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
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desumoylation
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deconjugating
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senp-1
- medicine
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sumo-modified
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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
results (
results (Substrates Products
Substrates Products on EC 3.4.22.B70 - SENP1 peptidase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(SUMO-1)-homeodomain-interacting protein kinase 2 conjugate + H2O
SUMO-1 + homeodomain-interacting protein kinase 2 conjugate
(SUMO-1)-K2P1 potassium channel + H2O
SUMO-1 + K2P1 potassium channel
silent K2P1 channels in excised plasma membrane patches are activated by SENP1
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-
?
(SUMO-1)-K2P1 subunit of potassium channel + H2O
SUMO-1 + K2P1 subunit of potassium channel
SUMO1 is conjugated to the epsilon-amino group of Lys274 of the K2P1 potassium channel. When mutated to Gln, Arg, Glu, Asp, Cys, or Ala, the channels are constitutively active and insensitive to SUMO1 and SENP1. Wild-type channels in plasma membrane have two K2P1 subunits and assemble with two SUMO1 monomers. Although channels engineered with one Lys274 site carry just one SUMO1 they are activated and silenced by SENP1 and SUMO1 like wild-type channels
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-
?
(SUMO-1)-Ran GTPase-activating protein 1 conjugate + H2O
SUMO-1 + Ran GTPase-activating protein 1
rates at which SUMO-1, SUMO-2 and SUMO-3 are deconjugated from RanGAP1 are indistinguishable
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-
?
(SUMO-1)-RanGAP1 conjugate + H2O
SUMO-1 + RanGAP1
SENP1 binding is accompanied by a conformational change in the substrate
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-
?
(SUMO-2)-Ran GTPase-activating protein 1 conjugate + H2O
SUMO-2 + Ran GTPase-activating protein 1
rates at which SUMO-1, SUMO-2 and SUMO-3 are deconjugated from RanGAP1 are indistinguishable
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-
?
(SUMO-2)-RanGAP1 conjugate + H2O
SUMO-2 + RanGAP1
SENP1 binding is accompanied by a conformational change in the substrate
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-
?
(SUMO-2)n-glutathione S-transferase-promyelocytic leukemia protein conjugate + H2O
?
glutathione S-transferase-promyelocytic leukemia protein bearing a polymeric chain of SUMO-2
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-
?
(SUMO-3)-Ran GTPase-activating protein 1 conjugate + H2O
SUMO-3 + Ran GTPase-activating protein 1
rates at which SUMO-1, SUMO-2 and SUMO-3 are deconjugated from RanGAP1 are indistinguishable
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-
?
CrSUMO148 precursor + H2O
CrSUMO148 + peptide
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CrSUMO148 is a SUMO homolog from Chlamydomonas reinhardtii with 148 amino acids. SENP1 solely cleaves CrSUMO148 at the peptide bond after the first diglycine motif, although there are four putative cleavage sites in the primary amino acid sequence
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-
?
CrSUMO148-conjugated protein + H2O
CrSUMO148 + protein
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CrSUMO96 is a SUMO homolog from Chlamydomonas reinhardtii with 148 amino acids
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-
?
CrSUMO96 precursor + H2O
CrSUMO96 + peptide
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CrSUMO96 is a SUMO homolog from Chlamydomonas reinhardtii with 96 amino acids. SENP1 shows more processing activity for CrSUMO97 than for CrSUMO96
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-
?
CrSUMO96-conjugated protein + H2O
CrSUMO96 + protein
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CrSUMO96 is a SUMO homolog from Chlamydomonas reinhardtii with 96 amino acids
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-
?
CrSUMO97 precursor + H2O
CrSUMO97 + peptide
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CrSUMO97 is a SUMO homolog from Chlamydomonas reinhardtii with 97 amino acids. SENP1 shows more processing activity for CrSUMO97 than for CrSUMO96
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-
?
CrSUMO97-conjugated protein + H2O
CrSUMO97 + protein
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CrSUMO96 is a SUMO homolog from Chlamydomonas reinhardtii with 97 amino acids
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-
?
polyCrSUMO148 + H2O
?
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CrSUMO148 is a SUMO homolog from Chlamydomonas reinhardtii with 148 amino acids. polyCrSUMO148 chains aree completely deconjugated by SENP1
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-
?
polyCrSUMO96 + H2O
?
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CrSUMO96 is a SUMO homolog from Chlamydomonas reinhardtii with 96 amino acids. polyCrSUMO96 chains aree completely deconjugated by SENP1. SENP1 displays a similar efficiency to deconjugate either polymeric CrSUMO96 or CrSUMO97 chains
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-
?
polyCrSUMO97 + H2O
?
