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Information on EC 3.4.22.B70 - SENP1 peptidase
for references in articles please use BRENDA:EC3.4.22.B70
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preliminary BRENDA-supplied EC number
EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.22 Cysteine endopeptidases
3.4.22.B70 SENP1 peptidase
The enzyme appears in viruses and cellular organisms
- 3.4.22.B70
-
desumoylation
-
deconjugating
-
senp-1
- medicine
-
sumo-modified
-
senp1-mediated
- drug development
- ranbp2
- sumo-2
- diagnostics
Reaction Schemes
showThe 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
sumo isopeptidase, sumo-specific protease 1, uspl1, sentrin/sumo-specific protease 1, sumo-specific isopeptidase, sentrin-specific protease 1, ubiquitin-specific protease-like 1, small ubiquitin-like modifier protein-specific protease 1, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SENP1
sentrin-specific protease 1
SUMO isopeptidase
SUMO protease
SUMO-specific protease
SUMO-specific protease 1
SENP1
-
-
SENP1
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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.
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
Q9P0U3 {SwissProt}
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
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
Substrates: silent K2P1 channels in excised plasma membrane patches are activated by SENP1
Products: -
Products: -
?
(SUMO-1)-K2P1 subunit of potassium channel + H2O
SUMO-1 + K2P1 subunit of potassium channel
Substrates: 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
Products: -
Products: -
?
(SUMO-1)-Ran GTPase-activating protein 1 conjugate + H2O
SUMO-1 + Ran GTPase-activating protein 1
Substrates: rates at which SUMO-1, SUMO-2 and SUMO-3 are deconjugated from RanGAP1 are indistinguishable
Products: -
Products: -
?
(SUMO-1)-RanGAP1 conjugate + H2O
SUMO-1 + RanGAP1
Substrates: SENP1 binding is accompanied by a conformational change in the substrate
Products: -
Products: -
?
(SUMO-2)-Ran GTPase-activating protein 1 conjugate + H2O
SUMO-2 + Ran GTPase-activating protein 1
Substrates: rates at which SUMO-1, SUMO-2 and SUMO-3 are deconjugated from RanGAP1 are indistinguishable
Products: -
Products: -
?
(SUMO-2)-RanGAP1 conjugate + H2O
SUMO-2 + RanGAP1
Substrates: SENP1 binding is accompanied by a conformational change in the substrate
Products: -
Products: -
?
(SUMO-2)n-glutathione S-transferase-promyelocytic leukemia protein conjugate + H2O
?
Substrates: glutathione S-transferase-promyelocytic leukemia protein bearing a polymeric chain of SUMO-2
Products: -
Products: -
?
(SUMO-3)-Ran GTPase-activating protein 1 conjugate + H2O
SUMO-3 + Ran GTPase-activating protein 1
Substrates: rates at which SUMO-1, SUMO-2 and SUMO-3 are deconjugated from RanGAP1 are indistinguishable
Products: -
Products: -
?
CrSUMO148 precursor + H2O
CrSUMO148 + peptide
-
Substrates: 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
Products: -
Products: -
?
CrSUMO148-conjugated protein + H2O
CrSUMO148 + protein
-
Substrates: CrSUMO96 is a SUMO homolog from Chlamydomonas reinhardtii with 148 amino acids
Products: -
Products: -
?
CrSUMO96 precursor + H2O
CrSUMO96 + peptide
-
Substrates: CrSUMO96 is a SUMO homolog from Chlamydomonas reinhardtii with 96 amino acids. SENP1 shows more processing activity for CrSUMO97 than for CrSUMO96
Products: -
Products: -
?
CrSUMO96-conjugated protein + H2O
CrSUMO96 + protein
-
Substrates: CrSUMO96 is a SUMO homolog from Chlamydomonas reinhardtii with 96 amino acids
Products: -
Products: -
?
CrSUMO97 precursor + H2O
CrSUMO97 + peptide
-
Substrates: CrSUMO97 is a SUMO homolog from Chlamydomonas reinhardtii with 97 amino acids. SENP1 shows more processing activity for CrSUMO97 than for CrSUMO96
Products: -
Products: -
?
CrSUMO97-conjugated protein + H2O
CrSUMO97 + protein
-
Substrates: CrSUMO96 is a SUMO homolog from Chlamydomonas reinhardtii with 97 amino acids
Products: -
Products: -
?
polyCrSUMO148 + H2O
?
-
Substrates: CrSUMO148 is a SUMO homolog from Chlamydomonas reinhardtii with 148 amino acids. polyCrSUMO148 chains aree completely deconjugated by SENP1
Products: -
Products: -
?
polyCrSUMO96 + H2O
?
-
Substrates: 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
Products: -
Products: -
?
polyCrSUMO97 + H2O
?
-
Substrates: 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
Products: -
Products: -
?
pro-small ubiquitin-related modifier + H2O
small ubiquitin-related modifier + ?
-
Substrates: SENP1 processes the precursor SUMO to its mature form by catalyzing the cleavage of a scissile peptide bond
Products: -
Products: -
?
Sharp-1 protein + H2O
?
Substrates: deSUMOylation by the enzyme
Products: -
Products: -
?
small ubiquitin-related modifier-protein + H2O
small ubiquitin-related modifier-protein + protein
-
Substrates: SUMO-specific proteases, SENPs, reversibly remove small ubiquitin-related modifier-protein, SUMO, from the SUMOylated proteins
Products: -
Products: -
r
SUMO-homeodomain-interacting protein kinase 1 conjugate + H2O
SUMO + homeodomain-interacting protein kinase 1 conjugate
Substrates: -
Products: -
Products: -
?
SUMO-STAT3 protein conjugate + H2O
SUMO + STAT3 protein
Substrates: -
Products: -
Products: -
?
SUMO1-7-amido-4-methylcoumarin + H2O
SUMO1 + 7-amido-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
SUMO1-7-amido-4-methylcoumarin + H2O
SUMO1 + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
SUMO2-7-amido-4-methylcoumarin + H2O
SUMO2 + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
SUMO3-7-amido-4-methylcoumarin + H2O
SUMO3 + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
SUMOylated androgen receptor + H2O
androgen receptor + SUMO1
-
Substrates: deconjugation
Products: -
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?
SUMOylated CD45 + H2O
?
Substrates: SENP1 can deconjugate SUMOylated CD45
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?
SUMOylated peroxisome proliferator-activated receptor coactivator 1alpha + H2O
deSUMOylated peroxisome proliferator-activated receptor coactivator 1alpha + SUMO1
-
Substrates: deSUMOylation
Products: -
Products: -
?
(SUMO-1)-androgen receptor conjugate + H2O
SUMO-1 + androgen receptor conjugate
Substrates: SENP1 markedly contributes to the androgen-stimulated proliferation of prostate cancer cells
Products: -
Products: -
?
(SUMO-1)-androgen receptor conjugate + H2O
SUMO-1 + androgen receptor conjugate
Substrates: -
Products: -
Products: -
?
(SUMO-1)-histone deacetylase 1 conjugate + H2O
SUMO-1 + histone deacetylase 1
Substrates: SENP1 regulates that androgen receptor-dependent transcription through desumoylation of histone deacetylase 1 (HDAC1)
Products: -
Products: -
?
(SUMO-1)-histone deacetylase 1 conjugate + H2O
SUMO-1 + histone deacetylase 1
Substrates: -
Products: -
Products: -
?
(SUMO-1)-homeodomain-interacting protein kinase 2 conjugate + H2O
SUMO-1 + homeodomain-interacting protein kinase 2 conjugate
Substrates: 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
Products: -
Products: -
?
(SUMO-1)-homeodomain-interacting protein kinase 2 conjugate + H2O
SUMO-1 + homeodomain-interacting protein kinase 2 conjugate
Substrates: -
Products: -
Products: -
?
Pin1 + H2O
?
-
Substrates: Pin1 is SUMOylated on Lys6 in the WW domain and on Lys63 in the PPIase domain, deSUMOlation by SENP1
Products: -
Products: -
?
Pin1 + H2O
?
-
Substrates: 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
Products: -
Products: -
?
SUMO-1 precursor + H2O
SUMO-1 + His-Ser-Thr-Val
Substrates: cleavage of the -Gly-Gly-/-His-Ser-Thr-Val bond. The maturation reaction is the first committed step for subsequent sumoylation
Products: -
Products: -
?
SUMO-1 precursor + H2O
SUMO-1 + His-Ser-Thr-Val
Substrates: 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
Products: -
Products: -
?
SUMO-1 precursor + H2O
SUMO-1 + His-Ser-Thr-Val
Substrates: 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
Substrates: pre-SUMO-1 is processed rapidly
Products: -
Products: -
?
SUMO-2 precursor + H2O
SUMO-2 + Val-Tyr
Substrates: cleavage of the -Gly-Gly-/-Val-Tyr. The maturation reaction is the first committed step for subsequent sumoylation
Products: -
Products: -
?
SUMO-2 precursor + H2O
SUMO-2 + Val-Tyr
Substrates: 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
Products: -
Products: -
?
SUMO-2 precursor + H2O
SUMO-2 + Val-Tyr
Substrates: 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
Products: -
Products: -
?
SUMO-2 precursor + H2O
SUMO-2 + Val-Tyr
Substrates: pre-SUMO-2 is processed slowly
Products: -
Products: -
?
SUMO-3 precursor + H2O
SUMO-3 + Val-Pro-Glu-Ser-Ser-Leu-Ala-Gly-His-Ser-Phe
Substrates: 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
Products: -
Products: -
?
SUMO-3 precursor + H2O
SUMO-3 + Val-Pro-Glu-Ser-Ser-Leu-Ala-Gly-His-Ser-Phe
Substrates: 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
Products: -
Products: -
?
SUMO-3 precursor + H2O
SUMO-3 + Val-Pro-Glu-Ser-Ser-Leu-Ala-Gly-His-Ser-Phe
Substrates: pre-SUMO-3 is processed at an intermediate rate
Products: -
Products: -
?
SUMO-7-amido-4-methylcoumarin + H2O
SuMo + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
SUMO-7-amido-4-methylcoumarin + H2O
SuMo + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
SUMO-Elk-1 conjugate + H2O
SUMO + Elk-1
Substrates: SENP1 participates in the dynamic regulation of Elk-1 SUMOylation
Products: -
Products: -
?
SUMO-GATA 1 conjugate + H2O
SUMO + GATA1
Substrates: SENP1 promotes GATA1 activation and subsequent erythropoiesis by deSUMOylating GATA1
Products: -
Products: -
?
SUMO-hypoxia-inducible factor 1 conjugate + H2O
SUMO + hypoxia-inducible factor 1
Substrates: -
Products: -
Products: -
?
SUMO-hypoxia-inducible factor 1 conjugate + H2O
SUMO + hypoxia-inducible factor 1
Substrates: deSUMOylation plays a critical role in prostate pathogenesis through induction of HIF1alpha-dependent angiogenesis and enhanced cell proliferation
Products: -
Products: -
?
SUMO-hypoxia-inducible factor 1 conjugate + H2O
SUMO + hypoxia-inducible factor 1
Substrates: -
Products: -
Products: -
?
SUMO-p53 + H2O
SUMO + p53
Substrates: SENP1 promotes cell proliferation by negatively regulating p53 activity
Products: -
Products: -
?
SUMO1ylated protein + H2O
SUMO1 + protein
-
Substrates: main substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme USPL1 neither binds nor cleaves ubiquitin, but is a potent SUMO isopeptidase both in vitro and in cells
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme USPL1 binds SUMO but not ubiquitin, no activity with ubiquitin-7-amido-4-methylcoumarin
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme USPL1 neither binds nor cleaves ubiquitin, but is a potent SUMO isopeptidase both in vitro and in cells
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme SUMO protease removes SUMO conjugate from proteins
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme USPL1 binds SUMO but not ubiquitin, no activity with ubiquitin-7-amido-4-methylcoumarin
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: molecular dynamics simulation is performed on apo-SENP1, SENP1-SUMO1, and SENP1-SUMO2 systems to investigate the molecular basis for SENP1's preference for SUMO1 over SUMO2
Products: -
Products: -
-
additional information
?
-
-
Substrates: recombinant enzyme Senp1 can deconjugate terminal Sumo1 moieties on poly-Sumo2/3 chains
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(SUMO-1)-androgen receptor conjugate + H2O
SUMO-1 + androgen receptor conjugate
Substrates: SENP1 markedly contributes to the androgen-stimulated proliferation of prostate cancer cells
Products: -
Products: -
?
