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SENP1

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Summary

SENP1 (SUMO specific peptidase 1, HGNC:17927) is a protein-coding gene on chromosome 12q13.11, encoding Sentrin-specific protease 1 (Q9P0U3). Protease that catalyzes two essential functions in the SUMO pathway.

This gene encodes a cysteine protease that specifically targets members of the small ubiquitin-like modifier (SUMO) protein family. This protease regulates SUMO pathways by deconjugating sumoylated proteins. This protease also functions to process the precursor SUMO proteins into their mature form. Alternate splicing results in multiple transcript variants.

Source: NCBI Gene 29843 — RefSeq curated summary.

At a glance

  • GWAS associations: 8
  • Clinical variants (ClinVar): 21 total
  • Druggable target: yes — 2 molecules with ChEMBL bioactivity
  • MANE Select transcript: NM_001267594

Identifiers

Gene identifiers

FieldValue
HGNC IDHGNC:17927
Approved symbolSENP1
NameSUMO specific peptidase 1
Location12q13.11
Locus typegene with protein product
StatusApproved
Ensembl geneENSG00000079387
Ensembl biotypeprotein_coding
OMIM612157
Entrez29843

Gene structure

Transcript identifiers

Ensembl transcripts: 18 — 12 protein_coding, 3 retained_intron, 2 protein_coding_CDS_not_defined, 1 nonsense_mediated_decay

ENST00000448372, ENST00000547181, ENST00000547886, ENST00000549518, ENST00000549595, ENST00000549882, ENST00000551358, ENST00000551592, ENST00000551798, ENST00000552189, ENST00000873200, ENST00000873201, ENST00000934574, ENST00000934575, ENST00000934576, ENST00000934577, ENST00000934578, ENST00000955595

RefSeq mRNA: 2 — MANE Select: NM_001267594 NM_001267594, NM_001267595

CCDS: CCDS44868

Canonical transcript exons

ENST00000549518 — 18 exons

ExonStartEnd
ENSE000023733494810602848106079
ENSE000034592694808359148083762
ENSE000034734444807432448074607
ENSE000035118254804800148048080
ENSE000035122124804892948049132
ENSE000035504304809634348096427
ENSE000035757684804635648046451
ENSE000035786524807166748071721
ENSE000035800634806506548065220
ENSE000035986854806559648065680
ENSE000036130654806371048063841
ENSE000036150574804697848047062
ENSE000036266954807469048074793
ENSE000036504364809799448098124
ENSE000036581884806692748066965
ENSE000036755094810146948101516
ENSE000036907394808880148088960
ENSE000038511724804289748045384

Expression profiles

Bgee: expression breadth ubiquitous, 216 present calls, max score 90.17.

FANTOM5 (CAGE): breadth ubiquitous, TPM avg 14.0387 / max 247.6457, expressed in 1796 samples.

FANTOM5 promoters (8 alternative TSS)

Promoter IDTPM avgSamples expressed
1307185.53741578
1307215.45451622
1307200.8954558
1307220.7347456
1307190.5922335
1307240.5113283
1307230.266097
1307170.047116

Top tissues by expression

238 total, by Bgee expression score (0-100, higher = more expressed):

TissueAnatomy IDExpression scoreQuality
testisUBERON:000047390.17gold quality
right testisUBERON:000453489.86gold quality
left testisUBERON:000453389.81gold quality
male germ line stem cell (sensu Vertebrata) in testisCL:0000089 ∩ UBERON:000047389.03gold quality
oviduct epitheliumUBERON:000480488.94gold quality
spermCL:000001988.89gold quality
buccal mucosa cellCL:000233686.54gold quality
calcaneal tendonUBERON:000370186.46gold quality
ventricular zoneUBERON:000305383.67gold quality
adrenal tissueUBERON:001830383.62gold quality
bone marrow cellCL:000209283.60gold quality
ganglionic eminenceUBERON:000402383.47gold quality
primordial germ cell in gonadCL:0000670 ∩ UBERON:000099182.50gold quality
vermiform appendixUBERON:000115482.34gold quality
smooth muscle tissueUBERON:000113581.97gold quality
cortical plateUBERON:000534381.89gold quality
colonic epitheliumUBERON:000039781.63gold quality
islet of LangerhansUBERON:000000681.19gold quality
lymph nodeUBERON:000002980.80gold quality
stromal cell of endometriumCL:000225580.62gold quality
rectumUBERON:000105280.44gold quality
tonsilUBERON:000237280.43gold quality
monocyteCL:000057680.34gold quality
leukocyteCL:000073880.25gold quality
fallopian tubeUBERON:000388979.38gold quality
cartilage tissueUBERON:000241879.03gold quality
bone marrowUBERON:000237178.99gold quality
popliteal arteryUBERON:000225078.77gold quality
tibial arteryUBERON:000761078.76gold quality
bloodUBERON:000017878.75gold quality

Single-cell (SCXA)

Detected in 3 experiment(s), a significant marker in 0.

ExperimentMarker?Max mean expression
E-MTAB-6379no612.89
E-GEOD-124858no169.20
E-ANND-3no6.27

Regulation

Is transcription factor: no

Upstream regulators (CollecTRI, top): AR, HIF1A, MTA1, ZBTB17

Literature-anchored findings (GeneRIF, showing 40)

