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Q9UHI8

- ATS1_HUMAN

UniProt

Q9UHI8 - ATS1_HUMAN

Protein

A disintegrin and metalloproteinase with thrombospondin motifs 1

Gene

ADAMTS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Cleaves aggrecan, a cartilage proteoglycan, and may be involved in its turnover By similarity. Has angiogenic inhibitor activity. Active metalloprotease, which may be associated with various inflammatory processes as well as development of cancer cachexia. May play a critical role in follicular rupture.By similarity1 Publication

    Catalytic activityi

    Cleaves aggrecan at the 1938-Glu-|-Leu-1939 site, within the chondroitin sulfate attachment domain.

    Cofactori

    Binds 1 zinc ion per subunit.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi198 – 1981Zinc; in inhibited formBy similarity
    Metal bindingi261 – 2611Calcium 1
    Metal bindingi261 – 2611Calcium 2
    Metal bindingi344 – 3441Calcium 1
    Metal bindingi344 – 3441Calcium 2; via carbonyl oxygen
    Metal bindingi351 – 3511Calcium 1
    Metal bindingi401 – 4011Zinc; catalytic
    Active sitei402 – 40211 PublicationPROSITE-ProRule annotation
    Metal bindingi405 – 4051Zinc; catalytic
    Metal bindingi411 – 4111Zinc; catalytic
    Metal bindingi462 – 4621Calcium 1; via carbonyl oxygen
    Metal bindingi465 – 4651Calcium 1
    Metal bindingi465 – 4651Calcium 2

    GO - Molecular functioni

    1. heparin binding Source: UniProtKB-KW
    2. metalloendopeptidase activity Source: Ensembl
    3. metallopeptidase activity Source: ProtInc
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. heart trabecula formation Source: Ensembl
    2. integrin-mediated signaling pathway Source: ProtInc
    3. kidney development Source: Ensembl
    4. negative regulation of cell proliferation Source: ProtInc
    5. ovulation from ovarian follicle Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Calcium, Heparin-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_118572. Degradation of the extracellular matrix.
    REACT_200626. O-glycosylation of TSR domain-containing proteins.
    REACT_201925. Degradation of the extracellular matrix.

    Protein family/group databases

    MEROPSiM12.222.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    A disintegrin and metalloproteinase with thrombospondin motifs 1 (EC:3.4.24.-)
    Short name:
    ADAM-TS 1
    Short name:
    ADAM-TS1
    Short name:
    ADAMTS-1
    Alternative name(s):
    METH-1
    Gene namesi
    Name:ADAMTS1
    Synonyms:KIAA1346, METH1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 21

    Organism-specific databases

    HGNCiHGNC:217. ADAMTS1.

    Subcellular locationi

    GO - Cellular componenti

    1. basement membrane Source: Ensembl
    2. cytoplasm Source: HPA
    3. cytoplasmic vesicle Source: Ensembl

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24536.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 4949Sequence AnalysisAdd
    BLAST
    Propeptidei50 – 252203By similarityPRO_0000029150Add
    BLAST
    Chaini253 – 967715A disintegrin and metalloproteinase with thrombospondin motifs 1PRO_0000029151Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi333 ↔ 3851 Publication
    Disulfide bondi362 ↔ 3671 Publication
    Disulfide bondi379 ↔ 4621 Publication
    Disulfide bondi417 ↔ 4461 Publication
    Disulfide bondi488 ↔ 5111 Publication
    Disulfide bondi499 ↔ 5211 Publication
    Disulfide bondi506 ↔ 5401 Publication
    Disulfide bondi534 ↔ 5451 Publication
    Glycosylationi547 – 5471N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi571 ↔ 608By similarity
    Disulfide bondi575 ↔ 613By similarity
    Disulfide bondi586 ↔ 598By similarity
    Glycosylationi720 – 7201N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi764 – 7641N-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

    MaxQBiQ9UHI8.
    PaxDbiQ9UHI8.
    PeptideAtlasiQ9UHI8.
    PRIDEiQ9UHI8.

    PTM databases

    PhosphoSiteiQ9UHI8.

    Miscellaneous databases

    PMAP-CutDBQ9UHI8.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9UHI8.
    BgeeiQ9UHI8.
    CleanExiHS_ADAMTS1.
    GenevestigatoriQ9UHI8.

    Organism-specific databases

    HPAiCAB016394.
    HPA031498.
    HPA031499.

    Interactioni

    Protein-protein interaction databases

    BioGridi114888. 4 interactions.
    IntActiQ9UHI8. 2 interactions.
    STRINGi9606.ENSP00000284984.

    Structurei

    Secondary structure

    1
    967
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi258 – 2669
    Helixi268 – 2747
    Helixi275 – 2773
    Helixi278 – 29316
    Helixi296 – 2983
    Beta strandi302 – 31110
    Helixi315 – 3173
    Helixi325 – 33612
    Helixi337 – 3393
    Beta strandi351 – 3599
    Beta strandi371 – 3733
    Turni381 – 3833
    Beta strandi385 – 3895
    Helixi395 – 40612
    Helixi415 – 4173
    Turni418 – 4203
    Helixi445 – 45612
    Turni457 – 4604
    Helixi461 – 4644
    Helixi478 – 4814
    Helixi484 – 4929
    Beta strandi510 – 5134
    Beta strandi520 – 5234
    Beta strandi538 – 5414
    Beta strandi544 – 5485

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JIHX-ray2.10A/B253-548[»]
    2V4BX-ray2.00A/B253-548[»]
    3Q2GX-ray2.30A/B256-548[»]
    3Q2HX-ray2.33A/B256-548[»]
    ProteinModelPortaliQ9UHI8.
    SMRiQ9UHI8. Positions 256-844.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UHI8.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini258 – 467210Peptidase M12BPROSITE-ProRule annotationAdd
    BLAST
    Domaini476 – 55984DisintegrinAdd
    BLAST
    Domaini559 – 61456TSP type-1 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini854 – 90552TSP type-1 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini908 – 96760TSP type-1 3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni725 – 849125SpacerAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi196 – 2038Cysteine switchBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi617 – 724108Cys-richAdd
    BLAST
    Compositional biasi843 – 8464Poly-Lys

    Domaini

    The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix.
    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 3 TSP type-1 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG291688.
    HOGENOMiHOG000004799.
    HOVERGENiHBG004313.
    InParanoidiQ9UHI8.
    KOiK08617.
    OMAiCPDNNGK.
    OrthoDBiEOG7WDN1M.
    PhylomeDBiQ9UHI8.
    TreeFamiTF331949.

    Family and domain databases

    Gene3Di3.40.390.10. 1 hit.
    InterProiIPR006586. ADAM_Cys-rich.
    IPR010294. ADAM_spacer1.
    IPR024079. MetalloPept_cat_dom.
    IPR013274. Pept_M12B_ADAM-TS1.
    IPR001590. Peptidase_M12B.
    IPR013273. Peptidase_M12B_ADAM-TS.
    IPR002870. Peptidase_M12B_N.
    IPR000884. Thrombospondin_1_rpt.
    [Graphical view]
    PfamiPF05986. ADAM_spacer1. 1 hit.
    PF01562. Pep_M12B_propep. 1 hit.
    PF01421. Reprolysin. 1 hit.
    PF00090. TSP_1. 3 hits.
    [Graphical view]
    PRINTSiPR01858. ADAMTS1.
    PR01857. ADAMTSFAMILY.
    SMARTiSM00608. ACR. 1 hit.
    SM00209. TSP1. 3 hits.
    [Graphical view]
    SUPFAMiSSF82895. SSF82895. 3 hits.
    PROSITEiPS50215. ADAM_MEPRO. 1 hit.
    PS50092. TSP1. 3 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9UHI8-1 [UniParc]FASTAAdd to Basket

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    MQRAVPEGFG RRKLGSDMGN AERAPGSRSF GPVPTLLLLA AALLAVSDAL    50
    GRPSEEDEEL VVPELERAPG HGTTRLRLHA FDQQLDLELR PDSSFLAPGF 100
    TLQNVGRKSG SETPLPETDL AHCFYSGTVN GDPSSAAALS LCEGVRGAFY 150
    LLGEAYFIQP LPAASERLAT AAPGEKPPAP LQFHLLRRNR QGDVGGTCGV 200
    VDDEPRPTGK AETEDEDEGT EGEDEGAQWS PQDPALQGVG QPTGTGSIRK 250
    KRFVSSHRYV ETMLVADQSM AEFHGSGLKH YLLTLFSVAA RLYKHPSIRN 300
    SVSLVVVKIL VIHDEQKGPE VTSNAALTLR NFCNWQKQHN PPSDRDAEHY 350
    DTAILFTRQD LCGSQTCDTL GMADVGTVCD PSRSCSVIED DGLQAAFTTA 400
    HELGHVFNMP HDDAKQCASL NGVNQDSHMM ASMLSNLDHS QPWSPCSAYM 450
    ITSFLDNGHG ECLMDKPQNP IQLPGDLPGT SYDANRQCQF TFGEDSKHCP 500
    DAASTCSTLW CTGTSGGVLV CQTKHFPWAD GTSCGEGKWC INGKCVNKTD 550
    RKHFDTPFHG SWGMWGPWGD CSRTCGGGVQ YTMRECDNPV PKNGGKYCEG 600
    KRVRYRSCNL EDCPDNNGKT FREEQCEAHN EFSKASFGSG PAVEWIPKYA 650
    GVSPKDRCKL ICQAKGIGYF FVLQPKVVDG TPCSPDSTSV CVQGQCVKAG 700
    CDRIIDSKKK FDKCGVCGGN GSTCKKISGS VTSAKPGYHD IITIPTGATN 750
    IEVKQRNQRG SRNNGSFLAI KAADGTYILN GDYTLSTLEQ DIMYKGVVLR 800
    YSGSSAALER IRSFSPLKEP LTIQVLTVGN ALRPKIKYTY FVKKKKESFN 850
    AIPTFSAWVI EEWGECSKSC ELGWQRRLVE CRDINGQPAS ECAKEVKPAS 900
    TRPCADHPCP QWQLGEWSSC SKTCGKGYKK RSLKCLSHDG GVLSHESCDP 950
    LKKPKHFIDF CTMAECS 967
    Length:967
    Mass (Da):105,358
    Last modified:January 23, 2007 - v4
    Checksum:i334119D6310A05A7
    GO

    Sequence cautioni

    The sequence AAD48080.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAA92584.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti468 – 4681Q → H in AAF15317. 1 PublicationCurated
    Sequence conflicti561 – 5611S → N in AAF15317. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti227 – 2271A → P.3 Publications
    Corresponds to variant rs428785 [ dbSNP | Ensembl ].
    VAR_030001

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF170084 mRNA. Translation: AAF15317.1.
    AF060152 mRNA. Translation: AAD48080.1. Different initiation.
    AF207664 mRNA. Translation: AAF23772.1.
    AB037767 mRNA. Translation: BAA92584.1. Different initiation.
    AP001697 Genomic DNA. Translation: BAA95502.1.
    CH471079 Genomic DNA. Translation: EAX09951.1.
    CH471079 Genomic DNA. Translation: EAX09952.1.
    AL162080 mRNA. Translation: CAB82413.1.
    CCDSiCCDS33524.1.
    PIRiT47158.
    RefSeqiNP_008919.3. NM_006988.3.
    UniGeneiHs.643357.

    Genome annotation databases

    EnsembliENST00000284984; ENSP00000284984; ENSG00000154734.
    GeneIDi9510.
    KEGGihsa:9510.
    UCSCiuc002ymf.3. human.

    Polymorphism databases

    DMDMi124053460.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF170084 mRNA. Translation: AAF15317.1 .
    AF060152 mRNA. Translation: AAD48080.1 . Different initiation.
    AF207664 mRNA. Translation: AAF23772.1 .
    AB037767 mRNA. Translation: BAA92584.1 . Different initiation.
    AP001697 Genomic DNA. Translation: BAA95502.1 .
    CH471079 Genomic DNA. Translation: EAX09951.1 .
    CH471079 Genomic DNA. Translation: EAX09952.1 .
    AL162080 mRNA. Translation: CAB82413.1 .
    CCDSi CCDS33524.1.
    PIRi T47158.
    RefSeqi NP_008919.3. NM_006988.3.
    UniGenei Hs.643357.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2JIH X-ray 2.10 A/B 253-548 [» ]
    2V4B X-ray 2.00 A/B 253-548 [» ]
    3Q2G X-ray 2.30 A/B 256-548 [» ]
    3Q2H X-ray 2.33 A/B 256-548 [» ]
    ProteinModelPortali Q9UHI8.
    SMRi Q9UHI8. Positions 256-844.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114888. 4 interactions.
    IntActi Q9UHI8. 2 interactions.
    STRINGi 9606.ENSP00000284984.

    Chemistry

    BindingDBi Q9UHI8.
    ChEMBLi CHEMBL5133.

    Protein family/group databases

    MEROPSi M12.222.

    PTM databases

    PhosphoSitei Q9UHI8.

    Polymorphism databases

    DMDMi 124053460.

    Proteomic databases

    MaxQBi Q9UHI8.
    PaxDbi Q9UHI8.
    PeptideAtlasi Q9UHI8.
    PRIDEi Q9UHI8.

    Protocols and materials databases

    DNASUi 9510.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000284984 ; ENSP00000284984 ; ENSG00000154734 .
    GeneIDi 9510.
    KEGGi hsa:9510.
    UCSCi uc002ymf.3. human.