(SUMO-1)-histone deacetylase 1 conjugate + H2O
SUMO-1 + histone deacetylase 1
Substrates: SENP1 regulates that androgen receptor-dependent transcription through desumoylation of histone deacetylase 1 (HDAC1)
Products: -
Products: -
?
(SUMO-1)-homeodomain-interacting protein kinase 2 conjugate + H2O
SUMO-1 + homeodomain-interacting protein kinase 2 conjugate
Substrates: 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
Products: -
Products: -
?
(SUMO-1)-K2P1 potassium channel + H2O
SUMO-1 + K2P1 potassium channel
Substrates: silent K2P1 channels in excised plasma membrane patches are activated by SENP1
Products: -
Products: -
?
Pin1 + H2O
?
-
Substrates: Pin1 is SUMOylated on Lys6 in the WW domain and on Lys63 in the PPIase domain, deSUMOlation by SENP1
Products: -
Products: -
?
pro-small ubiquitin-related modifier + H2O
small ubiquitin-related modifier + ?
-
Substrates: SENP1 processes the precursor SUMO to its mature form by catalyzing the cleavage of a scissile peptide bond
Products: -
Products: -
?
Sharp-1 protein + H2O
?
Substrates: deSUMOylation by the enzyme
Products: -
Products: -
?
small ubiquitin-related modifier-protein + H2O
small ubiquitin-related modifier-protein + protein
-
Substrates: SUMO-specific proteases, SENPs, reversibly remove small ubiquitin-related modifier-protein, SUMO, from the SUMOylated proteins
Products: -
Products: -
r
SUMO-1 precursor + H2O
SUMO-1 + His-Ser-Thr-Val
Substrates: cleavage of the -Gly-Gly-/-His-Ser-Thr-Val bond. The maturation reaction is the first committed step for subsequent sumoylation
Products: -
Products: -
?
SUMO-2 precursor + H2O
SUMO-2 + Val-Tyr
Substrates: cleavage of the -Gly-Gly-/-Val-Tyr. The maturation reaction is the first committed step for subsequent sumoylation
Products: -
Products: -
?
SUMO-3 precursor + H2O
SUMO-3 + Val-Pro-Glu-Ser-Ser-Leu-Ala-Gly-His-Ser-Phe
Substrates: 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
Products: -
Products: -
?
SUMO-Elk-1 conjugate + H2O
SUMO + Elk-1
Substrates: SENP1 participates in the dynamic regulation of Elk-1 SUMOylation
Products: -
Products: -
?
SUMO-GATA 1 conjugate + H2O
SUMO + GATA1
Substrates: SENP1 promotes GATA1 activation and subsequent erythropoiesis by deSUMOylating GATA1
Products: -
Products: -
?
SUMO-p53 + H2O
SUMO + p53
Substrates: SENP1 promotes cell proliferation by negatively regulating p53 activity
Products: -
Products: -
?
SUMO-STAT3 protein conjugate + H2O
SUMO + STAT3 protein
Substrates: -
Products: -
Products: -
?
SUMO1ylated protein + H2O
SUMO1 + protein
-
Substrates: main substrate
Products: -
Products: -
?
SUMO-hypoxia-inducible factor 1 conjugate + H2O
SUMO + hypoxia-inducible factor 1
Substrates: -
Products: -
Products: -
?
SUMO-hypoxia-inducible factor 1 conjugate + H2O
SUMO + hypoxia-inducible factor 1
Substrates: deSUMOylation plays a critical role in prostate pathogenesis through induction of HIF1alpha-dependent angiogenesis and enhanced cell proliferation
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme USPL1 neither binds nor cleaves ubiquitin, but is a potent SUMO isopeptidase both in vitro and in cells
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme USPL1 neither binds nor cleaves ubiquitin, but is a potent SUMO isopeptidase both in vitro and in cells
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme SUMO protease removes SUMO conjugate from proteins
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
the enzyme effectively removes SUMO-1 moiety, in the presence of Ca2+ rather than Mn2+, from the sumoylated homeodomain-interacting protein kinase 2 conjugate
Mn2+
the enzyme effectively removes SUMO-1 moiety, in the presence of Ca2+ rather than Mn2+, from the sumoylated homeodomain-interacting protein kinase 2 conjugate
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2-oxo-1,2-dihydropyridin-4-yl)methyl 3-[[(1H-indol-5-yl)oxy]methyl]-1-(methanesulfonyl)-1H-indole-5-carboxylate
-
(2Z)-3-(naphthalen-2-yl)-N-[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]prop-2-enamide
-
-
(6-cyano-2-oxo-1,2-dihydropyridin-4-yl)methyl 3-[[(1H-indol-5-yl)oxy]methyl]-1-(methanesulfonyl)-1H-indole-5-carboxylate
-
(S)-N-(1-benzylethyl)-3beta-hydroxyurs-12-en-28-carboxamide
0.002 mM, 23.2% inhibition ratio
1'-octanoyl-1',4'-dihydro-3'H-spiro[cyclopentane-1,2'-quinoxalin]-3'-one
-
1'-[(4-benzyl-1H-1,2,3-triazol-1-yl)acetyl]-1',4'-dihydro-3'H-spiro[cyclopentane-1,2'-quinoxalin]-3'-one
-
1'-[(4-cyclohexyl-1H-1,2,3-triazol-1-yl)acetyl]-1',4'-dihydro-3'H-spiro[cyclopentane-1,2'-quinoxalin]-3'-one
-
1'-[(4-phenyl-1H-1,2,3-triazol-1-yl)acetyl]-1',4'-dihydro-3'H-spiro[cyclopentane-1,2'-quinoxalin]-3'-one
-
1'-[(5-phenyl-1H-tetrazol-1-yl)acetyl]-1',4'-dihydro-3'H-spiro[cyclopentane-1,2'-quinoxalin]-3'-one
-
1'-[(5-phenyl-2H-tetrazol-2-yl)acetyl]-1',4'-dihydro-3'H-spiro[cyclopentane-1,2'-quinoxalin]-3'-one
-
1'-[(5-phenyl-2H-tetrazol-2-yl)acetyl]-1'H-spiro[cyclopentane-1,2'-thieno[3,4-b]pyrazin]-3'(4'H)-one
-
1'-[3-[3-(but-3-yn-1-yl)-3H-diaziren-3-yl]propanoyl]-1',4'-dihydro-3'H-spiro[cyclopentane-1,2'-quinoxalin]-3'-one
-
1'-[[4-(4-methoxyphenyl)-1H-1,2,3-triazol-1-yl]acetyl]-1',4'-dihydro-3'H-spiro[cyclopentane-1,2'-quinoxalin]-3'-one
-
1'H-spiro[cyclohexane-1,2'-thieno[3,4-b]pyrazin]-3'(4'H)-one
with cyclopentane (1/1)
-
1'H-spiro[cyclopentane-1,2'-thieno[3,4-b]pyrazin]-3'(4'H)-one
with cyclopentane (1/1)
-
1-(1H-indol-3-ylmethyl)-3-[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]urea
-
3% inhibition at 0.02 mM
1-(3-hydroxy-4-methylphenyl)-3-[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]urea
-
5% inhibition at 0.02 mM
1-(5-aminopentyl)-3-[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]urea
-
43% inhibition at 0.02 mM
1-(cyclohexylmethyl)-3-[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]urea
-
5% inhibition at 0.02 mM
1-(naphthalen-2-ylmethyl)-3-[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]urea
-
26% inhibition at 0.02 mM
1-naphthalen-1-yl-3-[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]urea
-
7% inhibition at 0.02 mM
1-naphthalen-2-yl-3-[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]urea
-
30% inhibition at 0.02 mM
1-[2-(1H-indol-3-yl)ethyl]-3-[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]urea
-
24% inhibition at 0.02 mM
1-[2-(naphthalen-2-yl)ethyl]-3-[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]urea
-
45% inhibition at 0.02 mM
2-(3-oxopiperazin-1-yl)ethyl 3beta-hydroxyurs-12-en-28-oate
0.002 mM, 78.4% inhibition ratio
2-(4-chlorophenyl)-2-oxoethyl 3-[[3-(benzyloxy)benzamido]methyl]benzoate
-
2-(4-methylpiperazin-1-yl)ethyl 3beta-hydroxyurs-12-en-28-oate
0.002 mM, 18.1% inhibition ratio
2-(methylamino)-2-oxoethyl 3beta-hydroxyurs-12-en-28-oate
0.002 mM, 35.5% inhibition ratio
2-(morpholin-4-yl)ethyl 3beta-hydroxyurs-12-en-28-oate
0.002 mM, 12.5% inhibition ratio
2-(piperazin-1-yl)ethyl 3beta-hydroxyurs-12-en-28-oate
0.002 mM, 24.4% inhibition ratio
2-(piperidin-1-yl)ethyl 3beta-hydroxyurs-12-en-28-oate
0.002 mM, 4.7% inhibition ratio
2-bromoethyl 3beta-hydroxyurs-12-en-28-oate
0.002 mM, 10.8% inhibition ratio
2-hydroxyethyl 3beta-hydroxyurs-12-en-28-oate
0.002 mM, 14.8% inhibition ratio
2-methoxy-2-oxoethyl 3beta-hydroxyurs-12-en-28-oate
0.002 mM, 7.9% inhibition ratio
2-tert-butoxy-2-oxoethyl 3beta-hydroxyurs-12-en-28-oate
0.002 mM, 10.7% inhibition ratio
2-[(2-hydroxyethyl)(methyl)amino]-2-oxoethyl 3beta-hydroxyurs-12-en-28-oate
0.002 mM, 91.9% inhibition ratio
2-[(2-hydroxyethyl)amino]-2-oxoethyl 3beta-hydroxyurs-12-en-28-oate
0.002 mM, above 100% inhibition ratio
2-[(2S)-2-(methoxycarbonyl)pyrrolidin-1-yl]ethyl 3beta-hydroxyurs-12-en-28-oate
0.002 mM, 10.4% inhibition ratio
2-[(tert-butoxycarbonyl)amino]ethyl 3beta-hydroxyurs-12-en-28-oate
0.002 mM, above 100% inhibition ratio
2-[4-(2-hydroxyethyl)piperazin-1-yl]ethyl 3beta-hydroxyurs-12-en-28-oate
0.002 mM, 25.8% inhibition ratio
2-[4-[3-(trifluoromethyl)phenyl]piperazin-1-yl]ethyl 3beta-hydroxyurs-12-en-28-oate
0.002 mM, 49.2% inhibition ratio
28-amino-28-oxours-12-en-3beta-yl acetate
0.002 mM, 29.8% inhibition ratio
28-oxo-28-[[(1R)-1-phenylethyl]amino]urs-12-en-3beta-yl acetate
0.002 mM, 24.3% inhibition ratio
28-[(2-bromoethyl)amino]-28-oxours-12-en-3beta-yl acetate
0.002 mM, 3.6% inhibition ratio
3,3-dimethyl-4-[(5-phenyl-2H-tetrazol-2-yl)acetyl]-3,4-dihydroquinoxalin-2(1H)-one
-
3-([1-[2-oxo-2-(3'-oxo-3',4'-dihydro-1'H-spiro[cyclopentane-1,2'-quinoxalin]-1'-yl)ethyl]-1H-1,2,3-triazol-4-yl]methyl)benzoic acid
-
3-[(acetyloxy)amino]-N-[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]benzamide
-
-
3-[(benzyloxy)amino]-N-[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]benzamide
-
-
3-[[(1H-indol-5-yl)oxy]methyl]-1-(methanesulfonyl)-N-[[6-(methylcarbamoyl)-2-oxo-1,2-dihydropyridin-4-yl]methyl]-1H-indole-5-carboxamide
-
3beta-(acetyloxy)urs-12-en-28-oic acid
0.002 mM, 27.8% inhibition ratio; 0.002 mM, 3.7% inhibition ratio
4-(morpholin-4-yl)butyl 3beta-hydroxyurs-12-en-28-oate
0.002 mM, 4.3% inhibition ratio
4-(piperazin-1-yl)butyl 3beta-hydroxyurs-12-en-28-oate
0.002 mM, 4.7% inhibition ratio
4-bromobutyl 3beta-hydroxyurs-12-en-28-oate
0.002 mM, 4.4% inhibition ratio
4-methyl-N-[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]benzenesulfonamide
-
17% inhibition at 0.02 mM
4-[(benzyloxy)amino]-N-[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]benzamide
-
-
5'-methoxy-1',4'-dihydro-3'H-spiro[cyclopentane-1,2'-quinoxalin]-3'-one
with cyclopentane (1/1)
-
6'-nitro-1',4'-dihydro-3'H-spiro[cyclopentane-1,2'-quinoxalin]-3'-one
with cyclopentane (1/1)
-
7'-methoxy-1',4'-dihydro-3'H-spiro[cyclopentane-1,2'-quinoxalin]-3'-one
with cyclopentane (1/1)
-
benzyl (3-[[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]carbamoyl]phenyl)carbamate
-
-
benzyl (4-[[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]carbamoyl]phenyl)carbamate
-
-
benzyl [4-(2-oxo-2-[[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]amino]ethoxy)phenyl]carbamate
-
23% inhibition at 0.02 mM
gallic acid
gallic acid acts as a potential inhibitor of SENP1 by interacting directly with the active site of SENP1 thereby decreasing the SUMO binding and the catalytic activity of SENP1. Inhibition of SUMO binding using gallic acid can be an effective strategy for the therapeutic intervention of cancer
methyl 3'-oxo-3',4'-dihydro-1'H-spiro[cyclopentane-1,2'-quinoxaline]-5'-carboxylate
with cyclopentane (1/1)
-
methyl 3'-oxo-3',4'-dihydro-1'H-spiro[cyclopentane-1,2'-quinoxaline]-6'-carboxylate
with cyclopentane (1/1)
-
methyl 3beta-(formyloxy)urs-12-en-28-oate
0.002 mM, above 100% inhibition ratio
methyl 4-([1-[2-oxo-2-(3'-oxo-3',4'-dihydro-1'H-spiro[cyclopentane-1,2'-quinoxalin]-1'-yl)ethyl]-1H-1,2,3-triazol-4-yl]methyl)benzoate
-
N-(2-bromoethyl)-3beta-hydroxyurs-12-en-28-carboxamide
0.002 mM, 90.6% inhibition ratio
N-(2-carboxyethyl)-3beta-hydroxyurs-12-en-28-carboxamide
0.002 mM, 75.5% inhibition ratio
N-(3beta-acetoxyurs-12-en-28-oyl)-2-methoxycarbonylpyrrolidine
0.002 mM, 29.5% inhibition ratio
N-(3beta-hydroxyurs-12-en-28-oyl)-2-carboxymethyl pyrrolidine
0.002 mM, 36.0% inhibition ratio
N-(carbamoylmethyl)-3beta-acetoxyurs-12-en-28-carboxamide
0.002 mM, 4.7% inhibition ratio
N-(carbamoylmethyl)-3beta-hydroxyurs-12-en-28-carboxamide
0.002 mM, 75.0% inhibition ratio
N-(carboxymethyl)-3beta-acetoxyurs-12-en-28-carboxamide
0.002 mM, 29.3% inhibition ratio
N-(carboxymethyl)-3beta-hydroxyurs-12-en-28-carboxamide
0.002 mM, above 100% inhibition ratio
N-(carboxymethyl)-N-methyl-3beta-hydroxyurs-12-en-28-carboxamide
0.002 mM, 39.1% inhibition ratio
N-(methoxycarbonylmethyl)-3beta-acetoxyurs-12-en-28-carboxamide
0.002 mM, 9.9% inhibition ratio
N-(methoxycarbonylmethyl)-N-methyl-3beta-acetoxyurs-12-en-28-carboxamide
0.002 mM, 17.7% inhibition ratio
N-(N-methylcarbamoylmethyl)-3beta-acetoxyurs-12-en-28-carboxamide
0.002 mM, 60.0% inhibition ratio
N-(N-methylcarbamoylmethyl)-3beta-hydroxyurs-12-en-28-carboxamide
0.002 mM, above 100% inhibition ratio
N-(N-methylcarbamoylmethyl)-N-methyl-3beta-acetoxyurs-12-en-28-carboxamide
0.002 mM, 10.1% inhibition ratio
N-(N-methylcarbamoylmethyl)-N-methyl-3beta-hydroxyurs-12-en-28-carboxamide
0.002 mM, 35.9% inhibition ratio
N-[2-(methoxycarbonyl)ethyl]-3beta-acetoxyurs-12-en-28-carboxamide
0.002 mM, 6.9% inhibition ratio
N-[2-(N-methylcarbamoyl)ethyl]-3beta-hydroxyurs-12-en-28-carboxamide
0.002 mM, above 100% inhibition ratio
N-[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]pyridine-2-carboxamide
-
7% inhibition at 0.02 mM
N-[N,N-bis(2-hydroxyethyl)carbamoylmethyl]-3beta-hydroxyurs-12-en-28-carboxamide
0.002 mM, 3.5% inhibition ratio
N-[N-(2,3-dihydroxypropyl)carbamoylmethyl]-3beta-hydroxyurs-12-en-28-carboxamide
0.002 mM, 41.8% inhibition ratio
N-[N-(2-hydroxyethyl)-N-methyl-carbamoylmethyl]-3beta-hydroxyurs-12-en-28-carboxamide
0.002 mM, above 100% inhibition ratio
N-[N-(2-hydroxyethyl)carbamoylmethyl]-3beta-hydroxyurs-12-en-28-carboxamide
0.002 mM, 19.2% inhibition ratio
naphthalen-2-yl [2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]sulfamate
-
-
phenyl [2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]carbamate
-
-
phenyl [[1-(2-hydroxyethyl)-2-oxo-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]carbamoyl]carbamate
-
-
phenyl [[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]carbamoyl]carbamate
-
-
phenyl [[2-oxo-1-(4-oxobutyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]carbamoyl]carbamate
-
-
SUMO-1-GG
product inhibition, competitive, inhibits cleavage of the SUMO-1 precursor, SUMO-2 precursor, (SUMO-1)-RanGAP1 conjugate and (SUMO-2)-RanGAP1 conjugate
-
SUMO-2-GG
product inhibition, competitive, inhibits cleavage of the SUMO-1 precursor, SUMO-2 precursor, (SUMO-1)-RanGAP1 conjugate and (SUMO-2)-RanGAP1 conjugate
-
tert-butyl [3-([[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]carbamoyl]amino)propyl]carbamate
-
4% inhibition at 0.02 mM
[(3beta-hydroxy-28-oxours-12-en-28-yl)oxy]acetic acid
0.002 mM, 67.3% inhibition ratio
[1-(tert-butoxycarbonyl)piperidin-4-yl]methyl 3beta-hydroxyurs-12-en-28-oate
0.002 mM, 3.9% inhibition ratio
[6-(methylcarbamoyl)-2-oxo-1,2-dihydropyridin-4-yl]methyl 3-[[(1H-indol-5-yl)oxy]methyl]-1-(methanesulfonyl)-1H-indole-5-carboxylate
-
haemagglutinin-SUMO-vinylmethylester
-
a suicide inhibitor, Strep-TEV-HA-SUMO-vinylmethylester
-
haemagglutinin-SUMO-vinylmethylester
a suicide inhibitor, Strep-TEV-HA-SUMO-vinylmethylester. Enzyme USPL1 requires its catalytic cysteine to react with the inhibitor
-
additional information
-
design, synthesis, and biological evaluation of benzodiazepine-based SUMO-specific protease 1 inhibitors, structureactivity relationship, overview
-
additional information
-
2-(4-chlorophenyl)-2-oxoethyl 4-benzamidobenzoate derivatives, evaluation of a class of SENP1 inhibitors by virtual screening, synthesis and biological evaluation, structure-activity relationship, overview
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
desumoylation is enhanced either by the forced translocation of SENP1 into the nucleus or by the SENP1 NES (nuclear export sequence) mutant
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Astrocytoma
Inhibition of SUMO-specific protease 1 induces apoptosis of astroglioma cells by regulating NF-?B/Akt pathways.
Breast Neoplasms
Exploring the association between genetic variation in the SUMO isopeptidase gene USPL1 and breast cancer through integration of data from the population-based GENICA study and external genetic databases.
Burkitt Lymphoma
Down-regulation of SENP1 Expression Increases Apoptosis of Burkitt Lymphoma Cells.
Carcinogenesis
Melatonin downregulates nuclear receptor RZR/ROR? expression causing growth-inhibitory and anti-angiogenesis activity in human gastric cancer cells in vitro and in vivo.
Colonic Neoplasms
SUMO-specific protease 1 regulates the in vitro and in vivo growth of colon cancer cells with the upregulated expression of CDK inhibitors.
Colorectal Neoplasms
MiR-133a-3p Targets SUMO-Specific Protease 1 to Inhibit Cell Proliferation and Cell Cycle Progress in Colorectal Cancer.
Heart Failure
Astragaloside IV alleviates heart failure by regulating SUMO-specific protease 1.
Keloid
Sumoylation enhances the activity of the TGF-?/SMAD and HIF-1 signaling pathways in keloids.
Leukemia
Deficiency of SUMO-specific protease 1 induces arsenic trioxide-mediated apoptosis by regulating XBP1 activity in human acute promyelocytic leukemia.
Leukemia, Promyelocytic, Acute
Deficiency of SUMO-specific protease 1 induces arsenic trioxide-mediated apoptosis by regulating XBP1 activity in human acute promyelocytic leukemia.
Lung Neoplasms
Up-regulation of microRNA-138 induce radiosensitization in lung cancer cells.
Neoplasm Metastasis
SUMO-specific protease 1 promotes prostate cancer progression and metastasis.
Neoplasms
Exploring the association between genetic variation in the SUMO isopeptidase gene USPL1 and breast cancer through integration of data from the population-based GENICA study and external genetic databases.
Neoplasms
Inhibition of SUMO-specific protease 1 induces apoptosis of astroglioma cells by regulating NF-?B/Akt pathways.
Neoplasms
SENP1 promotes proliferation of clear cell renal cell carcinoma through activation of glycolysis.
Neoplasms
Vialinin A and thelephantin G, potent inhibitors of tumor necrosis factor-? production, inhibit sentrin/SUMO-specific protease 1 enzymatic activity.
Osteosarcoma
Plasma Exosome-Derived Sentrin SUMO-Specific Protease 1: A Prognostic Biomarker in Patients With Osteosarcoma.
Pancreatic Neoplasms
A cellular and bioinformatics analysis of the SENP1 SUMO isopeptidase in pancreatic cancer.
Pancreatic Neoplasms
SUMO-specific protease 1 regulates pancreatic cancer cell proliferation and invasion by targeting MMP-9.
Prostatic Neoplasms
2-(4-Chlorophenyl)-2-oxoethyl 4-benzamidobenzoate derivatives, a novel class of SENP1 inhibitors: Virtual screening, synthesis and biological evaluation.
Prostatic Neoplasms
Induction of the SUMO-specific protease 1 transcription by the androgen receptor in prostate cancer cells.
Prostatic Neoplasms
Momordin Ic, a new natural SENP1 inhibitor, inhibits prostate cancer cell proliferation.
Prostatic Neoplasms
Prognostic impact of SUMO-specific protease 1 (SENP1) in prostate cancer patients undergoing radical prostatectomy.
Prostatic Neoplasms
Small ubiquitin-like modifier protein-specific protease 1 and prostate cancer.
Prostatic Neoplasms
SUMO-specific protease 1 (SENP1) reverses the hormone-augmented SUMOylation of androgen receptor and modulates gene responses in prostate cancer cells.
Prostatic Neoplasms
SUMO-specific protease 1 promotes prostate cancer progression and metastasis.
Prostatic Neoplasms
Triptolide inhibits the proliferation of prostate cancer cells and down-regulates SUMO-specific protease 1 expression.
