BRENDA - Enzyme Database show
show all sequences of 3.4.22.B75

The SUMO protease SENP7 is a critical component to ensure HP1 enrichment at pericentric heterochromatin

Maison, C.; Romeo, K.; Bailly, D.; Dubarry, M.; Quivy, J.P.; Almouzni, G.; Nat. Struct. Mol. Biol. 19, 458-460 (2012)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
recombinant expression of GFP-tagged wild-type and mutant enzyme SENP7
Mus musculus
Engineering
Amino acid exchange
Commentary
Organism
C979S
site-directed mutagenesis
Mus musculus
additional information
Depletion of SENP7 from NIH-3T3 cells by transfecting a plasmid encoding both a microRNA to downregulate SENP7 (miSENP7) and a GFP mRNA to enable identification of the transfected cells
Mus musculus
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
nucleus
-
Mus musculus
5634
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
SUMOylated HP1alpha + H2O
Mus musculus
SUMO deconjugation by enzyme SENP7
HP1alpha + SUMO
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Mus musculus
-
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
MEF cell
-
Mus musculus
-
NIH-3T3 cell
-
Mus musculus
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
SUMOylated HP1alpha + H2O
SUMO deconjugation by enzyme SENP7
732566
Mus musculus
HP1alpha + SUMO
-
-
-
?
Cloned(Commentary) (protein specific)
Commentary
Organism
recombinant expression of GFP-tagged wild-type and mutant enzyme SENP7
Mus musculus
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
C979S
site-directed mutagenesis
Mus musculus
additional information
Depletion of SENP7 from NIH-3T3 cells by transfecting a plasmid encoding both a microRNA to downregulate SENP7 (miSENP7) and a GFP mRNA to enable identification of the transfected cells
Mus musculus
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
nucleus
-
Mus musculus
5634
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
SUMOylated HP1alpha + H2O
Mus musculus
SUMO deconjugation by enzyme SENP7
HP1alpha + SUMO
-
-
?
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
MEF cell
-
Mus musculus
-
NIH-3T3 cell
-
Mus musculus
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
SUMOylated HP1alpha + H2O
SUMO deconjugation by enzyme SENP7
732566
Mus musculus
HP1alpha + SUMO
-
-
-
?
General Information
General Information
Commentary
Organism
malfunction
enzyme SENP7 depleted cells show reduced localization of HP1alpha at pericentric heterochromatin domains, while trimethylated histone H3 Lys9 (H3K9me3) remains present at these domains
Mus musculus
physiological function
the SUMO-specific protease SENP7 in mouse is a maintenance factor for HP1alpha accumulation at pericentric heterochromatin. Enzyme SENP7 interacts directly with HP1alpha, localizes at HP1-enriched pericentric domain,s and can deconjugate SUMOylated HP1alpha in vivo. SUMOylation promotes targeting of HP1alpha to pericentric heterochromatin. DeSUMOylation event enables HP1alpha retention at these domains
Mus musculus
General Information (protein specific)
General Information
Commentary
Organism
malfunction
enzyme SENP7 depleted cells show reduced localization of HP1alpha at pericentric heterochromatin domains, while trimethylated histone H3 Lys9 (H3K9me3) remains present at these domains
Mus musculus
physiological function
the SUMO-specific protease SENP7 in mouse is a maintenance factor for HP1alpha accumulation at pericentric heterochromatin. Enzyme SENP7 interacts directly with HP1alpha, localizes at HP1-enriched pericentric domain,s and can deconjugate SUMOylated HP1alpha in vivo. SUMOylation promotes targeting of HP1alpha to pericentric heterochromatin. DeSUMOylation event enables HP1alpha retention at these domains
Mus musculus
Other publictions for EC 3.4.22.B75
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
731599
Gonzalez-Prieto
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Cell Cycle
14
1859-1872
2015
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731614
Romeo
The SENP7 SUMO-protease presen ...
Mus musculus
Cell Rep.
10
771-782
2015
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3
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732884
Alegre
Structural insights into the S ...
Homo sapiens
Protein Sci.
23
433-441
2014
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2
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731715
Garvin
The deSUMOylase SENP7 promotes ...
Homo sapiens
EMBO Rep.
14
975-983
2013
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3
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732566
Maison
The SUMO protease SENP7 is a c ...
Mus musculus
Nat. Struct. Mol. Biol.
19
458-460
2012
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732812
Bawa-Khalfe
Differential expression of SUM ...
Homo sapiens
Proc. Natl. Acad. Sci. USA
109
17466-17471
2012
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714083
Shen
Characterization of SENP7, a S ...
Homo sapiens
Biochem. J.
421
223-230
2009
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714081
Drag
Activity profiling of human de ...
Homo sapiens
Biochem. J.
409
461-469
2008
2
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715494
Lima
Structure of the human SENP7 c ...
Homo sapiens
J. Biol. Chem.
283
32045-32055
2008
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