  • co-localizes with Herpes simplex virus 1 ICP0 in cell nucleus (PMID:12466471)
  • SENP1’s ability to enhance AR-dependent transcription is not mediated through desumoylation of AR, but rather through its ability to deconjugate histone deacetylase 1 (HDAC1), thereby reducing its deacetylase activity. (PMID:15199155)
  • p300 is essential for SENP1 to enhance c-Jun-dependent transcription because SENP1 can desumoylate the CRD1 domain of p300, thereby releasing the cis-repression of CRD1 on p300 (PMID:15701643)
  • as a result of (12;15)(q13;q25)translocation, the SUMO/Sentrin-specific protease 1 gene (SENP1) on chromosome 12 and the embryonic polarity-related mesoderm development gene (MESDC2) on chromosome 15 are disrupted and fused (PMID:15917269)
  • HIPK2 is a desumoylation target for the SUMO-specific protease SENP1 that shuttles between the cytoplasm and the nucleus. (PMID:16253240)
  • x-ray crystallographic structure of SENP1-SUMO-2 complex demonstrates structural basis for discrimination between SUMO paralogues during processing (PMID:16553580)
  • A study evalution the mechanisms of regulation of the sumoylation pathway by the SUMO-specific proteases is presented. (PMID:16712526)
  • studies indicate that overexpression of SENP1 is associated with prostate cancer developme (PMID:16925949)
  • discrimination between unprocessed SUMO-1 and SUMO-2 by SENP1 is based on a catalytic step rather than substrate binding and is likely to reflect differences in the ability of SENP1 to correctly orientate the scissile bonds in SUMO-1 and SUMO-2 (PMID:17099698)
  • SENP1 may act as redox sensors and effectors modulating the desumoylation pathway and specific cellular responses to oxidative stress (PMID:17704192)
  • SENP1 mediates TNF-induced desumoylation and translocation of HIPK1, leading to an enhanced ASK1-dependent apoptosis. (PMID:18219322)
  • SENP1 restored the promyelocytic leukemia protein mediated suppression of STAT3 activation. (PMID:18474224)
  • Sentrin-specific protease Senp1 repression induces tumor suppressor protein p53-mediated premature senescence; SUMO proteases may thus be required for proliferation of normal human cells. (PMID:18616636)
  • SENP1 reverses the ligand-induced SUMOylation of AR and helps fine tune the cellular responses to androgens in a target promoter-selective manner. (PMID:19116244)
  • epigenetic control of MMP-1 expression via histone H4 acetylation (PMID:20079608)
  • Results demonstrate that SENP1 is the most efficient SUMO protease acting on Elk-1, and that SENP3 has little effect on Elk-1. SENP2 has an intermediate effect, but its ability to activate Elk-1 is independent from its SUMO-deconjugating activity. (PMID:20337593)
  • Induction of SENP1 in endothelial cells contributes to hypoxia-driven VEGF expression and angiogenesis. (PMID:20841360)
  • Could use the urinary hTERT, SENP1, PPP1CA, and MCM5 mRNA to detect bladder cancer recurrence. (PMID:21106093)
  • crystal structure of human SENP1 was redetermined at 2.4 A degrees resolution with Rwork and Rfree values of 23.1% and 31.3%, respectively (PMID:21505236)
  • SENP1 might play a role in cell cycle regulation of colon cancer cells (PMID:21669491)
  • de-SUMOylation is essential for SENP1 modulating XBP1 transcriptional activity. (PMID:22370484)
  • The SENP1 levels are influenced by the presence of Nup153, whereas SENP2 is not sensitive to changes in Nup153 abundance. (PMID:22688647)
  • Results show the contribution of SENP1 to the progression of prostate cancer, and suggest that SENP1 may be a prognostic marker. (PMID:22733136)
  • mutation of K364 to arginine (R) or deSumoylation by small ubiquitin-like modifier (Sumo)-specific protease-1, a nuclear deSumoylase, enhanced the transactivation capacity of LEDGF and its cellular abundance (PMID:22748127)
  • Data show that the loss of OCT4 expression under hypoxia can be triggered by sumoylation, which was regulated by the SUMO1 peptidase SENP1. (PMID:23002208)
  • Data suggest that small ubiquitin-like modifier (SUMO)-specific protease 1 (SENP1) expression might contribute to the malignant progression of prostate cancer and as a potential prognostic factor for biochemical recurrence after prostatectomy. (PMID:23089540)
  • A critical role for SENP1-mediated desumoylation in promoting Pin1 function during tumorigenesis. (PMID:23633483)
  • Chromosome segregation depends on precise spatial and temporal control of sumoylation in mitosis; SENP1 and SENP2 are important mediators of this control. (PMID:24048451)
  • Many nucleoporins are mislocalized and, in some cases, reduced in level when SENP1 and SENP2 are codepleted. (PMID:24196834)
  • our data demonstrate that the miR-138/SENP1 cascade is relative to radiosensitization in lung cancer cells and is a potential radiotherapy target. (PMID:24691972)
  • cadmium-induction enhances AR transcriptional activity by decreasing AR SUMOylation (PMID:25014244)
  • SENP1 deficiency exacerbates ischemia-reperfusion injury in cardiomyocytes via a HIF1alpha-dependent pathway. (PMID:25082844)
  • Data suggest that up-regulation of SENP1 down-regulates insulin secretion and impairs intracellular calcium signaling in islet beta-cells; this secretory dysfunction is due to SENP1-induced apoptosis of islet beta-cells. (PMID:25139051)
  • SENP1 was upregulated in PDAC tissues; overexpressed SENP1 was associated with lymph node metastasis and TNM stage. (PMID:25217324)
  • results provide independent evidence in support of a role for SENP1 in chronic mountain sickness in individuals of Quechua ancestry and suggest the SENP1 and ANP32D signatures of selection are in tight linkage disequilibrium (LD). (PMID:25225945)
  • SENP1 uses remote substrate binding for conformational flexibility and activation (PMID:25263960)
  • Over-expression of small ubiquitin-like modifier proteases 1 predicts chemo-sensitivity and poor survival in non-small cell lung cancer.( (PMID:25430449)
  • SENP1 up-regulation in diseased heart is mediated via calcineurin-NFAT/MEF2C-PGC-1alpha pathway. (PMID:25446185)
  • low expression of miR-145 was correlated with high expression of SENP1 in Prostate cancer cell line and the SENP1 3’-untranslated region was a regulative target of miR-145 in vitro. (PMID:25645686)
  • results delineate a key role for Senp1in IL-6 induced proliferation and survival of MM cells, suggesting it may be a potential new therapeutic target in MM (PMID:25791478)

Cross-species orthologs

3 orthologs

OrganismSymbolGene ID
danio_reriosenp1ENSDARG00000078574
mus_musculusSenp1ENSMUSG00000033075
rattus_norvegicusSenp1ENSRNOG00000022260

Paralogs (3): SENP5 (ENSG00000119231), SENP3 (ENSG00000161956), SENP2 (ENSG00000163904)

Protein

Protein identifiers

Sentrin-specific protease 1 — Q9P0U3 (reviewed: Q9P0U3)

Alternative names: Sentrin/SUMO-specific protease SENP1

All UniProt accessions (3): Q9P0U3, F8VRZ8, F8W0I8

UniProt curated annotations — full annotation on UniProt →

Function. Protease that catalyzes two essential functions in the SUMO pathway. The first is the hydrolysis of an alpha-linked peptide bond at the C-terminal end of the small ubiquitin-like modifier (SUMO) propeptides, SUMO1, SUMO2 and SUMO3 leading to the mature form of the proteins. The second is the deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins, by cleaving an epsilon-linked peptide bond between the C-terminal glycine of the mature SUMO and the lysine epsilon-amino group of the target protein. Deconjugates SUMO1 from HIPK2. Deconjugates SUMO1 from HDAC1 and BHLHE40/DEC1, which decreases its transcriptional repression activity. Deconjugates SUMO1 from CLOCK, which decreases its transcriptional activation activity. Deconjugates SUMO2 from MTA1. Inhibits N(6)-methyladenosine (m6A) RNA methylation by mediating SUMO1 deconjugation from METTL3 and ALKBH5: METTL3 inhibits the m6A RNA methyltransferase activity, while ALKBH5 desumoylation promotes m6A demethylation. Desumoylates CCAR2 which decreases its interaction with SIRT1. Deconjugates SUMO1 from GPS2.

Subunit / interactions. Interacts with RBM33; promoting ALKBH5 desumoylation and subsequent activation.

Subcellular location. Nucleus. Cytoplasm.

Tissue specificity. Highly expressed in testis. Expressed at lower levels in thymus, pancreas, spleen, liver, ovary and small intestine.

Similarity. Belongs to the peptidase C48 family.

Isoforms (2)

UniProt IDNamesCanonical?
Q9P0U3-11yes
Q9P0U3-22

RefSeq proteins (2): NP_001254523, NP_001254524 (=MANE)

Domains & families (InterPro)

IDNameType
IPR003653Peptidase_C48_CDomain
IPR038765Papain-like_cys_pep_sfHomologous_superfamily

Pfam: PF02902

Enzyme classification (BRENDA):

  • EC 3.4.22.B70 — (BRENDA: organisms, substrates, inhibitors, Km, kcat entries)

UniProt features (60 total): mutagenesis site 14, helix 11, strand 10, region of interest 5, modified residue 4, short sequence motif 4, active site 3, sequence variant 3, turn 3, chain 1, compositionally biased region 1, splice variant 1

Structure

Experimental structures (PDB)

10 structures.

PDBMethodResolution (Å)
2XPHX-RAY DIFFRACTION2.4
2CKGX-RAY DIFFRACTION2.45
2IYCX-RAY DIFFRACTION2.45
2XREX-RAY DIFFRACTION2.45
2IY1X-RAY DIFFRACTION2.46
6NNQX-RAY DIFFRACTION2.62
2IY0X-RAY DIFFRACTION2.77
2G4DX-RAY DIFFRACTION2.8
2CKHX-RAY DIFFRACTION3.2
2IYDX-RAY DIFFRACTION3.2

Predicted structure (AlphaFold)

ModelpLDDTFraction very-high
AF-Q9P0U3-F161.600.35

Functional residue map

Curated UniProt residues grouped by drug-discovery relevance — catalytic, ligand-binding, modification, and mutation-validated positions. Source: UniProtKB sequence features.

Catalytic / active sites (3): 533; 550; 603 (nucleophile)

Post-translational modifications (4): 57, 117, 132, 157

Mutagenesis-validated functional residues (14):

PositionPhenotype
441no effect on sumo2 processing and sumo2 deconjugating activities.
465impairs sumo2 processing and sumo2 deconjugating activities.
468slightly impairs sumo2 processing activity. no effect on sumo2 deconjugating activity.
496impairs sumo2 processing activity. no effect on sumo2 deconjugating activity.
511impairs sumo2 processing activity. no effect on sumo2 deconjugating activity.
512impairs sumo2 processing and sumo2 deconjugating activities.
529impairs sumo2 processing activity. no effect on sumo2 deconjugating activity.
532no effect on sumo2 processing and sumo2 deconjugating activities.
533abolishes sumo2 processing and sumo2 deconjugating activities.
534abolishes sumo2 processing and sumo2 deconjugating activities.
550abolishes sumo2 processing and sumo2 deconjugating activities.
597abolishes sumo2 processing and sumo2 deconjugating activities.
603abolishes sumo2 processing and sumo2 deconjugating activities.
603exclusively nuclear. loss of ccar2 desumoylation.

