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P58397

- ATS12_HUMAN

UniProt

P58397 - ATS12_HUMAN

Protein

A disintegrin and metalloproteinase with thrombospondin motifs 12

Gene

ADAMTS12

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 2 (22 Sep 2009)
      Previous versions | rss
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    Functioni

    Metalloprotease that may play a role in the degradation of COMP. Cleaves also alpha-2 macroglobulin and aggregan. Has anti-tumorigenic properties.3 Publications

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Enzyme regulationi

    Inhibited by alpha-2 macroglobulin.1 Publication

    pH dependencei

    Optimum pH is between 7.5 and 9.5 with COMP for substrate.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi208 – 2081Zinc; in inhibited formBy similarity
    Metal bindingi392 – 3921Zinc; catalyticBy similarity
    Active sitei393 – 3931PROSITE-ProRule annotation
    Metal bindingi396 – 3961Zinc; catalyticBy similarity
    Metal bindingi402 – 4021Zinc; catalyticBy similarity

    GO - Molecular functioni

    1. metalloendopeptidase activity Source: BHF-UCL
    2. protein binding Source: IntAct
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cell-matrix adhesion Source: BHF-UCL
    2. cell migration Source: BHF-UCL
    3. cellular response to BMP stimulus Source: BHF-UCL
    4. cellular response to interleukin-1 Source: BHF-UCL
    5. cellular response to tumor necrosis factor Source: BHF-UCL
    6. negative regulation of cellular response to hepatocyte growth factor stimulus Source: BHF-UCL
    7. negative regulation of cellular response to vascular endothelial growth factor stimulus Source: BHF-UCL
    8. negative regulation of chondrocyte differentiation Source: BHF-UCL
    9. negative regulation of hepatocyte growth factor receptor signaling pathway Source: BHF-UCL
    10. proteoglycan catabolic process Source: BHF-UCL
    11. proteolysis involved in cellular protein catabolic process Source: BHF-UCL
    12. regulation of endothelial tube morphogenesis Source: BHF-UCL
    13. regulation of inflammatory response Source: BHF-UCL

    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

    MEROPSiM12.237.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    A disintegrin and metalloproteinase with thrombospondin motifs 12 (EC:3.4.24.-)
    Short name:
    ADAM-TS 12
    Short name:
    ADAM-TS12
    Short name:
    ADAMTS-12
    Gene namesi
    ORF Names:UNQ1918/PRO4389
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:14605. ADAMTS12.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular matrix Source: BHF-UCL
    2. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24538.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Sequence AnalysisAdd
    BLAST
    Propeptidei26 – 240215By similarityPRO_0000029186Add
    BLAST
    Chaini241 – 15941354A disintegrin and metalloproteinase with thrombospondin motifs 12PRO_0000029187Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi105 – 1051N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi125 – 1251N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi215 – 2151N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi322 ↔ 376By similarity
    Disulfide bondi351 ↔ 358By similarity
    Disulfide bondi370 ↔ 451By similarity
    Disulfide bondi409 ↔ 435By similarity
    Disulfide bondi478 ↔ 501By similarity
    Glycosylationi485 – 4851N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi489 ↔ 507By similarity
    Disulfide bondi496 ↔ 526By similarity
    Disulfide bondi520 ↔ 531By similarity
    Disulfide bondi554 ↔ 591By similarity
    Disulfide bondi558 ↔ 596By similarity
    Disulfide bondi569 ↔ 581By similarity
    Glycosylationi685 – 6851N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi790 – 7901N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi952 – 9521N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1105 – 11051N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1276 – 12761N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1301 – 13011N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1321 – 13211N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1372 – 13721N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1379 – 13791N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1504 – 15041N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    The precursor is cleaved by a furin endopeptidase.
    Subjected to an intracellular maturation process yielding a 120 kDa N-terminal fragment containing the metalloproteinase, disintegrin, one TSP type-1 and the Cys-rich domains and a 83 kDa C-terminal fragment containing the spacer 2 and four TSP type-1 domains.
    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

    PaxDbiP58397.
    PRIDEiP58397.

    PTM databases

    PhosphoSiteiP58397.

    Expressioni

    Tissue specificityi

    Expressed in skeletal muscle and fat. Detected at significant levels in fetal lung. Widely expressed in gastric carcinomas and in cancer cells of diverse origin.2 Publications

    Inductioni

    By IFN-alpha and by IL1B/interleukin-1 beta. Up-regulated in articular cartilage and synovium from arthritis patients. Up-regulared in chondrocytes.2 Publications

    Gene expression databases

    ArrayExpressiP58397.
    BgeeiP58397.
    CleanExiHS_ADAMTS12.
    GenevestigatoriP58397.

    Organism-specific databases

    HPAiHPA035973.