Stomach Neoplasms
Melatonin downregulates nuclear receptor RZR/ROR? expression causing growth-inhibitory and anti-angiogenesis activity in human gastric cancer cells in vitro and in vivo.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
enzyme-substrate complex formation kinetics, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.002 - 4
(2-oxo-1,2-dihydropyridin-4-yl)methyl 3-[[(1H-indol-5-yl)oxy]methyl]-1-(methanesulfonyl)-1H-indole-5-carboxylate
0.0218
(2Z)-3-(naphthalen-2-yl)-N-[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]prop-2-enamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0025 - 0.02
(6-cyano-2-oxo-1,2-dihydropyridin-4-yl)methyl 3-[[(1H-indol-5-yl)oxy]methyl]-1-(methanesulfonyl)-1H-indole-5-carboxylate
0.066
1',4'-dihydro-3'H-spiro[cyclobutane-1,2'-quinoxalin]-3'-one
Homo sapiens
pH 7.5, 25°C, substrate SUMO1-7-amido-4-methylcoumarin
0.261
1',4'-dihydro-3'H-spiro[cyclohexane-1,2'-quinoxalin]-3'-one
Homo sapiens
pH 7.5, 25°C, substrate SUMO1-7-amido-4-methylcoumarin
0.051
1',4'-dihydro-3'H-spiro[cyclooctane-1,2'-quinoxalin]-3'-one
Homo sapiens
pH 7.5, 25°C, substrate SUMO1-7-amido-4-methylcoumarin
0.116
1',4'-dihydro-3'H-spiro[cyclopentane-1,2'-quinoxalin]-3'-one
Homo sapiens
pH 7.5, 25°C, substrate SUMO1-7-amido-4-methylcoumarin
0.233
1',4'-dihydro-3'H-spiro[oxane-4,2'-quinoxalin]-3'-one
Homo sapiens
pH 7.5, 25°C, substrate SUMO1-7-amido-4-methylcoumarin
0.081
1',4'-dihydro-3'H-spiro[oxetane-3,2'-quinoxalin]-3'-one
Homo sapiens
pH 7.5, 25°C, substrate SUMO1-7-amido-4-methylcoumarin
0.0066
1'-octanoyl-1',4'-dihydro-3'H-spiro[cyclopentane-1,2'-quinoxalin]-3'-one
Homo sapiens
pH 7.5, 25°C, substrate SUMO1-7-amido-4-methylcoumarin
0.038
1'-[(4-benzyl-1H-1,2,3-triazol-1-yl)acetyl]-1',4'-dihydro-3'H-spiro[cyclopentane-1,2'-quinoxalin]-3'-one
Homo sapiens
pH 7.5, 25°C, substrate SUMO1-7-amido-4-methylcoumarin
0.019
1'-[(4-cyclohexyl-1H-1,2,3-triazol-1-yl)acetyl]-1',4'-dihydro-3'H-spiro[cyclopentane-1,2'-quinoxalin]-3'-one
Homo sapiens
pH 7.5, 25°C, substrate SUMO1-7-amido-4-methylcoumarin
0.023
1'-[(4-phenyl-1H-1,2,3-triazol-1-yl)acetyl]-1',4'-dihydro-3'H-spiro[cyclopentane-1,2'-quinoxalin]-3'-one
Homo sapiens
pH 7.5, 25°C, substrate SUMO1-7-amido-4-methylcoumarin
0.05
1'-[(5-phenyl-1H-tetrazol-1-yl)acetyl]-1',4'-dihydro-3'H-spiro[cyclopentane-1,2'-quinoxalin]-3'-one
Homo sapiens
pH 7.5, 25°C, substrate SUMO1-7-amido-4-methylcoumarin
0.0086
1'-[(5-phenyl-2H-tetrazol-2-yl)acetyl]-1',4'-dihydro-3'H-spiro[cyclopentane-1,2'-quinoxalin]-3'-one
Homo sapiens
pH 7.5, 25°C, substrate SUMO1-7-amido-4-methylcoumarin
0.01
1'-[(5-phenyl-2H-tetrazol-2-yl)acetyl]-1'H-spiro[cyclopentane-1,2'-thieno[3,4-b]pyrazin]-3'(4'H)-one
Homo sapiens
pH 7.5, 25°C, substrate SUMO1-7-amido-4-methylcoumarin
0.024
1'-[3-[3-(but-3-yn-1-yl)-3H-diaziren-3-yl]propanoyl]-1',4'-dihydro-3'H-spiro[cyclopentane-1,2'-quinoxalin]-3'-one
Homo sapiens
pH 7.5, 25°C, substrate SUMO1-7-amido-4-methylcoumarin
0.013
1'-[[4-(4-methoxyphenyl)-1H-1,2,3-triazol-1-yl]acetyl]-1',4'-dihydro-3'H-spiro[cyclopentane-1,2'-quinoxalin]-3'-one
Homo sapiens
pH 7.5, 25°C, substrate SUMO1-7-amido-4-methylcoumarin
0.061
1'H-spiro[cyclohexane-1,2'-thieno[3,4-b]pyrazin]-3'(4'H)-one
Homo sapiens
with cyclopentane (1/1), pH 7.5, 25°C, substrate SUMO1-7-amido-4-methylcoumarin
-
0.037
1'H-spiro[cyclopentane-1,2'-thieno[3,4-b]pyrazin]-3'(4'H)-one
Homo sapiens
with cyclopentane (1/1), pH 7.5, 25°C, substrate SUMO1-7-amido-4-methylcoumarin
-
0.05
2-(4-chlorophenyl)-2-oxoethyl 4-[(3,4-diethoxybenzoyl)amino]benzoate
Homo sapiens
above, pH and temperature not specified in the publication
0.05
2-(4-chlorophenyl)-2-oxoethyl 4-[(3,4-dimethoxybenzoyl)amino]benzoate
Homo sapiens
above, pH and temperature not specified in the publication
0.05
2-(4-chlorophenyl)-2-oxoethyl 4-[(3-aminobenzoyl)amino]benzoate
Homo sapiens
above, pH and temperature not specified in the publication
0.00174
2-(4-chlorophenyl)-2-oxoethyl 4-[(3-fluorobenzoyl)amino]benzoate
Homo sapiens
pH and temperature not specified in the publication
0.05
2-(4-chlorophenyl)-2-oxoethyl 4-[(3-hydroxybenzoyl)amino]benzoate
Homo sapiens
above, pH and temperature not specified in the publication
0.009
2-(4-chlorophenyl)-2-oxoethyl 4-[3-(benzoyloxy)benzamido]benzoate
Homo sapiens
pH 7.5, 25°C, substrate SUMO1-7-amido-4-methylcoumarin
0.00108
2-(4-chlorophenyl)-2-oxoethyl 4-[[3-(benzyloxy)benzoyl]amino]benzoate
Homo sapiens
pH and temperature not specified in the publication
0.0123
3,3-dimethyl-4-[(5-phenyl-2H-tetrazol-2-yl)acetyl]-3,4-dihydroquinoxalin-2(1H)-one
Homo sapiens
pH 7.5, 25°C, substrate SUMO1-7-amido-4-methylcoumarin
0.029
3-([1-[2-oxo-2-(3'-oxo-3',4'-dihydro-1'H-spiro[cyclopentane-1,2'-quinoxalin]-1'-yl)ethyl]-1H-1,2,3-triazol-4-yl]methyl)benzoic acid
Homo sapiens
pH 7.5, 25°C, substrate SUMO1-7-amido-4-methylcoumarin
0.1
3-[(acetyloxy)amino]-N-[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]benzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.1
3-[(benzyloxy)amino]-N-[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]benzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.051
3-[[(1H-indol-5-yl)oxy]methyl]-1-(methanesulfonyl)-N-[[6-(methylcarbamoyl)-2-oxo-1,2-dihydropyridin-4-yl]methyl]-1H-indole-5-carboxamide
0.776
4-[(5-phenyl-2H-tetrazol-2-yl)acetyl]-3,4-dihydroquinoxalin-2(1H)-one
Homo sapiens
pH 7.5, 25°C, substrate SUMO1-7-amido-4-methylcoumarin
0.1
4-[(benzyloxy)amino]-N-[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]benzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.11
5'-methoxy-1',4'-dihydro-3'H-spiro[cyclopentane-1,2'-quinoxalin]-3'-one
Homo sapiens
with cyclopentane (1/1), pH 7.5, 25°C, substrate SUMO1-7-amido-4-methylcoumarin
-
0.067
6'-nitro-1',4'-dihydro-3'H-spiro[cyclopentane-1,2'-quinoxalin]-3'-one
Homo sapiens
with cyclopentane (1/1), pH 7.5, 25°C, substrate SUMO1-7-amido-4-methylcoumarin
-
0.198
7'-methoxy-1',4'-dihydro-3'H-spiro[cyclopentane-1,2'-quinoxalin]-3'-one
Homo sapiens
with cyclopentane (1/1), pH 7.5, 25°C, substrate SUMO1-7-amido-4-methylcoumarin
-
0.0092
benzyl (3-[[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]carbamoyl]phenyl)carbamate
Homo sapiens
-
pH and temperature not specified in the publication
0.0155
benzyl (4-[[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]carbamoyl]phenyl)carbamate
Homo sapiens
-
pH and temperature not specified in the publication
0.061
methyl 3'-oxo-3',4'-dihydro-1'H-spiro[cyclopentane-1,2'-quinoxaline]-5'-carboxylate
Homo sapiens
with cyclopentane (1/1), pH 7.5, 25°C, substrate SUMO1-7-amido-4-methylcoumarin
-
0.202
methyl 3'-oxo-3',4'-dihydro-1'H-spiro[cyclopentane-1,2'-quinoxaline]-6'-carboxylate
Homo sapiens
with cyclopentane (1/1), pH 7.5, 25°C, substrate SUMO1-7-amido-4-methylcoumarin
-
0.0075
methyl 4-([1-[2-oxo-2-(3'-oxo-3',4'-dihydro-1'H-spiro[cyclopentane-1,2'-quinoxalin]-1'-yl)ethyl]-1H-1,2,3-triazol-4-yl]methyl)benzoate
Homo sapiens
pH 7.5, 25°C, substrate SUMO1-7-amido-4-methylcoumarin
0.0212
naphthalen-2-yl [2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]sulfamate
Homo sapiens
-
pH and temperature not specified in the publication
0.1
phenyl [2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]carbamate
Homo sapiens
-
pH and temperature not specified in the publication
0.1
phenyl [[1-(2-hydroxyethyl)-2-oxo-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]carbamoyl]carbamate
Homo sapiens
-
pH and temperature not specified in the publication
0.0272
phenyl [[2-oxo-1-(2-oxoethyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]carbamoyl]carbamate
Homo sapiens
-
pH and temperature not specified in the publication
0.1
phenyl [[2-oxo-1-(4-oxobutyl)-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]carbamoyl]carbamate
Homo sapiens
-
pH and temperature not specified in the publication
0.078
spiro[[1,4]benzoxazine-2,1'-cyclopentan]-3(4H)-one
Homo sapiens
pH 7.5, 25°C, substrate SUMO1-7-amido-4-methylcoumarin
0.013 - 2
[6-(methylcarbamoyl)-2-oxo-1,2-dihydropyridin-4-yl]methyl 3-[[(1H-indol-5-yl)oxy]methyl]-1-(methanesulfonyl)-1H-indole-5-carboxylate
0.002 - 4
(2-oxo-1,2-dihydropyridin-4-yl)methyl 3-[[(1H-indol-5-yl)oxy]methyl]-1-(methanesulfonyl)-1H-indole-5-carboxylate
Homo sapiens
with 0.01% CHAPS, pH and temperature not specified in the publication
0.033
(2-oxo-1,2-dihydropyridin-4-yl)methyl 3-[[(1H-indol-5-yl)oxy]methyl]-1-(methanesulfonyl)-1H-indole-5-carboxylate
Homo sapiens
with 0.1% BSA, pH and temperature not specified in the publication
0.0025
(6-cyano-2-oxo-1,2-dihydropyridin-4-yl)methyl 3-[[(1H-indol-5-yl)oxy]methyl]-1-(methanesulfonyl)-1H-indole-5-carboxylate
Homo sapiens
with 0.01% CHAPS, pH and temperature not specified in the publication
0.02
(6-cyano-2-oxo-1,2-dihydropyridin-4-yl)methyl 3-[[(1H-indol-5-yl)oxy]methyl]-1-(methanesulfonyl)-1H-indole-5-carboxylate
Homo sapiens
with 0.1% BSA, pH and temperature not specified in the publication
0.0056
2-(4-chlorophenyl)-2-oxoethyl 3-[[3-(benzyloxy)benzamido]methyl]benzoate
Homo sapiens
with 0.01% CHAPS, pH and temperature not specified in the publication
0.038
2-(4-chlorophenyl)-2-oxoethyl 3-[[3-(benzyloxy)benzamido]methyl]benzoate
Homo sapiens
with 0.1% BSA, pH and temperature not specified in the publication
0.00118
2-(4-chlorophenyl)-2-oxoethyl 4-(benzoylamino)benzoate
Homo sapiens
pH and temperature not specified in the publication
0.00354
2-(4-chlorophenyl)-2-oxoethyl 4-(benzoylamino)benzoate
Homo sapiens
pH and temperature not specified in the publication
0.00186
2-(4-chlorophenyl)-2-oxoethyl 4-[(3-methoxybenzoyl)amino]benzoate
Homo sapiens
pH and temperature not specified in the publication
0.00239
2-(4-chlorophenyl)-2-oxoethyl 4-[(3-methoxybenzoyl)amino]benzoate
Homo sapiens
pH and temperature not specified in the publication
0.051
3-[[(1H-indol-5-yl)oxy]methyl]-1-(methanesulfonyl)-N-[[6-(methylcarbamoyl)-2-oxo-1,2-dihydropyridin-4-yl]methyl]-1H-indole-5-carboxamide
Homo sapiens
with 0.1% BSA, pH and temperature not specified in the publication
0.051
3-[[(1H-indol-5-yl)oxy]methyl]-1-(methanesulfonyl)-N-[[6-(methylcarbamoyl)-2-oxo-1,2-dihydropyridin-4-yl]methyl]-1H-indole-5-carboxamide
Homo sapiens
with 0.01% CHAPS, pH and temperature not specified in the publication
0.013
[6-(methylcarbamoyl)-2-oxo-1,2-dihydropyridin-4-yl]methyl 3-[[(1H-indol-5-yl)oxy]methyl]-1-(methanesulfonyl)-1H-indole-5-carboxylate
Homo sapiens
with 0.01% CHAPS, pH and temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
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SwissProt
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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enzyme SENP1 levels are positively correlated with substrate Pin1 levels in human breast cancer specimens
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enzyme SENP1 is upregulated in pancreatic ductal adenocarcinoma tissues compared with adjacent normal tissues
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elevation of SENP1 mRNA in prostate cancer cells as compared with normal prostate epithelial cells
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elevation of SENP1 mRNA in prostate cancer cells as compared with normal prostate epithelial cells
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
enzyme USPL1 is a low-abundance protein that colocalizes with coilin in cajal bodies. USPL1 is an essential Cajal body component
brenda
SENP1 is localized in the cytoplasm where it is complexed with an antioxidant protein thioredoxin. Tumor necrosis factor (TNF) induces the release of SENP1 from thioredoxin as well as nuclear translocation of SENP1
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C603S is exclusively nuclear in comparison with the wild-type SENP1, which is consistently present in the cytoplasm, albeit at low steady state levels
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SENP1 shuttles between the cytoplasm and the nucleus. SENP1 contains the nuclear export sequence (NES) within the extreme carboxyl-terminal region, and SENP1 is exported to the cytoplasm in a NES-dependent manner
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SENP1 expresses nuclear export sequences that allow these 2 SENPs to shuttle in and out of the nucleus
