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Q76LX8

- ATS13_HUMAN

UniProt

Q76LX8 - ATS13_HUMAN

Protein

A disintegrin and metalloproteinase with thrombospondin motifs 13

Gene

ADAMTS13

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (19 Jul 2004)
      Previous versions | rss
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    Functioni

    Cleaves the vWF multimers in plasma into smaller forms thereby controlling vWF-mediated platelet thrombus formation.1 Publication

    Catalytic activityi

    Cleaves the vWF at the 842-Tyr-|-Met-843 in the A2 domain of the vWF subunit.
    The enzyme cleaves the von Willebrand factor at bond Tyr(842)-|-Met(843) within the A2 domain.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity
    Binds 4 calcium ions.Curated

    Enzyme regulationi

    Zinc and calcium ions cooperatively modulate enzyme activity. The cleavage of the pro-domain is not required for protease activity. Dependence on calcium for proteolytic activity is mediated by the high affinity site.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi83 – 831CalciumSequence Analysis
    Metal bindingi173 – 1731CalciumSequence Analysis
    Metal bindingi182 – 1821Calcium; high affinity
    Metal bindingi184 – 1841Calcium; high affinity
    Metal bindingi187 – 1871Calcium; high affinity
    Metal bindingi212 – 2121Calcium; high affinity
    Metal bindingi224 – 2241Zinc; catalyticBy similarity
    Active sitei225 – 2251PROSITE-ProRule annotation
    Metal bindingi228 – 2281Zinc; catalyticBy similarity
    Metal bindingi234 – 2341Zinc; catalyticBy similarity
    Metal bindingi281 – 2811CalciumSequence Analysis
    Metal bindingi284 – 2841CalciumSequence Analysis

    GO - Molecular functioni

    1. calcium ion binding Source: UniProtKB
    2. integrin binding Source: UniProtKB
    3. metalloendopeptidase activity Source: InterPro
    4. metallopeptidase activity Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. cell-matrix adhesion Source: UniProtKB
    2. glycoprotein metabolic process Source: UniProtKB
    3. integrin-mediated signaling pathway Source: UniProtKB
    4. peptide catabolic process Source: UniProtKB
    5. platelet activation Source: UniProtKB
    6. protein processing Source: UniProtKB
    7. proteolysis Source: UniProtKB
    8. response to interferon-gamma Source: Ensembl
    9. response to interleukin-4 Source: Ensembl
    10. response to tumor necrosis factor Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Blood coagulation, Hemostasis

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Enzyme and pathway databases

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

    Protein family/group databases

    MEROPSiM12.241.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    A disintegrin and metalloproteinase with thrombospondin motifs 13 (EC:3.4.24.87)
    Short name:
    ADAM-TS 13
    Short name:
    ADAM-TS13
    Short name:
    ADAMTS-13
    Alternative name(s):
    von Willebrand factor-cleaving protease
    Short name:
    vWF-CP
    Short name:
    vWF-cleaving protease
    Gene namesi
    Name:ADAMTS13
    Synonyms:C9orf8
    ORF Names:UNQ6102/PRO20085
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:1366. ADAMTS13.

    Subcellular locationi

    Secreted 1 Publication
    Note: Secretion enhanced by O-fucosylation of TSP type-1 repeats.

    GO - Cellular componenti

    1. cell surface Source: UniProtKB
    2. extracellular space Source: Ensembl
    3. proteinaceous extracellular matrix Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Thrombotic thrombocytopenic purpura congenital (TTP) [MIM:274150]: A hematologic disease characterized by hemolytic anemia with fragmentation of erythrocytes, thrombocytopenia, diffuse and non-focal neurologic findings, decreased renal function and fever. recessive.19 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti79 – 791I → M in TTP. 1 Publication
    Corresponds to variant rs281875297 [ dbSNP | Ensembl ].
    VAR_067770
    Natural varianti88 – 881V → M in TTP; reduces protein secretion and proteolytic activity. 1 Publication
    Corresponds to variant rs281875302 [ dbSNP | Ensembl ].
    VAR_027110
    Natural varianti96 – 961H → D in TTP. 1 Publication
    Corresponds to variant rs121908467 [ dbSNP | Ensembl ].
    VAR_027111
    Natural varianti102 – 1021R → C in TTP. 1 Publication
    Corresponds to variant rs121908469 [ dbSNP | Ensembl ].
    VAR_027112
    Natural varianti119 – 1191S → F in TTP. 1 Publication
    Corresponds to variant rs281875291 [ dbSNP | Ensembl ].
    VAR_067771
    Natural varianti178 – 1781I → T in TTP. 1 Publication
    Corresponds to variant rs281875289 [ dbSNP | Ensembl ].
    VAR_067772
    Natural varianti193 – 1931R → W in TTP; low activity. 2 Publications
    Corresponds to variant rs281875287 [ dbSNP | Ensembl ].
    VAR_027113
    Natural varianti196 – 1961T → I in TTP. 3 Publications
    Corresponds to variant rs121908470 [ dbSNP | Ensembl ].
    VAR_027114
    Natural varianti203 – 2031S → P in TTP. 1 Publication
    Corresponds to variant rs281875298 [ dbSNP | Ensembl ].
    VAR_067773
    Natural varianti232 – 2321L → Q in TTP. 1 Publication
    Corresponds to variant rs281875292 [ dbSNP | Ensembl ].
    VAR_067774
    Natural varianti234 – 2341H → Q in TTP. 1 Publication
    Corresponds to variant rs281875304 [ dbSNP | Ensembl ].
    VAR_027115
    Natural varianti235 – 2351D → H in TTP. 1 Publication
    Corresponds to variant rs281875337 [ dbSNP | Ensembl ].
    VAR_067775
    Natural varianti250 – 2501A → V in TTP; mild effect on protein secretion; strong reduction of proteolytic activity. 1 Publication
    Corresponds to variant rs121908478 [ dbSNP | Ensembl ].
    VAR_027116
    Natural varianti263 – 2631S → C in TTP. 2 Publications
    Corresponds to variant rs281875293 [ dbSNP | Ensembl ].
    VAR_067776
    Natural varianti268 – 2681R → P in TTP; affects protein secretion. 2 Publications
    Corresponds to variant rs121908477 [ dbSNP | Ensembl ].
    VAR_027117
    Natural varianti304 – 3041Y → C in TTP. 1 Publication
    Corresponds to variant rs281875285 [ dbSNP | Ensembl ].
    VAR_067777
    Natural varianti311 – 3111C → Y in TTP. 1 Publication
    Corresponds to variant rs281875336 [ dbSNP | Ensembl ].
    VAR_067778
    Natural varianti347 – 3471C → S in TTP. 1 Publication
    Corresponds to variant rs281875294 [ dbSNP | Ensembl ].
    VAR_067780
    Natural varianti349 – 3491R → C in TTP. 1 Publication
    Corresponds to variant rs281875288 [ dbSNP | Ensembl ].
    VAR_067781
    Natural varianti353 – 3531P → L in TTP. 3 Publications
    Corresponds to variant rs281875338 [ dbSNP | Ensembl ].
    VAR_067782
    Natural varianti390 – 3901W → C in TTP. 1 Publication
    Corresponds to variant rs281875306 [ dbSNP | Ensembl ].
    VAR_027118
    Natural varianti398 – 3981R → H in TTP. 1 Publication
    Corresponds to variant rs121908471 [ dbSNP | Ensembl ].
    VAR_027119
    Natural varianti507 – 5071R → Q in TTP. 2 Publications
    Corresponds to variant rs281875296 [ dbSNP | Ensembl ].
    VAR_067783
    Natural varianti508 – 5081C → Y in TTP; impairs protein secretion. 1 Publication
    Corresponds to variant rs281875305 [ dbSNP | Ensembl ].
    VAR_027122
    Natural varianti525 – 5251G → D in TTP. 1 Publication
    Corresponds to variant rs281875286 [ dbSNP | Ensembl ].
    VAR_067784
    Natural varianti528 – 5281R → G in TTP. 1 Publication
    Corresponds to variant rs121908473 [ dbSNP | Ensembl ].
    VAR_027123
    Natural varianti596 – 5961A → V in TTP. 1 Publication
    Corresponds to variant rs281875299 [ dbSNP | Ensembl ].
    VAR_067785
    Natural varianti606 – 6061A → P in TTP. 1 Publication
    Corresponds to variant rs281875290 [ dbSNP | Ensembl ].
    VAR_067786
    Natural varianti658 – 6581Y → C in TTP. 1 Publication
    Corresponds to variant rs281875335 [ dbSNP | Ensembl ].
    VAR_067787
    Natural varianti671 – 6711P → L in TTP. 1 Publication
    Corresponds to variant rs281875295 [ dbSNP | Ensembl ].
    VAR_067788
    Natural varianti673 – 6731I → F in TTP; impairs protein secretion. 1 Publication
    Corresponds to variant rs281875307 [ dbSNP | Ensembl ].
    VAR_027126
    Natural varianti692 – 6921R → C in TTP. 1 Publication
    Corresponds to variant rs121908475 [ dbSNP | Ensembl ].
    VAR_027127
    Natural varianti758 – 7581C → R in TTP. 1 Publication
    Corresponds to variant rs281875300 [ dbSNP | Ensembl ].
    VAR_067789
    Natural varianti908 – 9081C → S in TTP. 1 Publication
    Corresponds to variant rs281875301 [ dbSNP | Ensembl ].
    VAR_067790
    Natural varianti908 – 9081C → Y in TTP; impairs protein secretion. 1 Publication
    Corresponds to variant rs281875301 [ dbSNP | Ensembl ].
    VAR_027131
    Natural varianti951 – 9511C → G in TTP. 1 Publication
    Corresponds to variant rs121908468 [ dbSNP | Ensembl ].
    VAR_027132
    Natural varianti977 – 9793CAR → W in TTP. 1 Publication
    VAR_067791
    Natural varianti1024 – 10241C → G in TTP. 1 Publication
    Corresponds to variant rs121908472 [ dbSNP | Ensembl ].
    VAR_027133
    Natural varianti1060 – 10601R → W in TTP; affects protein secretion; the mutant protein has reduced protease activity. 3 Publications
    Corresponds to variant rs142572218 [ dbSNP | Ensembl ].
    VAR_067792
    Natural varianti1123 – 11231R → C in TTP; impairs protein secretion; the mutant protein has reduced protease activity. 2 Publications
    Corresponds to variant rs281875340 [ dbSNP | Ensembl ].
    VAR_027136
    Natural varianti1213 – 12131C → Y in TTP. 1 Publication
    Corresponds to variant rs121908474 [ dbSNP | Ensembl ].
    VAR_027137
    Natural varianti1219 – 12191R → W in TTP; affects protein secretion; the mutant protein has reduced protease activity. 1 Publication
    Corresponds to variant rs281875339 [ dbSNP | Ensembl ].
    VAR_067793
    Natural varianti1239 – 12391G → V in TTP; impairs protein secretion. 1 Publication
    Corresponds to variant rs281875303 [ dbSNP | Ensembl ].
    VAR_027138
    Natural varianti1336 – 13361R → W in TTP; impairs protein secretion and proteolytic activity. 1 Publication
    Corresponds to variant rs281875308 [ dbSNP | Ensembl ].
    VAR_027139

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi71 – 711R → K: Abolishes pro-domain removal but no loss of proteolytic activity; when associated with D-73. 1 Publication
    Mutagenesisi73 – 731R → D: Abolishes pro-domain removal but no loss of proteolytic activity; when associated with K-71. 1 Publication
    Mutagenesisi83 – 831E → A: No change in calcium dependence for proteolysis. 1 Publication
    Mutagenesisi173 – 1731D → A: No change in calcium dependence for proteolysis. 1 Publication
    Mutagenesisi184 – 1841E → A: Dramatically reduced affinity for calcium. 1 Publication
    Mutagenesisi187 – 1871D → A: Dramatically reduced affinity for calcium. 1 Publication
    Mutagenesisi212 – 2121E → A: Dramatically reduced affinity for calcium. 1 Publication
    Mutagenesisi399 – 3991S → A: No effect on cleavage of VWF and little change in secretion of ADAMTS13. Abolishes secretion of ADAMTS13; when associated with A-698. 1 Publication
    Mutagenesisi698 – 6981S → A: No effect on cleavage of VWF and greatly reduced secretion of ADAMTS13. Abolishes secretion of ADAMTS13; when associated with A-399. 1 Publication
    Mutagenesisi757 – 7571S → A: No effect on cleavage of VWF and little change in secretion of ADAMTS13. 1 Publication
    Mutagenesisi907 – 9071S → A: No effect on cleavage of VWF and greatly reduced secretion of ADAMTS13. Abolishes most of the secretion of ADAMTS13; when associated with A-965. 1 Publication
    Mutagenesisi965 – 9651S → A: No effect on cleavage of VWF and little change in secretion of ADAMTS13. Abolishes most of the secretion of ADAMTS13; when associated with A-907. 1 Publication
    Mutagenesisi1027 – 10271S → A: No effect on cleavage of VWF and little change in secretion of ADAMTS13. Abolishes most of the secretion of ADAMTS13; when associated with A-1087. 1 Publication
    Mutagenesisi1087 – 10871S → A: No effect on cleavage of VWF and little change in secretion of ADAMTS13. Abolishes most of the secretion of ADAMTS13; when associated with A-1027. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi274150. phenotype.
    Orphaneti93583. Congenital thrombotic thrombocytopenic purpura due to ADAMTS-13 deficiency.
    PharmGKBiPA24539.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2929Sequence AnalysisAdd
    BLAST
    Propeptidei30 – 74453 PublicationsPRO_0000247510Add
    BLAST
    Chaini75 – 14271353A disintegrin and metalloproteinase with thrombospondin motifs 13PRO_0000247511Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi142 – 1421N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi146 – 1461N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi155 ↔ 208By similarity
    Disulfide bondi202 ↔ 281By similarity
    Disulfide bondi242 ↔ 265By similarity
    Disulfide bondi311 ↔ 3371 Publication
    Disulfide bondi322 ↔ 3471 Publication
    Disulfide bondi332 ↔ 3661 Publication
    Disulfide bondi360 ↔ 3711 Publication
    Disulfide bondi396 ↔ 4331 Publication
    Disulfide bondi400 ↔ 4381 Publication
    Disulfide bondi411 ↔ 4231 Publication
    Disulfide bondi483 ↔ 5221 Publication
    Disulfide bondi508 ↔ 5271 Publication
    Disulfide bondi532 ↔ 5481 Publication
    Disulfide bondi545 ↔ 5551 Publication
    Glycosylationi552 – 5521N-linked (GlcNAc...)2 Publications
    Glycosylationi579 – 5791N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi614 – 6141N-linked (GlcNAc...)3 Publications
    Glycosylationi667 – 6671N-linked (GlcNAc...) (complex)3 Publications
    Glycosylationi698 – 6981O-linked (Fuc...)2 Publications
    Glycosylationi707 – 7071N-linked (GlcNAc...) (complex)2 Publications
    Glycosylationi757 – 7571O-linked (Fuc...)2 Publications
    Glycosylationi828 – 8281N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi907 – 9071O-linked (Fuc...)2 Publications
    Glycosylationi965 – 9651O-linked (Fuc...)2 Publications
    Glycosylationi1027 – 10271O-linked (Fuc...)2 Publications
    Glycosylationi1087 – 10871O-linked (Fuc...)2 Publications
    Glycosylationi1235 – 12351N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1354 – 13541N-linked (GlcNAc...)2 Publications