Function

Pathways and Gene Ontology

Reactome pathways

10 pathways

IDPathway
R-HSA-3065679SUMO is proteolytically processed
R-HSA-9035034RHOF GTPase cycle
R-HSA-162582Signal Transduction
R-HSA-194315Signaling by Rho GTPases
R-HSA-2990846SUMOylation
R-HSA-3215018Processing and activation of SUMO
R-HSA-392499Metabolism of proteins
R-HSA-597592Post-translational protein modification
R-HSA-9012999RHO GTPase cycle
R-HSA-9716542Signaling by Rho GTPases, Miro GTPases and RHOBTB3

MSigDB gene sets: 238 (showing top): GOBP_MYELOID_CELL_DIFFERENTIATION, GGGACCA_MIR133A_MIR133B, TGGTGCT_MIR29A_MIR29B_MIR29C, GOBP_NEGATIVE_REGULATION_OF_PROTEOLYSIS, GOBP_REGULATION_OF_PROTEASOMAL_UBIQUITIN_DEPENDENT_PROTEIN_CATABOLIC_PROCESS, GOBP_MYELOID_CELL_HOMEOSTASIS, GOBP_REGULATION_OF_MRNA_CATABOLIC_PROCESS, MODULE_255, GRAESSMANN_APOPTOSIS_BY_SERUM_DEPRIVATION_UP, GOBP_ERYTHROCYTE_HOMEOSTASIS, GRAESSMANN_RESPONSE_TO_MC_AND_SERUM_DEPRIVATION_UP, GRAESSMANN_APOPTOSIS_BY_DOXORUBICIN_DN, GRAESSMANN_RESPONSE_TO_MC_AND_DOXORUBICIN_DN, GOBP_MACROMOLECULE_CATABOLIC_PROCESS, MODULE_317

GO Biological Process (12): regulation of definitive erythrocyte differentiation (GO:0010724), protein sumoylation (GO:0016925), protein desumoylation (GO:0016926), negative regulation of proteasomal ubiquitin-dependent protein catabolic process (GO:0032435), proteasome-mediated ubiquitin-dependent protein catabolic process (GO:0043161), regulation of mRNA stability (GO:0043488), positive regulation of transcription by RNA polymerase II (GO:0045944), regulation of postsynapse assembly (GO:0150052), proteolysis (GO:0006508), regulation of macromolecule metabolic process (GO:0060255), mRNA destabilization (GO:0061157), regulation of primary metabolic process (GO:0080090)

GO Molecular Function (7): endopeptidase activity (GO:0004175), deSUMOylase activity (GO:0016929), SUMO-specific endopeptidase activity (GO:0070139), protein binding (GO:0005515), peptidase activity (GO:0008233), cysteine-type peptidase activity (GO:0008234), hydrolase activity (GO:0016787)

GO Cellular Component (8): nucleus (GO:0005634), nucleoplasm (GO:0005654), focal adhesion (GO:0005925), nuclear membrane (GO:0031965), glutamatergic synapse (GO:0098978), presynaptic cytosol (GO:0099523), postsynaptic cytosol (GO:0099524), cytoplasm (GO:0005737)

Reactome top-level categories

Rollup of top-8 pathways:

CategoryPathways
Processing and activation of SUMO1
RHO GTPase cycle1
Signaling by Rho GTPases, Miro GTPases and RHOBTB31
Post-translational protein modification1
SUMOylation1
Metabolism of proteins1
Signaling by Rho GTPases1
Signal Transduction1

GO top-level categories

Rollup of top GO terms by namespace:

CategoryTerms
peptidyl-lysine modification2
regulation of metabolic process2
peptidase activity2
cellular anatomical structure2
cytosol2
regulation of erythrocyte differentiation1
definitive erythrocyte differentiation1
protein modification by small protein conjugation1
protein modification by small protein removal1
regulation of proteasomal ubiquitin-dependent protein catabolic process1
proteasome-mediated ubiquitin-dependent protein catabolic process1
negative regulation of proteasomal protein catabolic process1
negative regulation of ubiquitin-dependent protein catabolic process1
ubiquitin-dependent protein catabolic process1
proteasomal protein catabolic process1
regulation of RNA stability1
regulation of mRNA catabolic process1
regulation of transcription by RNA polymerase II1
transcription by RNA polymerase II1
positive regulation of DNA-templated transcription1
regulation of synapse assembly1
postsynapse assembly1
regulation of postsynapse organization1
protein metabolic process1
macromolecule metabolic process1
negative regulation of gene expression1
regulation of mRNA stability1
RNA destabilization1
positive regulation of mRNA catabolic process1
primary metabolic process1
cysteine-type peptidase activity1
ubiquitin-like protein peptidase activity1
ubiquitin-like protein-specific endopeptidase activity1
binding1
hydrolase activity1
catalytic activity, acting on a protein1
catalytic activity1
intracellular membrane-bounded organelle1
nuclear lumen1
cell-substrate junction1

Protein interactions and networks

STRING

1786 interactions, top by confidence (×1000):

Protein AProtein BPartner UniProtScore
SENP1SUMO1P55856975
SENP1SUMO2P55855946
SENP1UBE2IP50550911
SENP1SAE1Q9UBE0889
SENP1UBA2Q9UBT2851
SENP1RANGAP1P46060843
SENP1PIAS4Q8N2W9802
SENP1PIAS3Q9Y6X2778
SENP1MESDQ14696739
SENP1PIAS1O75925732
SENP1KCNK1O00180729
SENP1NEDD8Q15843724
SENP1DESI1Q6ICB0719
SENP1RNF4P78317714
SENP1SUMO4Q6EEV6698

IntAct

82 interactions, top by confidence:

ABTypeScore
RANGAP1SUMO1psi-mi:“MI:0915”(physical association)0.960
SUMO1SENP1psi-mi:“MI:0407”(direct interaction)0.870
SUMO1SENP1psi-mi:“MI:0915”(physical association)0.870
SENP1SUMO1psi-mi:“MI:0915”(physical association)0.870
SUMO1SENP1psi-mi:“MI:0194”(cleavage reaction)0.870
RANGAP1SUMO2psi-mi:“MI:0915”(physical association)0.750
SENP1SUMO2psi-mi:“MI:0407”(direct interaction)0.740
SUMO2SENP1psi-mi:“MI:0915”(physical association)0.740
KBTBD7METTL15psi-mi:“MI:0914”(association)0.730
IRAK2SESTD1psi-mi:“MI:0914”(association)0.640
PRG2YPEL5psi-mi:“MI:0914”(association)0.640
IL13RA2METTL15psi-mi:“MI:0914”(association)0.530
LRP1NME4psi-mi:“MI:0914”(association)0.530
SKP2DPYSL4psi-mi:“MI:0914”(association)0.530
BRINP3BUB1psi-mi:“MI:0914”(association)0.530
ARL11SESTD1psi-mi:“MI:0914”(association)0.530
ECEL1CANXpsi-mi:“MI:0914”(association)0.530
NRASESYT2psi-mi:“MI:2364”(proximity)0.480
SENP1SUMO3psi-mi:“MI:0194”(cleavage reaction)0.440
SNIP1SENP1psi-mi:“MI:0915”(physical association)0.400
LRBASENP1psi-mi:“MI:0915”(physical association)0.400
RIPK4VWA8psi-mi:“MI:0914”(association)0.350

BioGRID (219): USP25 (Biochemical Activity), SUMO2 (Reconstituted Complex), SUMO1 (Biochemical Activity), SUMO3 (Biochemical Activity), SUMO2 (Biochemical Activity), SUMO1 (Biochemical Activity), SUMO1 (Biochemical Activity), SUMO3 (Biochemical Activity), RABGAP1 (Biochemical Activity), SUMO1 (Reconstituted Complex), SUMO3 (Reconstituted Complex), SUMO1 (Biochemical Activity), SUMO2 (Biochemical Activity), SUMO3 (Biochemical Activity), SP100 (Biochemical Activity)

ESM2 similar proteins: A3KMX0, A6QP06, D2HXI8, E1C2I2, E2RJI4, F4KBP5, O70445, O75113, O88700, P10242, P10243, P10244, P29352, P46200, P51960, P52550, P52551, P54132, P59110, Q03237, Q05935, Q2NKX8, Q5QJC4, Q5RBB1, Q5T890, Q5ZLE9, Q60DG4, Q65Z40, Q6A037, Q6DJS0, Q6NTJ3, Q6PJP8, Q7Z5K2, Q7ZXG4, Q8BHK9, Q8BPY9, Q8C0P0, Q8K298, Q94CU5, Q96GX5

Diamond homologs: A7MBJ2, D3ZF42, O42957, O65278, P59110, Q02724, Q09353, Q5R7K7, Q5RBB1, Q6NXL6, Q6P7W0, Q8BUH8, Q8GYL3, Q8WP32, Q91ZX6, Q94F30, Q96HI0, Q9BQF6, Q9EP97, Q9EQE1, Q9GZR1, Q9H4L4, Q9HC62, Q9P0U3, Q0WKV8, Q8RWN0, O13612, O13769, Q8L7S0, Q09275, Q2PS26, Q23238

SIGNOR signaling

4 interactions.

