoromethylcoumarin
-
Substrates: very low activity
Products: -
Products: -
?
BLM + H2O
hypoSUMOylated-BLM + SUMO-2/3
Substrates: SENP6 deconjugates SUMO2/3 polymers
Products: -
Products: -
?
ERCC1-XPF + H2O
hypoSUMOylated-XPF + SUMO-2/3
Substrates: SENP6 deconjugates SUMO2/3 polymers
Products: -
Products: -
?
SUMO-2 precursor + H2O
SUMO-2 + Val-Tyr
Substrates: SENP6 exhibits lower rates for processing pre-SUMO-1, pre-SUMO-2, or pre-SUMO3 in comparison with SENP2
Products: -
Products: -
?
SUMO-3 precursor + H2O
SUMO-3 + Val-Pro-Glu-Ser-Ser-Leu-Ala-Gly-His-Ser-Phe
Substrates: SENP6 exhibits lower rates for processing pre-SUMO-1, pre-SUMO-2, or pre-SUMO-3 in comparison with SENP2
Products: -
Products: -
?
SUMO-modified promyelocytic leukemia protein + H2O
SUMO + promyelocytic leukemia protein
Substrates: -
Products: -
Products: -
?
SUMO-PLM + H2O
?
Substrates: SENP6 preferentially targets poly-SUMO chains. Wild-type SENP6 strongly reduces the level of poly- or multimodified SUMOPML conjugates, but not the monomodified form
Products: -
Products: -
?
SUMOylated TRIM28 + H2O
?
Substrates: i.e. tripartite motif-containing 28, also called KAP1 or TIF1beta
Products: -
Products: -
?
hyper-SUMOylated LaminA + H2O
normally SUMOylated LaminA + SUMO
Substrates: -
Products: -
Products: -
?
hyper-SUMOylated LaminA + H2O
normally SUMOylated LaminA + SUMO
Substrates: SENP6 preferentially cleaves between SUMO molecules in polySUMO chains
Products: -
Products: -
?
SUMO-1 precursor + H2O
SUMO-1 + His-Ser-Thr-Val
Substrates: -
Products: -
Products: -
?
SUMO-1 precursor + H2O
SUMO-1 + His-Ser-Thr-Val
Substrates: SENP6 exhibits lower rates for processing pre-SUMO-1, pre-SUMO-2, or pre-SUMO3 in comparison with SENP2
Products: -
Products: -
?
SUMO-cohesin + H2O
?
Substrates: SENP6 regulates the SUMOylation status of the cohesin complex
Products: -
Products: -
?
SUMO-cohesin + H2O
?
Substrates: SENP6 preferentially targets poly-SUMO chains
Products: -
Products: -
?
additional information
?
-
Substrates: SUSP1 expressed in Escherichia coli cells efficiently releases SUMO-1 from SUMO-1-beta-galactosidase fusion but not from other ubiquitin-like protein fusions, including Smt3zb-galactosidase, suggesting its role in the generation of matured SUMO-1 specifically from its precursors
Products: -
Products: -
?
additional information
?
-
-
Substrates: SUSP1 expressed in Escherichia coli cells efficiently releases SUMO-1 from SUMO-1-beta-galactosidase fusion but not from other ubiquitin-like protein fusions, including Smt3zb-galactosidase, suggesting its role in the generation of matured SUMO-1 specifically from its precursors
Products: -
Products: -
?
additional information
?
-
-
Substrates: SENP6 reveals no detectable endopeptidase activity on the precursors of ubiquitin, Nedd8 and ISG15
Products: -
Products: -
?
additional information
?
-
Substrates: although SUMO-2/3 chains are the preferred substrate, SENP6 is also capable of cleaving mixed chains of SUMO-1 and SUMO-2/3
Products: -
Products: -
?
additional information
?
-
-
Substrates: isozyme SENP6 shows isoform specificity for SUMO2/3 over SUMO1
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
hyper-SUMOylated LaminA + H2O
normally SUMOylated LaminA + SUMO
Substrates: -
Products: -
Products: -
?
SUMO-cohesin + H2O
?
Substrates: SENP6 regulates the SUMOylation status of the cohesin complex
Products: -
Products: -
?
SUMO-modified promyelocytic leukemia protein + H2O
SUMO + promyelocytic leukemia protein
Substrates: -
Products: -
Products: -
?
