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

c-Myc is targeted to the proteasome for degradation in a SUMOylation-dependent manner, regulated by PIAS1, SENP7 and RNF4

Gonzalez-Prieto, R.; Cuijpers, S.A.; Kumar, R.; Hendriks, I.A.; Vertegaal, A.C.; Cell Cycle 14, 1859-1872 (2015)

Data extracted from this reference:

Engineering
Amino acid exchange
Commentary
Organism
additional information
lentivirus mediated SENP7 enzyme knockdown
Homo sapiens
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
nucleus
-
Homo sapiens
5634
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
SUMOylated c-Myc + H2O
Homo sapiens
-
deSUMOylated c-Myc + SUMO
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
-
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
breast cancer cell
-
Homo sapiens
-
colonic cancer cell
-
Homo sapiens
-
lung cancer cell
-
Homo sapiens
-
osteosarcoma cell
-
Homo sapiens
-
U2-OS cell
-
Homo sapiens
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
SENP7 is a SUMO protease with a preference for deconjugating SUMO2 and SUMO3, particularly in a polymeric form. Precursor SUMO1, SUMO2 and SUMO3 and SUMO1 polymers are poorly processed by SENP7
731599
Homo sapiens
?
-
-
-
-
SUMOylated c-Myc + H2O
-
731599
Homo sapiens
deSUMOylated c-Myc + SUMO
-
-
-
?
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
lentivirus mediated SENP7 enzyme knockdown
Homo sapiens
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
nucleus
-
Homo sapiens
5634
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
SUMOylated c-Myc + H2O
Homo sapiens
-
deSUMOylated c-Myc + SUMO
-
-
?
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
breast cancer cell
-
Homo sapiens
-
colonic cancer cell
-
Homo sapiens
-
lung cancer cell
-
Homo sapiens
-
osteosarcoma cell
-
Homo sapiens
-
U2-OS cell
-
Homo sapiens
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
SENP7 is a SUMO protease with a preference for deconjugating SUMO2 and SUMO3, particularly in a polymeric form. Precursor SUMO1, SUMO2 and SUMO3 and SUMO1 polymers are poorly processed by SENP7
731599
Homo sapiens
?
-
-
-
-
SUMOylated c-Myc + H2O
-
731599
Homo sapiens
deSUMOylated c-Myc + SUMO
-
-
-
?
General Information
General Information
Commentary
Organism
malfunction
increased SUMOylation of c-Myc occurs upon knockdown of the SUMO protease SENP7
Homo sapiens
metabolism
oncogene c-Myc-driven tumours are strongly dependent on the SUMO pathway. c-Myc is a target protein for SUMOylation, and SUMOylated c-Myc is subsequently ubiquitylated and degraded by the proteasome.. SUMO protease SENP7 is involved in c-Myc SUMOylation and regulation. Multiple SUMO monomers conjugated to c-Myc could be sufficient to direct SUMOylated c-Myc to the ubiquitin-proteasome pathway. PIAS1 and SENP7 regulate reversible SUMOylation of c-Myc
Homo sapiens
additional information
the catalytic domain of SENP7 consists of two separate parts interrupted by a stretch of amino acids. This feature is thought to contribute to its specificity for SUMO chains
Homo sapiens
physiological function
PIAS1 and SENP7 regulate reversible SUMOylation of c-Myc, SENP7 is responsible for removing SUMOs from c-Myc. Closely spaced SUMOs on c-Myc might be important for the regulation of SUMOylated c-Myc by SENP7 providing an alternative binding site for RNF4, a known regulator of SUMO polymers
Homo sapiens
General Information (protein specific)
General Information
Commentary
Organism
malfunction
increased SUMOylation of c-Myc occurs upon knockdown of the SUMO protease SENP7
Homo sapiens
metabolism
oncogene c-Myc-driven tumours are strongly dependent on the SUMO pathway. c-Myc is a target protein for SUMOylation, and SUMOylated c-Myc is subsequently ubiquitylated and degraded by the proteasome.. SUMO protease SENP7 is involved in c-Myc SUMOylation and regulation. Multiple SUMO monomers conjugated to c-Myc could be sufficient to direct SUMOylated c-Myc to the ubiquitin-proteasome pathway. PIAS1 and SENP7 regulate reversible SUMOylation of c-Myc
Homo sapiens
additional information
the catalytic domain of SENP7 consists of two separate parts interrupted by a stretch of amino acids. This feature is thought to contribute to its specificity for SUMO chains
Homo sapiens
physiological function
PIAS1 and SENP7 regulate reversible SUMOylation of c-Myc, SENP7 is responsible for removing SUMOs from c-Myc. Closely spaced SUMOs on c-Myc might be important for the regulation of SUMOylated c-Myc by SENP7 providing an alternative binding site for RNF4, a known regulator of SUMO polymers
Homo sapiens
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
c-Myc is targeted to the prote ...
Homo sapiens
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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732884
Alegre
Structural insights into the S ...
Homo sapiens
Protein Sci.
23
433-441
2014
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731715
Garvin
The deSUMOylase SENP7 promotes ...
Homo sapiens
EMBO Rep.
14
975-983
2013
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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
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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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