    Interactioni

    Subunit structurei

    Interacts with COMP.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    COMPP497473EBI-9028051,EBI-2531022
    CompQ9R0G63EBI-9028051,EBI-9028018From a different organism.

    Protein-protein interaction databases

    IntActiP58397. 3 interactions.
    STRINGi9606.ENSP00000344847.

    Structurei

    3D structure databases

    ProteinModelPortaliP58397.
    SMRiP58397. Positions 246-810.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini246 – 456211Peptidase M12BPROSITE-ProRule annotationAdd
    BLAST
    Domaini465 – 54480DisintegrinAdd
    BLAST
    Domaini542 – 59756TSP type-1 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini823 – 88361TSP type-1 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini887 – 94357TSP type-1 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini944 – 99754TSP type-1 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini1313 – 136654TSP type-1 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini1368 – 142255TSP type-1 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini1423 – 147149TSP type-1 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini1472 – 153261TSP type-1 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini1535 – 157541PLACPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni701 – 827127Spacer 1Add
    BLAST
    Regioni997 – 1316320Spacer 2Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi208 – 2136Cysteine switchBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi302 – 3054Poly-Glu
    Compositional biasi597 – 700104Cys-richAdd
    BLAST

    Domaini

    The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix.By similarity
    The C-terminal four TSP1-like repeats are necessary and sufficient for binding COMP.
    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 8 TSP type-1 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG237764.
    HOGENOMiHOG000015092.
    HOVERGENiHBG050620.
    InParanoidiP58397.
    KOiK08626.
    OMAiPFIMSRQ.
    OrthoDBiEOG7V765X.
    PhylomeDBiP58397.
    TreeFamiTF313537.

    Family and domain databases

    Gene3Di3.40.390.10. 2 hits.
    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.
    PF01421. Reprolysin. 1 hit.
    PF00090. TSP_1. 8 hits.
    [Graphical view]
    PRINTSiPR01857. ADAMTSFAMILY.
    SMARTiSM00209. TSP1. 8 hits.
    [Graphical view]
    SUPFAMiSSF82895. SSF82895. 8 hits.
    PROSITEiPS50215. ADAM_MEPRO. 1 hit.
    PS50900. PLAC. 1 hit.
    PS50092. TSP1. 6 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P58397-1) [UniParc]FASTAAdd to Basket

    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

    MPCAQRSWLA NLSVVAQLLN FGALCYGRQP QPGPVRFPDR RQEHFIKGLP     50
    EYHVVGPVRV DASGHFLSYG LHYPITSSRR KRDLDGSEDW VYYRISHEEK 100
    DLFFNLTVNQ GFLSNSYIME KRYGNLSHVK MMASSAPLCH LSGTVLQQGT 150
    RVGTAALSAC HGLTGFFQLP HGDFFIEPVK KHPLVEGGYH PHIVYRRQKV 200
    PETKEPTCGL KDSVNISQKQ ELWREKWERH NLPSRSLSRR SISKERWVET 250
    LVVADTKMIE YHGSENVESY ILTIMNMVTG LFHNPSIGNA IHIVVVRLIL 300
    LEEEEQGLKI VHHAEKTLSS FCKWQKSINP KSDLNPVHHD VAVLLTRKDI 350
    CAGFNRPCET LGLSHLSGMC QPHRSCNINE DSGLPLAFTI AHELGHSFGI 400
    QHDGKENDCE PVGRHPYIMS RQLQYDPTPL TWSKCSEEYI TRFLDRGWGF 450
    CLDDIPKKKG LKSKVIAPGV IYDVHHQCQL QYGPNATFCQ EVENVCQTLW 500
    CSVKGFCRSK LDAAADGTQC GEKKWCMAGK CITVGKKPES IPGGWGRWSP 550
    WSHCSRTCGA GVQSAERLCN NPEPKFGGKY CTGERKRYRL CNVHPCRSEA 600
    PTFRQMQCSE FDTVPYKNEL YHWFPIFNPA HPCELYCRPI DGQFSEKMLD 650
    AVIDGTPCFE GGNSRNVCIN GICKMVGCDY EIDSNATEDR CGVCLGDGSS 700
    CQTVRKMFKQ KEGSGYVDIG LIPKGARDIR VMEIEGAGNF LAIRSEDPEK 750
    YYLNGGFIIQ WNGNYKLAGT VFQYDRKGDL EKLMATGPTN ESVWIQLLFQ 800
    VTNPGIKYEY TIQKDGLDND VEQQMYFWQY GHWTECSVTC GTGIRRQTAH 850
    CIKKGRGMVK ATFCDPETQP NGRQKKCHEK ACPPRWWAGE WEACSATCGP 900
    HGEKKRTVLC IQTMVSDEQA LPPTDCQHLL KPKTLLSCNR DILCPSDWTV 950
    GNWSECSVSC GGGVRIRSVT CAKNHDEPCD VTRKPNSRAL CGLQQCPSSR 1000
    RVLKPNKGTI SNGKNPPTLK PVPPPTSRPR MLTTPTGPES MSTSTPAISS 1050
    PSPTTASKEG DLGGKQWQDS STQPELSSRY LISTGSTSQP ILTSQSLSIQ 1100
    PSEENVSSSD TGPTSEGGLV ATTTSGSGLS SSRNPITWPV TPFYNTLTKG 1150
    PEMEIHSGSG EEREQPEDKD ESNPVIWTKI RVPGNDAPVE STEMPLAPPL 1200
    TPDLSRESWW PPFSTVMEGL LPSQRPTTSE TGTPRVEGMV TEKPANTLLP 1250
    LGGDHQPEPS GKTANRNHLK LPNNMNQTKS SEPVLTEEDA TSLITEGFLL 1300
    NASNYKQLTN GHGSAHWIVG NWSECSTTCG LGAYWRRVEC STQMDSDCAA 1350
    IQRPDPAKRC HLRPCAGWKV GNWSKCSRNC SGGFKIREIQ CVDSRDHRNL 1400
    RPFHCQFLAG IPPPLSMSCN PEPCEAWQVE PWSQCSRSCG GGVQERGVFC 1450
    PGGLCDWTKR PTSTMSCNEH LCCHWATGNW DLCSTSCGGG FQKRTVQCVP 1500
    SEGNKTEDQD QCLCDHKPRP PEFKKCNQQA CKKSADLLCT KDKLSASFCQ 1550
    TLKAMKKCSV PTVRAECCFS CPQTHITHTQ RQRRQRLLQK SKEL 1594
    Length:1,594
    Mass (Da):177,676
    Last modified:September 22, 2009 - v2
    Checksum:iC88563125F0F90D8
    GO
    Isoform 2 (identifier: P58397-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         212-229: DSVNISQKQELWREKWER → GIVTHMSSWVEESVLFFW
         230-1594: Missing.