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Chloroquine
dose-dependently increases SENP6 protein, but not mRNA, in mouse macrophages, RAW264.7 cells. Chloroquine dose-dependently decreases the levels of microRNA-669n, which bound to 3'-UTR of SENP6 mRNA to inhibit its translation
truncated SUMO-2
-
whereas truncated SUMO-2 and -3 can substantially enhance SENP6 activity, neither truncated SUMO-1 nor truncated Nedd8 nor ubiquitin has this ability
-
truncated SUMO-3
-
whereas truncated SUMO-2 and -3 can substantially enhance SENP6 activity, neither truncated SUMO-1 nor truncated Nedd8 nor ubiquitin has this ability
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Precursor Cell Lymphoblastic Leukemia-Lymphoma
Molecular cytogenetic analysis of the breakpoint region at 6q21-22 in T-cell lymphoma/leukemia cell lines.
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
reproductive organs, such as testis, ovary, and prostate, contain much higher amounts of SUSP1 mRNA than colon and peripheral blood leukocyte
brenda
reproductive organs, such as testis, ovary, and prostate, contain much higher amounts of SUSP1 mRNA than colon and peripheral blood leukocyte
brenda
reproductive organs, such as testis, ovary, and prostate, contain much higher amounts of SUSP1 mRNA than colon and peripheral blood leukocyte
brenda
reproductive organs, such as testis, ovary, and prostate, contain much higher amounts of SUSP1 mRNA than colon and peripheral blood leukocyte
brenda
reproductive organs, such as testis, ovary, and prostate, contain much higher amounts of SUSP1 mRNA than colon and peripheral blood leukocyte
brenda
additional information
additional information
no or little SUSP1 mRNA in liver, lung, kidney, pancreas, spleen, thymus, heart, and skeletal muscle
brenda
additional information
-
no or little SUSP1 mRNA in liver, lung, kidney, pancreas, spleen, thymus, heart, and skeletal muscle
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
SUSP1 is exclusively localized to the cytoplasm of NIH3T3 and HeLa cells
brenda
expression of SENP6 appeared diffuse throughout the nucleoplasm
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
inhibition of SENP6 may be a crucial beneficial therapeutic strategy for ischaemic stroke
malfunction
physiological function
additional information
-
active site loop1 insertion is the determinant for the SUMO2/3 activity and specificity of SENP6, role of the SENP6/7-loop1 insertion in chain dismantling
malfunction
-
cells lacking SENP6 show defects in spindle assembly and metaphase chromosome congression. A subset of proteins becomes undetectable on inner kinetochores after SENP6 depletion, particularly the CENP-H/I/K complex
malfunction
depletion of SENP6 results in accumulation of endogenous SUMO-2/3 and SUMO-1 conjugates, and in accumulation of SUMO and promyelocytic leukemia protein in an increased number of promyelocytic leukemia nuclear bodies. Although SENP6 depletion drastically increases the size of promyelocytic leukemia nuclear bodies, the organizational structure of the body is not affected
malfunction
specifically inhibiting SENP6 decreased proinflammatory mediator expression and increased anti-inflammatory mediator expression, thereby protecting experimental animals against neurological damage
malfunction
depletion of SENP6 leads to hyperSUMOylation of lamins A and B and nuclear blebbing reminiscent of laminopathies
malfunction
SENP6 deficiency impairs chromatin association of the ATR cofactor ATRIP, thereby compromising the activation of Chk1 signaling in response to aphidicolin-induced replicative stress and sensitizing cells to DNA damage
malfunction
SENP6 depletion results in persistence of SUMO2/3 at DNA damage sites
malfunction
SENP6 deletions and associated unrestricted SUMOylation is a functional and clinically important driver of lymphomagenesis
physiological function
-
SENP6 is essential for inner kinetochore assembly. Balanced activities of SENP6 and RNF4 control vertebrate kinetochore assembly through SUMO-targeted destabilization of inner plate components
physiological function
