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Protein

Sentrin-specific protease 1

Gene

SENP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SUMO1, SUMO2 and SUMO3 to their mature forms and deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins. 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. Desumoylates CCAR2 which decreases its interaction with SIRT1 (PubMed:25406032).8 Publications

Catalytic activityi

Hydrolysis of the alpha-linked peptide bond in the sequence Gly-Gly-|-Ala-Thr-Tyr at the C-terminal end of the small ubiquitin-like modifier (SUMO) propeptide, Smt3, leading to the mature form of the protein. A second reaction involves the cleavage of an epsilon-linked peptide bond between the C-terminal glycine of the mature SUMO and the lysine epsilon-amino group of the target protein.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei5331
Active sitei5501
Active sitei603Nucleophile1

GO - Molecular functioni

GO - Biological processi

  • activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • apoptotic signaling pathway Source: UniProtKB
  • negative regulation of proteasomal ubiquitin-dependent protein catabolic process Source: Ensembl
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • protein desumoylation Source: UniProtKB
  • protein sumoylation Source: Reactome
  • proteolysis Source: ProtInc
  • regulation of definitive erythrocyte differentiation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

BioCyciZFISH:ENSG00000079387-MONOMER.
BRENDAi3.4.22.B70. 2681.
ReactomeiR-HSA-3065679. SUMO is proteolytically processed.
SIGNORiQ9P0U3.

Protein family/group databases

MEROPSiC48.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Sentrin-specific protease 1 (EC:3.4.22.68)
Alternative name(s):
Sentrin/SUMO-specific protease SENP1
Gene namesi
Name:SENP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:17927. SENP1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi441D → A: No effect on SUMO2 processing and SUMO2 deconjugating activities. 1 Publication1
Mutagenesisi465W → A: Impairs SUMO2 processing and SUMO2 deconjugating activities. 1 Publication1
Mutagenesisi468D → A: Slightly impairs SUMO2 processing activity. No effect on SUMO2 deconjugating activity. 1 Publication1
Mutagenesisi496F → A: Impairs SUMO2 processing activity. No effect on SUMO2 deconjugating activity. 1 Publication1
Mutagenesisi511R → A: Impairs SUMO2 processing activity. No effect on SUMO2 deconjugating activity. 1 Publication1
Mutagenesisi512W → A: Impairs SUMO2 processing and SUMO2 deconjugating activities. 1 Publication1
Mutagenesisi529H → A: Impairs SUMO2 processing activity. No effect on SUMO2 deconjugating activity. 1 Publication1
Mutagenesisi532V → A: No effect on SUMO2 processing and SUMO2 deconjugating activities. 1 Publication1
Mutagenesisi533H → A: Abolishes SUMO2 processing and SUMO2 deconjugating activities. 1 Publication1
Mutagenesisi534W → A: Abolishes SUMO2 processing and SUMO2 deconjugating activities. 1 Publication1
Mutagenesisi550D → A: Abolishes SUMO2 processing and SUMO2 deconjugating activities. 1 Publication1
Mutagenesisi597Q → A: Abolishes SUMO2 processing and SUMO2 deconjugating activities. 1 Publication1
Mutagenesisi603C → A or S: Abolishes SUMO2 processing and SUMO2 deconjugating activities. 3 Publications1
Mutagenesisi603C → S: Exclusively nuclear. Loss of CCAR2 desumoylation. 4 Publications1

Organism-specific databases

DisGeNETi29843.
OpenTargetsiENSG00000079387.
PharmGKBiPA134947038.

Chemistry databases

ChEMBLiCHEMBL1909484.
GuidetoPHARMACOLOGYi2414.

Polymorphism and mutation databases

BioMutaiSENP1.
DMDMi215273882.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001017161 – 644Sentrin-specific protease 1Add BLAST644

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei57PhosphoserineCombined sources1
Modified residuei117PhosphoserineCombined sources1
Modified residuei132PhosphoserineCombined sources1
Modified residuei157PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9P0U3.
MaxQBiQ9P0U3.
PaxDbiQ9P0U3.
PeptideAtlasiQ9P0U3.
PRIDEiQ9P0U3.

