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Q9BQF6 (SENP7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sentrin-specific protease 7

EC=3.4.22.68
Alternative name(s):
SUMO-1-specific protease 2
Sentrin/SUMO-specific protease SENP7
Gene names
Name:SENP7
Synonyms:KIAA1707, SSP2, SUSP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1050 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Protease that deconjugates SUMO2 and SUMO3 from targeted proteins, but not SUMO1. Catalyzes the deconjugation of poly-SUMO2 and poly-SUMO3 chains. Has very low efficiency in processing full-length SUMO proteins to their mature forms. Ref.10

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.

Sequence similarities

Belongs to the peptidase C48 family.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionHydrolase
Protease
Thiol protease
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentintracellular

Inferred from direct assay. Source: LIFEdb

nucleus

Inferred from direct assay. Source: LIFEdb

   Molecular_functioncysteine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Note: Experimental confirmation may be lacking for some isoforms.
Isoform 1 (identifier: Q9BQF6-1)

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: Q9BQF6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: Missing.
Isoform 3 (identifier: Q9BQF6-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-812: Missing.
     813-827: TRKENNLTEDNPNLS → MKKFLYIKSVFHTLR
Isoform 4 (identifier: Q9BQF6-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-33: Missing.
     95-225: Missing.
Isoform 5 (identifier: Q9BQF6-5)

The sequence of this isoform differs from the canonical sequence as follows:
     95-160: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10501050Sentrin-specific protease 7
PRO_0000101726

Regions

Region760 – 1050291Protease

Sites

Active site8601 By similarity
Active site9921 By similarity

Amino acid modifications

Modified residue251Phosphoserine Ref.9
Modified residue4431Phosphoserine Ref.9
Modified residue4441Phosphoserine Ref.9

Natural variations

Alternative sequence1 – 812812Missing in isoform 3.
VSP_039498
Alternative sequence1 – 3333Missing in isoform 2 and isoform 4.
VSP_039499
Alternative sequence95 – 225131Missing in isoform 4.
VSP_039501
Alternative sequence95 – 16066Missing in isoform 5.
VSP_039500
Alternative sequence813 – 82715TRKEN…NPNLS → MKKFLYIKSVFHTLR in isoform 3.
VSP_039502
Natural variant791K → Q.
Corresponds to variant rs6809436 [ dbSNP | Ensembl ].
VAR_029651
Natural variant6121Q → H. Ref.7
Corresponds to variant rs2433031 [ dbSNP | Ensembl ].
VAR_029652

Experimental info

Mutagenesis7751F → W: Slightly increased deconjugation activity. Ref.10
Mutagenesis7791V → E: Reduces deconjugation activity. Ref.10
Sequence conflict901K → R in CAB66534. Ref.3
Sequence conflict3411K → R in CAB66534. Ref.3
Sequence conflict3961N → Y in CAB66534. Ref.3
Sequence conflict7851L → H in AAL25651. Ref.1
Sequence conflict8941N → S in CAB66534. Ref.3
Sequence conflict9471Q → R in CAB66534. Ref.3
Sequence conflict10061D → N in AAL25651. Ref.1

Secondary structure

...................................... 1050
Helix Strand Turn

Details...

Sequences

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

Last modified July 13, 2010. Version 4.
Checksum: CB455A0B22709052

FASTA1,050119,658
        10         20         30         40         50         60 
MDKRKLGRRP SSSEIITEGK RKKSSSDLSE IRKMLNAKPE DVHVQSPLSK FRSSERWTLP 

        70         80         90        100        110        120 
LQWERSLRNK VISLDHKNKK HIRGCPVTSK SSPERQLKVM LTNVLWTDLG RKFRKTLPRN 

       130        140        150        160        170        180 
DANLCDANKV QSDSLPSTSV DSLETCQKLE PLRQSLNLSE RIPRVILTNV LGTELGRKYI 

       190        200        210        220        230        240 
RTPPVTEGSL SDTDNLQSEQ LSSSSDGSLE SYQNLNPHKS CYLSERGSQR SKTVDDNSAK 

       250        260        270        280        290        300 
QTAHNKEKRR KDDGISLLIS DTQPEDLNSG SRGCDHLEQE SRNKDVKYSD SKVELTLISR 

       310        320        330        340        350        360 
KTKRRLRNNL PDSQYCTSLD KSTEQTKKQE DDSTISTEFE KPSENYHQDP KLPEEITTKP 

       370        380        390        400        410        420 
TKSDFTKLSS LNSQELTLSN ATKSASAGST TETVENSNSI DIVGISSLVE KDENELNTIE 

       430        440        450        460        470        480 
KPILRGHNEG NQSLISAEPI VVSSDEEGPV EHKSSEILKL QSKQDRETTN ENESTSESAL 

       490        500        510        520        530        540 
LELPLITCES VQMSSELCPY NPVMENISSI MPSNEMDLQL DFIFTSVYIG KIKGASKGCV 

       550        560        570        580        590        600 
TITKKYIKIP FQVSLNEISL LVDTTHLKRF GLWKSKDDNH SKRSHAILFF WVSSDYLQEI 

       610        620        630        640        650        660 
QTQLEHSVLS QQSKSSEFIF LELHNPVSQR EELKLKDIMT EISIISGELE LSYPLSWVQA 

       670        680        690        700        710        720 
FPLFQNLSSK ESSFIHYYCV STCSFPAGVA VAEEMKLKSV SQPSNTDAAK PTYTFLQKQS 

       730        740        750        760        770        780 
SGCYSLSITS NPDEEWREVR HTGLVQKLIV YPPPPTKGGL GVTNEDLECL EEGEFLNDVI 

       790        800        810        820        830        840 
IDFYLKYLIL EKASDELVER SHIFSSFFYK CLTRKENNLT EDNPNLSMAQ RRHKRVRTWT 

       850        860        870        880        890        900 
RHINIFNKDY IFVPVNESSH WYLAVICFPW LEEAVYEDFP QTVSQQSQAQ QSQNDNKTID 

       910        920        930        940        950        960 
NDLRTTSTLS LSAEDSQSTE SNMSVPKKMC KRPCILILDS LKAASVQNTV QNLREYLEVE 

       970        980        990       1000       1010       1020 
WEVKLKTHRQ FSKTNMVDLC PKVPKQDNSS DCGVYLLQYV ESFFKDPIVN FELPIHLEKW 

      1030       1040       1050 
FPRHVIKTKR EDIRELILKL HLQQQKGSSS 

« Hide

Isoform 2 [UniParc].