postnatal loss of SENP6 causes premature aging. osteochondroprogenitor-specific SENP6 knockout mice exhibit smaller skeletons, with elevated apoptosis and cell senescence in osteochondroprogenitors and chondrocytes. In Senp6-/- cells, the two most significantly elevated pathways are p53 signaling and senescence-associated secreted phenotypes, and Trp53 loss partially rescues the skeletal and cellular phenotypes caused by Senp6 loss. SENP6 interacts with, desumoylates, and stabilizes TRIM28, suppressing p53 activity
physiological function
overexpression of SENP6 in RAW264.7 cells significantly decreases the LPS-induced release of proinflammatory proteins, TNF-alpha, IL-6 and IFN-gamma, while depletion of SENP6 in RAW264.7 cells significantly increases these proteins. In LPS-treated RAW264.7 cells, chloroquine dose-dependently decreases the levels of microRNA-669n, which bound to 3'-UTR of SENP6 mRNA to inhibit its translation. Overexpression of microR-669n decreases SENP6, resulting in increased production of TNF-alpha, IL-6 and IFN-gamma in RAW264.7 cells, while depletion of microR-669n increases SENP6
physiological function
SENP6 induces microglial polarization and neuroinflammation through de-SUMOylation of ANXA1 after cerebral ischaemia-reperfusion injury. SENP6 mediates the de-SUMOylation of ANXA1, thereby inhibiting the autophagic degradation of IKKalpha in an NBR1-dependent manner, activating the NF-kappaB signalling pathway and inducing the microglial inflammatory response after cerebral ischaemia
physiological function
SENP6 activity protects the nucleus against hyperSUMOylation-induced laminopathy-like alterations. SENP6 regulates lamin protein SUMOylation. SENP6 functions to suppress adventitious lamin SUMOylation
physiological function
general role of SENP6 in orchestrating chromatin dynamics and genome stability networks by balancing chromatin residency of protein complexes. SENP6 controls SUMOylation of cohesin and regulates sister chromatid cohesion. SENP6 regulates the ATR-Chk1 DNA damage checkpoint
physiological function
SENP6 regulates VEGFR2 trafficking from the Golgi to the endothelial cell surface. The SENP6-VEGFR2 pathway plays a critical role in pathological angiogenesis
physiological function
SENP6 is required for maintaining genomic stability. SENP6 regulates localization and nuclear condensation of DNA damage response proteins by group deSUMOylation. SENP6 deconjugates SUMO2/3 polymers on a group of DNA damage response proteins, including BRCA1-BARD1, 53BP1, BLMand ERCC1-XPF. SENP6 maintains these proteins in a hypo-SUMOylated state under unstressed conditions and counteracts their polySUMOylation after hydroxyurea-induced stress
physiological function
SENP6 is a tumor suppressor of B-cell lymphomagenesis. It is a critical determinant for SUMO homeostasis in B-cell lymphoma
physiological function
SENP6-mediated M18BP1 deSUMOylation regulates CENP-A centromeric localization
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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). SENP6_MOUSE
1132
0
127013
Swiss-Prot
Secretory Pathway (Reliability: 1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
SENP6 expression increases after advanced glycation end products stimulation of human umbilical vein endothelial cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Drag, M.; Mikolajczyk, J.; Krishnakumar, I.M.; Huang, Z.; Salvesen, G.S.
Activity profiling of human deSUMOylating enzymes (SENPs) with synthetic substrates suggests an unexpected specificity of two newly characterized members of the family
Biochem. J.
409
461-469
2008
Homo sapiens
brenda
Kim, K.I.; Baek, S.H.; Jeon, Y.J.; Nishimori, S.; Suzuki, T.; Uchida, S.; Shimbara, N.; Saitoh, H.; Tanaka, K.; Chung, C.H.
A new SUMO-1-specific protease, SUSP1, that is highly expressed in reproductive organs
J. Biol. Chem.
275
14102-14106
2000
Homo sapiens (Q9GZR1), Homo sapiens
brenda
Lima, C.D.; Reverter, D.
Structure of the human SENP7 catalytic domain and poly-SUMO deconjugation activities for SENP6 and SENP7
J. Biol. Chem.
283
32045-32055
2008
Homo sapiens (Q9GZR1)
brenda
Mukhopadhyay, D.; Arnaoutov, A.; Dasso, M.
The SUMO protease SENP6 is essential for inner kinetochore assembly
J. Cell Biol.
188
681-692
2010
Homo sapiens
brenda
Hattersley, N.; Shen, L.; Jaffray, E.G.; Hay, R.T.