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SENP1 is localized in the cytoplasm where it is complexed with an antioxidant protein thioredoxin. Tumor necrosis factor (TNF) induces the release of SENP1 from thioredoxin as well as nuclear translocation of SENP1
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C603S is exclusively nuclear in comparison with the wild-type SENP1, which is consistently present in the cytoplasm, albeit at low steady state levels. Presence of a single nonconsensus nuclear localization signal within the N-terminus of the protein. Residues within the predicted NLS1 region around positions 170-180 are critical for the nuclear localization of SENP1. SENP1 localization may be influenced by the expression of proteins that are targets of SUMO-1 modification, such as HDAC4 and PML, which affects the relative levels and localization of SUMO-1 conjugates within the cell
brenda
SENP1 shuttles between the cytoplasm and the nucleus. SENP1 contains the nuclear export sequence (NES) within the extreme carboxyl-terminal region, and SENP1 is exported to the cytoplasm in a NES-dependent manner. As sumoylations are nuclear events and most SUMO-conjugates are located within the nucleus, it appears that SENP1 might find its cellular targets subsequent to its nuclear relocalization
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the enzyme SENP1 is targeted to kinetochores in mitosis
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Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
evolution
malfunction
physiological function
additional information
drug target
gallic acid acts as a potential inhibitor of SENP1 by interacting directly with the active site of SENP1 thereby decreasing the SUMO binding and the catalytic activity of SENP1. Inhibition of SUMO binding using gallic acid can be an effective strategy for the therapeutic intervention of cancer
drug target
potential approach to treat platinum-resistant ovarian cancer by targeting SENP1/JAK2 pathway
drug target
potential application of SENP1 inhibitors for the treatment of platinum-resistant ovarian cancer patients
drug target
promising target for radiosensitization, inhibiting SENP1 upregulates cancer cell radiosensitivity
drug target
SENP1 is a critical p53 deSUMOylating enzyme and a promising therapeutic target in wild-type p53 containing cancer cells
evolution
USPL1 is a member of the C19 cysteine protease USP family, two families of SUMO isopeptidases are known, and USPL1 represents a third type of SUMO protease. W229, W237, Q405 and H421 are strictly conserved in USPL1 proteins, but different from residues in all other USPs
evolution
-
C13orf22l is a member of the C19 cysteine protease USP family, two families of SUMO isopeptidases are known, and C13orf22l represents a third type of SUMO protease. Zebrafish C13orf22l is a functional homologue of human USPL1
evolution
-
the enzyme belongs to the superfamily of Ubl-specific proteases being Cys proteases. In all SENPs, an aromatic side chain, such as that of Trp or Phe, forms the channel lid. The catalytic Cys residues are located within the closed catalytic channels for binding the C-termini of ubiquitin-likes, and the catalytic residues undergo conformational changes when these proteases form complexes with their substrates. SENP1 is a model system for the Ubl-specific proteases in the Cys protease superfamily because it shares the same biochemical mechanism and its catalytic Cys is similarly buried as those of other Ubl-specific proteases. The mode of substrate recognition and binding of SENP1 may be shared by other de-Ubl enzymes
malfunction
creation of SENP1 knockout mice based on a Cre-loxP system. Global deletion of SENP1 causes anemia and embryonic lethality between embryonic day 13.5 and postnatal day 1, correlating with erythropoiesis defects in the fetal liver
malfunction
SENP1 knockdown impairs exocytosis at stimulatory glucose levels and blunts glucose-dependent insulin secretion from mouse and human islets. SENP1 overexpression also disrupts the association of SUMO1 with synaptotagmin VII and mimics the effect of glucose to enhance exocytosis
malfunction
-
knockdown of SENP1 by SENP1-siRNA inhibits pancreatic cancer cell proliferation, migration, and invasion. Silencing of SENP1 results in downregulation of MMP-9, which is pivotal for PDAC cell growth and migration
malfunction
enzyme USPL1 depletion does not affect global sumoylation, but causes striking coilin mislocalization and impairs cell proliferation, functions that are not dependent on USPL1 catalytic activity
malfunction
-
many cells of enzyme heterozygous mutants c13orf22lhi3662Tg/hi3662Tg reveal a striking accumulation of coilin in nucleoli. Enzyme disruption is lethal to the embryo in zebrafish with strong necrotic phenotype in the central nervous system and eye at 2 days post fertilization and death at 4-5 days post fertilization
malfunction
-
the enzyme SENP1 inhibition by siRNA significantly suppresses neuroblastoma cell migration and invasion, overexpression of SENP1 promotes neuroblastoma cells migration and invasion
malfunction
-
inhibition of endogenous enzyme SENP1 via the SENP1 dominant-negative mutant or shRNA-induced Pin1 SUMOylation in vivo. Knockdown of endogenous enzyme SENP1 expression also reduces Pin1-mediated cyclin D1 activation and again the enhanced ability of Pin1K6/63R to activate the cyclin D1 promoter is not reduced by enzyme SENP1
malfunction
defects in adipocyte differentiation as well as PPARgamma expression in Senp1-/- mouse embryonic fibroblast cells induced by adipogenic stimuli. Deficiency in SUMOylation reduces Sharp-1 suppression of adipogenesis
malfunction
RNA interference-mediated knockdown of SENP1 delays sister chromatid separation at metaphase
malfunction
-
embryos homozygous for this mutant allele, Senp1M1Mku show phenotypic abnormalities beginning at embryonic day (E) 11.5 with the majority dying between E12.5 and E14.5. Enzyme defects lead to accumulation of Sumo1-modified proteins in homozygous embryos, a lethal process, phenotypes, overview. Senp1Gt mutants express a truncated Senp1 affecting Sumo2/3 levels
malfunction
-
differential localization of nucleoporins upon codepletion of SENP1 and SENP2 in HeLa cells, immunohistochemic analysis, overview
malfunction
-
specifically, either RNAi depletion of SENP1/SENP2 or expression of dominantly interfering mutants of these proteins results in increased sumoylation of endogenous Nup153. Catalytically inactive SENP1 maintains specific attributes, although it has enhanced interaction with sumoylated Nup153, overview. Truncated SENP1CD is modified by both SUMO1 and SUMO2
malfunction
acute lymphoblastic leukemia (ALL) cells knocking down SENP1 display compromised growth rather than significant alterations in chemosensitivity. Camptothecin derivatives 7-ethylcamptothecin and topotecan induce specific SENP1 reduction and severe apoptosis of ALL cells, showing strong anticancer effects against ALL. SENP1 could attenuate this inhibitory effect by targeting DNA topoisomerase I (TOP1) for de-SUMOylation, indicating that specific reduction in SENP1 induced by 7-ethylcamptothecin and/or topotecan inhibits the proliferation of ALL cells
malfunction
selective ablation of SENP1 in germinal center B cells results in impaired germinal center dark and light zone organization and reduced IgG1-switched germinal center B cells, leading to diminished production of class-switched antibodies with high-affinity in response to a TD antigen challenge
malfunction
SENP1 deficiency promotes ferroptosis and inhibites tumor progression through reducing SUMOylation of ACSL4
malfunction
SENP1 deficiency in myeloid cells promotes myeloid-derived suppressor cell (MDSC) expansion in bone marrow, spleen, and other organs. Senp1-/- myeloid-derived suppressor cells show stronger immunosuppressive activity than Senp1+/+ myeloid-derived suppressor cells. No defects in the differentiation of myeloid precursor cell are observed in Senp1-/- mice. Mechanistically, SENP1-mediated regulation of MDSC is dependent on STAT3 signaling. CD45 is a specific STAT3 phosphatase in MDSC. CD45 is SUMOylated in MDSC and SENP1 can deconjugate SUMOylated CD45. In Senp1-/- MDSC, CD45 is highly SUMOylated, which reduces its phosphatase activity toward STAT3, leading to STAT3-mediated MDSC development and function
malfunction
SENP1 deficiency in germinal center B cells leads to compromised humoral immune response
physiological function
-
abrogation of elevated SENP1 mRNA in prostate cancer cells significantly decreases androgen-mediated cell growth. Increased SENP1 expression directly modulates androgen receptor-dependent cell proliferation and transcription, SENP1 could play an important role in prostate carcinogenesis
physiological function
mediates TNF-induced desumoylation and cytoplasmic translocation of HIPK1 to enhance apoptosis signal-regulating kinase-1-dependent apoptosis
physiological function
-
modification of proteins by small ubiquitin-like modifier (SUMO) plays an important role in the function, compartmentalization, and stability of target proteins, contributing to the regulation of diverse processes. SUMO-1 modification can be regulated not only at the level of conjugation, it may also be reversed by a class of proteases known as the SUMO-specific proteases
physiological function
-
SENP1, can transform normal prostate epithelia to a dysplasic state and directly modulate several oncogenic pathways in prostate cells, including AR, c-Jun, and Cyclin D1
physiological function
SENP1, is required for glucose-dependent insulin secretion. SUMOylation acutely regulates insulin secretion by the direct and reversible inhibition of beta-cell exocytosis in response to intracellular Ca(2+) elevation
physiological function
may be required for proliferation of normal human cells
physiological function
SENP1 can regulate that androgen receptor-dependent transcription through desumoylation of histone deacetylase
physiological function
SENP1 reverses the ligand-induced SUMOylation of androgen receptor and helps fine tune the cellular responses to androgens in a target promoter-selective manner. SENP1 stimulates the activity of holo-androgen receptor on compound androgen response element-containing promoters. The effects of SENP1 on androgen receptor dependent transcription are dependent on catalytic activity and require intact SUMO acceptor sites in androgen receptor, indicating that their coactivating effects are mainly due to their direct isopeptidase activity on holo-androgen receptor
physiological function
SENP1 plays a key role in the regulation of the hypoxic response through regulation of HIF1alpha stability and SUMOylation can serve as a direct signal for ubiquitin-dependent degradation
physiological function
-
the enzyme SENP1 is involved in deconjugation of proteins, such as the androgen receptor, from small ubiquitin modifier, SUMO, proteins, a dynammic and reversible posttranslational modification. The enzyme is essential to cadmium-induced enhancement of androgen receptor activity
physiological function
-
SUMO-specific protease 1 regulates pancreatic cancer cell proliferation and invasion by targeting MMP-9. Enzyme SENP1 is positively associated with lymph node metastasis and TNM stage
physiological function
USPL1 is an essential Cajal body protein required for coilin localization and cell proliferation. USPL1 represents a third type of SUMO protease, with essential functions in Cajal body biology. The conserved areas in USPL1 might be involved in SUMO recognition
physiological function
-
C13orf22l is required for integrity of Cajal bodies in zebrafish embryos
physiological function
-
the SUMO protease SENP1 regulates cell migration and invasion in neuroblastoma and can regulate the expression of CDH1, MMP9 and MMP2, overview. SUMO proteases remove SUMO, i.e. small ubiquitin-like modifier, conjugate from proteins, and their expression is deregulated in diverse cancers. SUMOylation and deSUMOylation are dynamic mechanisms regulating a spectrum of protein activities
physiological function
-
the enzyme plays an important role in the occurrence and development of prostate cancer