PTM databases

iPTMnetiQ9P0U3.
PhosphoSitePlusiQ9P0U3.

Expressioni

Tissue specificityi

Highly expressed in testis. Expressed at lower levels in thymus, pancreas, spleen, liver, ovary and small intestine.1 Publication

Gene expression databases

BgeeiENSG00000079387.
CleanExiHS_SENP1.
ExpressionAtlasiQ9P0U3. baseline and differential.
GenevisibleiQ9P0U3. HS.

Organism-specific databases

HPAiHPA011765.
HPA046491.

Interactioni

Subunit structurei

Interacts with MTA1. Interacts with CCAR2 (via N-terminus).5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SUMO1P631654EBI-2822935,EBI-80140

Protein-protein interaction databases

BioGridi118930. 52 interactors.
DIPiDIP-29252N.
IntActiQ9P0U3. 16 interactors.
MINTiMINT-1714015.
STRINGi9606.ENSP00000394791.

Chemistry databases

BindingDBiQ9P0U3.

Structurei

Secondary structure

1644
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi425 – 434Combined sources10
Beta strandi435 – 438Combined sources4
Beta strandi445 – 447Combined sources3
Beta strandi450 – 452Combined sources3
Helixi454 – 458Combined sources5
Helixi468 – 481Combined sources14
Beta strandi482 – 484Combined sources3
Beta strandi490 – 492Combined sources3
Turni495 – 498Combined sources4
Helixi499 – 502Combined sources4
Helixi506 – 509Combined sources4
Turni510 – 515Combined sources6
Helixi518 – 520Combined sources3
Beta strandi521 – 530Combined sources10
Beta strandi533 – 540Combined sources8
Turni541 – 544Combined sources4
Beta strandi545 – 549Combined sources5
Helixi557 – 575Combined sources19
Beta strandi585 – 588Combined sources4
Beta strandi591 – 594Combined sources4
Helixi600 – 602Combined sources3
Helixi603 – 615Combined sources13
Helixi624 – 626Combined sources3
Helixi627 – 640Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CKGX-ray2.45A/B419-644[»]
2CKHX-ray3.20A419-644[»]
2G4DX-ray2.80A/C440-644[»]
2IY0X-ray2.77A419-643[»]
2IY1X-ray2.46A/C419-643[»]
2IYCX-ray2.45A/B419-643[»]
2IYDX-ray3.20A419-643[»]
2XPHX-ray2.40A/B415-644[»]
2XREX-ray2.45A/B415-644[»]
ProteinModelPortaliQ9P0U3.
SMRiQ9P0U3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9P0U3.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 200Interaction with CCAR21 PublicationAdd BLAST200
Regioni450 – 613ProteaseAdd BLAST164

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi171 – 177Nuclear localization signal1 Publication7
Motifi574 – 577Nuclear localization signalSequence analysis4
Motifi628 – 634Nuclear localization signalSequence analysis7
Motifi635 – 644Nuclear export signalCurated10

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi45 – 170Ser-richAdd BLAST126
Compositional biasi290 – 300His-richAdd BLAST11

Sequence similaritiesi

Belongs to the peptidase C48 family.Curated

Phylogenomic databases

eggNOGiKOG0778. Eukaryota.
COG5160. LUCA.
GeneTreeiENSGT00530000062941.
HOGENOMiHOG000154286.
HOVERGENiHBG057384.
InParanoidiQ9P0U3.
KOiK08592.
OMAiVNHNSIF.
OrthoDBiEOG091G092N.
PhylomeDBiQ9P0U3.
TreeFamiTF316289.

