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Q8TE56

- ATS17_HUMAN

UniProt

Q8TE56 - ATS17_HUMAN

Protein

A disintegrin and metalloproteinase with thrombospondin motifs 17

Gene

ADAMTS17

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 2 (18 May 2010)
      Previous versions | rss
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    Functioni

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi201 – 2011Zinc; in inhibited formBy similarity
    Metal bindingi389 – 3891Zinc; catalyticBy similarity
    Active sitei390 – 3901PROSITE-ProRule annotation
    Metal bindingi393 – 3931Zinc; catalyticBy similarity
    Metal bindingi399 – 3991Zinc; catalyticBy similarity

    GO - Molecular functioni

    1. metalloendopeptidase activity Source: InterPro
    2. zinc ion binding Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_200626. O-glycosylation of TSR domain-containing proteins.

    Protein family/group databases

    MEROPSiM12.027.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    A disintegrin and metalloproteinase with thrombospondin motifs 17 (EC:3.4.24.-)
    Short name:
    ADAM-TS 17
    Short name:
    ADAM-TS17
    Short name:
    ADAMTS-17
    Gene namesi
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:17109. ADAMTS17.

    Subcellular locationi

    GO - Cellular componenti

    1. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Weill-Marchesani-like syndrome (WMLS) [MIM:613195]: A disorder characterized by many of the key features of Weill-Marchesani syndrome, including lenticular myopia, ectopia lentis, glaucoma, spherophakia and short stature. However, the characteristic brachydactyly or decreased joint flexibility of Weill-Marchesani syndrome are absent.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Deafness, Dwarfism

    Organism-specific databases

    MIMi613195. phenotype.
    Orphaneti363992. Ichthyosis-short stature-brachydactyly-microspherophakia syndrome.
    PharmGKBiPA24543.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727Sequence AnalysisAdd
    BLAST
    Propeptidei28 – 223196By similarityPRO_0000029198Add
    BLAST
    Chaini224 – 1095872A disintegrin and metalloproteinase with thrombospondin motifs 17PRO_0000029199Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi167 – 1671N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi308 ↔ 373By similarity
    Disulfide bondi348 ↔ 355By similarity
    Disulfide bondi367 ↔ 447By similarity
    Disulfide bondi406 ↔ 431By similarity
    Disulfide bondi476 ↔ 500By similarity
    Glycosylationi483 – 4831N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi487 ↔ 508By similarity
    Disulfide bondi495 ↔ 527By similarity
    Disulfide bondi521 ↔ 532By similarity
    Disulfide bondi555 ↔ 592By similarity
    Disulfide bondi559 ↔ 597By similarity
    Disulfide bondi570 ↔ 582By similarity
    Glycosylationi785 – 7851N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi790 – 7901N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi832 – 8321N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi839 – 8391N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi873 ↔ 916By similarity
    Disulfide bondi877 ↔ 921By similarity
    Disulfide bondi888 ↔ 905By similarity
    Glycosylationi894 – 8941N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    The precursor is cleaved by a furin endopeptidase.By similarity
    Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion By similarity.By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PaxDbiQ8TE56.
    PRIDEiQ8TE56.

    PTM databases

    PhosphoSiteiQ8TE56.

    Expressioni

    Tissue specificityi

    Isoform 1 and isoform 2 are expressed at high levels in the lung, brain, whole eye and retina. Isoform 1 shows a weaker expression in the heart, kidney and skeletal muscle. Isoform 2 shows a weaker expression in the kidney, bone marrow and skeletal muscle. Isoform 1 and isoform 2 are expressed at high levels in the fetal heart, kidney, and whole eye, whereas a weak expression is seen in the fetal liver.1 Publication

    Gene expression databases

    ArrayExpressiQ8TE56.
    BgeeiQ8TE56.
    CleanExiHS_ADAMTS17.
    GenevestigatoriQ8TE56.