physiological function
-
Pin1 is SUMOylated on Lys6 in the WW domain and on Lys63 in the PPIase domain. Pin1 SUMOylation inhibits its protein activity and oncogenic function, the enzyme removes the SUMO conjugates and activates Pin1 promoting the ability of Pin1 to induce centrosome amplification and cell transformation, overview. Enzyme SENP1 also increases Pin1 protein stability in cell cultures, and Pin1 levels are positively correlated with SENP1 levels in human breast cancer specimens. Pin1 SUMOylation on Lys6/63 as a distinct mechanism to inhibit its activity and function but also identify a critical role for SENP1-mediated deSUMOylation in promoting Pin1 function during tumorigenesis
physiological function
the enzyme controls adipocyte differentiation. Adipocyte differentiation is regulated by a transcriptional cascade that mainly includes CCAAT/enhancer-binding protein family members and the nuclear receptor peroxisome proliferator-activated receptor gamma, PPARgamma. SENP1 is a specific de-SUMOylation protease for Sharp-1, a repressor for PPARgamma transcription and adipogenesis. SENP1 enhances adipogenesis through de-SUMOylation of Sharp-1, which then releases Sharp-1 repression of PPARgamma expression and adipocyte differentiation
physiological function
enzyme SENP1 is an important mediator of precise spatial and temporal control of sumoylation in mitosis required for chromosome segregation
physiological function
-
enzyme SENP1 plays a key role in tumor angiogenesis, because it regulates the stability of hypoxia-inducible factor 1alpha, which is a key player in the formation of new blood vessels to support tumor growth. It is highly expressed in human prostate cancer specimens and regulates androgen receptor activities The enzyme is responsible for processing small ubiquitin-like modifier, SUMO
physiological function
-
enzyme Senp1 is essential for desumoylating Sumo1-modified proteins but dispensable for Sumo2 and Sumo3 deconjugation in the mouse embryo, overview. Senp1 is the primary activity for desumoylation of Sumo1-modified proteins
physiological function
-
SENP1 is a specific protease to regulate the SUMOylation status of peroxisome proliferator-activated receptor coactivator 1alpha, i.e. PGC-1alpha. The enzyme SENP1 also promotes PGC-1alpha transcription activity, which is essential for the expression of mitochondrial genes and subsequently mitochondrial biogenesis. SENP1 is essential for expression of nuclear mitochondrial genes
physiological function
-
SENP1, as well as SENP2, regulates the proper localization of nucleoporins, overview. The enzyme interacts with the nucleoporin Nup153 via a dual interface that includes a bridging interaction with the soluble transport receptor importin beta and a SUMO-mediated mechanism. SENP1 and SENP2 are not required for localization of the transmembrane proteins nucleoporin POM121 and inner nuclear envelope protein Sun1 or expansion of the interphase nuclear envelope
physiological function
-
the SUMO proteases play roles both in processing SUMO during the biogenesis of this peptide moiety and also in reversing SUMO modification on specific targets to control the activities conferred by this posttranslational modification. Specificity of the role for SENP1 and SENP2 in maintaining desumoylation of Nup153
physiological function
transient middle cerebral artery occlusion in mice followed by 6, 12 and 24 h reperfusion significantly enhances SENP1 levels in the affected brain area, independent of transcription. The levels of SUMO1-conjugated proteins are decreased by schemia/reperfusion in cortical neurons of control littermate mice, but unchanged in that of animals with conditional ablation of SENP1 gene from adult principal neurons. The SENP1 cKO mice exhibit a significant increase in infarct volume in the cerebral cortex and more severe motor impairment in response to schemia/reperfusion as compared with the control littermates. Cortical neurons from schemia/reperfusion-injured SENP1 cKO mice become more apoptotic than that from control littermates. Overexpression of SENP1 in somatosensory cortices of adult wild-type (WT) mice suppresses schemia/reperfusion-induced neuronal apoptosis
physiological function
-
silencing of SENP1 promotes cellular apoptosis, and inhibits proliferation and migration of PC-3M cells. SENP1 silencing increases the SMAD4 expression at protein level, upregulates E-cadherin and downregulates vimentin expression. SMAD4 interference abolishes SENP1-mediated upregulation of E-cadherin. SENP1 overexpression in LNCaP cells reduces SMAD4 protein, and promotes epithelial mesenchymal transition via decreasing E-cadherin and increasing vimentin
physiological function
SENP1 physically interacts with the chromatin remodeler chromodomain helicase DNA-binding protein CHD3. CHD3-and SENP1-KO cells reveal a large degree of overlap in differential chromatin openness between these two mutant cell lines. CHD3 and SENP1 may associate with CCCTC-binding factor (CTCF) and SUMOylated chromatin-associated factors. SENP1 and CHD3 proteins co-regulate the expression of several genes
physiological function
an enrichment of inflammation signatures is observed in HUVECs with SENP1 3'-untranslated region (3'UTR) overexpression which is positively correlated with TGFBR2 signaling pathway. TGFBR2 is competing endogenous RNA target of SENP1 and the downstream effectors Smad2/3 are also overexpressed in HUVECs with SENP1 3'UTR overexpression. Injection of SENP1 siRNA following LPS treatment attenuates lipopolysaccharide-induced sepsis. TGFBR2 overexpression partially abrogates SENP1 siRNA-mediated inhibition on lipopolysaccharide-induced sepsis
physiological function
SENP1 regulates the development and function of myeloid-derived suppressor cells. SENP1 deficiency in myeloid cells promotes myeloid-derived suppressor cell expansion in bone marrow, spleen, and other organs. Senp1-/- myeloid-derived suppressor cell show stronger immunosuppressive activity than Senp1+/+ myeloid-derived suppressor cells. No defects in the differentiation of myeloid precursor cells are observed in Senp1-/- mice. SENP1-mediated regulation of myeloid-derived suppressor cell is dependent on STAT3 signaling. CD45 is SUMOylated in myeloid-derived suppressor cells and SENP1 can deconjugate SUMOylated CD45
physiological function
SENP1 plays an essential role in many diseases such as cardiovascular disease, diabetes and cancer via targeting GATA2, NEMO, Pin1, SMAD4 and HIF-1a for deSUMOylation
physiological function
SENP1 promotes cell proliferation by negatively regulating p53 activity. SENP1 deSUMOylates a variety of target proteins and plays critical roles in diverse cellular processes, including cell cycle, transcription, metabolism, DNA repair, immune response and hypoxia response, and is essential for animal development
physiological function
SENP1 is required for the production of high-affinity class-switched IgG1 antibody. SENP1 controls the Paired box protein 5 (PAX5) protein level through deSUMOylation, leading to increased expression of activation-induced cytidine deaminase (AID). Thus, this study highlights the important role of SUMOylation as a unique regulatory mechanism to control GC B cell response
physiological function
-
SENP1 facilitates olfactory mucosa mesenchymal stem cells (OM-MSC) differentiation through activating optineurin(OPTN)-mediated mitophagy to mitigate the neurologic impairment following intracerebral hemorrhage
physiological function
SENP1 inhibits ferroptosis and promotes head and neck squamous cell carcinoma by regulating ACSL4 protein stability via SUMO1. SENP1 is an oncogene with a key role in progression of HNSCC and ferroptosis. SENP1 decreases the stability of ACSL4 protein through deSUMOylation and indirectly inhibits its influence on phospholipid metabolic pathways downstream of ferroptosis
physiological function
the enzyme is involved in the maturation of SUMOs and the deconjugation of SUMOs from their substrate proteins. SENP1 deSUMOylates and stabilizes hypoxia-inducible factor 1 during hypoxia
physiological function
SENP1 controls JAK2 function by regulating its cellular localization via deSUMOylation, and deSUMOylation of JAK2 by SENP1 indirectly regulates JAK2/STAT signaling pathway by shuttling JAK2 between cytoplasm and nucleus. Elevated expression level of SENP1 promotes cytoplasmic accumulation of JAK2, resulting in the activation of JAK2/STAT pathway. Activated JAK2/STAT/anti-apoptosis signaling leads to platinum.resistance in ovarian cancer cells. The SENP1/JAK2 axis is activated in platinum-resistant ovarian cancer in a manner dependent on a transcription factor RUNX2 and activated RUNX2/SENP1/JAK2 is critical for platinum-resistance in ovarian cancer
physiological function
SENP1 is the main specific isopeptidase to catalyze deSUMOylation modification. SUMOylation and deSUMOylation plays an important role in DNA damage response and the formation of radiotherapy resistance
physiological function
the enzyme is critical for myeloid-derived suppressor cell development and function. Suppressive function of SENP1 in modulating MDSC expansion and function via CD45-STAT3 signaling axis
physiological function
SENP1 serves a central role in inhibiting cardiac hypertrophy and cardiac dysfunction
physiological function
SENP1 may be important to metastatic progression and the development of drug-resistant clear cell renal cell carcinoma
physiological function
the enzyme is required for the production of high-affinity class-switched IgG1 antibody. SENP1 controls the Paired box protein 5 protein level through deSUMOylation, leading to increased expression of activation-induced cytidine deaminase. SUMOylation is an important posttranslational mechanism regulating germinal center B cell response
physiological function
SENP1 is a critical p53 deSUMOylating enzyme
additional information
-
enzyme SENP1 silencing has no influence on androgen receptor expression
additional information
enzyme USPL1 has a catalytic domain with a C236-H456-D472 triad. Two tryptophanes close to the catalytic cysteine are needed to stably position the C-terminal diglycine motif of SUMO in the substrate tunnel
additional information
-
NMR enzyme-substrate complex analysis, the distally bound beta-grasp domain of SUMO1 induces realignment of the catalytic residues that enhance the enzyme activity, mode of substrate recognition and binding, molecular dynamics, overview
additional information
-
SENP1 is a target of SUMO modification and has targeting preference for SUMO paralogues and substrates
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SENP1_MOUSE
640
0
72511
Swiss-Prot
Secretory Pathway (Reliability: 5)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
in the crystal structure of human SENP1 complexed with unprocessed SUMO1, PDB: 2IY1, the catalytic Cys603 is located in a cleft which, upon substrate binding, closes to form a channel-like structure
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
sumoylation
-
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 resulted in the detection of the conjugated form
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of the human SENP1 catalytic domain are obtained at room temperature by hanging-drop vapour diffusion. When interpreting a medium-resolution electron-density map of the catalytic domain of human sentrin-specific protease 1 (SENP1), a strong feature indicative of an ordered divalent cation is noted. This is assigned as Co2+, an essential component of the crystallization mixture. The ion displays tetrahedral coordination by Glu430 and His640 from one molecule and the corresponding residues from a symmetry-related molecule. Analysis of the data derived from a previous structure of SENP1 suggest that Co2+ has been overlooked and rerefinement support this conclusion. Highthroughput automated re-refinement protocols also failed to mark the Co2+ position