The SUMO protease SENP6 is a direct regulator of PML nuclear bodies
Mol. Biol. Cell
22
78-90
2010
Homo sapiens (Q9GZR1)
brenda
Alegre, K.O.; Reverter, D.
Structural insights into the SENP6 loop1 structure in complex with SUMO2
Protein Sci.
23
433-441
2014
Homo sapiens
brenda
Long, Y.; Liu, X.; Wang, N.; Zhou, H.; Zheng, J.
Chloroquine attenuates LPS-mediated macrophage activation through miR-669n-regulated SENP6 protein translation
Am. J. Transl. Res.
7
2335-2345
2015
Mus musculus (Q6P7W0)
brenda
Li, J.; Lu, D.; Dou, H.; Liu, H.; Weaver, K.; Wang, W.; Li, J.; Yeh, E.T.H.; Williams, B.O.; Zheng, L.; Yang, T.
Desumoylase SENP6 maintains osteochondroprogenitor homeostasis by suppressing the p53 pathway
Nat. Commun.
9
143
2018
Mus musculus (Q6P7W0)
brenda
Mao, M.; Xia, Q.; Zhan, G.F.; Chu, Q.J.; Li, X.; Lian, H.K.
SENP6 induces microglial polarization and neuroinflammation through de-SUMOylation of Annexin-A1 after cerebral ischaemia-reperfusion injury
Cell Biosci.
12
113
2022
Mus musculus (Q6P7W0)
brenda
Wagner, K.; Kunz, K.; Piller, T.; Tascher, G.; Hoelper, S.; Stehmeier, P.; Keiten-Schmitz, J.; Schick, M.; Keller, U.; Mueller, S.
The SUMO isopeptidase SENP6 functions as a rheostat of chromatin residency in genome maintenance and chromosome dynamics
Cell Rep.
29
480-494.e5
2019
Homo sapiens (Q9GZR1)
brenda
Liczmanska, M.; Tatham, M.H.; Mojsa, B.; Eugui-Anta, A.; Rojas-Fernandez, A.; Ibrahim, A.F.M.; Hay, R.T.
SUMO protease SENP6 protects the nucleus from hyperSUMOylation-induced laminopathy-like alterations
Cell Rep.
42
112960
2023
Homo sapiens (Q9GZR1)
brenda
Fu, H.; Liu, N.; Dong, Q.; Ma, C.; Yang, J.; Xiong, J.; Zhang, Z.; Qi, X.; Huang, C.; Zhu, B.
SENP6-mediated M18BP1 deSUMOylation regulates CENP-A centromeric localization
Cell Res.
29
254-257
2019
Homo sapiens (Q9GZR1)
brenda
He, Q.; Chen, Z.; Li, J.; Liu, J.; Zuo, Z.; Lin, B.; Song, K.; Zhou, C.; Lai, H.; Huang, Q.; Guo, X.
SENP6-mediated deSUMOylation of VEGFR2 enhances its cell membrane transport in angiogenesis
Int. J. Mol. Sci.
24
2544
2023
Homo sapiens (Q9GZR1)
brenda
Schick, M.; Zhang, L.; Maurer, S.; Maurer, H.C.; Isaakaidis, K.; Schneider, L.; Patra, U.; Schunck, K.; Rohleder, E.; Hofstetter, J.; Baluapuri, A.; Scherger, A.K.; Slotta-Huspenina, J.; Hettler, F.; Weber, J.; Engleitner, T.; Maresch, R.; Slawska, J.; Lewis, R.; Istvanffy, R.; Habringer, S.; Steiger, K.; Baiker, A.; Oostendorp, R.A.J.; Miething, C.; Lenhof, H.-P.; Bassermann, F.; Chapuy, B.; Wirth, M.; Wolf, E.; Rad, R.; Mller, S.; Keller, U.
Genetic alterations of the SUMO isopeptidase SENP6 drive lymphomagenesis and genetic instability in diffuse large B-cell lymphoma
Nat. Commun.
13
281
2022
Homo sapiens (Q9GZR1)
brenda
Claessens, L.A.; Verlaan-de Vries, M.; de Graaf, I.J.; Vertegaal, A.C.O.
SENP6 regulates localization and nuclear condensation of DNA damage response proteins by group deSUMOylation
Nat. Commun.
14
5893
2023
Homo sapiens (Q9GZR1)
brenda
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