    Organism-specific databases

    CTDi 9510.
    GeneCardsi GC21M028208.
    HGNCi HGNC:217. ADAMTS1.
    HPAi CAB016394.
    HPA031498.
    HPA031499.
    MIMi 605174. gene.
    neXtProti NX_Q9UHI8.
    PharmGKBi PA24536.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG291688.
    HOGENOMi HOG000004799.
    HOVERGENi HBG004313.
    InParanoidi Q9UHI8.
    KOi K08617.
    OMAi CPDNNGK.
    OrthoDBi EOG7WDN1M.
    PhylomeDBi Q9UHI8.
    TreeFami TF331949.

    Enzyme and pathway databases

    Reactomei REACT_118572. Degradation of the extracellular matrix.
    REACT_200626. O-glycosylation of TSR domain-containing proteins.
    REACT_201925. Degradation of the extracellular matrix.

    Miscellaneous databases

    ChiTaRSi ADAMTS1. human.
    EvolutionaryTracei Q9UHI8.
    GeneWikii ADAMTS1.
    GenomeRNAii 9510.
    NextBioi 35638.
    PMAP-CutDB Q9UHI8.
    PROi Q9UHI8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UHI8.
    Bgeei Q9UHI8.
    CleanExi HS_ADAMTS1.
    Genevestigatori Q9UHI8.

    Family and domain databases

    Gene3Di 3.40.390.10. 1 hit.
    InterProi IPR006586. ADAM_Cys-rich.
    IPR010294. ADAM_spacer1.
    IPR024079. MetalloPept_cat_dom.
    IPR013274. Pept_M12B_ADAM-TS1.
    IPR001590. Peptidase_M12B.
    IPR013273. Peptidase_M12B_ADAM-TS.
    IPR002870. Peptidase_M12B_N.
    IPR000884. Thrombospondin_1_rpt.
    [Graphical view ]
    Pfami PF05986. ADAM_spacer1. 1 hit.
    PF01562. Pep_M12B_propep. 1 hit.
    PF01421. Reprolysin. 1 hit.
    PF00090. TSP_1. 3 hits.
    [Graphical view ]
    PRINTSi PR01858. ADAMTS1.
    PR01857. ADAMTSFAMILY.
    SMARTi SM00608. ACR. 1 hit.
    SM00209. TSP1. 3 hits.
    [Graphical view ]
    SUPFAMi SSF82895. SSF82895. 3 hits.
    PROSITEi PS50215. ADAM_MEPRO. 1 hit.
    PS50092. TSP1. 3 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, characterization and mapping on human chromosome 21 of the orthologue of murine Adamts-1."
      Casas C., Pritchard M.A., Estivill X., Arbones M.L.
      Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PRO-227.
    2. "METH-1, a human ortholog of ADAMTS-1, and METH-2 are members of a new family of proteins with angio-inhibitory activity."
      Vazquez F., Hastings G., Ortega M.-A., Lane T.F., Oikemus S., Lombardo M., Iruela-Arispe M.L.
      J. Biol. Chem. 274:23349-23357(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PRO-227, FUNCTION.
      Tissue: Heart.
    3. "Differential gene expression by endothelial cells in distinct angiogenic states."
      Glienke J., Schmitt A.O., Pilarsky C., Hinzmann B., Weiss B., Rosenthal A., Thierauch K.H.
      Eur. J. Biochem. 267:2820-2830(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PRO-227.
      Tissue: Endothelial cell.
    4. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
      DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    5. "The DNA sequence of human chromosome 21."
      Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A.
      , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
      Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 418-967.
      Tissue: Melanoma.
    8. "Crystal structures of human ADAMTS-1 reveal a conserved catalytic domain and a disintegrin-like domain with a fold homologous to cysteine-rich domains."
      Gerhardt S., Hassall G., Hawtin P., McCall E., Flavell L., Minshull C., Hargreaves D., Ting A., Pauptit R.A., Parker A.E., Abbott W.M.
      J. Mol. Biol. 373:891-902(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 253-548 ALONE AND IN COMPLEX WITH INHIBITOR, ACTIVE SITE, COFACTOR, ZINC-BINDING SITES, CALCIUM-BINDING SITES, DISULFIDE BONDS.

    Entry informationi

    Entry nameiATS1_HUMAN
    AccessioniPrimary (citable) accession number: Q9UHI8
    Secondary accession number(s): D3DSD5
    , Q9NSJ8, Q9P2K0, Q9UH83, Q9UP80
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 146 of the entry and version 4 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 21
      Human chromosome 21: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3