    Interactioni

    Protein-protein interaction databases

    BioGridi128083. 1 interaction.
    STRINGi9606.ENSP00000268070.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8TE56.
    SMRiQ8TE56. Positions 234-711.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini232 – 452221Peptidase M12BPROSITE-ProRule annotationAdd
    BLAST
    Domaini453 – 54290DisintegrinAdd
    BLAST
    Domaini543 – 59856TSP type-1 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini800 – 86061TSP type-1 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini861 – 92262TSP type-1 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini925 – 96844TSP type-1 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini972 – 102958TSP type-1 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini1045 – 108440PLACPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni702 – 77978SpacerAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi199 – 2068Cysteine switchBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi60 – 12061Arg-richAdd
    BLAST
    Compositional biasi599 – 701103Cys-richAdd
    BLAST

    Domaini

    The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

    Sequence similaritiesi

    Contains 1 disintegrin domain.Curated
    Contains 1 peptidase M12B domain.PROSITE-ProRule annotation
    Contains 1 PLAC domain.PROSITE-ProRule annotation
    Contains 5 TSP type-1 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG259740.
    HOGENOMiHOG000004800.
    HOVERGENiHBG050621.
    InParanoidiQ8TE56.
    KOiK08631.
    OMAiASEWSQC.
    OrthoDBiEOG722J7P.
    PhylomeDBiQ8TE56.
    TreeFamiTF313537.

    Family and domain databases

    Gene3Di3.40.390.10. 1 hit.
    InterProiIPR010294. ADAM_spacer1.
    IPR024079. MetalloPept_cat_dom.
    IPR001590. Peptidase_M12B.
    IPR013273. Peptidase_M12B_ADAM-TS.
    IPR002870. Peptidase_M12B_N.
    IPR010909. PLAC.
    IPR000884. Thrombospondin_1_rpt.
    IPR007087. Znf_C2H2.
    [Graphical view]
    PfamiPF05986. ADAM_spacer1. 1 hit.
    PF01562. Pep_M12B_propep. 1 hit.
    PF08686. PLAC. 1 hit.
    PF01421. Reprolysin. 1 hit.
    PF00090. TSP_1. 4 hits.
    [Graphical view]
    PRINTSiPR01857. ADAMTSFAMILY.
    SMARTiSM00209. TSP1. 5 hits.
    [Graphical view]
    SUPFAMiSSF82895. SSF82895. 5 hits.
    PROSITEiPS50215. ADAM_MEPRO. 1 hit.
    PS50900. PLAC. 1 hit.
    PS50092. TSP1. 5 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms may exist.

    Isoform 1 (identifier: Q8TE56-1) [UniParc]FASTAAdd to Basket

    Also known as: a

    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.

    « Hide

    MCDGALLPPL VLPVLLLLVW GLDPGTAVGD AAADVEVVLP WRVRPDDVHL     50
    PPLPAAPGPR RRRRPRTPPA APRARPGERA LLLHLPAFGR DLYLQLRRDL 100
    RFLSRGFEVE EAGAARRRGR PAELCFYSGR VLGHPGSLVS LSACGAAGGL 150
    VGLIQLGQEQ VLIQPLNNSQ GPFSGREHLI RRKWSLTPSP SAEAQRPEQL 200
    CKVLTEKKKP TWGRPSRDWR ERRNAIRLTS EHTVETLVVA DADMVQYHGA 250
    EAAQRFILTV MNMVYNMFQH QSLGIKINIQ VTKLVLLRQR PAKLSIGHHG 300
    ERSLESFCHW QNEEYGGARY LGNNQVPGGK DDPPLVDAAV FVTRTDFCVH 350
    KDEPCDTVGI AYLGGVCSAK RKCVLAEDNG LNLAFTIAHE LGHNLGMNHD 400
    DDHSSCAGRS HIMSGEWVKG RNPSDLSWSS CSRDDLENFL KSKVSTCLLV 450
    TDPRSQHTVR LPHKLPGMHY SANEQCQILF GMNATFCRNM EHLMCAGLWC 500
    LVEGDTSCKT KLDPPLDGTE CGADKWCRAG ECVSKTPIPE HVDGDWSPWG 550
    AWSMCSRTCG TGARFRQRKC DNPPPGPGGT HCPGASVEHA VCENLPCPKG 600
    LPSFRDQQCQ AHDRLSPKKK GLLTAVVVDD KPCELYCSPL GKESPLLVAD 650
    RVLDGTPCGP YETDLCVHGK CQKIGCDGII GSAAKEDRCG VCSGDGKTCH 700
    LVKGDFSHAR GTALKDSGKG SINSDWKIEL PGEFQIAGTT VRYVRRGLWE 750
    KISAKGPTKL PLHLMVLLFH DQDYGIHYEY TVPVNRTAEN QSEPEKPQDS 800
    LFIWTHSGWE GCSVQCGGGE RRTIVSCTRI VNKTTTLVND SDCPQASRPE 850
    PQVRRCNLHP CQSRWVAGPW SPCSATCEKG FQHREVTCVY QLQNGTHVAT 900
    RPLYCPGPRP AAVQSCEGQD CLSIWEASEW SQCSASCGKG VWKRTVACTN 950
    SQGKCDASTR PRAEEACEDY SGCYEWKTGD WSTCSSTCGK GLQSRVVQCM 1000
    HKVTGRHGSE CPALSKPAPY RQCYQEVCND RINANTITSP RLAALTYKCT 1050
    RDQWTVYCRV IREKNLCQDM RWYQRCCQTC RDFYANKMRQ PPPNS 1095
    Length:1,095
    Mass (Da):121,127
    Last modified:May 18, 2010 - v2
    Checksum:iA5D7A40484754D5D
    GO
    Isoform 2 (identifier: Q8TE56-2) [UniParc]FASTAAdd to Basket