SENP1 crystallization is performed at 20°C using a sitting drop vapour-diffusion method. Single diamond-shaped crystals are grown after 2 days from equal volumes of protein solution (20 mg/ml in 20 mM Tris/HCl, pH 8.0, and 50 mM NaCl) and reservoir solution containing 100 mM CoCl2, 0.1 M Mes, pH 6.5, and 1.8 M (NH4)2SO4. The structure of SENP1 is determined to 2.45 A. NaBH4 is used to trap a stable thiohemiacetal transition-state analogue between Cys602 of SENP1 and Gly92 of SUMO-2, determination of the structure of this complex to 3.2 A. Crystallization and structure determination of the SENP1-SUMO-2 complex
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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
-
site-directed mutagenesis, the active site mutant precipitates SUMO1ylated proteins but not SUMO2/3-modified substrate
additional information
C603S
-
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
-
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
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
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
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
-
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
-
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
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged catalytic domain SENP1c, aa419-aa643 from Escherichia coli strain BL21 by nickel affinity chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of the His-tagged catalytic domain of SENP1, SENP1c, aa419-aa643, from PC-3 cell cDNA library, cloned into pET28a(+) vector, and expressed in Escherichia coli strain BL21
-
crystallization of a complex of SENP1 C603A bound to full-length SUMO-1 and determination of the structure by X-ray crystallography. Two structures of SENP1 C603A in complex with the SUMO-1 precursor and RanGAP1-SUMO-1
expression of wild-type and mutant enzymes in MEF, 293T, and 3T3-L1 cells, real-time quantitative PCR expression analysis
gene SP1, recombinant expression of GFP-tagged or untagged SENP1 and the catalytically dead enzyme mutant transiently in HeLa cells
-
overexpression of a catalytically inactive/dominant negative Cys-to-Ser SENP1 mutant
-
recombinant expression of wild-type Flag-tagged C13orf22l and C13orf22lcat mutant comprising amino acid residues 312-649 in HeLa cells
-
recombinant expression of YFP-tagged enzyme USPL1 in HeLa cell nucleoplasm, and of HA-tagged enzyme in Cajal bodies, co-expression with suicide inhibitor Strep-TEV-HA-SUMO-vinylmethylester, recombinant expression of truncated enzyme variant USPL1cat as His-GST-TEV-USPL1cat
the catalytic core domain of SENP1 (amino acids 415-643) and mutants are cloned into the vector pEHISTEV and expressed as a N-terminally His-tagged protein. The recombinant proteins are expressed in Escherichia coli Bl21(DE3) cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
a combination of high SENP1 and HIF2alpha expression gives particularly poor prognosis for clear cell renal cell carcinoma patients
SENP1 expression can be induced by hypoxia. Induction of SENP1 expression is mediated by hypoxia-inducible factor HIF-1alpha
SENP1 is markedly upregulated in osteosarcoma cellsexpression rate of SENP1 in osteosarcoma tissues is 88.33%, whereas that in adjacent tissues is 46.67%
SENP1 mRNA expression is decreased in astrocytes compared to that in olfactory mucosa mesenchymal stem cell
-
SENP1 mRNA expression is increased in neurons compared to that in olfactory mucosa mesenchymal stem cell
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
drug development
medicine
diagnostics
-
SENP1 may serve as a potential diagnostic and therapeutic target of pancreatic ductal adenocarcinoma
diagnostics
-
enzyme SENP1 is an important cancer metastasis-related molecule and may be a prognostic marker and a therapeutic target for metastasis in prostate cancer patients
diagnostics
utility of SENP1 as an effective predictive biomarker for targeted treatment of head and neck squamous cell carcinoma. SENP1 could serve as an important biomarker for prognosis of patients
diagnostics
osteosarcoma patients with higher plasma exosome-derived SENP1 levels have worse disease-free survival and overall survival. Plasma exosome-derived SENP1 levels is a novel and independent prognostic predictor in clinical applications
diagnostics
SENP1 as an important pathogenic factor in HIF2alphahi/SENP1hi clear cell renal cell carcinoma and a potential biomarker and therapeutic target in clear cell renal cell carcinoma patients with particularly poor prognosis
drug development
-
SENP1 is a potential therapeutic target for the treatment of prostate cancers
drug development
-
the enzyme is a drug target for development of small molecule drugs against prostate cancer
drug development
-
SENP1 is an essential gene and is a potential target for developing therapeutic agents for cancer
medicine
SENP1 overexpression induces transformation of the normal prostate gland and gradually facilitates the onset of high-grade prostatic intraepithelial neoplasiade. SUMOylation plays a critical role in prostate pathogenesis through induction of HIF1alpha-dependent angiogenesis and enhanced cell proliferation
medicine
-
diagnostic value of measuring the urinary content of SENP1 mRNAs for detection of tumor recurrence
medicine
-
SENP1 is overexpressed in most of colon cancer tissues. SENP1 regulates the in vitro and in vivo growth of colon cancer cells with the upregulated expression of CDK inhibitors
medicine
-
SENP1, can transform normal prostate epithelia to a dysplasic state and directly modulate several oncogenic pathways in prostate cells, including AR, c-Jun, and Cyclin D1
medicine
SENP1 expression has strong prognostic impact in a molecularly defined subset of cancers. In the subgroup of ERG positive, PTEN undeleted cancers, the prognostic role of SENP1 expression is independent of the preoperative PSA level, tumor stage, Gleason grade, and the status of the resection
medicine
the expression of SENP1 is positively correlated with the malignant grades of astrocytoma. The NF-kappaB and Akt signaling pathways in glioblastoma multiforme tissues are activated. Knock-down of endogenous SENP1 promotes cell apoptosis. Downregulation of SENP1 expression can inhibit the phosphorylation of IkappaBalpha and Akt, and also the expression of its downstream regulation factors Bcl-xL and cyclinD1
medicine
a combination of high SENP1 and HIF2alpha expression gives particularly poor prognosis for clear cell renal cell carcinoma patients and suggest that SENP1 may be an attractive new target for treating metastatic renal cell carcinoma
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Xu, Z.; Chau, S.F.; Lam, K.H.; Chan, H.Y.; Ng, T.B.; Au, S.W.
Crystal structure of the SENP1 mutant C603S-SUMO complex reveals the hydrolytic mechanism of SUMO-specific protease
Biochem. J.
398
345-352
2006
Homo sapiens (Q9P0U3)
brenda
Cheng, J.; Kang, X.; Zhang, S.; Yeh, E.T.
SUMO-specific protease 1 is essential for stabilization of HIF1alpha during hypoxia
Cell
131
584-595
2007
Mus musculus (P59110)
brenda
Bawa-Khalfe, T.; Cheng, J.; Wang, Z.; Yeh, E.T.
Induction of the SUMO-specific protease 1 transcription by the androgen receptor in prostate cancer cells
J. Biol. Chem.
282
37341-37349
2007
Homo sapiens
brenda
Shen, L.; Tatham, M.H.; Dong, C.; Zagorska, A.; Naismith, J.H.; Hay, R.T.
SUMO protease SENP1 induces isomerization of the scissile peptide bond
Nat. Struct. Mol. Biol.
13
1069-1077
2006
Homo sapiens (Q9P0U3)
brenda
Rimsa, V.; Eadsforth, T.; Hunter, W.N.
The role of Co2+ in the crystallization of human SENP1 and comments on the limitations of automated refinement protocols
Acta Crystallogr. Sect. F
67
442-445
2011
Homo sapiens (Q9P0U3), Homo sapiens
brenda
Yates, K.E.; Korbel, G.A.; Shtutman, M.; Roninson, I.B.; DiMaio, D.
Repression of the SUMO-specific protease Senp1 induces p53-dependent premature senescence in normal human fibroblasts
Aging Cell
7
609-621
2008
Homo sapiens (Q9P0U3)
brenda
Ohbayashi, N.; Kawakami, S.; Muromoto, R.; Togi, S.; Ikeda, O.; Kamitani, S.; Sekine, Y.; Honjoh, T.; Matsuda, T.
The IL-6 family of cytokines modulates STAT3 activation by desumoylation of PML through SENP1 induction
Biochem. Biophys. Res. Commun.
371
823-828
2008
Homo sapiens (Q9P0U3)
brenda
Xu, Z.; Au, S.W.
Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1
Biochem. J.
386
325-330
2005
Homo sapiens (Q9P0U3)
brenda
Shen, L.N.; Dong, C.; Liu, H.; Naismith, J.H.; Hay, R.T.
The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing
Biochem. J.
397
279-288
2006
Homo sapiens (Q9P0U3)
brenda
Witty, J.; Aguilar-Martinez, E.; Sharrocks, A.D.
SENP1 participates in the dynamic regulation of Elk-1 SUMOylation
Biochem. J.
428
247-254
2010
Homo sapiens (Q9P0U3)
brenda
Brems-Eskildsen, A.S.; Zieger, K.; Toldbod, H.; Holcomb, C.; Higuchi, R.; Mansilla, F.; Munksgaard, P.P.; Borre, M.; Orntoft, T.F.; Dyrskjot, L.
Prediction and diagnosis of bladder cancer recurrence based on urinary content of hTERT, SENP1, PPP1CA, and MCM5 transcripts
BMC Cancer
10
646
2010
Homo sapiens
brenda
Xu, Y.; Li, J.; Zuo, Y.; Deng, J.
Wang, L.S.; Chen, G.Q.: SUMO-specific protease 1 regulates the in vitro and in vivo growth of colon cancer cells with the upregulated expression of CDK inhibitors
Cancer Lett.
309
78-84
2011
Homo sapiens
brenda
Li, X.; Luo, Y.; Yu, L.; Lin, Y.; Luo, D.; Zhang, H.; He, Y.; Kim, Y.O.; Kim, Y.; Tang, S.; Min, W.
SENP1 mediates TNF-induced desumoylation and cytoplasmic translocation of HIPK1 to enhance ASK1-dependent apoptosis
Cell Death Differ.
15
739-750
2008
Homo sapiens (Q9P0U3)
brenda
Dai, X.Q.; Plummer, G.; Casimir, M.; Kang, Y.; Hajmrle, C.; Gaisano, H.Y.; Manning Fox, J.E.; MacDonald, P.E.
SUMOylation regulates insulin exocytosis downstream of secretory granule docking in rodents and humans
Diabetes
60
838-847
2011
Mus musculus (P59110)
brenda
Kim, Y.H.; Sung, K.S.; Lee, S.J.; Kim, Y.O.; Choi, C.Y.; Kim, Y.
Desumoylation of homeodomain-interacting protein kinase 2 (HIPK2) through the cytoplasmic-nuclear shuttling of the SUMO-specific protease SENP1
FEBS Lett.
579
6272-6278
2005
Homo sapiens (Q9P0U3)
brenda
Bawa-Khalfe, T.; Yeh, E.T.
SUMO losing balance: SUMO proteases disrupt SUMO homeostasis to facilitate cancer development and progression
Genes Cancer
1
748-752
2010
Homo sapiens
brenda
Bailey, D.; O'Hare, P.
Characterization of the localization and proteolytic activity of the SUMO-specific protease, SENP1
J. Biol. Chem.
279
692-703
2004
Homo sapiens
brenda
Bawa-Khalfe, T.; Cheng, J.; Lin, S.H.; Ittmann, M.M.; Yeh, E.T.
SENP1 induces prostatic intraepithelial neoplasia through multiple mechanisms
J. Biol. Chem.
285
25859-25866
2010
Mus musculus (P59110)
brenda
Xu, Y.; Zuo, Y.; Zhang, H.; Kang, X.; Yue, F.; Yi, Z.; Liu, M.; Yeh, E.T.; Chen, G.; Cheng, J.
Induction of SENP1 in endothelial cells contributes to hypoxia-driven VEGF expression and angiogenesis
J. Biol. Chem.
285
36682-36688
2010
Homo sapiens (Q9P0U3)
brenda
Yu, L.; Ji, W.; Zhang, H.; Renda, M.J.; He, Y.; Lin, S.; Cheng, E.C.; Chen, H.; Krause, D.S.; Min, W.
SENP1-mediated GATA1 deSUMOylation is critical for definitive erythropoiesis
J. Exp. Med.
207
1183-1195
2010
Mus musculus (P59110)
brenda
Cheng, J.; Wang, D.; Wang, Z.; Yeh, E.T.
SENP1 enhances androgen receptor-dependent transcription through desumoylation of histone deacetylase 1
Mol. Cell. Biol.
24
6021-6028
2004
Homo sapiens (Q9P0U3)
brenda
Kaikkonen, S.; Jskelinen, T.; Karvonen, U.; Rytinki, M.M.; Makkonen, H.; Gioeli, D.; Paschal, B.M.; Palvimo, J.J.
SUMO-specific protease 1 (SENP1) reverses the hormone-augmented SUMOylation of androgen receptor and modulates gene responses in prostate cancer cells
Mol. Endocrinol.
23
292-307
2009
Homo sapiens (Q9P0U3)
brenda
Shin, Y.C.; Liu, B.Y.; Tsai, J.Y.; Wu, J.T.; Chang, L.K.; Chang, S.C.
Biochemical characterization of the small ubiquitin-like modifiers of Chlamydomonas reinhardtii
Planta
232
649-662
2010
Homo sapiens
brenda
Plant, L.D.; Dementieva, I.S.; Kollewe, A.; Olikara, S.; Marks, J.D.; Goldstein, S.A.
One SUMO is sufficient to silence the dimeric potassium channel K2P1
Proc. Natl. Acad. Sci. USA
107
10743-10748
2010
Homo sapiens (Q9P0U3), Homo sapiens
brenda
Qiao, Z.; Wang, W.; Wang, L.; Wen, D.; Zhao, Y.; Wang, Q.; Meng, Q.; Chen, G.; Wu, Y.; Zhou, H.
Design, synthesis, and biological evaluation of benzodiazepine-based SUMO-specific protease 1 inhibitors
Bioorg. Med. Chem. Lett.
