ADAMTS17:A disintegrin and metalloproteinase with thrombospondin motifs 17

Gene Name
A disintegrin and metalloproteinase with thrombospondin motifs 17
Protein ID
Chromosome ID
HPP Status
Protein Name
A disintegrin and metalloproteinase with thrombospondin motifs 17

A disintegrin and metalloproteinase with thrombospondin motifs 17


a disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motif, 17

ADAM metallopeptidase with thrombospondin type 1 motif, 17



EC 3.4.24.-

[Reference: ]
Chromosomal Position
15q26.3 | Start:99971589 End:99971589

Entrez Gene Summary for ADAMTS17
This gene encodes a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) protein family. ADAMTS family members share several distinct protein modules, including a propeptide region, a metalloproteinase domain, a disintegrin-like domain, and a thrombospondin type 1 (TS) motif. Individual members of this family differ in the number of C-terminal TS motifs, and some have unique C-terminal domains. The protein encoded by this gene has a high sequence similarity to the protein encoded by ADAMTS19, another family member. The function of this protein has not been determined. (provided by RefSeq, Jul 2008)

[Reference: ]
External IDs
Hgnc ID: 17109 EntrezGene ID: 170691 Ensembl ID: ENSG00000140470
[Reference: ]
Reference Source

Gene Reference Into Function (GeneRIF)

PubMed IDGeneRIF TextLast Update
19266077Observational study of gene-disease association. (HuGE Navigator)2009-03-25
19836009Homozygous mutation in ADAMTS17 causes lenticular myopia, ectopia lentis, glaucoma, spheropakia, and short stature.2010-01-21
20200978Observational study of gene-disease association. (HuGE Navigator)2010-04-07
20546612Observational study of gene-disease association. (HuGE Navigator)2010-09-15
21037509Observational study of gene-disease association, gene-environment interaction, and pharmacogenomic / toxicogenomic. (HuGE Navigator)2010-12-05
21555518ADAMTS17 is a target gene of the BACH1 transcription factor according to ChIP-seq analysis in HEK 293 cells.2011-09-14
22486325Recessive ADAMTS17 mutations are a recurrent cause of isolated spherophakia with short stature.2013-03-30
23661674Endothelial protease nexin-1 is a novel regulator of A disintegrin and metalloproteinase 17 maturation and endothelial protein C receptor shedding via furin inhibition.2013-08-31
24906090higher Adamts17 expression is found in several human cancer cell subtypes, especially in breast ductal carcinoma and there is an inverse correlation between higher Adamts17 expression and patients' survival.2015-05-16
24940034A mutation in WMS-like gene ADAMTS17 also causes WMS.2014-06-20
24940034The mutation in the Weill-Marchesani syndrome (WMS)- gene ADAMTS17 also causes WMS in an Indian family.2014-10-04


Relevant citations within the PubMed literature


Putative/known Functions


Homologues, Orthologues, Paralogues and Family

Sequence Similarity and Functional Annotation

Sequence Similarity

Db NameQuery UniSubject UniSequence LengthAlignment LengthIdentityCoverageMismatchesGap OpeningsQuery StartQuery EndSubject StartSubject EndEvalueBit Score
Reviewed non-human mammalian with experimental evidenceATS17_HUMANSEM5A_RAT10955750.885.212715435985956517.00E-0650
Islam MT, Garg G, Hancock WS, Risk BA, Baker MS, Ranganathan S (2014) Protannotator: A Semiautomated Pipeline for Chromosome-Wise Functional Annotation of the "Missing" Human Proteome. J Proteome Res. 13, 76-83.

InterProScan Annotation

Uniprot IDInterpro IDGo IDTypeNameCategoryDescription
ATS17_HUMANIPR001590GO:0004222DomainPeptidase M12B, ADAM/reprolysinMolecular Functionmetalloendopeptidase activity
ATS17_HUMANIPR001590GO:0006508DomainPeptidase M12B, ADAM/reprolysinBiological Processproteolysis
ATS17_HUMANIPR002870GO:0004222DomainPeptidase M12B, propeptideMolecular Functionmetalloendopeptidase activity
ATS17_HUMANIPR002870GO:0006508DomainPeptidase M12B, propeptideBiological Processproteolysis
ATS17_HUMANIPR002870GO:0008270DomainPeptidase M12B, propeptideMolecular Functionzinc ion binding
ATS17_HUMANIPR006586GO:0004222DomainADAM, cysteine-richMolecular Functionmetalloendopeptidase activity
ATS17_HUMANIPR006586GO:0006508DomainADAM, cysteine-richBiological Processproteolysis
ATS17_HUMANIPR010294GO:0004222DomainADAM-TS Spacer 1Molecular Functionmetalloendopeptidase activity
ATS17_HUMANIPR010294GO:0031012DomainADAM-TS Spacer 1Cellular Componentextracellular matrix
ATS17_HUMANIPR010909GO:0008233DomainPLACMolecular Functionpeptidase activity
ATS17_HUMANIPR013273GO:0005578FamilyPeptidase M12B, ADAM-TSCellular Componentproteinaceous extracellular matrix
ATS17_HUMANIPR013273GO:0008237FamilyPeptidase M12B, ADAM-TSMolecular Functionmetallopeptidase activity
ATS17_HUMANIPR013273GO:0008270FamilyPeptidase M12B, ADAM-TSMolecular Functionzinc ion binding
ATS17_HUMANIPR024079GO:0008237DomainMetallopeptidase, catalytic domainMolecular Functionmetallopeptidase activity
Islam MT, Garg G, Hancock WS, Risk BA, Baker MS, Ranganathan S (2014) Protannotator: A Semiautomated Pipeline for Chromosome-Wise Functional Annotation of the "Missing" Human Proteome. J Proteome Res. 13, 76-83.

Post Translational Modifications

Protein Protein Interactions

Best Available Mass Spectra without FDR


Evidence File
Fenyö, David; Beavis, Ronald C. (2015). "The GPMDB REST interface". Bioinformatics 31 (12): 2056–2058. doi:10.1093/bioinformatics/btv107. ISSN 1367-4803. ">Global Proteome Machine Database - THE GPM


Peptide SequenceScoresPride IDSpectrum IDAnnotation
No results found.
Evidence File
Vizcaino JA, et al. 2016 update of the PRIDE database and related tools. Nucleic Acids Res. 2016 Jan 1;44(D1):D447-D456. ">PRIDE Archive

Proteomics DB

Evidence File
Wilhelm, M et al. (2014) Mass-spectrometry-based draft of the human proteome. Nature. 509:582-7. ">Proteomics DB