Tag | Content |
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CPLM ID | CPLM-020049 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Sentrin-specific protease 7 |
Protein Synonyms/Alias | SUMO-1-specific protease 2; Sentrin/SUMO-specific protease SENP7 |
Gene Name | SENP7 |
Gene Synonyms/Alias | KIAA1707; SSP2; SUSP2 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
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698 | VAEEMKLKSVSQPSN | ubiquitination | [1] | 710 | PSNTDAAKPTYTFLQ | ubiquitination | [1] | 982 | NMVDLCPKVPKQDNS | ubiquitination | [1] | 1046 | KLHLQQQKGSSS*** | ubiquitination | [1] |
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Reference | [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments. Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA. Mol Cell Proteomics. 2013 Mar;12(3):825-31. [ PMID: 23266961] |
Functional Description | 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. |
Sequence Annotation | REGION 760 1050 Protease. ACT_SITE 860 860 By similarity. ACT_SITE 992 992 By similarity. MOD_RES 25 25 Phosphoserine. MOD_RES 443 443 Phosphoserine. MOD_RES 444 444 Phosphoserine. |
Keyword | 3D-structure; Alternative splicing; Complete proteome; Hydrolase; Phosphoprotein; Polymorphism; Protease; Reference proteome; Thiol protease; Ubl conjugation pathway. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1050 AA |
Protein Sequence | MDKRKLGRRP SSSEIITEGK RKKSSSDLSE IRKMLNAKPE DVHVQSPLSK FRSSERWTLP 60 LQWERSLRNK VISLDHKNKK HIRGCPVTSK SSPERQLKVM LTNVLWTDLG RKFRKTLPRN 120 DANLCDANKV QSDSLPSTSV DSLETCQKLE PLRQSLNLSE RIPRVILTNV LGTELGRKYI 180 RTPPVTEGSL SDTDNLQSEQ LSSSSDGSLE SYQNLNPHKS CYLSERGSQR SKTVDDNSAK 240 QTAHNKEKRR KDDGISLLIS DTQPEDLNSG SRGCDHLEQE SRNKDVKYSD SKVELTLISR 300 KTKRRLRNNL PDSQYCTSLD KSTEQTKKQE DDSTISTEFE KPSENYHQDP KLPEEITTKP 360 TKSDFTKLSS LNSQELTLSN ATKSASAGST TETVENSNSI DIVGISSLVE KDENELNTIE 420 KPILRGHNEG NQSLISAEPI VVSSDEEGPV EHKSSEILKL QSKQDRETTN ENESTSESAL 480 LELPLITCES VQMSSELCPY NPVMENISSI MPSNEMDLQL DFIFTSVYIG KIKGASKGCV 540 TITKKYIKIP FQVSLNEISL LVDTTHLKRF GLWKSKDDNH SKRSHAILFF WVSSDYLQEI 600 QTQLEHSVLS QQSKSSEFIF LELHNPVSQR EELKLKDIMT EISIISGELE LSYPLSWVQA 660 FPLFQNLSSK ESSFIHYYCV STCSFPAGVA VAEEMKLKSV SQPSNTDAAK PTYTFLQKQS 720 SGCYSLSITS NPDEEWREVR HTGLVQKLIV YPPPPTKGGL GVTNEDLECL EEGEFLNDVI 780 IDFYLKYLIL EKASDELVER SHIFSSFFYK CLTRKENNLT EDNPNLSMAQ RRHKRVRTWT 840 RHINIFNKDY IFVPVNESSH WYLAVICFPW LEEAVYEDFP QTVSQQSQAQ QSQNDNKTID 900 NDLRTTSTLS LSAEDSQSTE SNMSVPKKMC KRPCILILDS LKAASVQNTV QNLREYLEVE 960 WEVKLKTHRQ FSKTNMVDLC PKVPKQDNSS DCGVYLLQYV ESFFKDPIVN FELPIHLEKW 1020 FPRHVIKTKR EDIRELILKL HLQQQKGSSS 1050 |
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