    Also known as: b

    The sequence of this isoform differs from the canonical sequence as follows:
         1-243: Missing.
         713-745: ALKDSGKGSINSDWKIELPGEFQIAGTTVRYVR → GYIEAAVIPAGARRIRVVEDKPAHSFLGKTQMT
         746-1095: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:502
    Mass (Da):54,757
    Checksum:i6CABF495FDC4AE21
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti702 – 7021V → A in BAD18500. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti216 – 2161S → L.1 Publication
    Corresponds to variant rs7496668 [ dbSNP | Ensembl ].
    VAR_057081
    Natural varianti482 – 4821M → T.1 Publication
    Corresponds to variant rs28567966 [ dbSNP | Ensembl ].
    VAR_057082
    Natural varianti566 – 5661R → T.1 Publication
    VAR_064041
    Natural varianti1094 – 10941N → S.2 Publications
    Corresponds to variant rs2573652 [ dbSNP | Ensembl ].
    VAR_060317

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 243243Missing in isoform 2. 1 PublicationVSP_040331Add
    BLAST
    Alternative sequencei713 – 74533ALKDS…VRYVR → GYIEAAVIPAGARRIRVVED KPAHSFLGKTQMT in isoform 2. 1 PublicationVSP_040332Add
    BLAST
    Alternative sequencei746 – 1095350Missing in isoform 2. 1 PublicationVSP_040333Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ315735 mRNA. Translation: CAC86016.1.
    DQ217943 Genomic DNA. Translation: ABB70740.1.
    AK131344 mRNA. Translation: BAD18500.1.
    AC015723 Genomic DNA. No translation available.
    AC022710 Genomic DNA. No translation available.
    AC084855 Genomic DNA. No translation available.
    AC113187 Genomic DNA. No translation available.
    CCDSiCCDS10383.1. [Q8TE56-1]
    RefSeqiNP_620688.2. NM_139057.2. [Q8TE56-1]
    UniGeneiHs.513200.

    Genome annotation databases

    EnsembliENST00000268070; ENSP00000268070; ENSG00000140470. [Q8TE56-1]
    GeneIDi170691.
    KEGGihsa:170691.
    UCSCiuc002bvv.1. human. [Q8TE56-1]
    uc002bvx.1. human. [Q8TE56-2]

    Polymorphism databases

    DMDMi296434401.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ315735 mRNA. Translation: CAC86016.1 .
    DQ217943 Genomic DNA. Translation: ABB70740.1 .
    AK131344 mRNA. Translation: BAD18500.1 .
    AC015723 Genomic DNA. No translation available.
    AC022710 Genomic DNA. No translation available.
    AC084855 Genomic DNA. No translation available.
    AC113187 Genomic DNA. No translation available.
    CCDSi CCDS10383.1. [Q8TE56-1 ]
    RefSeqi NP_620688.2. NM_139057.2. [Q8TE56-1 ]
    UniGenei Hs.513200.

    3D structure databases

    ProteinModelPortali Q8TE56.
    SMRi Q8TE56. Positions 234-711.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 128083. 1 interaction.
    STRINGi 9606.ENSP00000268070.

