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Q9P0U3 (SENP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sentrin-specific protease 1

EC=3.4.22.68
Alternative name(s):
Sentrin/SUMO-specific protease SENP1
Gene names
Name:SENP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length644 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.6 Ref.8 Ref.10 Ref.11 Ref.12

Catalytic activity

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.

Subcellular location

Nucleus. Cytoplasm. Note: Shuttles between cytoplasm and nucleus. Ref.1 Ref.5 Ref.8

Tissue specificity

Highly expressed in testis. Expressed at lower levels in thymus, pancreas, spleen, liver, ovary and small intestine. Ref.7

Sequence similarities

Belongs to the peptidase C48 family.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionHydrolase
Protease
Thiol protease
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from mutant phenotype PubMed 1087798. Source: UniProtKB

apoptotic signaling pathway

Inferred from mutant phenotype PubMed 1087798. Source: UniProtKB

cellular protein metabolic process

Traceable author statement. Source: Reactome

negative regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from genetic interaction PubMed 17981124. Source: MGI

post-translational protein modification

Traceable author statement. Source: Reactome

protein desumoylation

Inferred from sequence or structural similarity. Source: UniProtKB

protein sumoylation

Traceable author statement. Source: Reactome

proteolysis

Traceable author statement Ref.1. Source: ProtInc

regulation of definitive erythrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

focal adhesion

Inferred from direct assay. Source: HPA

nuclear membrane

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionSUMO-specific protease activity

Inferred from sequence or structural similarity. Source: UniProtKB

endopeptidase activity

Traceable author statement Ref.1. Source: ProtInc

protein binding

Inferred from physical interaction PubMed 22878415. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SUMO1P631652EBI-2822935,EBI-80140

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9P0U3-1)

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.
Isoform 2 (identifier: Q9P0U3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     593-593: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 644644Sentrin-specific protease 1
PRO_0000101716

Regions

Region450 – 613164Protease
Motif171 – 1777Nuclear localization signal Probable
Motif574 – 5774Nuclear localization signal Potential
Motif628 – 6347Nuclear localization signal Potential
Motif635 – 64410Nuclear export signal Probable
Compositional bias45 – 170126Ser-rich
Compositional bias290 – 30011His-rich

Sites

Active site5331
Active site5501
Active site6031Nucleophile

Amino acid modifications

Modified residue1571Phosphoserine Ref.9

Natural variations

Alternative sequence5931Missing in isoform 2.
VSP_035777
Natural variant1931I → V. Ref.4
Corresponds to variant rs17854369 [ dbSNP | Ensembl ].
VAR_029648
Natural variant2801A → T.
Corresponds to variant rs35130318 [ dbSNP | Ensembl ].
VAR_047547
Natural variant3501D → G. Ref.4
Corresponds to variant rs17854368 [ dbSNP | Ensembl ].
VAR_029649

Experimental info

Mutagenesis4411D → A: No effect on SUMO2 processing and SUMO2 deconjugating activities. Ref.12
Mutagenesis4651W → A: Impairs SUMO2 processing and SUMO2 deconjugating activities. Ref.12
Mutagenesis4681D → A: Slightly impairs SUMO2 processing activity. No effect on SUMO2 deconjugating activity. Ref.12
Mutagenesis4961F → A: Impairs SUMO2 processing activity. No effect on SUMO2 deconjugating activity. Ref.12
Mutagenesis5111R → A: Impairs SUMO2 processing activity. No effect on SUMO2 deconjugating activity. Ref.12
Mutagenesis5121W → A: Impairs SUMO2 processing and SUMO2 deconjugating activities. Ref.12
Mutagenesis5291H → A: Impairs SUMO2 processing activity. No effect on SUMO2 deconjugating activity. Ref.12
Mutagenesis5321V → A: No effect on SUMO2 processing and SUMO2 deconjugating activities. Ref.12
Mutagenesis5331H → A: Abolishes SUMO2 processing and SUMO2 deconjugating activities. Ref.12
Mutagenesis5341W → A: Abolishes SUMO2 processing and SUMO2 deconjugating activities. Ref.12
Mutagenesis5501D → A: Abolishes SUMO2 processing and SUMO2 deconjugating activities. Ref.12
Mutagenesis5971Q → A: Abolishes SUMO2 processing and SUMO2 deconjugating activities. Ref.12
Mutagenesis6031C → A or S: Abolishes SUMO2 processing and SUMO2 deconjugating activities. Ref.5 Ref.12 Ref.13
Mutagenesis6031C → S: Exclusively nuclear. Ref.5 Ref.12 Ref.13

