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Q76LX8

- ATS13_HUMAN

UniProt

Q76LX8 - ATS13_HUMAN

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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

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

Protein has several cofactor binding sites:
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity
  • Ca2+CuratedNote: Binds 4 Ca(2+) 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. 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
Complete GO annotation...

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
Complete GO annotation...

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...)1 Publication
Glycosylationi579 – 5791N-linked (GlcNAc...)Sequence Analysis
Glycosylationi614 – 6141N-linked (GlcNAc...)2 Publications
Glycosylationi667 – 6671N-linked (GlcNAc...) (complex)2 Publications
Glycosylationi698 – 6981O-linked (Fuc...)1 Publication
Glycosylationi707 – 7071N-linked (GlcNAc...) (complex)1 Publication
Glycosylationi757 – 7571O-linked (Fuc...)1 Publication
Glycosylationi828 – 8281N-linked (GlcNAc...)Sequence Analysis
Glycosylationi907 – 9071O-linked (Fuc...)1 Publication
Glycosylationi965 – 9651O-linked (Fuc...)1 Publication
Glycosylationi1027 – 10271O-linked (Fuc...)1 Publication
Glycosylationi1087 – 10871O-linked (Fuc...)1 Publication
Glycosylationi1235 – 12351N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1354 – 13541N-linked (GlcNAc...)1 Publication

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

BgeeiQ76LX8.
CleanExiHS_ADAMTS13.
ExpressionAtlasiQ76LX8. baseline and differential.
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 – 3033Combined sources
Helixi307 – 3148Combined sources
Helixi331 – 3344Combined sources
Beta strandi337 – 3404Combined sources
Beta strandi348 – 3514Combined sources
Beta strandi359 – 3613Combined sources
Beta strandi364 – 3674Combined sources
Beta strandi370 – 3734Combined sources
Helixi374 – 3774Combined sources
Beta strandi399 – 4013Combined sources
Beta strandi403 – 4064Combined sources
Beta strandi417 – 4193Combined sources
Beta strandi430 – 4334Combined sources
Helixi442 – 45110Combined sources
Turni452 – 4554Combined sources
Beta strandi470 – 4723Combined sources
Turni474 – 4763Combined sources
Helixi479 – 4835Combined sources
Beta strandi486 – 4894Combined sources
Beta strandi495 – 4973Combined sources
Beta strandi519 – 5235Combined sources
Beta strandi526 – 5305Combined sources
Beta strandi534 – 5363Combined sources
Beta strandi554 – 5629Combined sources
Beta strandi569 – 5768Combined sources
Beta strandi581 – 5888Combined sources
Beta strandi592 – 5998Combined sources
Beta strandi602 – 6054Combined sources
Beta strandi608 – 6103Combined sources
Beta strandi614 – 6185Combined sources
Beta strandi623 – 63210Combined sources
Beta strandi634 – 6363Combined sources
Beta strandi638 – 64710Combined sources
Beta strandi653 – 6619Combined sources
Helixi663 – 6653Combined sources
Helixi667 – 6693Combined sources
Beta strandi673 – 6808Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000118885.
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

        10         20         30         40         50
MHQRHPRARC PPLCVAGILA CGFLLGCWGP SHFQQSCLQA LEPQAVSSYL
60 70 80 90 100
SPGAPLKGRP PSPGFQRQRQ RQRRAAGGIL HLELLVAVGP DVFQAHQEDT
110 120 130 140 150
ERYVLTNLNI GAELLRDPSL GAQFRVHLVK MVILTEPEGA PNITANLTSS
160 170 180 190 200
LLSVCGWSQT INPEDDTDPG HADLVLYITR FDLELPDGNR QVRGVTQLGG
210 220 230 240 250
ACSPTWSCLI TEDTGFDLGV TIAHEIGHSF GLEHDGAPGS GCGPSGHVMA
260 270 280 290 300
SDGAAPRAGL AWSPCSRRQL LSLLSAGRAR CVWDPPRPQP GSAGHPPDAQ
310 320 330 340 350
PGLYYSANEQ CRVAFGPKAV ACTFAREHLD MCQALSCHTD PLDQSSCSRL
360 370 380 390 400
LVPLLDGTEC GVEKWCSKGR CRSLVELTPI AAVHGRWSSW GPRSPCSRSC
410 420 430 440 450
GGGVVTRRRQ CNNPRPAFGG RACVGADLQA EMCNTQACEK TQLEFMSQQC
460 470 480 490 500
ARTDGQPLRS SPGGASFYHW GAAVPHSQGD ALCRHMCRAI GESFIMKRGD
510 520 530 540 550
SFLDGTRCMP SGPREDGTLS LCVSGSCRTF GCDGRMDSQQ VWDRCQVCGG
560 570 580 590 600
DNSTCSPRKG SFTAGRAREY VTFLTVTPNL TSVYIANHRP LFTHLAVRIG
610 620 630 640 650
GRYVVAGKMS ISPNTTYPSL LEDGRVEYRV ALTEDRLPRL EEIRIWGPLQ
660 670 680 690 700
EDADIQVYRR YGEEYGNLTR PDITFTYFQP KPRQAWVWAA VRGPCSVSCG
710 720 730 740 750
AGLRWVNYSC LDQARKELVE TVQCQGSQQP PAWPEACVLE PCPPYWAVGD
760 770 780 790 800
FGPCSASCGG GLRERPVRCV EAQGSLLKTL PPARCRAGAQ QPAVALETCN
810 820 830 840 850
PQPCPARWEV SEPSSCTSAG GAGLALENET CVPGADGLEA PVTEGPGSVD
860 870 880 890 900
EKLPAPEPCV GMSCPPGWGH LDATSAGEKA PSPWGSIRTG AQAAHVWTPA
910 920 930 940 950
AGSCSVSCGR GLMELRFLCM DSALRVPVQE ELCGLASKPG SRREVCQAVP
960 970 980 990 1000
CPARWQYKLA ACSVSCGRGV VRRILYCARA HGEDDGEEIL LDTQCQGLPR
1010 1020 1030 1040 1050
PEPQEACSLE PCPPRWKVMS LGPCSASCGL GTARRSVACV QLDQGQDVEV
1060 1070 1080 1090 1100
DEAACAALVR PEASVPCLIA DCTYRWHVGT WMECSVSCGD GIQRRRDTCL
1110 1120 1130 1140 1150
GPQAQAPVPA DFCQHLPKPV TVRGCWAGPC VGQGTPSLVP HEEAAAPGRT
1160 1170 1180 1190 1200
TATPAGASLE WSQARGLLFS PAPQPRRLLP GPQENSVQSS ACGRQHLEPT
1210 1220 1230 1240 1250
GTIDMRGPGQ ADCAVAIGRP LGEVVTLRVL ESSLNCSAGD MLLLWGRLTW
1260 1270 1280 1290 1300
RKMCRKLLDM TFSSKTNTLV VRQRCGRPGG GVLLRYGSQL APETFYRECD
1310 1320 1330 1340 1350
MQLFGPWGEI VSPSLSPATS NAGGCRLFIN VAPHARIAIH ALATNMGAGT
1360 1370 1380 1390 1400
EGANASYILI RDTHSLRTTA FHGQQVLYWE SESSQAEMEF SEGFLKAQAS
1410 1420
LRGQYWTLQS WVPEMQDPQS WKGKEGT
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.Curated
The sequence CAB66743.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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

BindingDBi Q76LX8.
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.
GeneTreei ENSGT00760000118885.
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

Bgeei Q76LX8.
CleanExi HS_ADAMTS13.
ExpressionAtlasi Q76LX8. baseline and differential.
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

« Hide 'large scale' publications
  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