    Show »
    Length:229
    Mass (Da):26,003
    Checksum:i11FBCB40E82091F6
    GO
    Isoform 3 (identifier: P58397-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         630-714: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,509
    Mass (Da):168,460
    Checksum:i5BF525F456FC8EE5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti824 – 8241Missing in CAC20419. (PubMed:11279086)Curated
    Sequence conflicti1336 – 13361R → K in CAC20419. (PubMed:11279086)Curated
    Sequence conflicti1341 – 13411S → T in CAC20419. (PubMed:11279086)Curated
    Sequence conflicti1578 – 15781H → R in AAI31734. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti110 – 1101Q → E.
    Corresponds to variant rs16891862 [ dbSNP | Ensembl ].
    VAR_057074
    Natural varianti1000 – 10001R → Q.
    Corresponds to variant rs13362345 [ dbSNP | Ensembl ].
    VAR_057075
    Natural varianti1177 – 11771W → R.
    Corresponds to variant rs3813474 [ dbSNP | Ensembl ].
    VAR_059761
    Natural varianti1495 – 14951T → I.1 Publication
    Corresponds to variant rs25754 [ dbSNP | Ensembl ].
    VAR_058972
    Natural varianti1591 – 15911S → P.
    Corresponds to variant rs16891281 [ dbSNP | Ensembl ].
    VAR_059762

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei212 – 22918DSVNI…EKWER → GIVTHMSSWVEESVLFFW in isoform 2. 2 PublicationsVSP_013141Add
    BLAST
    Alternative sequencei230 – 15941365Missing in isoform 2. 2 PublicationsVSP_013142Add
    BLAST
    Alternative sequencei630 – 71485Missing in isoform 3. 1 PublicationVSP_038151Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ250725 mRNA. Translation: CAC20419.1.
    AY358745 mRNA. Translation: AAQ89105.1.
    AC008880 Genomic DNA. No translation available.
    AC034232 Genomic DNA. No translation available.
    AC109491 Genomic DNA. No translation available.
    AC139777 Genomic DNA. No translation available.
    BC058841 mRNA. Translation: AAH58841.1.
    BC131733 mRNA. Translation: AAI31734.1.
    BC139900 mRNA. Translation: AAI39901.1.
    CCDSiCCDS34140.1. [P58397-1]
    RefSeqiNP_112217.2. NM_030955.2. [P58397-1]
    UniGeneiHs.12680.