Secondary structure

........................................ 644
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: 941951A8B341EC64

FASTA64473,481
        10         20         30         40         50         60 
MDDIADRMRM DAGEVTLVNH NSVFKTHLLP QTGFPEDQLS LSDQQILSSR QGHLDRSFTC 

        70         80         90        100        110        120 
STRSAAYNPS YYSDNPSSDS FLGSGDLRTF GQSANGQWRN STPSSSSSLQ KSRNSRSLYL 

       130        140        150        160        170        180 
ETRKTSSGLS NSFAGKSNHH CHVSAYEKSF PIKPVPSPSW SGSCRRSLLS PKKTQRRHVS 

       190        200        210        220        230        240 
TAEETVQEEE REIYRQLLQM VTGKQFTIAK PTTHFPLHLS RCLSSSKNTL KDSLFKNGNS 

       250        260        270        280        290        300 
CASQIIGSDT SSSGSASILT NQEQLSHSVY SLSSYTPDVA FGSKDSGTLH HPHHHHSVPH 

       310        320        330        340        350        360 
QPDNLAASNT QSEGSDSVIL LKVKDSQTPT PSSTFFQAEL WIKELTSVYD SRARERLRQI 

       370        380        390        400        410        420 
EEQKALALQL QNQRLQEREH SVHDSVELHL RVPLEKEIPV TVVQETQKKG HKLTDSEDEF 

       430        440        450        460        470        480 
PEITEEMEKE IKNVFRNGNQ DEVLSEAFRL TITRKDIQTL NHLNWLNDEI INFYMNMLME 

       490        500        510        520        530        540 
RSKEKGLPSV HAFNTFFFTK LKTAGYQAVK RWTKKVDVFS VDILLVPIHL GVHWCLAVVD 

       550        560        570        580        590        600 
FRKKNITYYD SMGGINNEAC RILLQYLKQE SIDKKRKEFD TNGWQLFSKK SQEIPQQMNG 

       610        620        630        640 
SDCGMFACKY ADCITKDRPI NFTQQHMPYF RKRMVWEILH RKLL 

« Hide

Isoform 2 [UniParc].

Checksum: 1556864F1BDEE337
Show »

FASTA64373,351

References

« Hide 'large scale' references
[1]"Differential regulation of sentrinized proteins by a novel sentrin-specific protease."
Gong L., Millas S., Maul G.G., Yeh E.T.H.
J. Biol. Chem. 275:3355-3359(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION.
Tissue: Placenta.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Stomach.
[3]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS VAL-193 AND GLY-350.
Tissue: Testis.
[5]"Characterization of the localization and proteolytic activity of the SUMO-specific protease, SENP1."
Bailey D., O'Hare P.
J. Biol. Chem. 279:692-703(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEAR LOCALIZATION SIGNAL, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-603.
[6]"SENP1 enhances androgen receptor-dependent transcription through desumoylation of histone deacetylase 1."
Cheng J., Wang D., Wang Z., Yeh E.T.H.
Mol. Cell. Biol. 24:6021-6028(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1."
Xu Z., Au S.W.N.
Biochem. J. 386:325-330(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[8]"Desumoylation of homeodomain-interacting protein kinase 2 (HIPK2) through the cytoplasmic-nuclear shuttling of the SUMO-specific protease SENP1."
Kim Y.H., Sung K.S., Lee S.-J., Kim Y.-O., Choi C.Y., Kim Y.
FEBS Lett. 579:6272-6278(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEAR EXPORT SIGNAL, SUBCELLULAR LOCATION, FUNCTION.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"SUMOylation of DEC1 protein regulates its transcriptional activity and enhances its stability."
Hong Y., Xing X., Li S., Bi H., Yang C., Zhao F., Liu Y., Ao X., Chang A.K., Wu H.
PLoS ONE 6:E23046-E23046(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"CLOCK is a substrate of SUMO and sumoylation of CLOCK upregulates the transcriptional activity of estrogen receptor-alpha."
Li S., Wang M., Ao X., Chang A.K., Yang C., Zhao F., Bi H., Liu Y., Xiao L., Wu H.
Oncogene 32:4883-4891(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"The structure of SENP1-SUMO-2 complex suggests a structural basis for discrimination between SUMO paralogues during processing."
Shen L.N., Dong C., Liu H., Naismith J.H., Hay R.T.
Biochem. J. 397:279-288(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 419-644, X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 419-644 IN COMPLEX WITH SUMO3, MUTAGENESIS OF ASP-441; TRP-465; ASP-468; PHE-496; ARG-511; TRP-512; HIS-529; VAL-532; HIS-533; TRP-534; ASP-550; GLN-597 AND CYS-603, FUNCTION.
[13]"Crystal structure of the SENP1 mutant C603S-SUMO complex reveals the hydrolytic mechanism of SUMO-specific protease."
Xu Z., Chau S.F., Lam K.H., Chan H.Y., Ng T.B., Au S.W.N.
Biochem. J. 398:345-352(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 439-644 IN COMPLEX WITH SUMO1, MUTAGENESIS OF CYS-603.
[14]"SUMO protease SENP1 induces isomerization of the scissile peptide bond."
Shen L., Tatham M.H., Dong C., Zagorska A., Naismith J.H., Hay R.T.
Nat. Struct. Mol. Biol. 13:1069-1077(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) OF 439-644 IN COMPLEX WITH RANGAP1 AND SUMO1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF149770 mRNA. Translation: AAF31171.1.
AK292060 mRNA. Translation: BAF84749.1.
AC074029 Genomic DNA. No translation available.
BC045639 mRNA. Translation: AAH45639.2.
CCDSCCDS44868.2. [Q9P0U3-1]
RefSeqNP_001254523.1. NM_001267594.1. [Q9P0U3-1]
NP_001254524.1. NM_001267595.1. [Q9P0U3-1]
UniGeneHs.371957.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ9P0U3.
SMRQ9P0U3. Positions 418-644.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118930. 21 interactions.
DIPDIP-29252N.
IntActQ9P0U3. 4 interactions.
MINTMINT-1714015.
STRING9606.ENSP00000394791.

