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Q8TE59

- ATS19_HUMAN

UniProt

Q8TE59 - ATS19_HUMAN

Protein

A disintegrin and metalloproteinase with thrombospondin motifs 19

Gene

ADAMTS19

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 2 (18 May 2010)
      Previous versions | rss
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    Functioni

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi294 – 2941Zinc; in inhibited formBy similarity
    Metal bindingi482 – 4821Zinc; catalyticBy similarity
    Active sitei483 – 4831PROSITE-ProRule annotation
    Metal bindingi486 – 4861Zinc; catalyticBy similarity
    Metal bindingi492 – 4921Zinc; 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

    MEROPSiM12.029.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    A disintegrin and metalloproteinase with thrombospondin motifs 19 (EC:3.4.24.-)
    Short name:
    ADAM-TS 19
    Short name:
    ADAM-TS19
    Short name:
    ADAMTS-19
    Gene namesi
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:17111. ADAMTS19.

    Subcellular locationi

    GO - Cellular componenti

    1. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24545.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Propeptidei22 – 316295By similarityPRO_0000029202Add
    BLAST
    Chaini317 – 1207891A disintegrin and metalloproteinase with thrombospondin motifs 19PRO_0000029203Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi260 – 2601N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi401 ↔ 466By similarity
    Disulfide bondi441 ↔ 448By similarity
    Disulfide bondi460 ↔ 540By similarity
    Disulfide bondi499 ↔ 524By similarity
    Disulfide bondi569 ↔ 593By similarity
    Disulfide bondi580 ↔ 601By similarity
    Disulfide bondi588 ↔ 620By similarity
    Disulfide bondi614 ↔ 625By similarity
    Disulfide bondi645 ↔ 680By similarity
    Disulfide bondi649 ↔ 685By similarity
    Disulfide bondi660 ↔ 670By similarity
    Glycosylationi797 – 7971N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi907 – 9071N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi949 – 9491N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi988 ↔ 1031By similarity
    Disulfide bondi992 ↔ 1036By similarity
    Disulfide bondi1003 ↔ 1020By similarity
    Glycosylationi1009 – 10091N-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

    PaxDbiQ8TE59.
    PRIDEiQ8TE59.

    PTM databases

    PhosphoSiteiQ8TE59.

    Expressioni

    Tissue specificityi

    Expressed in fetal lung, but not in any adult tissues examined. Expression was detected in an osteosarcoma cDNA library.

    Gene expression databases

    BgeeiQ8TE59.
    CleanExiHS_ADAMTS19.
    GenevestigatoriQ8TE59.

    Organism-specific databases

    HPAiHPA056171.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000274487.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8TE59.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini325 – 545221Peptidase M12BPROSITE-ProRule annotationAdd
    BLAST
    Domaini546 – 63388DisintegrinAdd
    BLAST
    Domaini634 – 68653TSP type-1 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini915 – 97561TSP type-1 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini976 – 103762TSP type-1 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini1039 – 108345TSP type-1 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini1087 – 114458TSP type-1 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini1160 – 119940PLACPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni791 – 914124SpacerAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi292 – 2998Cysteine switchBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi88 – 216129Pro-richAdd
    BLAST
    Compositional biasi687 – 790104Cys-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.
    InParanoidiQ8TE59.
    KOiK08633.
    OMAiEKECKTK.
    OrthoDBiEOG722J7P.
    PhylomeDBiQ8TE59.
    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.
    [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]

    Sequencei

    Sequence statusi: Complete.

