| Tag | Content |
|---|
| CPLM ID | CPLM-018052 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | A disintegrin and metalloproteinase with thrombospondin motifs 17 |
Protein Synonyms/Alias | ADAM-TS 17; ADAM-TS17; ADAMTS-17 |
Gene Name | ADAMTS17 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 419 | IMSGEWVKGRNPSDL | ubiquitination | [1] |
|
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 | |
Sequence Annotation | DOMAIN 232 452 Peptidase M12B.
DOMAIN 453 542 Disintegrin.
DOMAIN 543 598 TSP type-1 1.
DOMAIN 800 860 TSP type-1 2.
DOMAIN 861 922 TSP type-1 3.
DOMAIN 925 968 TSP type-1 4.
DOMAIN 972 1029 TSP type-1 5.
DOMAIN 1045 1084 PLAC.
REGION 702 779 Spacer.
MOTIF 199 206 Cysteine switch (By similarity).
ACT_SITE 390 390 By similarity.
METAL 201 201 Zinc; in inhibited form (By similarity).
METAL 389 389 Zinc; catalytic (By similarity).
METAL 393 393 Zinc; catalytic (By similarity).
METAL 399 399 Zinc; catalytic (By similarity).
CARBOHYD 167 167 N-linked (GlcNAc...) (Potential).
CARBOHYD 483 483 N-linked (GlcNAc...) (Potential).
CARBOHYD 785 785 N-linked (GlcNAc...) (Potential).
CARBOHYD 790 790 N-linked (GlcNAc...) (Potential).
CARBOHYD 832 832 N-linked (GlcNAc...) (Potential).
CARBOHYD 839 839 N-linked (GlcNAc...) (Potential).
CARBOHYD 894 894 N-linked (GlcNAc...) (Potential).
DISULFID 367 447 By similarity.
DISULFID 406 431 By similarity.
DISULFID 555 592 By similarity.
DISULFID 559 597 By similarity.
DISULFID 570 582 By similarity.
DISULFID 873 916 By similarity.
DISULFID 877 921 By similarity.
DISULFID 888 905 By similarity. |
Keyword | Alternative splicing; Cleavage on pair of basic residues; Complete proteome; Deafness; Disulfide bond; Dwarfism; Extracellular matrix; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Polymorphism; Protease; Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1095 AA |
Protein Sequence | MCDGALLPPL VLPVLLLLVW GLDPGTAVGD AAADVEVVLP WRVRPDDVHL PPLPAAPGPR 60
RRRRPRTPPA APRARPGERA LLLHLPAFGR DLYLQLRRDL RFLSRGFEVE EAGAARRRGR 120
PAELCFYSGR VLGHPGSLVS LSACGAAGGL VGLIQLGQEQ VLIQPLNNSQ GPFSGREHLI 180
RRKWSLTPSP SAEAQRPEQL CKVLTEKKKP TWGRPSRDWR ERRNAIRLTS EHTVETLVVA 240
DADMVQYHGA EAAQRFILTV MNMVYNMFQH QSLGIKINIQ VTKLVLLRQR PAKLSIGHHG 300
ERSLESFCHW QNEEYGGARY LGNNQVPGGK DDPPLVDAAV FVTRTDFCVH KDEPCDTVGI 360
AYLGGVCSAK RKCVLAEDNG LNLAFTIAHE LGHNLGMNHD DDHSSCAGRS HIMSGEWVKG 420
RNPSDLSWSS CSRDDLENFL KSKVSTCLLV TDPRSQHTVR LPHKLPGMHY SANEQCQILF 480
GMNATFCRNM EHLMCAGLWC LVEGDTSCKT KLDPPLDGTE CGADKWCRAG ECVSKTPIPE 540
HVDGDWSPWG AWSMCSRTCG TGARFRQRKC DNPPPGPGGT HCPGASVEHA VCENLPCPKG 600
LPSFRDQQCQ AHDRLSPKKK GLLTAVVVDD KPCELYCSPL GKESPLLVAD RVLDGTPCGP 660
YETDLCVHGK CQKIGCDGII GSAAKEDRCG VCSGDGKTCH LVKGDFSHAR GTALKDSGKG 720
SINSDWKIEL PGEFQIAGTT VRYVRRGLWE KISAKGPTKL PLHLMVLLFH DQDYGIHYEY 780
TVPVNRTAEN QSEPEKPQDS LFIWTHSGWE GCSVQCGGGE RRTIVSCTRI VNKTTTLVND 840
SDCPQASRPE PQVRRCNLHP CQSRWVAGPW SPCSATCEKG FQHREVTCVY QLQNGTHVAT 900
RPLYCPGPRP AAVQSCEGQD CLSIWEASEW SQCSASCGKG VWKRTVACTN SQGKCDASTR 960
PRAEEACEDY SGCYEWKTGD WSTCSSTCGK GLQSRVVQCM HKVTGRHGSE CPALSKPAPY 1020
RQCYQEVCND RINANTITSP RLAALTYKCT RDQWTVYCRV IREKNLCQDM RWYQRCCQTC 1080
RDFYANKMRQ PPPNS 1095 |
Gene Ontology | GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell. GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0006508; P:proteolysis; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |