Q9BQF6 (SENP7_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 95.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended 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 |
| ||||
| Organism | Homo sapiens (Human) [Reference proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo![]() |
Protein attributes
| Sequence length | 1050 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence 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 process | Ubl conjugation pathway |
| Coding sequence diversity | Alternative splicing Polymorphism |
| Molecular function | Hydrolase Protease Thiol protease |
| PTM | Phosphoprotein |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | proteolysis Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | nucleus Inferred from direct assay. Source: LIFEdb |
| Molecular_function | cysteine-type peptidase activity Non-traceable author statement. Source: UniProtKB |
| 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 key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1050 | 1050 | Sentrin-specific protease 7 | PRO_0000101726 | ||||||||||||||||||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||||||||||||||||||
| Region | 760 – 1050 | 291 | Protease | |||||||||||||||||||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||||||||||||||||||
| Active site | 860 | 1 | By similarity | |||||||||||||||||||||||||||||||||||||||||||
| Active site | 992 | 1 | By similarity | |||||||||||||||||||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 25 | 1 | Phosphoserine Ref.9 | |||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 443 | 1 | Phosphoserine Ref.9 | |||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 444 | 1 | Phosphoserine Ref.9 | |||||||||||||||||||||||||||||||||||||||||||
Natural variations | ||||||||||||||||||||||||||||||||||||||||||||||
| Alternative sequence | 1 – 812 | 812 | Missing in isoform 3. | VSP_039498 | ||||||||||||||||||||||||||||||||||||||||||
| Alternative sequence | 1 – 33 | 33 | Missing in isoform 2 and isoform 4. | VSP_039499 | ||||||||||||||||||||||||||||||||||||||||||
| Alternative sequence | 95 – 225 | 131 | Missing in isoform 4. | VSP_039501 | ||||||||||||||||||||||||||||||||||||||||||
| Alternative sequence | 95 – 160 | 66 | Missing in isoform 5. | VSP_039500 | ||||||||||||||||||||||||||||||||||||||||||
| Alternative sequence | 813 – 827 | 15 | TRKEN…NPNLS → MKKFLYIKSVFHTLR in isoform 3. | VSP_039502 | ||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 79 | 1 | K → Q. Corresponds to variant rs6809436 [ dbSNP | Ensembl ]. | VAR_029651 | ||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 612 | 1 | Q → H. Ref.7 Corresponds to variant rs2433031 [ dbSNP | Ensembl ]. | VAR_029652 | ||||||||||||||||||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 775 | 1 | F → W: Slightly increased deconjugation activity. Ref.10 | |||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 779 | 1 | V → E: Reduces deconjugation activity. Ref.10 | |||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 90 | 1 | K → R in CAB66534. Ref.3 | |||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 341 | 1 | K → R in CAB66534. Ref.3 | |||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 396 | 1 | N → Y in CAB66534. Ref.3 | |||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 785 | 1 | L → H in AAL25651. Ref.1 | |||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 894 | 1 | N → S in CAB66534. Ref.3 | |||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 947 | 1 | Q → R in CAB66534. Ref.3 | |||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 1006 | 1 | D → N in AAL25651. Ref.1 | |||||||||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 747 – 752 | 6 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 756 – 758 | 3 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 760 – 763 | 4 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 764 – 768 | 5 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 778 – 791 | 14 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 795 – 799 | 5 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 801 – 803 | 3 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 807 – 812 | 6 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 828 – 833 | 6 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 837 – 840 | 4 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 845 – 847 | 3 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 849 – 857 | 9 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 860 – 867 | 8 | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 933 – 938 | 6 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 946 – 965 | 20 | ||||||||||||||||||||||||||||||||||||||||||||
| Turn | 973 – 975 | 3 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 992 – 1005 | 14 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 1023 – 1027 | 5 | ||||||||||||||||||||||||||||||||||||||||||||
| Helix | 1029 – 1046 | 18 | ||||||||||||||||||||||||||||||||||||||||||||
Sequences
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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. 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. 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, MASS SPECTROMETRY. 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. | ||||||||||||
| IPI | IPI00218776. IPI00218777. IPI00296449. IPI00816671. IPI00969153. | ||||||||||||
| RefSeq | NP_001070671.1. NM_001077203.1. NP_065705.3. NM_020654.3. | ||||||||||||
| UniGene | Hs.529551. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | Q9BQF6. | ||||||||||||
| SMR | Q9BQF6. Positions 744-1047. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| IntAct | Q9BQF6. 2 interactions. | ||||||||||||
| STRING | 9606.ENSP00000377655. | ||||||||||||
Protein family/group databases | |||||||||||||
| MEROPS | C48.009. | ||||||||||||
PTM databases | |||||||||||||
| PhosphoSite | Q9BQF6. | ||||||||||||
Polymorphism databases | |||||||||||||
| DMDM | 300669717. | ||||||||||||
Proteomic databases | |||||||||||||
| PaxDb | Q9BQF6. | ||||||||||||
| PRIDE | Q9BQF6. | ||||||||||||
Protocols and materials databases | |||||||||||||
| DNASU | 57337. | ||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENST00000314261; ENSP00000313624; ENSG00000138468. ENST00000348610; ENSP00000342159; ENSG00000138468. ENST00000358203; ENSP00000350936; ENSG00000138468. ENST00000394085; ENSP00000377647; ENSG00000138468. ENST00000394091; ENSP00000377651; ENSG00000138468. ENST00000394095; ENSP00000377655; ENSG00000138468. | ||||||||||||
| GeneID | 57337. | ||||||||||||
| KEGG | hsa:57337. | ||||||||||||
| UCSC | uc003dus.3. human. uc003dut.3. human. uc003duw.3. human. uc003dux.3. human. | ||||||||||||
Organism-specific databases | |||||||||||||
| CTD | 57337. | ||||||||||||
| GeneCards | GC03M101043. | ||||||||||||
| H-InvDB | HIX0003507. | ||||||||||||
| HGNC | HGNC:30402. SENP7. | ||||||||||||
| HPA | HPA027259. | ||||||||||||
| MIM | 612846. gene. | ||||||||||||
| neXtProt | NX_Q9BQF6. | ||||||||||||
| PharmGKB | PA134925171. | ||||||||||||
| HUGE | Search... | ||||||||||||
| GenAtlas | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | COG5160. | ||||||||||||
| HOVERGEN | HBG079864. | ||||||||||||
| KO | K08596. | ||||||||||||
| OMA | FFKDPIV. | ||||||||||||
| OrthoDB | EOG4ZW5C5. | ||||||||||||
Gene expression databases | |||||||||||||
| Bgee | Q9BQF6. | ||||||||||||
| CleanEx | HS_SENP7. | ||||||||||||
| Genevestigator | Q9BQF6. | ||||||||||||
| GermOnline | ENSG00000138468. Homo sapiens. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR003653. Peptidase_C48. [Graphical view] | ||||||||||||
| Pfam | PF02902. Peptidase_C48. 1 hit. [Graphical view] | ||||||||||||
| PROSITE | PS50600. ULP_PROTEASE. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| BindingDB | Q9BQF6. | ||||||||||||
| ChEMBL | CHEMBL1741213. | ||||||||||||
| EvolutionaryTrace | Q9BQF6. | ||||||||||||
| GenomeRNAi | 57337. | ||||||||||||
| NextBio | 63454. | ||||||||||||
| SOURCE | Search... | ||||||||||||
Entry information
| Entry name | SENP7_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q9BQF6 Secondary accession number(s): A1L3A5 Q9HBT5 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any 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
| Peptidase families Classification of peptidase families and list of entries |
| Human chromosome 3 Human chromosome 3: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