AEffectBMechanism
SENP1up-regulatesHIF1Adesumoylation
SENP1“up-regulates activity”GCM1desumoylation
SENP1“down-regulates quantity by destabilization”AKT1desumoylation
SENP1“down-regulates quantity by destabilization”AKTdesumoylation

Enriched among interaction partners

Reactome pathways and GO biological processes over-represented among this gene’s 93 IntAct physical interaction partners (hypergeometric vs the genome-wide background, BH-FDR, gene-set size 15–500, ranked by fold). A functional readout of the neighbourhood — distinct from this gene’s own memberships above, and biased toward well-studied / hub proteins, so read it as themes rather than proof.

Reactome pathways:

PathwayPartnersFoldFDR
SUMOylation of DNA replication proteins520.7×2e-04
Signaling by BRAF and RAF1 fusions617.0×1e-04

GO biological processes:

GO termPartnersFoldFDR
protein sumoylation519.3×3e-03
proteasome-mediated ubiquitin-dependent protein catabolic process95.6×9e-03

Disease & clinical

Clinical variants and AI predictions

ClinVar

21 variants total. Per-class counts are floors (≥ shown; pagination cap):

ClassificationCount (floor)
Pathogenic0
Likely pathogenic0
Uncertain significance0
Likely benign0
Benign2

Top pathogenic / likely-pathogenic (0)

SpliceAI

2453 predictions. Top by Δscore:

VariantEffectΔscore
12:48046350:GCTCA:Gdonor_loss1.0000
12:48046351:CTCA:Cdonor_loss1.0000
12:48046352:TCA:Tdonor_loss1.0000
12:48046353:CACC:Cdonor_loss1.0000
12:48046354:A:Cdonor_loss1.0000
12:48046447:ATCTC:Aacceptor_gain1.0000
12:48046449:CTC:Cacceptor_gain1.0000
12:48046450:TC:Tacceptor_gain1.0000
12:48046451:CC:Cacceptor_gain1.0000
12:48046452:C:CCacceptor_gain1.0000
12:48046452:C:Tacceptor_loss1.0000
12:48046453:T:Aacceptor_loss1.0000
12:48046461:C:CTacceptor_gain1.0000
12:48046462:A:Tacceptor_gain1.0000
12:48046974:GTAC:Gdonor_loss1.0000
12:48046975:TACC:Tdonor_loss1.0000
12:48046977:C:Gdonor_loss1.0000
12:48046977:CCTGG:Cdonor_gain1.0000
12:48047073:C:CTacceptor_gain1.0000
12:48047991:C:CAdonor_gain1.0000
12:48047995:ACT:Adonor_loss1.0000
12:48047997:TTACA:Tdonor_loss1.0000
12:48047999:A:ACdonor_gain1.0000
12:48047999:ACAA:Adonor_loss1.0000
12:48048000:C:Adonor_loss1.0000
12:48048000:C:CAdonor_gain1.0000
12:48048000:CA:Cdonor_gain1.0000
12:48048000:CAA:Cdonor_gain1.0000
12:48048000:CAAG:Cdonor_gain1.0000
12:48048000:CAAGA:Cdonor_gain1.0000

AlphaMissense

4263 scored. Top likely-pathogenic:

VariantProtein changeam_pathogenicity
12:48046356:C:AQ624H1.000
12:48046356:C:GQ624H1.000
12:48046396:G:TA611D1.000
12:48046406:A:GC608R1.000
12:48046410:A:CF606L1.000
12:48046410:A:TF606L1.000
12:48046411:A:CF606C1.000
12:48046411:A:GF606S1.000
12:48046412:A:GF606L1.000
12:48046417:C:AG604V1.000
12:48046417:C:TG604E1.000
12:48046418:C:AG604W1.000
12:48046418:C:GG604R1.000
12:48046418:C:TG604R1.000
12:48046419:A:CC603W1.000
12:48046420:C:AC603F1.000
12:48046420:C:TC603Y1.000
12:48046421:A:GC603R1.000
12:48046422:G:CD602E1.000
12:48046422:G:TD602E1.000
12:48046423:T:AD602V1.000
12:48046423:T:CD602G1.000
12:48046423:T:GD602A1.000
12:48046424:C:GD602H1.000
12:48046431:A:CN599K1.000
12:48046431:A:TN599K1.000
12:48046432:T:AN599I1.000
12:48046437:C:AQ597H1.000
12:48046437:C:GQ597H1.000
12:48047004:A:GW584R1.000

dbSNP variants (sampled 300 via entrez): RS1000042701 (12:48069985 A>C), RS1000156233 (12:48065096 T>A,C), RS1000215278 (12:48050677 A>G), RS1000224071 (12:48095084 C>T), RS1000268385 (12:48098379 T>C), RS1000292202 (12:48102098 T>C), RS1000322883 (12:48098684 G>A), RS1000405114 (12:48088922 A>C,T), RS1000422581 (12:48047549 C>T), RS1000453828 (12:48047872 T>C), RS1000524650 (12:48082889 G>A,C), RS1000567343 (12:48050355 C>G), RS1000573673 (12:48086276 C>A), RS1000682233 (12:48076643 CT>C,CTT,CTTTT,CTTTTT,CTTTTTT), RS1000733979 (12:48088685 A>G)

Disease associations

OMIM: gene MIM:612157 | disease phenotypes:

GenCC curated gene-disease

Mondo (0):

Orphanet (0):

HPO phenotypes

0 total (0 of 0 shown, HPO-id order):

GWAS associations

8 associations (top):

StudyTraitp-value
GCST006976_65Macular thickness5.000000e-10
GCST007843_21Rheumatoid arthritis3.000000e-12
GCST007954_42Glycated hemoglobin levels1.000000e-15
GCST90002383_3Hematocrit2.000000e-18
GCST90002384_307Hemoglobin4.000000e-14
GCST90002385_227High light scatter reticulocyte count4.000000e-13
GCST90002386_322High light scatter reticulocyte percentage of red cells3.000000e-09
GCST90002405_303Reticulocyte count1.000000e-11

EFO canonical traits (4, from GWAS)

EFO IDTrait name
EFO:0004541HbA1c measurement
EFO:0004348hematocrit
EFO:0004509hemoglobin measurement
EFO:0007986reticulocyte count

Drugs & pharmacology

Drug and pharmacology data

Is drug target: yes

ChEMBL targets (2): CHEMBL1909484 (SINGLE PROTEIN), CHEMBL6066555 (PROTEIN COMPLEX)

Molecules with ChEMBL bioactivity

2 molecules (phase ≥1), by development phase (incl. off-target/promiscuous compounds). Patent mentions across the top 20 by phase: 64,162 (via chembl_molecule»patent_compound — counts attach to the compound, not the gene–compound relationship, so off-target/promiscuous molecules can dominate).

