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Information on EC 3.4.22.68 - Ulp1 peptidase and Organism(s) Homo sapiens and UniProt Accession Q9HC62

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.68 Ulp1 peptidase
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This record set is specific for:
Homo sapiens
UNIPROT: Q9HC62 not found.
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Hydrolysis of the alpha-linked peptide bond in the sequence Gly-Gly-/-Ala-Thr-Tyr at the C-terminal end of the small ubiquitin-like modifier (SUMO) propeptide, Smt3, leading to the mature form of the protein. A second reaction involves the cleavage of an epsilon-linked peptide bond between the C-terminal glycine of the mature SUMO and the lysine epsilon-amino group of the target protein
Synonyms
senp1, senp2, sumo protease, senp6, sumo-specific protease, senp7, smt3ip1, ulp1 protease, sumo protease 1, sumo-specific protease 2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C48.001
-
-
-
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SENP7
-
-
small ubiquitin-like modifier protease
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Small ubiquitin-related modifier protein 1 conjugate proteinase
-
-
-
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Smt3-protein conjugate proteinase
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-
-
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SUMO protease
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Ulp1
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-
-
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Ulp1 endopeptidase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
252852-50-9
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
small ubiquitin-related modifier-CENP-I + H2O
small ubiquitin-related modifier-protein + CENP-I
show the reaction diagram
-
SUMO-specific proteases, SENPs, reversibly remove small ubiquitin-related modifier-protein, SUMO, from the SUMOylated proteins
-
-
r
small ubiquitin-related modifier-protein + H2O
small ubiquitin-related modifier-protein + protein
show the reaction diagram
-
SUMO-specific proteases, SENPs, reversibly remove small ubiquitin-related modifier-protein, SUMO, from the SUMOylated proteins
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-
r
additional information
?
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substrate specificities of different SENPS with different SUMOs, wild-types and mutants, very detailed overview. the SENP6 and SENP7 subclass displays a clear proteolytic cleavage preference for SUMO2/3 isoformsm structural determinants, overview. Identification of a unique sequence insertion in the SENP6 and SENP7 subclass that is essential for their proteolytic activity and that forms a more extensive interface with SUMO during the proteolytic reaction. Structure-based comparisons combined with biochemical and mutagenesis analysis reveal Loop 1 insertion in SENP6 and SENP7 as a platform to discriminate between SUMO1 and SUMO2/3 isoforms in this subclass of the SUMO protease family. Loop 1 SENP7 interacts with SUMO2. Deconjugation of diSUMO2(D71K) with SENP7 loop 1 mutant constructs, although proteolytic cleavage of diSUMO2(D71K) substrate shows a decrease in the proteolytic activity for all SENP7 constructs tested, including the wild type form. Mutation D71K, on the surface of SUMO2 distant from the cleavage site, can produce marked defects in the proteolytic activity of SENP7, with an approximately loss of 20fold with respect to the diSUMO2 wild type reaction
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-
?
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
small ubiquitin-related modifier-CENP-I + H2O
small ubiquitin-related modifier-protein + CENP-I
show the reaction diagram
-
SUMO-specific proteases, SENPs, reversibly remove small ubiquitin-related modifier-protein, SUMO, from the SUMOylated proteins
-
-
r
small ubiquitin-related modifier-protein + H2O
small ubiquitin-related modifier-protein + protein
show the reaction diagram
-
SUMO-specific proteases, SENPs, reversibly remove small ubiquitin-related modifier-protein, SUMO, from the SUMOylated proteins
-
-
r
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
Michaelis-Menten steady-state kinetics are performed for SENP6 by introduction of S9C and C52A point mutants into SUMO1 and SUMO1 mutant A68N/H71D to allow for fluorophore addition
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
SENP6 and SENP7
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SENP2_HUMAN
589
0
67855
Swiss-Prot
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K691A
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site-directed mutagenesis of SENP7
K691E
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site-directed mutagenesis of SENP7
P686G/P687G/P688G/P689G
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site-directed mutagenesis of SENP7
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant catalytic domains of human SENP2-(364-589), SENP6-(637-1112), and SENP7-(662-984) and of mutant SENP-7s from Escherichia coli by metal affinity chromatography and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of catalytic domains of human SENP2-(364-589), SENP6-(637-1112), and SENP7-(662-984) and of mutant SENP-7s in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
Alegre, K.; Reverter, D.
Swapping small ubiquitin-like modifier (SUMO) isoform specificity of SUMO proteases SENP6 and SENP7
J. Biol. Chem.
286
36142-36151
2011
Homo sapiens
Manually annotated by BRENDA team