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CrSUMO97 is a SUMO homolog from Chlamydomonas reinhardtii with 97 amino acids. polyCrSUMO97 chains aree completely deconjugated by SENP1. SENP1 displays a similar efficiency to deconjugate either polymeric CrSUMO96 or CrSUMO97 chains
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-
?
pro-small ubiquitin-related modifier + H2O
small ubiquitin-related modifier + ?
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SENP1 processes the precursor SUMO to its mature form by catalyzing the cleavage of a scissile peptide bond
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?
small ubiquitin-related modifier-protein + H2O
small ubiquitin-related modifier-protein + protein
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SUMO-specific proteases, SENPs, reversibly remove small ubiquitin-related modifier-protein, SUMO, from the SUMOylated proteins
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r
SUMO-homeodomain-interacting protein kinase 1 conjugate + H2O
SUMO + homeodomain-interacting protein kinase 1 conjugate
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-
-
?
SUMOylated androgen receptor + H2O
androgen receptor + SUMO1
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deconjugation
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-
?
SUMOylated peroxisome proliferator-activated receptor coactivator 1alpha + H2O
deSUMOylated peroxisome proliferator-activated receptor coactivator 1alpha + SUMO1
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deSUMOylation
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-
?
(SUMO-1)-androgen receptor conjugate + H2O
SUMO-1 + androgen receptor conjugate
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-
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?
(SUMO-1)-androgen receptor conjugate + H2O
SUMO-1 + androgen receptor conjugate
SENP1 markedly contributes to the androgen-stimulated proliferation of prostate cancer cells
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-
?
(SUMO-1)-histone deacetylase 1 conjugate + H2O
SUMO-1 + histone deacetylase 1
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-
-
?
(SUMO-1)-histone deacetylase 1 conjugate + H2O
SUMO-1 + histone deacetylase 1
SENP1 regulates that androgen receptor-dependent transcription through desumoylation of histone deacetylase 1 (HDAC1)
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-
?
(SUMO-1)-homeodomain-interacting protein kinase 2 conjugate + H2O
SUMO-1 + homeodomain-interacting protein kinase 2 conjugate
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-
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?
(SUMO-1)-homeodomain-interacting protein kinase 2 conjugate + H2O
SUMO-1 + homeodomain-interacting protein kinase 2 conjugate
desumoylation of homeodomain-interacting protein kinase 2 (HIPK2) may be regulated by the cytoplasmic-nuclear shuttling of SENP1. Desumoylation induces dissociation of homeodomain-interacting protein kinase 2 conjugate from nuclear bodies
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-
?
Pin1 + H2O
?
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Pin1 is SUMOylated on Lys6 in the WW domain and on Lys63 in the PPIase domain, deSUMOlation by SENP1
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-
?
Pin1 + H2O
?
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Pin1 is SUMOylated on Lys6 in the WW domain and on Lys63 in the PPIase domain, deSUMOlation by SENP1. SENP1 is more efficient in deSUMOylating Pin1 than SENP2, whereas SENP3 is barely active
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-
?
SUMO-1 precursor + H2O
SUMO-1 + His-Ser-Thr-Val
cleavage of the -Gly-Gly-/-His-Ser-Thr-Val bond. The maturation reaction is the first committed step for subsequent sumoylation
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-
?
SUMO-1 precursor + H2O
SUMO-1 + His-Ser-Thr-Val
pre-SUMO-1 is processed rapidly
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-
?
SUMO-1 precursor + H2O
SUMO-1 + His-Ser-Thr-Val
SENP1 is capable of processing all SUMO-1, -2 and -3 in vitro but with different efficiencies. Cleavage of the -Gly-Gly-/-His-Ser-Thr-Val bond. Over 90% of SUMO-1 is hydrolysed
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-
?
SUMO-1 precursor + H2O
SUMO-1 + His-Ser-Thr-Val
SENP1 preferentially processes SUMO-1 over SUMO-2. Discrimination between unprocessed SUMO-1 and SUMO-2 by SENP1 is based on a catalytic step rather than substrate binding. SENP1 binding is accompanied by a conformational change in the substrate
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-
?
SUMO-2 precursor + H2O
SUMO-2 + Val-Tyr
cleavage of the -Gly-Gly-/-Val-Tyr. The maturation reaction is the first committed step for subsequent sumoylation
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-
?
SUMO-2 precursor + H2O
SUMO-2 + Val-Tyr
pre-SUMO-2 is processed slowly
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-
?
SUMO-2 precursor + H2O
SUMO-2 + Val-Tyr
SENP1 is capable of processing all SUMO-1, -2 and -3 in vitro but with different efficiencies. Over 90% of SUMO-2 is hydrolysed. Cleavage of the -Gly-Gly-/-Val-Tyr
-
-
?