MoleculeNamePhasePatents
CHEMBL11417STREPTONIGRIN243,337
CHEMBL169URSOLIC ACID220,825

PharmGKB: 1 entry (VIP=true, CPIC=false)

GtoPdb / IUPHAR curated pharmacology

(IUPHAR/BPS Guide to Pharmacology — expert-curated)

Target class: enzyme — C48: Ulp1 endopeptidase

Most potent curated ligand interactions (1 total), top 1:

LigandActionAffinityParameter
compound 8e [PMID: 23044371]Inhibition5.73pIC50

Binding affinities (BindingDB)

146 measured of 167 human assays (198 total across all organisms); most potent 50 below. Values come from heterogeneous assays and are not directly comparable.

LigandMeasureValuePatent
4-chloro-2-[2-(2-quinolinyl)vinyl]phenyl acetateEC50836 nM
cid_53299662IC501050 nM
(5R)-3-(3-chloro-2-hydroxyphenyl)-5-(4-fluorophenyl)cyclohex-2-en-1-oneIC501140 nM
(5R)-3-(3-chloro-2-hydroxyphenyl)-5-(4-chlorophenyl)cyclohex-2-en-1-oneIC501150 nM
(5Z)-2-anilino-5-[(5-bromo-3-ethoxy-2-hydroxyphenyl)methylidene]-1,3-thiazol-4-oneIC501180 nM
(2Z)-2-(1-pentyl-2H-tetrazol-5-ylidene)benzo[g]quinoxalin-3-oneIC501290 nM
SMR000283017IC501840 nM
cid_42628166IC501930 nM
SMR002134470IC501930 nM
2-[5-(2-furanyl)-1H-1,2,4-triazol-3-yl]-1,3-dioxo-5-isoindolecarboxylic acidIC502060 nM
SPI-02IC502100 nMUS-9791447: Methods of identifying SENP1 inhibitors
SPI-04IC502400 nMUS-9791447: Methods of identifying SENP1 inhibitors
SPI-10IC502400 nMUS-9791447: Methods of identifying SENP1 inhibitors
N-benzyl-2-imino-6-nitrochromene-3-carboxamideIC502450 nM
4-amino-5-[(E)-(3-ethoxy-4-keto-cyclohexa-2,5-dien-1-ylidene)methyl]-4-thiazolin-2-oneEC502470 nM
SMR000591516IC502850 nM
4-[(Z)-(3-chloro-5-methoxy-4-oxocyclohexa-2,5-dien-1-ylidene)methyl]-1,2,3,10-tetrahydroacridine-9-carboxylic acidIC502960 nM
6-bromo-2-oxo-1-benzopyran-3-carbothioamideIC503310 nM
NSC8676IC503800 nMUS-9791447: Methods of identifying SENP1 inhibitors
NSC70551IC503900 nMUS-9791447: Methods of identifying SENP1 inhibitors
cid_2944998IC504300 nM
(5Z)-5-[(2-hydroxynaphthalen-1-yl)methylidene]imidazolidine-2,4-dioneIC504340 nM
cid_3785106IC504360 nM
MLS002302564IC504360 nM
5-(3-chlorobenzyl)-3,5-dihydro-4H-pyridazino[4,5-b]indol-4-oneIC504440 nM
Furan-2-carboxylic acid 4-(3-carboxymethyl-4-oxo-2-thioxo-thiazolidin-5-ylidenemethyl)-2-methoxy-phenyl esterIC504520 nM
cid_3307928IC504610 nM
Acetic acid 4-[4-(4-chloro-benzoyl)-1,3-dioxo-octahydro-pyrrolo[3,4-a]pyrrolizin-2-yl]-phenyl esterIC504650 nM
SMR000619901IC504750 nM
N-(4-acetamidophenyl)-2-[[2-[(5,6-dimethyl-4-thieno[2,3-d]pyrimidinyl)thio]-1-oxoethyl]-ethylamino]acetamideIC504900 nM
1-(4-methylphenyl)-4-oxidanylidene-7-phenyl-3-(phenylmethyl)pyrimido[1,2-b]pyridazin-5-ium-2-olateIC505800 nM
MLS000574264IC505840 nM
SPI-01IC505900 nMUS-9791447: Methods of identifying SENP1 inhibitors
MLS001178502IC506140 nM
2-(4-benzylpiperazin-1-yl)benzo[cd]indoleIC507010 nM
3-acetyl-5-[4-(allyloxy)-3-bromo-5-methoxybenzylidene]-2-thioxo-4-imidazolidinoneIC507010 nM
(3-azanyl-6-propan-2-yl-thieno[2,3-b]quinolin-2-yl)-(3,4-dihydro-1H-isoquinolin-2-yl)methanoneIC507080 nM
cid_1474031IC507310 nM
MLS000704595EC507650 nM
MLS000774439IC507670 nM
MLS000061945IC508040 nM
2-(1-naphthyl)-N-[2,2,2-trichloro-1-({[(2-chlorophenyl)amino]carbonothioyl}amino)ethyl]acetamideIC508360 nM
cid_51361317IC508470 nM
cid_2542429IC509060 nM
2-(7-methoxy-4-methylquinolin-2-yl)sulfanyl-1-morpholin-4-ylethanoneIC509610 nM
Benzo[cd]indol-2-yl-(4-methoxy-phenyl)-amineIC5010000 nM
SMR000543182IC5010100 nM
MLS000589038IC5010100 nM
MLS000716266IC5010200 nM
MLS000529875EC5010300 nM

ChEMBL bioactivities

114 potent at pChembl≥5 of 174 total, top 50 by pChembl (potency: 10 = 0.1 nM, 6 = 1 µM).

pChemblTypeValueUnitMolecule
8.19IC506.4nMURSOLIC ACID
6.29IC50510nMCHEMBL5185218
6.28IC50520nMSTREPTONIGRIN
6.12IC50760nMCHEMBL4780770
6.10IC50790nMCHEMBL4791433
6.03Ki930nMVIALININ A
6.00IC501000nMCHEMBL4792569
6.00IC501000nMCHEMBL5289965
5.97IC501080nMCHEMBL2159857
5.97Ki1070nMVIALININ A
5.93IC501175nMCHEMBL2159858
5.92IC501200nMCHEMBL5289965
5.90IC501260nMCHEMBL1797137
5.89IC501300nMCHEMBL4793952
5.89IC501300nMCHEMBL4776158
5.89IC501300nMCHEMBL5206456
5.89IC501300nMCHEMBL5275516
5.85IC501400nMCHEMBL5289965
5.82IC501520nMCHEMBL4587307
5.82IC501500nMCHEMBL3236516
5.80IC501600nMVIALININ A
5.79IC501640nMVIALININ A
5.76IC501735nMCHEMBL2159859
5.73IC501856nMCHEMBL2159862
5.73IC501880nMCHEMBL4781794
5.72IC501890nMVIALININ A
5.72IC501900nMVIALININ A
5.68IC502100nMCHEMBL4780586
5.68IC502100nMCHEMBL5175111
5.62IC502385nMCHEMBL2159861
5.62IC502400nMCHEMBL4796113
5.62IC502400nMCHEMBL5287963
5.62IC502400nMCHEMBL5269877
5.62IC502400nMCHEMBL2009952
5.62IC502400nMCHEMBL5315304
5.61IC502480nMCHEMBL4587307
5.60IC502500nMCHEMBL4780660
5.60IC502500nMCHEMBL3236516
5.59IC502580nMURSOLIC ACID
5.58IC502600nMCHEMBL4780417
5.58IC502600nMCHEMBL4796293
5.58IC502600nMURSOLIC ACID
5.57IC502710nMCHEMBL2012939
5.55IC502800nMCHEMBL4778697
5.54IC502900nMCHEMBL4785280
5.51IC503100nMCHEMBL4784778
5.51IC503100nMCHEMBL4792715
5.48IC503300nMCHEMBL3799152
5.46IC503500nMCHEMBL3981565
5.46IC503500nMCHEMBL4789800

PubChem BioAssay actives

109 with measured affinity, of 355 total; 50 most potent distinct compounds. Largely complementary to BindingDB; screening values are coarse (µM, 4 dp), so sub-nM hits tie at the floor.