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

    Q8TE59-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRLTHICCCC LLYQLGFLSN GIVSELQFAP DREEWEVVFP ALWRREPVDP     50
    AGGSGGSADP GWVRGVGGGG SARAQAAGSS REVRSVAPVP LEEPVEGRSE 100
    SRLRPPPPSE GEEDEELESQ ELPRGSSGAA ALSPGAPASW QPPPPPQPPP 150
    SPPPAQHAEP DGDEVLLRIP AFSRDLYLLL RRDGRFLAPR FAVEQRPNPG 200
    PGPTGAASAP QPPAPPDAGC FYTGAVLRHP GSLASFSTCG GGLMGFIQLN 250
    EDFIFIEPLN DTMAITGHPH RVYRQKRSME EKVTEKSALH SHYCGIISDK 300
    GRPRSRKIAE SGRGKRYSYK LPQEYNIETV VVADPAMVSY HGADAARRFI 350
    LTILNMVFNL FQHKSLSVQV NLRVIKLILL HETPPELYIG HHGEKMLESF 400
    CKWQHEEFGK KNDIHLEMST NWGEDMTSVD AAILITRKDF CVHKDEPCDT 450
    VGIAYLSGMC SEKRKCIIAE DNGLNLAFTI AHEMGHNMGI NHDNDHPSCA 500
    DGLHIMSGEW IKGQNLGDVS WSRCSKEDLE RFLRSKASNC LLQTNPQSVN 550
    SVMVPSKLPG MTYTADEQCQ ILFGPLASFC QEMQHVICTG LWCKVEGEKE 600
    CRTKLDPPMD GTDCDLGKWC KAGECTSRTS APEHLAGEWS LWSPCSRTCS 650
    AGISSRERKC PGLDSEARDC NGPRKQYRIC ENPPCPAGLP GFRDWQCQAY 700
    SVRTSSPKHI LQWQAVLDEE KPCALFCSPV GKEQPILLSE KVMDGTSCGY 750
    QGLDICANGR CQKVGCDGLL GSLAREDHCG VCNGNGKSCK IIKGDFNHTR 800
    GAGYVEVLVI PAGARRIKVV EEKPAHSYLA LRDAGKQSIN SDWKIEHSGA 850
    FNLAGTTVHY VRRGLWEKIS AKGPTTAPLH LLVLLFQDQN YGLHYEYTIP 900
    SDPLPENQSS KAPEPLFMWT HTSWEDCDAT CGGGERKTTV SCTKIMSKNI 950
    SIVDNEKCKY LTKPEPQIRK CNEQPCQTRW MMTEWTPCSR TCGKGMQSRQ 1000
    VACTQQLSNG TLIRARERDC IGPKPASAQR CEGQDCMTVW EAGVWSECSV 1050
    KCGKGIRHRT VRCTNPRKKC VLSTRPREAE DCEDYSKCYV WRMGDWSKCS 1100
    ITCGKGMQSR VIQCMHKITG RHGNECFSSE KPAAYRPCHL QPCNEKINVN 1150
    TITSPRLAAL TFKCLGDQWP VYCRVIREKN LCQDMRWYQR CCETCRDFYA 1200
    QKLQQKS 1207
    Length:1,207
    Mass (Da):134,048
    Last modified:May 18, 2010 - v2
    Checksum:i21EFB26660DEB6D9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti367 – 3671S → G in CAC84565. (PubMed:11867212)Curated
    Sequence conflicti1048 – 10481C → F in CAC84565. (PubMed:11867212)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti360 – 3601L → I in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036154
    Natural varianti582 – 5821E → G.
    Corresponds to variant rs10062501 [ dbSNP | Ensembl ].
    VAR_057087
    Natural varianti1089 – 10891Y → F.
    Corresponds to variant rs11749126 [ dbSNP | Ensembl ].
    VAR_024599

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ311904 mRNA. Translation: CAC84565.1.
    AC008425 Genomic DNA. No translation available.
    AC008528 Genomic DNA. No translation available.
    AC008591 Genomic DNA. No translation available.
    AC106781 Genomic DNA. No translation available.
    AC129713 Genomic DNA. No translation available.
    CCDSiCCDS4146.1.
    RefSeqiNP_598377.3. NM_133638.3.
    UniGeneiHs.23751.

    Genome annotation databases

    EnsembliENST00000274487; ENSP00000274487; ENSG00000145808.
    GeneIDi171019.
    KEGGihsa:171019.
    UCSCiuc003kvb.1. human.

    Polymorphism databases

    DMDMi296434402.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ311904 mRNA. Translation: CAC84565.1 .
    AC008425 Genomic DNA. No translation available.
    AC008528 Genomic DNA. No translation available.
    AC008591 Genomic DNA. No translation available.
    AC106781 Genomic DNA. No translation available.
    AC129713 Genomic DNA. No translation available.
    CCDSi CCDS4146.1.
    RefSeqi NP_598377.3. NM_133638.3.
    UniGenei Hs.23751.

    3D structure databases

    ProteinModelPortali Q8TE59.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000274487.

    Protein family/group databases

    MEROPSi M12.029.

    PTM databases

    PhosphoSitei Q8TE59.

    Polymorphism databases

    DMDMi 296434402.

    Proteomic databases

    PaxDbi Q8TE59.
    PRIDEi Q8TE59.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000274487 ; ENSP00000274487 ; ENSG00000145808 .
    GeneIDi 171019.
    KEGGi hsa:171019.
    UCSCi uc003kvb.1. human.

    Organism-specific databases

    CTDi 171019.
    GeneCardsi GC05P128824.
    H-InvDB HIX0024810.
    HGNCi HGNC:17111. ADAMTS19.
    HPAi HPA056171.
    MIMi 607513. gene.
    neXtProti NX_Q8TE59.
    PharmGKBi PA24545.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG259740.
    HOGENOMi HOG000004800.
    HOVERGENi HBG050621.
    InParanoidi Q8TE59.
    KOi K08633.
    OMAi EKECKTK.
    OrthoDBi EOG722J7P.
    PhylomeDBi Q8TE59.
    TreeFami TF313537.

    Enzyme and pathway databases

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

    Miscellaneous databases

    GenomeRNAii 171019.
    NextBioi 89186.
    PROi Q8TE59.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8TE59.
    CleanExi HS_ADAMTS19.
    Genevestigatori Q8TE59.

    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.
    [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].
    2. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: VARIANT [LARGE SCALE ANALYSIS] ILE-360.

    Entry informationi

    Entry nameiATS19_HUMAN
    AccessioniPrimary (citable) accession number: Q8TE59
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 25, 2003
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 115 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 5
      Human chromosome 5: 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

    Dasty 3