    Post-translational modificationi

    Glycosylated. 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 ADAMTS13. May also be C-glycosylated on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and also N-glycosylated. These other glycosylations can also facilitate secretion.5 Publications
    The precursor is processed by a furin endopeptidase which cleaves off the pro-domain.

    Keywords - PTMi

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

    Proteomic databases

    PaxDbiQ76LX8.
    PRIDEiQ76LX8.

    PTM databases

    PhosphoSiteiQ76LX8.

    Expressioni

    Tissue specificityi

    Plasma. Expressed primarily in liver.1 Publication

    Gene expression databases

    ArrayExpressiQ76LX8.
    BgeeiQ76LX8.
    CleanExiHS_ADAMTS13.
    GenevestigatoriQ76LX8.

    Organism-specific databases

    HPAiHPA042014.
    HPA042844.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    VWFP042755EBI-981764,EBI-981819

    Protein-protein interaction databases

    BioGridi116274. 1 interaction.
    DIPiDIP-36050N.
    IntActiQ76LX8. 1 interaction.
    MINTiMINT-4713142.
    STRINGi9606.ENSP00000360997.

    Structurei

    Secondary structure

    1
    1427
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi301 – 3033
    Helixi307 – 3148
    Helixi331 – 3344
    Beta strandi337 – 3404
    Beta strandi348 – 3514
    Beta strandi359 – 3613
    Beta strandi364 – 3674
    Beta strandi370 – 3734
    Helixi374 – 3774
    Beta strandi399 – 4013
    Beta strandi403 – 4064
    Beta strandi417 – 4193
    Beta strandi430 – 4334
    Helixi442 – 45110
    Turni452 – 4554
    Beta strandi470 – 4723
    Turni474 – 4763
    Helixi479 – 4835
    Beta strandi486 – 4894
    Beta strandi495 – 4973
    Beta strandi519 – 5235
    Beta strandi526 – 5305
    Beta strandi534 – 5363
    Beta strandi554 – 5629
    Beta strandi569 – 5768
    Beta strandi581 – 5888
    Beta strandi592 – 5998
    Beta strandi602 – 6054
    Beta strandi608 – 6103
    Beta strandi614 – 6185
    Beta strandi623 – 63210
    Beta strandi634 – 6363
    Beta strandi638 – 64710
    Beta strandi653 – 6619
    Helixi663 – 6653
    Helixi667 – 6693
    Beta strandi673 – 6808

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3GHMX-ray2.60A287-685[»]
    3GHNX-ray2.80A287-685[»]
    3VN4X-ray2.80A287-685[»]
    ProteinModelPortaliQ76LX8.
    SMRiQ76LX8. Positions 82-682.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ76LX8.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini80 – 286207Peptidase M12BPROSITE-ProRule annotationAdd
    BLAST
    Domaini287 – 38397DisintegrinAdd
    BLAST
    Domaini384 – 43956TSP type-1 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini682 – 73049TSP type-1 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini742 – 80564TSP type-1 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini808 – 85952TSP type-1 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini896 – 95055TSP type-1 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini951 – 101161TSP type-1 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini1012 – 106857TSP type-1 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini1072 – 113160TSP type-1 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini1192 – 1298107CUB 1Add
    BLAST
    Domaini1299 – 1427129CUB 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni440 – 556117Cysteine-richAdd
    BLAST
    Regioni556 – 685130SpacerAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi498 – 5003Cell attachment siteSequence Analysis

    Domaini

    The pro-domain is not required for folding or secretion and does not perform the common function of maintening enzyme latency.
    The globular cysteineless spacer domain adopts a jelly-roll topology, and is necessary to recognize and cleave vWF. The C-terminal TSP type-1 and CUB domains may modulate this interaction.

    Sequence similaritiesi

    Contains 2 CUB domains.Curated
    Contains 1 disintegrin domain.Curated
    Contains 1 peptidase M12B domain.PROSITE-ProRule annotation
    Contains 8 TSP type-1 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG239882.
    HOGENOMiHOG000231627.
    HOVERGENiHBG080358.
    InParanoidiQ76LX8.
    KOiK08627.
    OMAiCDMQLFG.
    PhylomeDBiQ76LX8.
    TreeFamiTF313537.

    Family and domain databases

    Gene3Di3.40.390.10. 1 hit.
    InterProiIPR000859. CUB_dom.
    IPR024079. MetalloPept_cat_dom.
    IPR001590. Peptidase_M12B.
    IPR013273. Peptidase_M12B_ADAM-TS.
    IPR000884. Thrombospondin_1_rpt.
    [Graphical view]
    PfamiPF01421. Reprolysin. 1 hit.
    PF00090. TSP_1. 5 hits.
    [Graphical view]
    PRINTSiPR01857. ADAMTSFAMILY.
    SMARTiSM00209. TSP1. 7 hits.
    [Graphical view]
    SUPFAMiSSF49854. SSF49854. 2 hits.
    SSF82895. SSF82895. 5 hits.
    PROSITEiPS50215. ADAM_MEPRO. 1 hit.
    PS50092. TSP1. 4 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q76LX8-1) [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

    MHQRHPRARC PPLCVAGILA CGFLLGCWGP SHFQQSCLQA LEPQAVSSYL     50
    SPGAPLKGRP PSPGFQRQRQ RQRRAAGGIL HLELLVAVGP DVFQAHQEDT 100
    ERYVLTNLNI GAELLRDPSL GAQFRVHLVK MVILTEPEGA PNITANLTSS 150
    LLSVCGWSQT INPEDDTDPG HADLVLYITR FDLELPDGNR QVRGVTQLGG 200
    ACSPTWSCLI TEDTGFDLGV TIAHEIGHSF GLEHDGAPGS GCGPSGHVMA 250
    SDGAAPRAGL AWSPCSRRQL LSLLSAGRAR CVWDPPRPQP GSAGHPPDAQ 300
    PGLYYSANEQ CRVAFGPKAV ACTFAREHLD MCQALSCHTD PLDQSSCSRL 350
    LVPLLDGTEC GVEKWCSKGR CRSLVELTPI AAVHGRWSSW GPRSPCSRSC 400
    GGGVVTRRRQ CNNPRPAFGG RACVGADLQA EMCNTQACEK TQLEFMSQQC 450
    ARTDGQPLRS SPGGASFYHW GAAVPHSQGD ALCRHMCRAI GESFIMKRGD 500
    SFLDGTRCMP SGPREDGTLS LCVSGSCRTF GCDGRMDSQQ VWDRCQVCGG 550
    DNSTCSPRKG SFTAGRAREY VTFLTVTPNL TSVYIANHRP LFTHLAVRIG 600
    GRYVVAGKMS ISPNTTYPSL LEDGRVEYRV ALTEDRLPRL EEIRIWGPLQ 650
    EDADIQVYRR YGEEYGNLTR PDITFTYFQP KPRQAWVWAA VRGPCSVSCG 700
    AGLRWVNYSC LDQARKELVE TVQCQGSQQP PAWPEACVLE PCPPYWAVGD 750
    FGPCSASCGG GLRERPVRCV EAQGSLLKTL PPARCRAGAQ QPAVALETCN 800
    PQPCPARWEV SEPSSCTSAG GAGLALENET CVPGADGLEA PVTEGPGSVD 850
    EKLPAPEPCV GMSCPPGWGH LDATSAGEKA PSPWGSIRTG AQAAHVWTPA 900
    AGSCSVSCGR GLMELRFLCM DSALRVPVQE ELCGLASKPG SRREVCQAVP 950
    CPARWQYKLA ACSVSCGRGV VRRILYCARA HGEDDGEEIL LDTQCQGLPR 1000
    PEPQEACSLE PCPPRWKVMS LGPCSASCGL GTARRSVACV QLDQGQDVEV 1050
    DEAACAALVR PEASVPCLIA DCTYRWHVGT WMECSVSCGD GIQRRRDTCL 1100
    GPQAQAPVPA DFCQHLPKPV TVRGCWAGPC VGQGTPSLVP HEEAAAPGRT 1150
    TATPAGASLE WSQARGLLFS PAPQPRRLLP GPQENSVQSS ACGRQHLEPT 1200
    GTIDMRGPGQ ADCAVAIGRP LGEVVTLRVL ESSLNCSAGD MLLLWGRLTW 1250
    RKMCRKLLDM TFSSKTNTLV VRQRCGRPGG GVLLRYGSQL APETFYRECD 1300
    MQLFGPWGEI VSPSLSPATS NAGGCRLFIN VAPHARIAIH ALATNMGAGT 1350
    EGANASYILI RDTHSLRTTA FHGQQVLYWE SESSQAEMEF SEGFLKAQAS 1400
    LRGQYWTLQS WVPEMQDPQS WKGKEGT 1427
    Length:1,427
    Mass (Da):153,604
    Last modified:July 19, 2004 - v1
    Checksum:iA2103AFABC1A4445
    GO
    Isoform 2 (identifier: Q76LX8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1135-1190: Missing.

    Show »
    Length:1,371
    Mass (Da):147,804
    Checksum:iAE4C713AE5B64DFC
    GO
    Isoform 3 (identifier: Q76LX8-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         275-305: Missing.
         1135-1190: Missing.

    Show »
    Length:1,340
    Mass (Da):144,517
    Checksum:i0BFBEF4C3D58B2C2
    GO
    Isoform 4 (identifier: Q76LX8-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2-329: Missing.
         658-692: YRRYGEEYGNLTRPDITFTYFQPKPRQAWVWAAVR → GGVRAQLMHISWWSRPGLGERDLCARGRWPGGSSD
         693-1427: Missing.

    Show »
    Length:364
    Mass (Da):39,864
    Checksum:iDA42FC5F5345F3A0
    GO

    Sequence cautioni

    The sequence AAQ88485.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAB66743.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti101 – 1011E → R AA sequence (PubMed:11574066)Curated

    Polymorphismi

    Genetic variations in ADAMTS13 coding region influence plasmatic ADAMTS13 activity levels. Dependent on the sequence context, the same polymorphisms might be either positive or negative modifiers of gene expression, thereby altering the phenotype of ADAMTS13 deficiency.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti7 – 71R → W Does not affect protein secretion. 2 Publications
    Corresponds to variant rs34024143 [ dbSNP | Ensembl ].
    VAR_027109
    Natural varianti79 – 791I → M in TTP. 1 Publication
    Corresponds to variant rs281875297 [ dbSNP | Ensembl ].
    VAR_067770
    Natural varianti88 – 881V → M in TTP; reduces protein secretion and proteolytic activity. 1 Publication
    Corresponds to variant rs281875302 [ dbSNP | Ensembl ].
    VAR_027110
    Natural varianti96 – 961H → D in TTP. 1 Publication
    Corresponds to variant rs121908467 [ dbSNP | Ensembl ].
    VAR_027111
    Natural varianti102 – 1021R → C in TTP. 1 Publication
    Corresponds to variant rs121908469 [ dbSNP | Ensembl ].
    VAR_027112
    Natural varianti119 – 1191S → F in TTP. 1 Publication
    Corresponds to variant rs281875291 [ dbSNP | Ensembl ].
    VAR_067771
    Natural varianti178 – 1781I → T in TTP. 1 Publication
    Corresponds to variant rs281875289 [ dbSNP | Ensembl ].
    VAR_067772
    Natural varianti193 – 1931R → W in TTP; low activity. 2 Publications
    Corresponds to variant rs281875287 [ dbSNP | Ensembl ].
    VAR_027113
    Natural varianti196 – 1961T → I in TTP. 3 Publications
    Corresponds to variant rs121908470 [ dbSNP | Ensembl ].
    VAR_027114
    Natural varianti203 – 2031S → P in TTP. 1 Publication
    Corresponds to variant rs281875298 [ dbSNP | Ensembl ].
    VAR_067773
    Natural varianti232 – 2321L → Q in TTP. 1 Publication
    Corresponds to variant rs281875292 [ dbSNP | Ensembl ].
    VAR_067774
    Natural varianti234 – 2341H → Q in TTP. 1 Publication
    Corresponds to variant rs281875304 [ dbSNP | Ensembl ].
    VAR_027115
    Natural varianti235 – 2351D → H in TTP. 1 Publication
    Corresponds to variant rs281875337 [ dbSNP | Ensembl ].
    VAR_067775
    Natural varianti250 – 2501A → V in TTP; mild effect on protein secretion; strong reduction of proteolytic activity. 1 Publication
    Corresponds to variant rs121908478 [ dbSNP | Ensembl ].
    VAR_027116
    Natural varianti263 – 2631S → C in TTP. 2 Publications
    Corresponds to variant rs281875293 [ dbSNP | Ensembl ].
    VAR_067776
    Natural varianti268 – 2681R → P in TTP; affects protein secretion. 2 Publications
    Corresponds to variant rs121908477 [ dbSNP | Ensembl ].
    VAR_027117
    Natural varianti304 – 3041Y → C in TTP. 1 Publication
    Corresponds to variant rs281875285 [ dbSNP | Ensembl ].
    VAR_067777
    Natural varianti311 – 3111C → Y in TTP. 1 Publication
    Corresponds to variant rs281875336 [ dbSNP | Ensembl ].
    VAR_067778
    Natural varianti339 – 3391T → R.1 Publication
    Corresponds to variant rs149517360 [ dbSNP | Ensembl ].
    VAR_067779
    Natural varianti347 – 3471C → S in TTP. 1 Publication
    Corresponds to variant rs281875294 [ dbSNP | Ensembl ].
    VAR_067780
    Natural varianti349 – 3491R → C in TTP. 1 Publication
    Corresponds to variant rs281875288 [ dbSNP | Ensembl ].
    VAR_067781
    Natural varianti353 – 3531P → L in TTP. 3 Publications
    Corresponds to variant rs281875338 [ dbSNP | Ensembl ].
    VAR_067782
    Natural varianti390 – 3901W → C in TTP. 1 Publication
    Corresponds to variant rs281875306 [ dbSNP | Ensembl ].
    VAR_027118
    Natural varianti398 – 3981R → H in TTP. 1 Publication
    Corresponds to variant rs121908471 [ dbSNP | Ensembl ].
    VAR_027119
    Natural varianti448 – 4481Q → E Does not affect protein secretion; normal proteolytic activity. 8 Publications
    Corresponds to variant rs2301612 [ dbSNP | Ensembl ].
    VAR_027120
    Natural varianti456 – 4561Q → H.1 Publication
    Corresponds to variant rs36220239 [ dbSNP | Ensembl ].
    VAR_027162
    Natural varianti457 – 4571P → L.2 Publications
    Corresponds to variant rs36220240 [ dbSNP | Ensembl ].
    VAR_027163
    Natural varianti475 – 4751P → S.1 Publication
    Corresponds to variant rs11575933 [ dbSNP | Ensembl ].
    VAR_027121
    Natural varianti507 – 5071R → Q in TTP. 2 Publications
    Corresponds to variant rs281875296 [ dbSNP | Ensembl ].
    VAR_067783
    Natural varianti508 – 5081C → Y in TTP; impairs protein secretion. 1 Publication
    Corresponds to variant rs281875305 [ dbSNP | Ensembl ].
    VAR_027122
    Natural varianti525 – 5251G → D in TTP. 1 Publication
    Corresponds to variant rs281875286 [ dbSNP | Ensembl ].
    VAR_067784
    Natural varianti528 – 5281R → G in TTP. 1 Publication
    Corresponds to variant rs121908473 [ dbSNP | Ensembl ].
    VAR_027123
    Natural varianti596 – 5961A → V in TTP. 1 Publication
    Corresponds to variant rs281875299 [ dbSNP | Ensembl ].
    VAR_067785
    Natural varianti606 – 6061A → P in TTP. 1 Publication
    Corresponds to variant rs281875290 [ dbSNP | Ensembl ].
    VAR_067786
    Natural varianti618 – 6181P → A.3 Publications
    Corresponds to variant rs28647808 [ dbSNP | Ensembl ].
    VAR_027124
    Natural varianti625 – 6251R → H.2 Publications
    Corresponds to variant rs36090624 [ dbSNP | Ensembl ].
    VAR_027125
    Natural varianti658 – 6581Y → C in TTP. 1 Publication
    Corresponds to variant rs281875335 [ dbSNP | Ensembl ].
    VAR_067787
    Natural varianti671 – 6711P → L in TTP. 1 Publication
    Corresponds to variant rs281875295 [ dbSNP | Ensembl ].
    VAR_067788
    Natural varianti673 – 6731I → F in TTP; impairs protein secretion. 1 Publication
    Corresponds to variant rs281875307 [ dbSNP | Ensembl ].
    VAR_027126
    Natural varianti692 – 6921R → C in TTP. 1 Publication
    Corresponds to variant rs121908475 [ dbSNP | Ensembl ].
    VAR_027127
    Natural varianti732 – 7321A → V.2 Publications
    Corresponds to variant rs41314453 [ dbSNP | Ensembl ].
    VAR_027128
    Natural varianti740 – 7401E → K.1 Publication
    Corresponds to variant rs36221451 [ dbSNP | Ensembl ].
    VAR_027164
    Natural varianti758 – 7581C → R in TTP. 1 Publication
    Corresponds to variant rs281875300 [ dbSNP | Ensembl ].
    VAR_067789
    Natural varianti900 – 9001A → V.3 Publications
    Corresponds to variant rs685523 [ dbSNP | Ensembl ].
    VAR_027129
    Natural varianti903 – 9031S → L.2 Publications
    Corresponds to variant rs78977446 [ dbSNP | Ensembl ].
    VAR_027130
    Natural varianti908 – 9081C → S in TTP. 1 Publication
    Corresponds to variant rs281875301 [ dbSNP | Ensembl ].
    VAR_067790
    Natural varianti908 – 9081C → Y in TTP; impairs protein secretion. 1 Publication
    Corresponds to variant rs281875301 [ dbSNP | Ensembl ].
    VAR_027131
    Natural varianti951 – 9511C → G in TTP. 1 Publication
    Corresponds to variant rs121908468 [ dbSNP | Ensembl ].
    VAR_027132
    Natural varianti977 – 9793CAR → W in TTP. 1 Publication
    VAR_067791
    Natural varianti982 – 9821G → R.1 Publication
    Corresponds to variant rs36222275 [ dbSNP | Ensembl ].
    VAR_027165
    Natural varianti1024 – 10241C → G in TTP. 1 Publication
    Corresponds to variant rs121908472 [ dbSNP | Ensembl ].
    VAR_027133
    Natural varianti1033 – 10331A → T.2 Publications
    Corresponds to variant rs28503257 [ dbSNP | Ensembl ].
    VAR_027134
    Natural varianti1060 – 10601R → W in TTP; affects protein secretion; the mutant protein has reduced protease activity. 3 Publications
    Corresponds to variant rs142572218 [ dbSNP | Ensembl ].
    VAR_067792
    Natural varianti1095 – 10951R → W in a patient with thrombotic thrombocytopenic purpura. 1 Publication
    VAR_027135
    Natural varianti1123 – 11231R → C in TTP; impairs protein secretion; the mutant protein has reduced protease activity. 2 Publications
    Corresponds to variant rs281875340 [ dbSNP | Ensembl ].
    VAR_027136
    Natural varianti1213 – 12131C → Y in TTP. 1 Publication
    Corresponds to variant rs121908474 [ dbSNP | Ensembl ].
    VAR_027137
    Natural varianti1219 – 12191R → W in TTP; affects protein secretion; the mutant protein has reduced protease activity. 1 Publication
    Corresponds to variant rs281875339 [ dbSNP | Ensembl ].
    VAR_067793
    Natural varianti1226 – 12261T → I.1 Publication
    Corresponds to variant rs36222894 [ dbSNP | Ensembl ].
    VAR_027166
    Natural varianti1239 – 12391G → V in TTP; impairs protein secretion. 1 Publication
    Corresponds to variant rs281875303 [ dbSNP | Ensembl ].
    VAR_027138
    Natural varianti1314 – 13141S → L Found in a patient with hemolytic uremic syndrome. 1 Publication
    Corresponds to variant rs142060916 [ dbSNP | Ensembl ].
    VAR_067794
    Natural varianti1336 – 13361R → W in TTP; impairs protein secretion and proteolytic activity. 1 Publication
    Corresponds to variant rs281875308 [ dbSNP | Ensembl ].
    VAR_027139

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2 – 329328Missing in isoform 4. 1 PublicationVSP_055537Add
    BLAST
    Alternative sequencei275 – 30531Missing in isoform 3. 1 PublicationVSP_020002Add
    BLAST
    Alternative sequencei658 – 69235YRRYG…WAAVR → GGVRAQLMHISWWSRPGLGE RDLCARGRWPGGSSD in isoform 4. 1 PublicationVSP_055538Add
    BLAST
    Alternative sequencei693 – 1427735Missing in isoform 4. 1 PublicationVSP_055539Add
    BLAST
    Alternative sequencei1135 – 119056Missing in isoform 2 and isoform 3. 1 PublicationVSP_020003Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB069698 mRNA. Translation: BAB69487.2.
    AY055376 mRNA. Translation: AAL17652.1.
    AF414401 mRNA. Translation: AAL11095.1.
    AJ305314 mRNA. Translation: CAC83682.1.
    AJ420810 mRNA. Translation: CAD12729.1.
    AJ011374 mRNA. Translation: CAB66157.1.
    DQ422807 Genomic DNA. Translation: ABD72606.1.
    AL158826, AL593848 Genomic DNA. Translation: CAI12850.1.
    AL158826, AL593848 Genomic DNA. Translation: CAI12851.1.
    AL158826, AL593848 Genomic DNA. Translation: CAI12852.1.
    CH471090 Genomic DNA. Translation: EAW88086.1.
    AY358118 mRNA. Translation: AAQ88485.1. Different initiation.
    AL136809 mRNA. Translation: CAB66743.1. Different initiation.
    CCDSiCCDS6970.1. [Q76LX8-1]
    CCDS6971.1. [Q76LX8-3]
    CCDS6972.1. [Q76LX8-2]
    RefSeqiNP_620594.1. NM_139025.4. [Q76LX8-1]
    NP_620595.1. NM_139026.4. [Q76LX8-3]
    NP_620596.2. NM_139027.4. [Q76LX8-2]
    UniGeneiHs.131433.

    Genome annotation databases

    EnsembliENST00000355699; ENSP00000347927; ENSG00000160323. [Q76LX8-2]
    ENST00000356589; ENSP00000348997; ENSG00000160323. [Q76LX8-3]
    ENST00000371910; ENSP00000360978; ENSG00000160323.
    ENST00000371929; ENSP00000360997; ENSG00000160323. [Q76LX8-1]
    GeneIDi11093.
    KEGGihsa:11093.
    UCSCiuc004cdt.1. human. [Q76LX8-2]
    uc004cdu.1. human. [Q76LX8-3]
    uc004cdv.4. human. [Q76LX8-1]

    Polymorphism databases

    DMDMi74749836.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    ADAMTS13 entry

    SeattleSNPs
    Mendelian genes ADAM metallopeptidase with thrombospondin type 1 motif, 13 (ADAMTS13)

    Leiden Open Variation Database (LOVD)

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB069698 mRNA. Translation: BAB69487.2 .
    AY055376 mRNA. Translation: AAL17652.1 .
    AF414401 mRNA. Translation: AAL11095.1 .
    AJ305314 mRNA. Translation: CAC83682.1 .
    AJ420810 mRNA. Translation: CAD12729.1 .
    AJ011374 mRNA. Translation: CAB66157.1 .
    DQ422807 Genomic DNA. Translation: ABD72606.1 .
    AL158826 , AL593848 Genomic DNA. Translation: CAI12850.1 .
    AL158826 , AL593848 Genomic DNA. Translation: CAI12851.1 .
    AL158826 , AL593848 Genomic DNA. Translation: CAI12852.1 .
    CH471090 Genomic DNA. Translation: EAW88086.1 .
    AY358118 mRNA. Translation: AAQ88485.1 . Different initiation.
    AL136809 mRNA. Translation: CAB66743.1 . Different initiation.
    CCDSi CCDS6970.1. [Q76LX8-1 ]
    CCDS6971.1. [Q76LX8-3 ]
    CCDS6972.1. [Q76LX8-2 ]
    RefSeqi NP_620594.1. NM_139025.4. [Q76LX8-1 ]
    NP_620595.1. NM_139026.4. [Q76LX8-3 ]
    NP_620596.2. NM_139027.4. [Q76LX8-2 ]
    UniGenei Hs.131433.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3GHM X-ray 2.60 A 287-685 [» ]
    3GHN X-ray 2.80 A 287-685 [» ]
    3VN4 X-ray 2.80 A 287-685 [» ]
    ProteinModelPortali Q76LX8.
    SMRi Q76LX8. Positions 82-682.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116274. 1 interaction.
    DIPi DIP-36050N.
    IntActi Q76LX8. 1 interaction.
    MINTi MINT-4713142.
    STRINGi 9606.ENSP00000360997.

    Chemistry

    ChEMBLi CHEMBL2346492.

    Protein family/group databases

    MEROPSi M12.241.

    PTM databases

    PhosphoSitei Q76LX8.

    Polymorphism databases

    DMDMi 74749836.

    Proteomic databases

    PaxDbi Q76LX8.
    PRIDEi Q76LX8.

    Protocols and materials databases

    DNASUi 11093.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000355699 ; ENSP00000347927 ; ENSG00000160323 . [Q76LX8-2 ]
    ENST00000356589 ; ENSP00000348997 ; ENSG00000160323 . [Q76LX8-3 ]
    ENST00000371910 ; ENSP00000360978 ; ENSG00000160323 .
    ENST00000371929 ; ENSP00000360997 ; ENSG00000160323 . [Q76LX8-1 ]
    GeneIDi 11093.
    KEGGi hsa:11093.
    UCSCi uc004cdt.1. human. [Q76LX8-2 ]
    uc004cdu.1. human. [Q76LX8-3 ]
    uc004cdv.4. human. [Q76LX8-1 ]

    Organism-specific databases

    CTDi 11093.
    GeneCardsi GC09P136279.
    HGNCi HGNC:1366. ADAMTS13.
    HPAi HPA042014.
    HPA042844.
    MIMi 274150. phenotype.
    604134. gene.
    neXtProti NX_Q76LX8.
    Orphaneti 93583. Congenital thrombotic thrombocytopenic purpura due to ADAMTS-13 deficiency.
    PharmGKBi PA24539.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG239882.
    HOGENOMi HOG000231627.
    HOVERGENi HBG080358.
    InParanoidi Q76LX8.
    KOi K08627.
    OMAi CDMQLFG.
    PhylomeDBi Q76LX8.
    TreeFami TF313537.

    Enzyme and pathway databases

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

    Miscellaneous databases

    EvolutionaryTracei Q76LX8.
    GeneWikii ADAMTS13.
    GenomeRNAii 11093.
    NextBioi 42166.
    PROi Q76LX8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q76LX8.
    Bgeei Q76LX8.
    CleanExi HS_ADAMTS13.
    Genevestigatori Q76LX8.

    Family and domain databases

    Gene3Di 3.40.390.10. 1 hit.
    InterProi IPR000859. CUB_dom.
    IPR024079. MetalloPept_cat_dom.
    IPR001590. Peptidase_M12B.
    IPR013273. Peptidase_M12B_ADAM-TS.
    IPR000884. Thrombospondin_1_rpt.
    [Graphical view ]
    Pfami PF01421. Reprolysin. 1 hit.
    PF00090. TSP_1. 5 hits.
    [Graphical view ]
    PRINTSi PR01857. ADAMTSFAMILY.
    SMARTi SM00209. TSP1. 7 hits.
    [Graphical view ]
    SUPFAMi SSF49854. SSF49854. 2 hits.
    SSF82895. SSF82895. 5 hits.
    PROSITEi PS50215. ADAM_MEPRO. 1 hit.
    PS50092. TSP1. 4 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel human metalloprotease synthesized in the liver and secreted into the blood: possibly, the von Willebrand factor-cleaving protease?"
      Soejima K., Mimura N., Hirashima M., Maeda H., Hamamoto T., Nakagaki T., Nozaki C.
      J. Biochem. 130:475-480(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 75-103, TISSUE SPECIFICITY.
      Tissue: Liver.
    2. "Structure of von Willebrand factor-cleaving protease (ADAMTS13), a metalloprotease involved in thrombotic thrombocytopenic purpura."
      Zheng X., Chung D., Takayama T.K., Majerus E.M., Sadler J.E., Fujikawa K.
      J. Biol. Chem. 276:41059-41063(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), GLYCOSYLATION, VARIANT VAL-900.
      Tissue: Liver.
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INVOLVEMENT IN THROMBOTIC THROMBOCYTOPENIC PURPURA, VARIANTS TTP ASP-96; CYS-102; ILE-196; HIS-398; GLY-528; CYS-692; GLY-951; GLY-1024 AND TYR-1213, VARIANTS TRP-7; GLU-448; ALA-618; HIS-625; VAL-732; VAL-900 AND THR-1033.
      Tissue: Liver.
    4. "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] (ISOFORMS 2 AND 3).
      Tissue: Liver.
    5. "Cloning of a sugar transporter gene, a G-beta subunit like gene and three novel genes in human chromosome 9q34."
      Young J.M., Woodward K.J., Aziz S., Burley M., Kwiatkowski D.J., Povey S.
      Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
      Tissue: Brain.
    6. SeattleSNPs variation discovery resource
      Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS TRP-7; GLU-448; HIS-456; LEU-457; ALA-618; HIS-625; LYS-740; VAL-900; ARG-982; THR-1033 AND ILE-1226.
    7. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 275-1427, VARIANT GLU-448.
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1191-1427.
      Tissue: Testis.
    11. "Partial amino acid sequence of purified von Willebrand factor-cleaving protease."
      Gerritsen H.E., Robles R., Laemmle B., Furlan M.
      Blood 98:1654-1661(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 75-89.
    12. "Purification of human von Willebrand factor-cleaving protease and its identification as a new member of the metalloproteinase family."
      Fujikawa K., Suzuki H., McMullen B., Chung D.
      Blood 98:1662-1666(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 75-94.
    13. "Cleavage of von Willebrand factor requires the spacer domain of the metalloprotease ADAMTS13."
      Zheng X., Nishio K., Majerus E.M., Sadler J.E.
      J. Biol. Chem. 278:30136-30141(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, SUBCELLULAR LOCATION.
    14. "Cleavage of the ADAMTS13 propeptide is not required for protease activity."
      Majerus E.M., Zheng X., Tuley E.A., Sadler J.E.
      J. Biol. Chem. 278:46643-46648(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, MUTAGENESIS OF ARG-71 AND ARG-73.
    15. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-614; ASN-667 AND ASN-1354.
      Tissue: Plasma.
    16. "Zinc and calcium ions cooperatively modulate ADAMTS13 activity."
      Anderson P.J., Kokame K., Sadler J.E.
      J. Biol. Chem. 281:850-857(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    17. Cited for: GLYCOSYLATION AT SER-698; SER-757; SER-907; SER-965; SER-1027 AND SER-1087, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF SER-399; SER-698; SER-757; SER-907; SER-965; SER-1027 AND SER-1087.
    18. "A functional calcium-binding site in the metalloprotease domain of ADAMTS13."
      Gardner M.D., Chion C.K., de Groot R., Shah A., Crawley J.T., Lane D.A.
      Blood 113:1149-1157(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, CALCIUM-BINDING SITES, MUTAGENESIS OF GLU-83; ASP-173; GLU-184; ASP-187 AND GLU-212.
    19. Cited for: GLYCOSYLATION AT ASN-667 AND ASN-707.
    20. "ADAMTS13 mutations and polymorphisms in congenital thrombotic thrombocytopenic purpura."
      Lotta L.A., Garagiola I., Palla R., Cairo A., Peyvandi F.
      Hum. Mutat. 31:11-19(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON VARIANTS.
    21. "Crystal structures of the noncatalytic domains of ADAMTS13 reveal multiple discontinuous exosites for von Willebrand factor."
      Akiyama M., Takeda S., Kokame K., Takagi J., Miyata T.
      Proc. Natl. Acad. Sci. U.S.A. 106:19274-19279(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 287-685, FUNCTION, GLYCOSYLATION AT ASN-552 AND ASN-614, SPACER DOMAIN, DISULFIDE BONDS.
    22. "Mutations and common polymorphisms in ADAMTS13 gene responsible for von Willebrand factor-cleaving protease activity."
      Kokame K., Matsumoto M., Soejima K., Yagi H., Ishizashi H., Funato M., Tamai H., Konno M., Kamide K., Kawano Y., Miyata T., Fujimura Y.
      Proc. Natl. Acad. Sci. U.S.A. 99:11902-11907(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TTP PRO-268 AND TYR-508, VARIANTS GLU-448 AND SER-475, CHARACTERIZATION OF VARIANTS TTP PRO-268 AND TYR-508, CHARACTERIZATION OF VARIANTS GLU-448 AND SER-475.
    23. Cited for: VARIANTS TTP GLN-232; CYS-263 AND LEU-353.
    24. "ADAMTS13 gene defects in two brothers with constitutional thrombotic thrombocytopenic purpura and normalization of von Willebrand factor-cleaving protease activity by recombinant human ADAMTS13."
      Antoine G., Zimmermann K., Plaimauer B., Grillowitzer M., Studt J.D., Lammle B., Scheiflinger F.
      Br. J. Haematol. 120:821-824(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT TTP TRP-1336, VARIANT VAL-732.
    25. "Mutation analysis and clinical implications of von Willebrand factor-cleaving protease deficiency."
      Assink K., Schiphorst R., Allford S., Karpman D., Etzioni A., Brichard B., van de Kar N., Monnens L., van den Heuvel L.
      Kidney Int. 63:1995-1999(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TTP HIS-235; TYR-311 AND LEU-353, VARIANT LEU-457.
    26. "Congenital thrombotic thrombocytopenic purpura in association with a mutation in the second CUB domain of ADAMTS13."
      Pimanda J.E., Maekawa A., Wind T., Paxton J., Chesterman C.N., Hogg P.J.
      Blood 103:627-629(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT TTP ILE-196, VARIANT GLU-448.
    27. "Molecular characterization of ADAMTS13 gene mutations in Japanese patients with Upshaw-Schulman syndrome."
      Matsumoto M., Kokame K., Soejima K., Miura M., Hayashi S., Fujii Y., Iwai A., Ito E., Tsuji Y., Takeda-Shitaka M., Iwadate M., Umeyama H., Yagi H., Ishizashi H., Banno F., Nakagaki T., Miyata T., Fujimura Y.
      Blood 103:1305-1310(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TTP TRP-193; PHE-673; TYR-908 AND CYS-1123, VARIANT GLU-448, CHARACTERIZATION OF VARIANTS TTP TRP-193; PHE-673; TYR-908 AND CYS-1123.
    28. "Identification of novel mutations in ADAMTS13 in an adult patient with congenital thrombotic thrombocytopenic purpura."
      Uchida T., Wada H., Mizutani M., Iwashita M., Ishihara H., Shibano T., Suzuki M., Matsubara Y., Soejima K., Matsumoto M., Fujimura Y., Ikeda Y., Murata M.
      Blood 104:2081-2083(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT TTP VAL-250, CHARACTERIZATION OF VARIANT TTP VAL-250.
    29. "Ten candidate ADAMTS13 mutations in six French families with congenital thrombotic thrombocytopenic purpura (Upshaw-Schulman syndrome)."
      Veyradier A., Lavergne J.M., Ribba A.S., Obert B., Loirat C., Meyer D., Girma J.P.
      J. Thromb. Haemost. 2:424-429(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TTP MET-79; PRO-203; PRO-268; GLN-507; VAL-596; ARG-758 AND SER-908.
    30. "Two novel ADAMTS13 gene mutations in thrombotic thrombocytopenic purpura/hemolytic-uremic syndrome (TTP/HUS)."
      Licht C., Stapenhorst L., Simon T., Budde U., Schneppenheim R., Hoppe B.
      Kidney Int. 66:955-958(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT TTP CYS-390.
    31. "Identification of two novel mutations in ADAMTS13 gene in a patient with hereditary thrombotic thrombocytopenic purpura."
      Liu F., Jin J., Dong N.Z., Wang Y.G., Ruan C.G.
      Zhonghua Xue Ye Xue Za Zhi 26:521-524(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS LEU-903 AND TRP-1095.
    32. "Modulation of ADAMTS13 secretion and specific activity by a combination of common amino acid polymorphisms and a missense mutation."
      Plaimauer B., Fuhrmann J., Mohr G., Wernhart W., Bruno K., Ferrari S., Konetschny C., Antoine G., Rieger M., Scheiflinger F.
      Blood 107:118-125(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANTS TRP-7; GLU-448; ALA-618 AND VAL-732, CHARACTERIZATION OF VARIANT TTP TRP-1336, DISCUSSION OF MUTUAL MODULATORY EFFECTS OF POLYMORPHISMS.
    33. "Mechanisms of the interaction between two ADAMTS13 gene mutations leading to severe deficiency of enzymatic activity."
      Peyvandi F., Lavoretano S., Palla R., Valsecchi C., Merati G., De Cristofaro R., Rossi E., Mannuccio Mannucci P.
      Hum. Mutat. 27:330-336(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TTP MET-88 AND VAL-1239, CHARACTERIZATION OF VARIANTS TTP MET-88 AND VAL-1239.
    34. "Novel ADAMTS-13 mutations in an adult with delayed onset thrombotic thrombocytopenic purpura."
      Tao Z., Anthony K., Peng Y., Choi H., Nolasco L., Rice L., Moake J.L., Dong J.F.
      J. Thromb. Haemost. 4:1931-1935(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT TTP TRP-1060, CHARACTERIZATION OF VARIANTS TTP TRP-1060.
    35. "Novel compound heterozygote mutations (H234Q/R1206X) of the ADAMTS13 gene in an adult patient with Upshaw-Schulman syndrome showing predominant episodes of repeated acute renal failure."
      Shibagaki Y., Matsumoto M., Kokame K., Ohba S., Miyata T., Fujimura Y., Fujita T.
      Nephrol. Dial. Transplant. 21:1289-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT TTP GLN-234, VARIANT LEU-903.
    36. Cited for: VARIANTS TTP ILE-196; CYS-263; SER-347; LEU-353; GLN-507; LEU-671 AND TRP-1060.
    37. "In-vitro and in-vivo consequences of mutations in the von Willebrand factor cleaving protease ADAMTS13 in thrombotic thrombocytopenic purpura."
      Donadelli R., Banterla F., Galbusera M., Capoferri C., Bucchioni S.,