CompoundAssayTypeValueUnit
(1S,2R,4aS,6aR,6aS,6bR,8aR,10S,12aR,14bS)-10-hydroxy-1,2,6a,6b,9,9,12a-heptamethyl-2,3,4,5,6,6a,7,8,8a,10,11,12,13,14b-tetradecahydro-1H-picene-4a-carboxylic acid1859337: Inhibition of SENP1 (unknown origin)ic500.0064uM
(1S,2R,4aS,6aR,6aS,6bR,8aR,10S,12aR,14bS)-10-hydroxy-1,2,6a,6b,9,9,12a-heptamethyl-N-[2-(methylamino)-2-oxoethyl]-2,3,4,5,6,6a,7,8,8a,10,11,12,13,14b-tetradecahydro-1H-picene-4a-carboxamide1888105: Inhibition of recombinant human SENP1 catalytic domain using RanGAP1 as substrate preincubated for 10 mins followed by substrate addition and measured after 30 mins by Western blot analysisic500.5100uM
5-amino-6-(7-amino-6-methoxy-5,8-dioxoquinolin-2-yl)-4-(2-hydroxy-3,4-dimethoxyphenyl)-3-methylpyridine-2-carboxylic acid1859338: Inhibition of human SENP1 using AMC-tagged SUMO1 as substrate incubated for 10 mins by fluorescence based analysisic500.5200uM
5-(ethylamino)-3-phenylmethoxy-N-[[3-(thiophene-2-carbonylamino)phenyl]methyl]-1-benzothiophene-2-carboxamide1741433: Inhibition of recombinant human SNEP1 (419 to 644 residues) expressed in Escherichia coli (DE3) cells using RanGAP-SUMO2 substrate preincubated for 10 mins followed by substrate addition and measured after 25 min by Coomassie blue staining based SDS-PAGE analysisic500.7600uM
5-(dimethylamino)-3-phenylmethoxy-N-[[3-(thiophene-2-carbonylamino)phenyl]methyl]-1-benzothiophene-2-carboxamide1741433: Inhibition of recombinant human SNEP1 (419 to 644 residues) expressed in Escherichia coli (DE3) cells using RanGAP-SUMO2 substrate preincubated for 10 mins followed by substrate addition and measured after 25 min by Coomassie blue staining based SDS-PAGE analysisic500.7900uM
[3,4-dihydroxy-2,5-bis(4-hydroxyphenyl)-6-(2-phenylacetyl)oxyphenyl] 2-phenylacetate1637030: Binding affinity to recombinant human 6His-tagged SENP1 catalytic domain expressed in Escherichia coliki0.9300uM
5-(methylamino)-3-phenylmethoxy-N-[[3-(thiophene-2-carbonylamino)phenyl]methyl]-1-benzothiophene-2-carboxamide1741433: Inhibition of recombinant human SNEP1 (419 to 644 residues) expressed in Escherichia coli (DE3) cells using RanGAP-SUMO2 substrate preincubated for 10 mins followed by substrate addition and measured after 25 min by Coomassie blue staining based SDS-PAGE analysisic501.0000uM
(2-cyano-6-oxo-1H-pyridin-4-yl)methyl 3-(1H-indol-5-yloxymethyl)-1-methylsulfonylindole-5-carboxylate1926188: Inhibition of human recombinant His6 tagged SENP1 catalytic domain expressed in Escherichia coli BL21 (DE3) using SUMO1-AMC as substrate incubated for 15 mins followed by substrate addition by fluorescence based analysisic501.0000uM
[2-(4-chlorophenyl)-2-oxoethyl] 4-[(3-phenylmethoxybenzoyl)amino]benzoate694180: Inhibition of recombinant His-tagged SENP1 catalytic domain expressed in Escherichia coli BL21(DE3) using His-tagged deltaRanGAP-SUMO2 as substrate incubated for 10 mins prior to substrate addition measured after 45 mins by SDS-PAGE analysisic501.0800uM
[2-(4-chlorophenyl)-2-oxoethyl] 4-[(3-bromobenzoyl)amino]benzoate694180: Inhibition of recombinant His-tagged SENP1 catalytic domain expressed in Escherichia coli BL21(DE3) using His-tagged deltaRanGAP-SUMO2 as substrate incubated for 10 mins prior to substrate addition measured after 45 mins by SDS-PAGE analysisic501.1750uM
2-[(1S,2R,4aS,6aR,6aS,6bR,8aR,10S,12aR,14bS)-10-hydroxy-1,2,6a,6b,9,9,12a-heptamethyl-2,3,4,5,6,6a,7,8,8a,10,11,12,13,14b-tetradecahydro-1H-picene-4a-carbonyl]oxyacetic acid1888105: Inhibition of recombinant human SENP1 catalytic domain using RanGAP1 as substrate preincubated for 10 mins followed by substrate addition and measured after 30 mins by Western blot analysisic501.2600uM
[2-(4-chlorophenyl)-2-oxoethyl] 4-(1-benzothiophene-2-carbonylamino)benzoate1926186: Inhibition of SENP1 (unknown origin)ic501.3000uM
ethyl 2-[[3-phenylmethoxy-2-[[3-(thiophene-2-carbonylamino)phenyl]methylcarbamoyl]-1-benzothiophen-5-yl]amino]acetate1741433: Inhibition of recombinant human SNEP1 (419 to 644 residues) expressed in Escherichia coli (DE3) cells using RanGAP-SUMO2 substrate preincubated for 10 mins followed by substrate addition and measured after 25 min by Coomassie blue staining based SDS-PAGE analysisic501.3000uM
3-phenylmethoxy-N-[[3-(thiophene-2-carbonylamino)phenyl]methyl]-1-benzothiophene-2-carboxamide1741433: Inhibition of recombinant human SNEP1 (419 to 644 residues) expressed in Escherichia coli (DE3) cells using RanGAP-SUMO2 substrate preincubated for 10 mins followed by substrate addition and measured after 25 min by Coomassie blue staining based SDS-PAGE analysisic501.3000uM
[3-[(E)-4-(4-chlorophenoxy)-3-oxobut-1-enyl]-2-oxo-3,3a,4,5,6,6a-hexahydrocyclopenta[b]furan-5-yl] 4-phenylbenzoate1859349: Inhibition of SENP1 (unknown origin) assessed as reduction in deSUMOylation of RanGAP1-SUMO2 using RanGAP1-SUMO2 as substrate preincubated for 10 mins followed by substrate addition and measured after 45 mins by coomassie brilliant blue staining based SDS-PAGE analysisic501.3000uM
[4,5-dihydroxy-2-(4-hydroxybenzoyl)oxy-3,6-bis(4-hydroxyphenyl)phenyl] 4-hydroxybenzoate1926195: Inhibition of human SENP1 catalytic domain assessed as reduction in deSUMOylation of RanGAP1-SUMO2 using RanGAP1-SUMO2 as substrate by fluorescence based analysisic501.5000uM
[3,4-dihydroxy-2,5-bis(4-hydroxyphenyl)-6-[2-(4-hydroxyphenyl)acetyl]oxyphenyl] 2-(4-hydroxyphenyl)acetate1637028: Inhibition of recombinant human 6His-tagged SENP1 catalytic domain expressed in Escherichia coli preincubated for 15 mins followed by addition of SUMO1-AMC as substrate measured after 1 hr by fluorescence analysisic501.5200uM
[2-(4-chlorophenyl)-2-oxoethyl] 4-[(3-fluorobenzoyl)amino]benzoate694180: Inhibition of recombinant His-tagged SENP1 catalytic domain expressed in Escherichia coli BL21(DE3) using His-tagged deltaRanGAP-SUMO2 as substrate incubated for 10 mins prior to substrate addition measured after 45 mins by SDS-PAGE analysisic501.7350uM
[2-(4-chlorophenyl)-2-oxoethyl] 4-[(3-nitrobenzoyl)amino]benzoate694180: Inhibition of recombinant His-tagged SENP1 catalytic domain expressed in Escherichia coli BL21(DE3) using His-tagged deltaRanGAP-SUMO2 as substrate incubated for 10 mins prior to substrate addition measured after 45 mins by SDS-PAGE analysisic501.8560uM
4-amino-3-[[4-[4-[(1-amino-4-sulfonaphthalen-2-yl)diazenyl]-2-methylphenyl]-3-methylphenyl]diazenyl]naphthalene-1-sulfonic acid1800082: SUMO Cleavage Assay from Article 10.1021/cb400177q: “Identification and Characterization of a New Chemotype of Noncovalent SENP Inhibitors.”ic501.8600uM
2-[(E)-2-[4-[(2-aminonaphthalen-1-yl)diazenyl]-2-sulfophenyl]ethenyl]-5-(naphthalen-1-yldiazenyl)benzenesulfonic acid1741429: Inhibition of human His-tagged SENP1 (419 to 644 residues) expressed in Escherichia coli (DE3) cells using DUB-Glo as substrate preincubated for 10 mins followed by substrate addition and measured after 30 mins by luciferase assayic501.8800uM
5-[(2-aminonaphthalen-1-yl)diazenyl]-2-[(E)-2-[4-[(2-aminonaphthalen-1-yl)diazenyl]-2-sulfophenyl]ethenyl]benzenesulfonic acid1800082: SUMO Cleavage Assay from Article 10.1021/cb400177q: “Identification and Characterization of a New Chemotype of Noncovalent SENP Inhibitors.”ic501.8800uM
3-amino-4-[[4-[4-[(2-amino-6-sulfonaphthalen-1-yl)diazenyl]-3-methylphenyl]-2-methylphenyl]diazenyl]naphthalene-2,7-disulfonic acid1800082: SUMO Cleavage Assay from Article 10.1021/cb400177q: “Identification and Characterization of a New Chemotype of Noncovalent SENP Inhibitors.”ic502.0800uM
5-amino-3-phenylmethoxy-N-[[3-(thiophene-2-carbonylamino)phenyl]methyl]-1-benzothiophene-2-carboxamide1741433: Inhibition of recombinant human SNEP1 (419 to 644 residues) expressed in Escherichia coli (DE3) cells using RanGAP-SUMO2 substrate preincubated for 10 mins followed by substrate addition and measured after 25 min by Coomassie blue staining based SDS-PAGE analysisic502.1000uM
5-amino-8-[[4-[(E)-2-[4-[(4-amino-7-sulfonaphthalen-1-yl)diazenyl]-2-sulfophenyl]ethenyl]-3-sulfophenyl]diazenyl]naphthalene-2-sulfonate1800082: SUMO Cleavage Assay from Article 10.1021/cb400177q: “Identification and Characterization of a New Chemotype of Noncovalent SENP Inhibitors.”ic502.3200uM