SUMO-2 precursor + H2O
SUMO-2 + Val-Tyr
SENP1 preferentially processes SUMO-1 over SUMO-2. Discrimination between unprocessed SUMO-1 and SUMO-2 by SENP1 is based on a catalytic step rather than substrate binding. SENP1 binding is accompanied by a conformational change in the substrate
-
-
?
SUMO-3 precursor + H2O
SUMO-3 + Val-Pro-Glu-Ser-Ser-Leu-Ala-Gly-His-Ser-Phe
cleavage of the -Gly-Gly-/-Val-Pro-Glu-Ser-Ser-Leu-Ala-Gly-His-Ser-Phe bond. The maturation reaction is the first committed step for subsequent sumoylation
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-
?
SUMO-3 precursor + H2O
SUMO-3 + Val-Pro-Glu-Ser-Ser-Leu-Ala-Gly-His-Ser-Phe
pre-SUMO-3 is processed at an intermediate rate
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-
?
SUMO-3 precursor + H2O
SUMO-3 + Val-Pro-Glu-Ser-Ser-Leu-Ala-Gly-His-Ser-Phe
SENP1 is capable of processing all SUMO-1, -2 and -3 in vitro but with different efficiencies. 50% of SUMO-3 is hydrolysed. Cleavage of the -Gly-Gly-/-Val-Pro-Glu-Ser-Ser-Leu-Ala-Gly-His-Ser-Phe bond
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-
?
SUMO-7-amido-4-methylcoumarin + H2O
SuMo + 7-amino-4-methylcoumarin
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-
-
?
SUMO-Elk-1 conjugate + H2O
SUMO + Elk-1
SENP1 participates in the dynamic regulation of Elk-1 SUMOylation
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-
?
SUMO-GATA 1 conjugate + H2O
SUMO + GATA1
SENP1 promotes GATA1 activation and subsequent erythropoiesis by deSUMOylating GATA1
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-
?
SUMO-hypoxia-inducible factor 1 conjugate + H2O
SUMO + hypoxia-inducible factor 1
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-
-
?
SUMO-hypoxia-inducible factor 1 conjugate + H2O
SUMO + hypoxia-inducible factor 1
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-
-
?
SUMO-hypoxia-inducible factor 1 conjugate + H2O
SUMO + hypoxia-inducible factor 1
deSUMOylation plays a critical role in prostate pathogenesis through induction of HIF1alpha-dependent angiogenesis and enhanced cell proliferation
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-
?
additional information
?
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enzyme USPL1 neither binds nor cleaves ubiquitin, but is a potent SUMO isopeptidase both in vitro and in cells
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-
?
additional information
?
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enzyme USPL1 binds SUMO but not ubiquitin, no activity with ubiquitin-7-amido-4-methylcoumarin
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-
?
additional information
?
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SENP1 appears catalytically competent in their apo forms. Upon SUMO interaction, local conformational rearrangement of Trp465, His529 and Trp534 occurs, while Cys603 separates from the catalytic triad to attack the carbonyl-C of Gly97 of SUMO. After the cleavage event, SUMO is released from the complex and converted into its apo form ready for the next reaction cycle
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-
?
additional information
?
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SENP1 is potent in removing both SUMO-1 and SUMO-2 from cellular proteins. SENP1 does not seem to differentiate between SUMO-1 and SUMO-2
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-
?
additional information
?
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enzyme USPL1 neither binds nor cleaves ubiquitin, but is a potent SUMO isopeptidase both in vitro and in cells
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?
additional information
?
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nucleoporin Nup153 binds to SENP1 by interacting with the unique N-terminal domain of Nup153 as well as a specific region within the C-terminal FG-rich region. Nup153 is a substrate for SUMOylation, with this modification kept in check by the SUMO protease
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-
?
additional information
?
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the enzyme SUMO protease removes SUMO conjugate from proteins
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?
additional information
?
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enzyme USPL1 binds SUMO but not ubiquitin, no activity with ubiquitin-7-amido-4-methylcoumarin
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?
additional information
?
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the enzyme SENP1 interacts with SUMO1-FL, SUMO1-GG, SUMO11-92 (containing residues 1-92, with C-terminus truncated) or peptides corresponding to the C-terminus of SUMO1. The exchange rates between free SENP1 and SENP1 in complex with SUMO1-FL or SUMO1-GG are mostly slow to intermediate, relative to the NMR chemical shift timescale, and both SUMO-GG and SUMO-FL produce similar chemical shift perturbation. The beta-grasp domain of SUMO1 interacts with enzyme SENP1 in a manner similar to that in the context of SUMO1-FL, effects of beta-grasp domain on the enzyme, overview
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?
additional information
?
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recombinant enzyme Senp1 can deconjugate terminal Sumo1 moieties on poly-Sumo2/3 chains
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?