21
6389-6392
2011
Homo sapiens
brenda
Chen, Y.; Wen, D.; Huang, Z.; Huang, M.; Luo, Y.; Liu, B.; Lu, H.; Wu, Y.; Peng, Y.; Zhang, J.
2-(4-Chlorophenyl)-2-oxoethyl 4-benzamidobenzoate derivatives, a novel class of SENP1 inhibitors: Virtual screening, synthesis and biological evaluation
Bioorg. Med. Chem. Lett.
22
6867-6870
2012
Homo sapiens
brenda
Yan, X.M.; Xu, Z.Q.; Zhou, Y.; Wang, J.; Pan, J.; Yuan, L.Q.; Fu, M.C.; Xia, H.L.; Cao, X.; Zhang, T.
SENP1 regulates cell migration and invasion in neuroblastoma
Biotechnol. Appl. Biochem.
63
435-440
2016
Homo sapiens
brenda
Chen, C.H.; Chang, C.C.; Lee, T.H.; Luo, M.; Huang, P.; Liao, P.H.; Wei, S.; Li, F.A.; Chen, R.H.; Zhou, X.Z.; Shih, H.M.; Lu, K.P.
SENP1 deSUMOylates and regulates Pin1 protein activity and cellular function
Cancer Res.
73
3951-3962
2013
Homo sapiens
brenda
Sharma, P.; Yamada, S.; Lualdi, M.; Dasso, M.; Kuehn, M.R.
Senp1 is essential for desumoylating Sumo1-modified proteins but dispensable for Sumo2 and Sumo3 deconjugation in the mouse embryo
Cell Rep.
3
1640-1650
2013
Mus musculus
brenda
Schulz, S.; Chachami, G.; Kozaczkiewicz, L.; Winter, U.; Stankovic-Valentin, N.; Haas, P.; Hofmann, K.; Urlaub, H.; Ovaa, H.; Wittbrodt, J.; Meulmeester, E.; Melchior, F.
Ubiquitin-specific protease-like 1 (USPL1) is a SUMO isopeptidase with essential, non-catalytic functions
EMBO Rep.
13
930-938
2012
Homo sapiens (Q5W0Q7), Danio rerio
brenda
Cai, R.; Yu, T.; Huang, C.; Xia, X.; Liu, X.; Gu, J.; Xue, S.; Yeh, E.T.; Cheng, J.
SUMO-specific protease 1 regulates mitochondrial biogenesis through PGC-1alpha
J. Biol. Chem.
287
44464-44470
2012
Homo sapiens
brenda
Liu, B.; Wang, T.; Mei, W.; Li, D.; Cai, R.; Zuo, Y.; Cheng, J.
Small ubiquitin-like modifier (SUMO) protein-specific protease 1 de-SUMOylates Sharp-1 protein and controls adipocyte differentiation
J. Biol. Chem.
289
22358-22364
2014
Homo sapiens (Q9P0U3)
brenda
Cubenas-Potts, C.; Goeres, J.D.; Matunis, M.J.
SENP1 and SENP2 affect spatial and temporal control of sumoylation in mitosis
Mol. Biol. Cell
24
3483-3495
2013
Homo sapiens (Q9P0U3)
brenda
Chow, K.H.; Elgort, S.; Dasso, M.; Powers, M.A.; Ullman, K.S.
The SUMO proteases SENP1 and SENP2 play a critical role in nucleoporin homeostasis and nuclear pore complex function
Mol. Biol. Cell
25
160-168
2014
Homo sapiens
brenda
Chen, C.H.; Namanja, A.T.; Chen, Y.
Conformational flexibility and changes underlying activation of the SUMO-specific protease SENP1 by remote substrate binding
Nat. Commun.
5
4968
2014
Homo sapiens
brenda
Chow, K.H.; Elgort, S.; Dasso, M.; Ullman, K.S.
Two distinct sites in Nup153 mediate interaction with the SUMO proteases SENP1 and SENP2
Nucleus
3
349-358
2012
Homo sapiens
brenda
Wu, R.; Cui, Y.; Yuan, X.; Yuan, H.; Wang, Y.; He, J.; Zhao, J.; Peng, S.
SUMO-specific protease 1 modulates cadmium-augmented transcriptional activity of androgen receptor (AR) by reversing AR SUMOylation
Toxicol. Lett.
229
405-413
2014
Homo sapiens
brenda
Ma, C.; Wu, B.; Huang, X.; Yuan, Z.; Nong, K.; Dong, B.; Bai, Y.; Zhu, H.; Wang, W.; Ai, K.
SUMO-specific protease 1 regulates pancreatic cancer cell proliferation and invasion by targeting MMP-9
Tumour Biol.
35
12729-12735
2014
Homo sapiens
brenda
Zhang, C.; Li, J.; Qiu, X.; Chen, Y.; Zhang, X.
SUMO protease SENP1 acts as a ceRNA for TGFBR2 and thus activates TGFBR2/Smad signaling responsible for LPS-induced sepsis
Biomed. Pharmacother.
112
108620
2019
Homo sapiens (Q9P0U3)
brenda
Burdelski, C.; Menan, D.; Tsourlakis, M.C.; Kluth, M.; Hube-Magg, C.; Melling, N.; Minner, S.; Koop, C.; Graefen, M.; Heinzer, H.; Wittmer, C.; Sauter, G.; Simon, R.; Schlomm, T.; Steurer, S.; Krech, T.
The prognostic value of SUMO1/Sentrin specific peptidase 1 (SENP1) in prostate cancer is limited to ERG-fusion positive tumors lacking PTEN deletion
BMC Cancer
15
538
2015
Homo sapiens (Q9P0U3)
brenda
Huang, X.; Zuo, Y.; Wang, X.; Wu, X.; Tan, H.; Fan, Q.; Dong, B.; Xue, W.; Chen, G.Q.; Cheng, J.
SUMO-specific protease 1 is critical for myeloid-derived suppressor cell development and function
Cancer Res.
79
3891-3902
2019
Mus musculus (P59110)
brenda
Zhang, H.; Wang, Y.; Zhu, A.; Huang, D.; Deng, S.; Cheng, J.; Zhu, M.X.; Li, Y.
SUMO-specific protease 1 protects neurons from apoptotic death during transient brain ischemia/reperfusion
Cell Death Dis.
7
e2484
2016
Mus musculus (P59110)
brenda
Xia, W.; Tian, H.; Cai, X.; Kong, H.; Fu, W.; Xing, W.; Wang, Y.; Zou, M.; Hu, Y.; Xu, D.
Inhibition of SUMO-specific protease 1 induces apoptosis of astroglioma cells by regulating NF-kappaB/Akt pathways
Gene
595
175-179
2016
Homo sapiens (Q9P0U3), Homo sapiens
brenda
Zhang, X.; Wang, H.; Wang, H.; Xiao, F.; Seth, P.; Xu, W.; Jia, Q.; Wu, C.; Yang, Y.; Wang, L.
SUMO-specific cysteine protease 1 promotes epithelial mesenchymal transition of prostate cancer cells via regulating SMAD4 deSUMOylation
Int. J. Mol. Sci.
18
808
2017
Homo sapiens
brenda
Rodriguez-Castaneda, F.; Lemma, R.B.; Cuervo, I.; Bengtsen, M.; Moen, L.M.; Ledsaak, M.; Eskeland, R.; Gabrielsen, O.S.
The SUMO protease SENP1 and the chromatin remodeler CHD3 interact and jointly affect chromatin accessibility and gene expression
J. Biol. Chem.
293
15439-15454
2018
Homo sapiens (Q9P0U3)
brenda
Niu, Q.; Hou, W.; Yan, Y.; Sun, S.; Lin, Y.; Fang, H.; Ma, C.; Dong, C.; Cheng, Y.; Xu, Y.; Ding, M.; Wang, S.; Cui, Z.; Chen, Y.; Li, H.; Li, H.; Xiao, N.
Antileukemic effects of topoisomerase I inhibitors mediated by de-SUMOylase SENP1
Biochim. Biophys. Acta Mol. Basis Dis.
1868
166492
2022
Homo sapiens (Q9P0U3)
brenda
Li, J.; Wu, R.; Yung, M.M.H.; Sun, J.; Li, Z.; Yang, H.; Zhang, Y.; Liu, S.S.; Cheung, A.N.Y.; Ngan, H.Y.S.; Braisted, J.C.; Zheng, W.; Wei, H.; Gao, Y.; Nemes, P.; Pei, H.; Chan, D.W.; Li, Y.; Zhu, W.
SENP1-mediated deSUMOylation of JAK2 regulates its kinase activity and platinum drug resistance
Cell Death Dis.
12
341
2021
Homo sapiens (Q9P0U3)
brenda
Lindenmann, U.; Brand, M.; Gall, F.; Frasson, D.; Hunziker, L.; Kroslakova, I.; Sievers, M.; Riedl, R.
Discovery of a class of potent and selective non-competitive sentrin-specific protease 1 inhibitors
ChemMedChem
15
675-679
2020
Homo sapiens (Q9P0U3)
brenda
Wei, H.; Guo, J.; Sun, X.; Gou, W.; Ning, H.; Fang, Z.; Liu, Q.; Hou, W.; Li, Y.
Discovery and radiosensitization research of ursolic acid derivatives as SENP1 inhibitors
Eur. J. Med. Chem.
227
113918
2022
Homo sapiens (Q9P0U3)
brenda
Liu, J.; Li, Y.; Bian, X.; Xue, N.; Yu, J.; Dai, S.; Liu, X.
Astragaloside IV alleviates heart failure by regulating SUMO-specific protease 1
Exp. Ther. Med.
22
1076
2021
Mus musculus (P59110)
brenda
Wang, L.; Wu, J.; Song, S.; Chen, H.; Hu, Y.; Xu, B.; Liu, J.
Plasma exosome-derived sentrin SUMO-specific protease 1 a prognostic biomarker in patients with osteosarcoma
Front. Oncol.
11
625109
2021
Homo sapiens (Q9P0U3)
brenda
Brand, M.; Bommeli, E.B.; Ruetimann, M.; Lindenmann, U.; Riedl, R.
Discovery of a Dual SENP1 and SENP2 Inhibitor
Int. J. Mol. Sci.
23
12085
2022
Homo sapiens (Q9P0U3)
brenda
He, J.; Peng, J.; Li, Y.; Jiang, J.; Li, J.; Lin, L.; Wang, J.; Xia, Y.
SENP1 facilitates OM-MSC differentiation through activating OPTN-mediated mitophagy to mitigate the neurologic impairment following ICH
iScience
27
109865
2024
Rattus norvegicus
brenda
Taghvaei, S.; Sabouni, F.; Minuchehr, Z.; Taghvaei, A.
Identification of novel anti-cancer agents, applying in silico method for SENP1 protease inhibition
J. Biomol. Struct. Dyn.
40
6228-6242
2022
Homo sapiens (Q9P0U3)
brenda
Shi, Y.; Yasen, M.; Wang, Z.; Du, T.; Ding, Y.; Li, X.; Chai, Z.; Jie, C.; Ju, G.; Ji, M.
The allosteric effect of the upper half of SENP1 contributes to its substrate selectivity for SUMO1 over SUMO2
J. Biomol. Struct. Dyn.
41
12372-12386
2023
Homo sapiens (Q9P0U3)
brenda
Chauhan, K.M.; Chen, Y.; Chen, Y.; Liu, A.T.; Sun, X.X.; Dai, M.S.
The SUMO-specific protease SENP1 deSUMOylates p53 and regulates its activity
J. Cell. Biochem.
122
189-197
2021
Homo sapiens (Q9P0U3), Homo sapiens (Q5W0Q7)
brenda
Lee, M.H.; Sung, K.; Beebe, D.; Huang, W.; Shapiro, D.; Miyamoto, S.; Abel, E.J.
The SUMO protease SENP1 promotes aggressive behaviors of high HIF2? expressing renal cell carcinoma cells
Oncogenesis
11
65
2022
Homo sapiens (Q9P0U3)
brenda
Xu, X.; Mao, Y.; Feng, Z.; Dai, F.; Gu, T.; Zheng, J.
SENP1 inhibits ferroptosis and promotes head and neck squamous cell carcinoma by regulating ACSL4 protein stability via SUMO1
Oncol. Rep.
51
34
2024
Homo sapiens (Q9P0U3)
brenda
Qi, J.; Yan, L.; Sun, J.; Huang, C.; Su, B.; Cheng, J.; Shen, L.
SUMO-specific protease 1 regulates germinal center B cell response through deSUMOylation of PAX5
Proc. Natl. Acad. Sci. USA
121
e2314619121
2024
Mus musculus (P59110)
brenda
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