[2-(4-chlorophenyl)-2-oxoethyl] 4-[(3-methoxybenzoyl)amino]benzoate694180: Inhibition of recombinant His-tagged SENP1 catalytic domain expressed in Escherichia coli BL21(DE3) using His-tagged deltaRanGAP-SUMO2 as substrate incubated for 10 mins prior to substrate addition measured after 45 mins by SDS-PAGE analysisic502.3850uM
N-[(3-benzamidophenyl)methyl]-3-phenylmethoxy-1-benzothiophene-2-carboxamide1741433: Inhibition of recombinant human SNEP1 (419 to 644 residues) expressed in Escherichia coli (DE3) cells using RanGAP-SUMO2 substrate preincubated for 10 mins followed by substrate addition and measured after 25 min by Coomassie blue staining based SDS-PAGE analysisic502.4000uM
1713438671926186: Inhibition of SENP1 (unknown origin)ic502.4000uM
241860381926186: Inhibition of SENP1 (unknown origin)ic502.4000uM
3-phenylmethoxy-N-[[3-[[4-(trifluoromethyl)benzoyl]amino]phenyl]methyl]-1-benzothiophene-2-carboxamide1741433: Inhibition of recombinant human SNEP1 (419 to 644 residues) expressed in Escherichia coli (DE3) cells using RanGAP-SUMO2 substrate preincubated for 10 mins followed by substrate addition and measured after 25 min by Coomassie blue staining based SDS-PAGE analysisic502.5000uM
N-[[3-[(3-methoxybenzoyl)amino]phenyl]methyl]-3-phenylmethoxy-1-benzothiophene-2-carboxamide1741433: Inhibition of recombinant human SNEP1 (419 to 644 residues) expressed in Escherichia coli (DE3) cells using RanGAP-SUMO2 substrate preincubated for 10 mins followed by substrate addition and measured after 25 min by Coomassie blue staining based SDS-PAGE analysisic502.6000uM
3-phenylmethoxy-5-(prop-2-enoylamino)-N-[[3-(thiophene-2-carbonylamino)phenyl]methyl]-1-benzothiophene-2-carboxamide1741433: Inhibition of recombinant human SNEP1 (419 to 644 residues) expressed in Escherichia coli (DE3) cells using RanGAP-SUMO2 substrate preincubated for 10 mins followed by substrate addition and measured after 25 min by Coomassie blue staining based SDS-PAGE analysisic502.6000uM
3,6-bis(4-hydroxyphenyl)-4,5-dimethylbenzene-1,2-diol1637029: Inhibition of full-length recombinant human 6His-tagged SENP1 expressed in Escherichia coli BL21 (DE3) preincubated for 15 mins followed by addition of SUMO1-AMC as substrate measured after 1 hr by fluorescence analysisic502.7100uM
N-[[3-[(3,4-difluorobenzoyl)amino]phenyl]methyl]-3-phenylmethoxy-1-benzothiophene-2-carboxamide1741433: Inhibition of recombinant human SNEP1 (419 to 644 residues) expressed in Escherichia coli (DE3) cells using RanGAP-SUMO2 substrate preincubated for 10 mins followed by substrate addition and measured after 25 min by Coomassie blue staining based SDS-PAGE analysisic502.8000uM
N-[[3-(naphthalene-2-carbonylamino)phenyl]methyl]-3-phenylmethoxy-1-benzothiophene-2-carboxamide1741433: Inhibition of recombinant human SNEP1 (419 to 644 residues) expressed in Escherichia coli (DE3) cells using RanGAP-SUMO2 substrate preincubated for 10 mins followed by substrate addition and measured after 25 min by Coomassie blue staining based SDS-PAGE analysisic502.9000uM
N-[[3-[(3-bromobenzoyl)amino]phenyl]methyl]-3-phenylmethoxy-1-benzothiophene-2-carboxamide1741433: Inhibition of recombinant human SNEP1 (419 to 644 residues) expressed in Escherichia coli (DE3) cells using RanGAP-SUMO2 substrate preincubated for 10 mins followed by substrate addition and measured after 25 min by Coomassie blue staining based SDS-PAGE analysisic503.1000uM
N-[[3-[(3,4-dimethoxybenzoyl)amino]phenyl]methyl]-3-phenylmethoxy-1-benzothiophene-2-carboxamide1741433: Inhibition of recombinant human SNEP1 (419 to 644 residues) expressed in Escherichia coli (DE3) cells using RanGAP-SUMO2 substrate preincubated for 10 mins followed by substrate addition and measured after 25 min by Coomassie blue staining based SDS-PAGE analysisic503.1000uM
3-phenyl-N-[[3-[[(E)-3-phenylprop-2-enoyl]amino]phenyl]methyl]benzamide1297528: Inhibition of human recombinant His-tagged SENP1 (419 to 644 residues) expressed in Escherichia coli BL21 (DE3) using RanGAP-SUMO as substrate incubated for 10 mins prior to substrate addition followed by further 25 mins incubation by coomassie blue staining based SDS-PAGE/Odyssey infrared scanning assayic503.3000uM
3-(4-methoxyphenyl)-N-[[3-(3-phenylpropanoylamino)phenyl]methyl]benzamide1324837: Inhibition of SENP1 catalytic domain (419 to 644 residues) (unknown origin) expressed in Escherichia coli BL21 (DE3) assessed as reduction in deSUMOylation preincubated for 10 mins followed by addition of RanGAP-SUMO as substrate measured after 25 mins by coomassie staining-based SDS-PAGE analysisic503.5000uM
N-[[3-[(4-nitrobenzoyl)amino]phenyl]methyl]-3-phenylmethoxy-1-benzothiophene-2-carboxamide1741433: Inhibition of recombinant human SNEP1 (419 to 644 residues) expressed in Escherichia coli (DE3) cells using RanGAP-SUMO2 substrate preincubated for 10 mins followed by substrate addition and measured after 25 min by Coomassie blue staining based SDS-PAGE analysisic503.5000uM
[2-(4-chlorophenyl)-2-oxoethyl] 4-benzamidobenzoate694180: Inhibition of recombinant His-tagged SENP1 catalytic domain expressed in Escherichia coli BL21(DE3) using His-tagged deltaRanGAP-SUMO2 as substrate incubated for 10 mins prior to substrate addition measured after 45 mins by SDS-PAGE analysisic503.5420uM
N-[[3-[(2-methylbenzoyl)amino]phenyl]methyl]-3-phenylmethoxy-1-benzothiophene-2-carboxamide1741433: Inhibition of recombinant human SNEP1 (419 to 644 residues) expressed in Escherichia coli (DE3) cells using RanGAP-SUMO2 substrate preincubated for 10 mins followed by substrate addition and measured after 25 min by Coomassie blue staining based SDS-PAGE analysisic503.6000uM
6-methoxy-3-phenylmethoxy-N-[[3-(thiophene-2-carbonylamino)phenyl]methyl]-1-benzothiophene-2-carboxamide1741433: Inhibition of recombinant human SNEP1 (419 to 644 residues) expressed in Escherichia coli (DE3) cells using RanGAP-SUMO2 substrate preincubated for 10 mins followed by substrate addition and measured after 25 min by Coomassie blue staining based SDS-PAGE analysisic503.6000uM
[3-[[2-[[(3S)-2-[[(2S)-5-amino-2-[[2-(4-hydroxy-3-nitrophenyl)acetyl]amino]-5-oxopentanoyl]amino]-3-hydroxybutanoyl]amino]acetyl]amino]-2-oxopropyl] anthracene-9-carboxylate1799555: Fluorogenic Assay from Article 10.1016/j.chembiol.2011.05.008: “Development of small molecule inhibitors and probes of human SUMO deconjugating proteases.”ic503.6000uM
[2-(methylcarbamoyl)-6-oxo-1H-pyridin-4-yl]methyl 3-(1H-indol-5-yloxymethyl)-1-methylsulfonylindole-5-carboxylate1926188: Inhibition of human recombinant His6 tagged SENP1 catalytic domain expressed in Escherichia coli BL21 (DE3) using SUMO1-AMC as substrate incubated for 15 mins followed by substrate addition by fluorescence based analysisic503.7000uM
2,5-dihydroxy-3,6-bis(4-hydroxyphenyl)cyclohexa-2,5-diene-1,4-dione1637029: Inhibition of full-length recombinant human 6His-tagged SENP1 expressed in Escherichia coli BL21 (DE3) preincubated for 15 mins followed by addition of SUMO1-AMC as substrate measured after 1 hr by fluorescence analysisic503.7900uM
N-[[3-[(3-aminobenzoyl)amino]phenyl]methyl]-3-phenylmethoxy-1-benzothiophene-2-carboxamide1741433: Inhibition of recombinant human SNEP1 (419 to 644 residues) expressed in Escherichia coli (DE3) cells using RanGAP-SUMO2 substrate preincubated for 10 mins followed by substrate addition and measured after 25 min by Coomassie blue staining based SDS-PAGE analysisic503.8000uM
N-[[3-[(3-chlorobenzoyl)amino]phenyl]methyl]-3-phenylmethoxy-1-benzothiophene-2-carboxamide1741433: Inhibition of recombinant human SNEP1 (419 to 644 residues) expressed in Escherichia coli (DE3) cells using RanGAP-SUMO2 substrate preincubated for 10 mins followed by substrate addition and measured after 25 min by Coomassie blue staining based SDS-PAGE analysisic503.8000uM
1713514601926186: Inhibition of SENP1 (unknown origin)ic503.8000uM
5-[(2-chloroacetyl)amino]-3-phenylmethoxy-N-[[3-(thiophene-2-carbonylamino)phenyl]methyl]-1-benzothiophene-2-carboxamide1741433: Inhibition of recombinant human SNEP1 (419 to 644 residues) expressed in Escherichia coli (DE3) cells using RanGAP-SUMO2 substrate preincubated for 10 mins followed by substrate addition and measured after 25 min by Coomassie blue staining based SDS-PAGE analysisic503.9000uM