Family and domain databases

InterProiIPR003653. Peptidase_C48_C.
IPR033387. SENP1.
[Graphical view]
PANTHERiPTHR12606:SF30. PTHR12606:SF30. 1 hit.
PfamiPF02902. Peptidase_C48. 1 hit.
[Graphical view]
PROSITEiPS50600. ULP_PROTEASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9P0U3-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDDIADRMRM DAGEVTLVNH NSVFKTHLLP QTGFPEDQLS LSDQQILSSR
60 70 80 90 100
QGHLDRSFTC STRSAAYNPS YYSDNPSSDS FLGSGDLRTF GQSANGQWRN
110 120 130 140 150
STPSSSSSLQ KSRNSRSLYL ETRKTSSGLS NSFAGKSNHH CHVSAYEKSF
160 170 180 190 200
PIKPVPSPSW SGSCRRSLLS PKKTQRRHVS TAEETVQEEE REIYRQLLQM
210 220 230 240 250
VTGKQFTIAK PTTHFPLHLS RCLSSSKNTL KDSLFKNGNS CASQIIGSDT
260 270 280 290 300
SSSGSASILT NQEQLSHSVY SLSSYTPDVA FGSKDSGTLH HPHHHHSVPH
310 320 330 340 350
QPDNLAASNT QSEGSDSVIL LKVKDSQTPT PSSTFFQAEL WIKELTSVYD
360 370 380 390 400
SRARERLRQI EEQKALALQL QNQRLQEREH SVHDSVELHL RVPLEKEIPV
410 420 430 440 450
TVVQETQKKG HKLTDSEDEF PEITEEMEKE IKNVFRNGNQ DEVLSEAFRL
460 470 480 490 500
TITRKDIQTL NHLNWLNDEI INFYMNMLME RSKEKGLPSV HAFNTFFFTK
510 520 530 540 550
LKTAGYQAVK RWTKKVDVFS VDILLVPIHL GVHWCLAVVD FRKKNITYYD
560 570 580 590 600
SMGGINNEAC RILLQYLKQE SIDKKRKEFD TNGWQLFSKK SQEIPQQMNG
610 620 630 640
SDCGMFACKY ADCITKDRPI NFTQQHMPYF RKRMVWEILH RKLL
Length:644
Mass (Da):73,481
Last modified:November 25, 2008 - v2
Checksum:i941951A8B341EC64
GO
Isoform 2 (identifier: Q9P0U3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     593-593: Missing.

Note: No experimental confirmation available.
Show »
Length:643
Mass (Da):73,351
Checksum:i1556864F1BDEE337
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_029648193I → V.1 PublicationCorresponds to variant rs17854369dbSNPEnsembl.1
Natural variantiVAR_047547280A → T.Corresponds to variant rs35130318dbSNPEnsembl.1
Natural variantiVAR_029649350D → G.1 PublicationCorresponds to variant rs17854368dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_035777593Missing in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF149770 mRNA. Translation: AAF31171.1.
AK292060 mRNA. Translation: BAF84749.1.
AC074029 Genomic DNA. No translation available.
BC045639 mRNA. Translation: AAH45639.2.
CCDSiCCDS44868.2. [Q9P0U3-1]
RefSeqiNP_001254523.1. NM_001267594.1. [Q9P0U3-1]
NP_001254524.1. NM_001267595.1. [Q9P0U3-1]
UniGeneiHs.371957.