    Protein family/group databases

    MEROPSi M12.027.

    PTM databases

    PhosphoSitei Q8TE56.

    Polymorphism databases

    DMDMi 296434401.

    Proteomic databases

    PaxDbi Q8TE56.
    PRIDEi Q8TE56.

    Protocols and materials databases

    DNASUi 170691.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000268070 ; ENSP00000268070 ; ENSG00000140470 . [Q8TE56-1 ]
    GeneIDi 170691.
    KEGGi hsa:170691.
    UCSCi uc002bvv.1. human. [Q8TE56-1 ]
    uc002bvx.1. human. [Q8TE56-2 ]

    Organism-specific databases

    CTDi 170691.
    GeneCardsi GC15M100511.
    H-InvDB HIX0012615.
    HGNCi HGNC:17109. ADAMTS17.
    MIMi 607511. gene.
    613195. phenotype.
    neXtProti NX_Q8TE56.
    Orphaneti 363992. Ichthyosis-short stature-brachydactyly-microspherophakia syndrome.
    PharmGKBi PA24543.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG259740.
    HOGENOMi HOG000004800.
    HOVERGENi HBG050621.
    InParanoidi Q8TE56.
    KOi K08631.
    OMAi ASEWSQC.
    OrthoDBi EOG722J7P.
    PhylomeDBi Q8TE56.
    TreeFami TF313537.

    Enzyme and pathway databases

    Reactomei REACT_200626. O-glycosylation of TSR domain-containing proteins.

    Miscellaneous databases

    ChiTaRSi ADAMTS17. human.
    GenomeRNAii 170691.
    NextBioi 89106.
    PROi Q8TE56.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8TE56.
    Bgeei Q8TE56.
    CleanExi HS_ADAMTS17.
    Genevestigatori Q8TE56.

    Family and domain databases

    Gene3Di 3.40.390.10. 1 hit.
    InterProi IPR010294. ADAM_spacer1.
    IPR024079. MetalloPept_cat_dom.
    IPR001590. Peptidase_M12B.
    IPR013273. Peptidase_M12B_ADAM-TS.
    IPR002870. Peptidase_M12B_N.
    IPR010909. PLAC.
    IPR000884. Thrombospondin_1_rpt.
    IPR007087. Znf_C2H2.
    [Graphical view ]
    Pfami PF05986. ADAM_spacer1. 1 hit.
    PF01562. Pep_M12B_propep. 1 hit.
    PF08686. PLAC. 1 hit.
    PF01421. Reprolysin. 1 hit.
    PF00090. TSP_1. 4 hits.
    [Graphical view ]
    PRINTSi PR01857. ADAMTSFAMILY.
    SMARTi SM00209. TSP1. 5 hits.
    [Graphical view ]
    SUPFAMi SSF82895. SSF82895. 5 hits.
    PROSITEi PS50215. ADAM_MEPRO. 1 hit.
    PS50900. PLAC. 1 hit.
    PS50092. TSP1. 5 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, expression analysis, and structural characterization of seven novel human ADAMTSs, a family of metalloproteinases with disintegrin and thrombospondin-1 domains."
      Cal S., Obaya A.J., Llamazares M., Garabaya C., Quesada V., Lopez-Otin C.
      Gene 283:49-62(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-1094.
    2. "Genetic variation in ADAMTS17 gene."
      Tan J., Davila S., Hibberd M.L., Seielstad M.
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-566.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Thymus.
    4. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Homozygous mutations in ADAMTS10 and ADAMTS17 cause lenticular myopia, ectopia lentis, glaucoma, spherophakia, and short stature."
      Morales J., Al-Sharif L., Khalil D.S., Shinwari J.M., Bavi P., Al-Mahrouqi R.A., Al-Rajhi A., Alkuraya F.S., Meyer B.F., Al Tassan N.
      Am. J. Hum. Genet. 85:558-568(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS LEU-216; THR-482 AND SER-1094, INVOLVEMENT IN WMLS, ALTERNATIVE SPLICING, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiATS17_HUMAN
    AccessioniPrimary (citable) accession number: Q8TE56
    Secondary accession number(s): Q2I7G4, Q6ZN75
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 28, 2003
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 118 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

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