3.4.22.B70: SENP1 peptidase
This is an abbreviated version!
For detailed information about SENP1 peptidase, go to the full flat file.
Word Map on EC 3.4.22.B70
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3.4.22.B70
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desumoylation
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deconjugating
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senp-1
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medicine
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sumo-modified
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senp1-mediated
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drug development
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ranbp2
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sumo-2
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diagnostics
- 3.4.22.B70
-
desumoylation
-
deconjugating
-
senp-1
- medicine
-
sumo-modified
-
senp1-mediated
- drug development
- ranbp2
- sumo-2
- diagnostics
Reaction
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 SUMO-1, SUMO-2 and SUMO-3 from targeted proteins. Deconjugates SUMO-1 from homeodomain-interacting protein kinase 2. Deconjugates SUMO-1 from histone deacetylase 1, which decreases its transcriptional repression activity. 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
C13orf22l, SENP, SENP1, sentrin-specific protease 1, sentrin/SUMO-specific protease 1, small ubiquitin-like modifier protein-specific protease 1, small ubiquitin-related modifier-specific isopeptidase, SUMO isopeptidase, SUMO protease, SUMO protein-specific protease 1, SUMO-specific isopeptidase, SUMO-specific protease, SUMO-specific protease 1, ubiquitin-specific protease-like 1, USPL1
ECTree
3.4.22.B70 SENP1 peptidaseAdvanced search results
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results (Engineering
Engineering on EC 3.4.22.B70 - SENP1 peptidase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C236S
site-directed mutagenesis, the mutant is not inhibited by suicide inhibitor Strep-TEV-HA-SUMO-vinylmethylester in contrast to the wild-type enzyme
C602A
completely inactive in processing of SUMO-2 and in deconjugating SUMO-2
C603A
the mutant is unable to desumoylate the (SUMO-1)-homeodomain-interacting protein kinase 2 conjugate
C603S
D441A
mutant protein is indistinguishable from that of the wild-type protein in both processing and deconjugation
D468A
mutated protein is only slightly impaired in processing and not at all in deconjugation
D550A
completely inactive in processing of SUMO-2 and in deconjugating SUMO-2
F496A
altered protein retains significant levels of deconjugation activity
H529A
altered protein retains significant levels of deconjugation activity
H533A
completely inactive in processing of SUMO-2 and in deconjugating SUMO-2
Q596A
mutant of SENP1 is severely impaired in both deconjugation and processing
W229L
site-directed mutagenesis, mutation to the residue found in USP2 and other ubiquitin-specific USPs dramatically impairs SUMO binding and cleavage
W237F
site-directed mutagenesis, mutation to the residue found in USP2 and other ubiquitin-specific USPs dramatically impairs SUMO binding and cleavage
W512A
mutant has a reduced deconjugation activity in vitro, its deconjugation activity in vivo is only impaired to a small extent
C599S
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site-directed mutagenesis, the active site mutant precipitates SUMO1ylated proteins but not SUMO2/3-modified substrate
additional information
C603S
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inactive mutant enzyme. C603S is exclusively nuclear in comparison with the wild-type SENP1, which is consistently present in the cytoplasm, albeit t low steady state levels. SENP1 is itself a target for SUMO-1 modification but that this modification is normally rapidly reversed by an autocatalytic activity removing the SUMO-1, with little of the modified form accumulating. In the mutant SENP1 (C603S), the absence of proteolytic activity resul in the detection of the conjugated form
additional information
residues 415643 of SENP1 are expressed and purified from Escherichia coli and are shown to be catalytically active in SUMO processing and deconjugation
additional information
the deletion of the C-terminal portion to aa 634 induces the nuclear localization of SENP1. Further deletion to aa 574 results in the diffused localization of SENP1 both to the nucleus and the cytoplasm. This result suggests that there might be a motif for the nuclear localization of SENP1 in the region from aa 574 to 633
additional information
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very few cells express the exogenous SENP1 436-644 core domain construct, and in any positive cells expression is at extremely low levels. The SENP1 436-644 C603S construct, however, is readily detected, often with very high levels of expression
additional information
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construction of a SENP1 catalytically inactive/dominant negative Cys-to-Ser SENP1 mutant or a SENP1 shRNA construct, enzyme SENP1 silencing by expression of siRNA
additional information
wild-type and inactive USPL1 variants rescue proliferation and coilin localization. Construction of His-GST-TEV-USPL1cat variants and analysis of their SUMO-AMC hydrolysis and SUMO binding. Four mutants show severe and two mutants moderate loss of activity, accompanied by severe or moderate reduction in binding
additional information
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construction of several allelic defective enzyme mutants and a truncated mutant Senp1, overview, and a Senp1-beta-geo fusion protein, Expression of the amino half of Senp1 reduces Senp2 levels