Genome annotation databases

EnsembliENST00000448372; ENSP00000394791; ENSG00000079387. [Q9P0U3-1]
ENST00000549518; ENSP00000447328; ENSG00000079387. [Q9P0U3-1]
ENST00000549595; ENSP00000450076; ENSG00000079387. [Q9P0U3-2]
GeneIDi29843.
KEGGihsa:29843.
UCSCiuc001rqx.5. human. [Q9P0U3-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF149770 mRNA. Translation: AAF31171.1.
AK292060 mRNA. Translation: BAF84749.1.
AC074029 Genomic DNA. No translation available.
BC045639 mRNA. Translation: AAH45639.2.
CCDSiCCDS44868.2. [Q9P0U3-1]
RefSeqiNP_001254523.1. NM_001267594.1. [Q9P0U3-1]
NP_001254524.1. NM_001267595.1. [Q9P0U3-1]
UniGeneiHs.371957.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CKGX-ray2.45A/B419-644[»]
2CKHX-ray3.20A419-644[»]
2G4DX-ray2.80A/C440-644[»]
2IY0X-ray2.77A419-643[»]
2IY1X-ray2.46A/C419-643[»]
2IYCX-ray2.45A/B419-643[»]
2IYDX-ray3.20A419-643[»]
2XPHX-ray2.40A/B415-644[»]
2XREX-ray2.45A/B415-644[»]
ProteinModelPortaliQ9P0U3.
SMRiQ9P0U3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118930. 52 interactors.
DIPiDIP-29252N.
IntActiQ9P0U3. 16 interactors.
MINTiMINT-1714015.
STRINGi9606.ENSP00000394791.

Chemistry databases

BindingDBiQ9P0U3.
ChEMBLiCHEMBL1909484.
GuidetoPHARMACOLOGYi2414.

Protein family/group databases

MEROPSiC48.002.

PTM databases

iPTMnetiQ9P0U3.
PhosphoSitePlusiQ9P0U3.

Polymorphism and mutation databases

BioMutaiSENP1.
DMDMi215273882.

Proteomic databases

EPDiQ9P0U3.
MaxQBiQ9P0U3.
PaxDbiQ9P0U3.
PeptideAtlasiQ9P0U3.
PRIDEiQ9P0U3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000448372; ENSP00000394791; ENSG00000079387. [Q9P0U3-1]
ENST00000549518; ENSP00000447328; ENSG00000079387. [Q9P0U3-1]
ENST00000549595; ENSP00000450076; ENSG00000079387. [Q9P0U3-2]
GeneIDi29843.
KEGGihsa:29843.
UCSCiuc001rqx.5. human. [Q9P0U3-1]

Organism-specific databases

CTDi29843.
DisGeNETi29843.
GeneCardsiSENP1.
HGNCiHGNC:17927. SENP1.
HPAiHPA011765.
HPA046491.
MIMi612157. gene.
neXtProtiNX_Q9P0U3.
OpenTargetsiENSG00000079387.
PharmGKBiPA134947038.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0778. Eukaryota.
COG5160. LUCA.
GeneTreeiENSGT00530000062941.
HOGENOMiHOG000154286.
HOVERGENiHBG057384.
InParanoidiQ9P0U3.
KOiK08592.
OMAiVNHNSIF.
OrthoDBiEOG091G092N.
PhylomeDBiQ9P0U3.
TreeFamiTF316289.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000079387-MONOMER.
BRENDAi3.4.22.B70. 2681.
ReactomeiR-HSA-3065679. SUMO is proteolytically processed.
SIGNORiQ9P0U3.

Miscellaneous databases

ChiTaRSiSENP1. human.
EvolutionaryTraceiQ9P0U3.
GeneWikiiSENP1.
GenomeRNAii29843.
PROiQ9P0U3.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000079387.
CleanExiHS_SENP1.
ExpressionAtlasiQ9P0U3. baseline and differential.
GenevisibleiQ9P0U3. HS.

Family and domain databases

InterProiIPR003653. Peptidase_C48_C.
IPR033387. SENP1.
[Graphical view]
PANTHERiPTHR12606:SF30. PTHR12606:SF30. 1 hit.
PfamiPF02902. Peptidase_C48. 1 hit.
[Graphical view]
PROSITEiPS50600. ULP_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSENP1_HUMAN
AccessioniPrimary (citable) accession number: Q9P0U3
Secondary accession number(s): A8K7P5, Q86XC8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2002
Last sequence update: November 25, 2008
Last modified: November 30, 2016
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.