Checksum: F0C8278BCC440AA8
Show »

FASTA1,017115,871
Isoform 3 [UniParc].

Checksum: 9661C4384D6A30D7
Show »

FASTA23828,124
Isoform 4 [UniParc].

Checksum: B03DA49EB00C0007
Show »

FASTA886101,195
Isoform 5 [UniParc].

Checksum: E5EBB74CAC3E39C5
Show »

FASTA984112,159

References

« Hide 'large scale' references
[1]Choi S.J., Jeon Y.-J., Kim K.I., Nishimori S., Suzuki T., Uchida S., Shimbara N., Tanaka K., Chung C.H.
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]"SENP7, a novel human sentrin-specific protease."
Gong L., Yeh E.T.H.
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Tissue: Placenta.
[3]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
Tissue: Brain.
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Fetal kidney.
[5]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., 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. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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).
[7]"Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 295-1050, VARIANT HIS-612.
Tissue: Brain.
[8]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-443 AND SER-444, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[10]"Structure of the human SENP7 catalytic domain and poly-SUMO deconjugation activities for SENP6 and SENP7."
Lima C.D., Reverter D.
J. Biol. Chem. 283:32045-32055(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 728-1050, FUNCTION, MUTAGENESIS OF PHE-775 AND VAL-779.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF199458 mRNA. Translation: AAL25651.1.
AF217504 mRNA. Translation: AAG09703.1.
AL136599 mRNA. Translation: CAB66534.1.
BX537943 mRNA. Translation: CAD97911.1.
AC068764 Genomic DNA. No translation available.
AC073861 Genomic DNA. No translation available.
AC110994 Genomic DNA. No translation available.
BC129988 mRNA. Translation: AAI29989.1.
AB051494 mRNA. Translation: BAB21798.1.
RefSeqNP_001070671.1. NM_001077203.2.
NP_001269730.1. NM_001282801.1.
NP_001269731.1. NM_001282802.1.
NP_001269732.1. NM_001282803.1.
NP_001269733.1. NM_001282804.1.
NP_065705.3. NM_020654.4.
UniGeneHs.529551.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3EAYX-ray2.40A728-1050[»]
ProteinModelPortalQ9BQF6.
SMRQ9BQF6. Positions 744-1047.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121491. 2 interactions.
IntActQ9BQF6. 3 interactions.
MINTMINT-4717645.
STRING9606.ENSP00000377655.

Chemistry

BindingDBQ9BQF6.
ChEMBLCHEMBL1741213.

Protein family/group databases

MEROPSC48.009.

PTM databases

PhosphoSiteQ9BQF6.

Polymorphism databases

DMDM300669717.

Proteomic databases

PaxDbQ9BQF6.
PRIDEQ9BQF6.

Protocols and materials databases

DNASU57337.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000314261; ENSP00000313624; ENSG00000138468. [Q9BQF6-5]
ENST00000348610; ENSP00000342159; ENSG00000138468. [Q9BQF6-2]
ENST00000358203; ENSP00000350936; ENSG00000138468. [Q9BQF6-4]
ENST00000394085; ENSP00000377647; ENSG00000138468. [Q9BQF6-3]
ENST00000394091; ENSP00000377651; ENSG00000138468. [Q9BQF6-4]
ENST00000394095; ENSP00000377655; ENSG00000138468. [Q9BQF6-1]
GeneID57337.
KEGGhsa:57337.
UCSCuc003dus.3. human. [Q9BQF6-3]
uc003dut.3. human. [Q9BQF6-1]
uc003duw.3. human. [Q9BQF6-5]
uc003dux.3. human. [Q9BQF6-4]

Organism-specific databases

CTD57337.
GeneCardsGC03M101043.
H-InvDBHIX0003507.
HGNCHGNC:30402. SENP7.
HPAHPA027259.
MIM612846. gene.
neXtProtNX_Q9BQF6.
PharmGKBPA134925171.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5160.
HOVERGENHBG079864.
KOK08596.
OMAFIFLELH.
OrthoDBEOG780RMX.
PhylomeDBQ9BQF6.
TreeFamTF350136.

Gene expression databases

ArrayExpressQ9BQF6.
BgeeQ9BQF6.
CleanExHS_SENP7.
GenevestigatorQ9BQF6.

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

EvolutionaryTraceQ9BQF6.
GeneWikiSENP7.
GenomeRNAi57337.
NextBio63454.
PROQ9BQF6.
SOURCESearch...

Entry information

Entry nameSENP7_HUMAN
AccessionPrimary (citable) accession number: Q9BQF6
Secondary accession number(s): A1L3A5 expand/collapse secondary AC list , A8MW39, B7WNW8, Q7Z3F4, Q96PS5, Q9C0F6, Q9HBT5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: July 13, 2010
Last modified: April 16, 2014
This is version 105 of the entry and version 4 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 3

Human chromosome 3: entries, gene names and cross-references to MIM