CTD chemical–gene interactions

43 total (human), top 30 by PubMed support.

ChemicalActions (top 5)PubMed papers
Arsenicaffects reaction, increases expression, decreases reaction, increases reaction, decreases expression (+3 more)3
(+)-JQ1 compounddecreases expression2
Arsenic Trioxideincreases ubiquitination, affects binding, decreases reaction, affects reaction, increases reaction (+1 more)2
Oxygenaffects reaction, increases expression, decreases abundance, decreases expression2
Cadmium Chlorideincreases expression, decreases reaction, decreases expression, increases abundance2
CB-5083affects binding, decreases reaction, increases reaction, increases ubiquitination1
FR900359decreases phosphorylation1
TAK-243decreases sumoylation1
geldanamycinincreases expression1
triphenyl phosphateaffects expression1
testosterone undecanoateaffects cotreatment, increases expression1
trichostatin Adecreases expression1
cobaltous chloridedecreases abundance, decreases expression1
coumarinincreases phosphorylation1
4-aminophenylarsenoxideaffects binding, decreases reaction1
testosterone-3-carboxymethyloxime-bovine serum albumin conjugateincreases expression1
hinokiflavonedecreases activity1
abrineincreases expression1
2-methyl-2H-pyrazole-3-carboxylic acid (2-methyl-4-o-tolylazophenyl)amidedecreases expression, decreases reaction1
jinfukangdecreases expression1
Oxaliplatindecreases expression1
Air Pollutantsaffects expression, increases abundance1
Vehicle Emissionsdecreases expression, decreases reaction1
Benzo(a)pyreneincreases methylation1
Cadmiumdecreases expression, increases abundance1
Coumestrolincreases expression1
Doxorubicindecreases expression1
Ethyl Methanesulfonateincreases expression1
Ethylmaleimideaffects binding, decreases reaction1
Hydrogen Peroxideaffects expression1

ChEMBL screening assays

47 unique, capped per target: 45 binding, 2 functional

Representative assays (with source publication via chembl_document):

Assay IDTypeDescriptionSource paper
CHEMBL1913304BindingInhibition of histidine-tagged human SENP1 catalytic domain at 20 uM preincubated for 10 mins by SUMO-CHOP-PLA2 reporter fluorescence assayDesign, synthesis, and biological evaluation of benzodiazepine-based SUMO-specific protease 1 inhibitors. — Bioorg Med Chem Lett
CHEMBL2114742FunctionalPubChem BioAssay. Dose response confirmation of small molecule inhibitors of the catalytic domain of the SUMO protease, SENP1 in a kinetic FRET assay. (Class of assay: confirmatory)PubChem BioAssay data set

Cellosaurus cell lines

3 cell lines: 3 cancer cell line

First 10 cell lines (id-ordered, not curated):

CellosaurusNameCategorySex
CVCL_B8P8Abcam HCT 116 SENP1 KOCancer cell lineMale
CVCL_B9RLAbcam A-549 SENP1 KOCancer cell lineMale
CVCL_TK56HAP1 SENP1 (-)Cancer cell lineMale

Clinical trials (associated diseases)

0 trials via MONDO — disease-level, not drug-specific.

No linked Atlas pages yet — the cross-entity mesh grows as the corpus expands.

About this page

Generated deterministically by Sugi Atlas from primary biomedical databases via BioBTree. Every record on this page traces to a primary source.

Generated
Atlas version
v1.1.4
BioBTree
v2.0.2

Sources 81

This page pulls from 81 datasets indexed by BioBTree:

alphafoldalphamissenseantibodybgeebgee_evidencebindingdbbiogrid_interactionbrendabrenda_kineticsccdscellosauruschembl_activitychembl_assaychembl_documentchembl_moleculechembl_targetciviccivic_evidenceclingen_dosageclingen_gene_validityclinical_trialsclinvarcollectrictd_gene_interactiondbsnpdepmapdiamond_similarityefoensemblentrezesm2_similarityexonfantom5_genefantom5_promotergenccgenerifgogoparentgtopdbgtopdb_interactiongwasgwas_studyhgnchpointactinterprointogenjasparmeshmimmirdbmondomsigdborphanetorthologparalogpatentpatent_compoundpdbpfampharmgkb_clinicalpharmgkb_genepharmgkb_guidelinepharmgkb_variantpubchempubchem_activitypubchem_assaypubmedreactomereactomeparentrefseqrhearnacentralscxa_expressionscxa_gene_experimentsignorspliceaistring_interactiontranscriptufeatureuniprot