    Genome annotation databases

    EnsembliENST00000352040; ENSP00000344847; ENSG00000151388. [P58397-3]
    ENST00000504830; ENSP00000422554; ENSG00000151388. [P58397-1]
    GeneIDi81792.
    KEGGihsa:81792.
    UCSCiuc003jia.1. human. [P58397-1]
    uc010iuq.1. human. [P58397-3]

    Polymorphism databases

    DMDMi259016182.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ250725 mRNA. Translation: CAC20419.1 .
    AY358745 mRNA. Translation: AAQ89105.1 .
    AC008880 Genomic DNA. No translation available.
    AC034232 Genomic DNA. No translation available.
    AC109491 Genomic DNA. No translation available.
    AC139777 Genomic DNA. No translation available.
    BC058841 mRNA. Translation: AAH58841.1 .
    BC131733 mRNA. Translation: AAI31734.1 .
    BC139900 mRNA. Translation: AAI39901.1 .
    CCDSi CCDS34140.1. [P58397-1 ]
    RefSeqi NP_112217.2. NM_030955.2. [P58397-1 ]
    UniGenei Hs.12680.

    3D structure databases

    ProteinModelPortali P58397.
    SMRi P58397. Positions 246-810.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P58397. 3 interactions.
    STRINGi 9606.ENSP00000344847.

    Protein family/group databases

    MEROPSi M12.237.

    PTM databases

    PhosphoSitei P58397.

    Polymorphism databases

    DMDMi 259016182.

    Proteomic databases

    PaxDbi P58397.
    PRIDEi P58397.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000352040 ; ENSP00000344847 ; ENSG00000151388 . [P58397-3 ]
    ENST00000504830 ; ENSP00000422554 ; ENSG00000151388 . [P58397-1 ]
    GeneIDi 81792.
    KEGGi hsa:81792.
    UCSCi uc003jia.1. human. [P58397-1 ]
    uc010iuq.1. human. [P58397-3 ]

    Organism-specific databases

    CTDi 81792.
    GeneCardsi GC05M033495.
    HGNCi HGNC:14605. ADAMTS12.
    HPAi HPA035973.
    MIMi 606184. gene.
    neXtProti NX_P58397.
    PharmGKBi PA24538.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG237764.
    HOGENOMi HOG000015092.
    HOVERGENi HBG050620.
    InParanoidi P58397.
    KOi K08626.
    OMAi PFIMSRQ.
    OrthoDBi EOG7V765X.
    PhylomeDBi P58397.
    TreeFami TF313537.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi ADAMTS12. human.
    GeneWikii ADAMTS12.
    GenomeRNAii 81792.
    NextBioi 72100.
    PROi P58397.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P58397.
    Bgeei P58397.
    CleanExi HS_ADAMTS12.
    Genevestigatori P58397.

    Family and domain databases

    Gene3Di 3.40.390.10. 2 hits.
    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.
    PF01421. Reprolysin. 1 hit.
    PF00090. TSP_1. 8 hits.
    [Graphical view ]
    PRINTSi PR01857. ADAMTSFAMILY.
    SMARTi SM00209. TSP1. 8 hits.
    [Graphical view ]
    SUPFAMi SSF82895. SSF82895. 8 hits.
    PROSITEi PS50215. ADAM_MEPRO. 1 hit.
    PS50900. PLAC. 1 hit.
    PS50092. TSP1. 6 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification, characterization, and intracellular processing of ADAM-TS12, a novel human disintegrin with a complex structural organization involving multiple thrombospondin-1 repeats."
      Cal S., Argueelles J.M., Fernandez P.L., Lopez-Otin C.
      J. Biol. Chem. 276:17932-17940(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANT ILE-1495.
      Tissue: Fetal lung.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    3. "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].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    5. "ADAMTS-12 associates with and degrades cartilage oligomeric matrix protein."
      Liu C.-J., Kong W., Xu K., Luan Y., Ilalov K., Sehgal B., Yu S., Howell R.D., Di Cesare P.E.
      J. Biol. Chem. 281:15800-15808(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH COMP, PH DEPENDENCE, TISSUE SPECIFICITY, INDUCTION.
    6. "The ADAMTS12 metalloproteinase exhibits anti-tumorigenic properties through modulation of the Ras-dependent ERK signalling pathway."
      Llamazares M., Obaya A.J., Moncada-Pazos A., Heljasvaara R., Espada J., Lopez-Otin C., Cal S.
      J. Cell Sci. 120:3544-3552(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Inhibition of ADAMTS-7 and ADAMTS-12 degradation of cartilage oligomeric matrix protein by alpha-2-macroglobulin."
      Luan Y., Kong L., Howell D.R., Ilalov K., Fajardo M., Bai X.-H., Di Cesare P.E., Goldring M.B., Abramson S.B., Liu C.-J.
      Osteoarthritis Cartilage 16:1413-1420(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, INDUCTION.

    Entry informationi

    Entry nameiATS12_HUMAN
    AccessioniPrimary (citable) accession number: P58397
    Secondary accession number(s): A2RRN9, A5D6V6, Q6UWL3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 16, 2001
    Last sequence update: September 22, 2009
    Last modified: October 1, 2014
    This is version 133 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