Chemistry

BindingDBQ9P0U3.
ChEMBLCHEMBL1909484.

Protein family/group databases

MEROPSC48.002.

PTM databases

PhosphoSiteQ9P0U3.

Polymorphism databases

DMDM215273882.

Proteomic databases

MaxQBQ9P0U3.
PaxDbQ9P0U3.
PRIDEQ9P0U3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000004980; ENSP00000004980; ENSG00000079387. [Q9P0U3-1]
ENST00000448372; ENSP00000394791; ENSG00000079387. [Q9P0U3-2]
ENST00000549518; ENSP00000447328; ENSG00000079387. [Q9P0U3-1]
ENST00000549595; ENSP00000450076; ENSG00000079387. [Q9P0U3-2]
ENST00000551330; ENSP00000446681; ENSG00000079387. [Q9P0U3-1]
GeneID29843.
KEGGhsa:29843.
UCSCuc001rqx.4. human. [Q9P0U3-1]
uc031qhb.1. human. [Q9P0U3-2]

Organism-specific databases

CTD29843.
GeneCardsGC12M048436.
HGNCHGNC:17927. SENP1.
HPAHPA011765.
HPA046491.
MIM612157. gene.
neXtProtNX_Q9P0U3.
PharmGKBPA134947038.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5160.
HOGENOMHOG000154286.
HOVERGENHBG057384.
InParanoidQ9P0U3.
KOK08592.
OMAVNHNSIF.
OrthoDBEOG7D59MP.
PhylomeDBQ9P0U3.
TreeFamTF316289.

Enzyme and pathway databases

BRENDA3.4.22.68. 2681.
ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressQ9P0U3.
BgeeQ9P0U3.
CleanExHS_SENP1.
GenevestigatorQ9P0U3.

Family and domain databases

InterProIPR003653. Peptidase_C48.
[Graphical view]
PfamPF02902. Peptidase_C48. 1 hit.
[Graphical view]
PROSITEPS50600. ULP_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSENP1. human.
EvolutionaryTraceQ9P0U3.
GeneWikiSENP1.
GenomeRNAi29843.
NextBio52379.
PROQ9P0U3.
SOURCESearch...

Entry information

Entry nameSENP1_HUMAN
AccessionPrimary (citable) accession number: Q9P0U3
Secondary accession number(s): A8K7P5, Q86XC8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2002
Last sequence update: November 25, 2008
Last modified: July 9, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM