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Q76LX8 (ATS13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 13

Short name=ADAM-TS 13
Short name=ADAM-TS13
Short name=ADAMTS-13
EC=3.4.24.87
Alternative name(s):
von Willebrand factor-cleaving protease
Short name=vWF-CP
Short name=vWF-cleaving protease
Gene names
Name:ADAMTS13
Synonyms:C9orf8
ORF Names:UNQ6102/PRO20085
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1427 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cleaves the vWF multimers in plasma into smaller forms.

Catalytic activity

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.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Binds 4 calcium ions Potential.

Enzyme regulation

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. Ref.12 Ref.14 Ref.16

Subcellular location

Secreted. Note: Secretion enhanced by O-fucosylation of TSP type-1 repeats. Ref.11

Tissue specificity

Plasma. Expressed primarily in liver. Ref.1

Domain

The pro-domain is not required for folding or secretion and does not perform the common function of maintening enzyme latency.

The spacer domain is necessary to recognize and cleave vWF. The C-terminal TSP type-1 and CUB domains may modulate this interaction.

Post-translational modification

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. Ref.2 Ref.15 Ref.17

The precursor is processed by a furin endopeptidase which cleaves off the pro-domain.

Polymorphism

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.

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.37 Ref.38

Sequence similarities

Contains 2 CUB domains.

Contains 1 disintegrin domain.

Contains 1 peptidase M12B domain.

Contains 8 TSP type-1 domains.

Sequence caution

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.

Ontologies

Keywords
   Biological processBlood coagulation
Hemostasis
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainRepeat
Signal
   LigandCalcium
Metal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Zymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell-matrix adhesion

Non-traceable author statement Ref.2. Source: UniProtKB

glycoprotein metabolic process

Non-traceable author statement Ref.2. Source: UniProtKB

integrin-mediated signaling pathway

Non-traceable author statement Ref.2. Source: UniProtKB

peptide catabolic process

Inferred from direct assay Ref.10. Source: UniProtKB

platelet activation

Non-traceable author statement Ref.2. Source: UniProtKB

protein processing

Traceable author statement Ref.2. Source: UniProtKB

proteolysis

Inferred from direct assay Ref.10. Source: UniProtKB

response to interferon-gamma

Inferred from electronic annotation. Source: Ensembl

response to interleukin-4

Inferred from electronic annotation. Source: Ensembl

response to tumor necrosis factor

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell surface

Non-traceable author statement Ref.2. Source: UniProtKB

extracellular space

Inferred from electronic annotation. Source: Ensembl

proteinaceous extracellular matrix

Traceable author statement Ref.2. Source: UniProtKB

   Molecular_functioncalcium ion binding

Traceable author statement Ref.2. Source: UniProtKB

integrin binding

Traceable author statement Ref.2. Source: UniProtKB

metalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

metallopeptidase activity

Traceable author statement Ref.2. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 12775718. Source: UniProtKB

zinc ion binding

Traceable author statement Ref.2. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

VWFP042755EBI-981764,EBI-981819

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q76LX8-1)

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.
Isoform 2 (identifier: Q76LX8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1135-1190: Missing.
Isoform 3 (identifier: Q76LX8-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Potential
Propeptide30 – 7445
PRO_0000247510
Chain75 – 14271353A disintegrin and metalloproteinase with thrombospondin motifs 13
PRO_0000247511

Regions

Domain80 – 286207Peptidase M12B
Domain287 – 38397Disintegrin
Domain384 – 43956TSP type-1 1
Domain682 – 73049TSP type-1 2
Domain742 – 80564TSP type-1 3
Domain808 – 85952TSP type-1 4
Domain896 – 95055TSP type-1 5
Domain951 – 101161TSP type-1 6
Domain1012 – 106857TSP type-1 7
Domain1072 – 113160TSP type-1 8
Domain1192 – 1298107CUB 1
Domain1299 – 1427129CUB 2
Region440 – 556117Cysteine-rich
Region556 – 685130Spacer
Motif498 – 5003Cell attachment site Potential

Sites

Active site2251 By similarity
Metal binding831Calcium Potential
Metal binding1731Calcium Potential
Metal binding1821Calcium; high affinity
Metal binding1841Calcium; high affinity
Metal binding1871Calcium; high affinity
Metal binding2121Calcium; high affinity
Metal binding2241Zinc; catalytic By similarity
Metal binding2281Zinc; catalytic By similarity
Metal binding2341Zinc; catalytic By similarity
Metal binding2811Calcium Potential
Metal binding2841Calcium Potential

Amino acid modifications

Glycosylation1421N-linked (GlcNAc...) Potential
Glycosylation1461N-linked (GlcNAc...) Potential
Glycosylation5521N-linked (GlcNAc...) Potential
Glycosylation5791N-linked (GlcNAc...) Potential
Glycosylation6141N-linked (GlcNAc...) Ref.13
Glycosylation6671N-linked (GlcNAc...) (complex) Ref.13 Ref.17
Glycosylation6981O-linked (Fuc...) Ref.15
Glycosylation7071N-linked (GlcNAc...) (complex) Ref.17
Glycosylation7571O-linked (Fuc...) Ref.15
Glycosylation8281N-linked (GlcNAc...) Potential
Glycosylation9071O-linked (Fuc...) Ref.15
Glycosylation9651O-linked (Fuc...) Ref.15
Glycosylation10271O-linked (Fuc...) Ref.15
Glycosylation10871O-linked (Fuc...) Ref.15
Glycosylation12351N-linked (GlcNAc...) Potential
Glycosylation13541N-linked (GlcNAc...) Ref.13
Disulfide bond155 ↔ 208 By similarity
Disulfide bond202 ↔ 281 By similarity
Disulfide bond242 ↔ 265 By similarity
Disulfide bond311 ↔ 337 By similarity
Disulfide bond322 ↔ 347 By similarity
Disulfide bond332 ↔ 366 By similarity
Disulfide bond360 ↔ 371 By similarity
Disulfide bond396 ↔ 433 By similarity
Disulfide bond400 ↔ 438 By similarity
Disulfide bond411 ↔ 423 By similarity

Natural variations

Alternative sequence275 – 30531Missing in isoform 3.
VSP_020002
Alternative sequence1135 – 119056Missing in isoform 2 and isoform 3.
VSP_020003
Natural variant71R → W Does not affect protein secretion. Ref.3 Ref.5 Ref.29
Corresponds to variant rs34024143 [ dbSNP | Ensembl ].
VAR_027109
Natural variant791I → M in TTP. Ref.26
Corresponds to variant rs281875297 [ dbSNP | Ensembl ].
VAR_067770
Natural variant881V → M in TTP; reduces protein secretion and proteolytic activity. Ref.30
Corresponds to variant rs281875302 [ dbSNP | Ensembl ].
VAR_027110
Natural variant961H → D in TTP. Ref.3
Corresponds to variant rs121908467 [ dbSNP | Ensembl ].
VAR_027111
Natural variant1021R → C in TTP. Ref.3
Corresponds to variant rs121908469 [ dbSNP | Ensembl ].
VAR_027112
Natural variant1191S → F in TTP. Ref.35
Corresponds to variant rs281875291 [ dbSNP | Ensembl ].
VAR_067771
Natural variant1781I → T in TTP. Ref.36
Corresponds to variant rs281875289 [ dbSNP | Ensembl ].
VAR_067772
Natural variant1931R → W in TTP; low activity. Ref.24 Ref.36
Corresponds to variant rs281875287 [ dbSNP | Ensembl ].
VAR_027113
Natural variant1961T → I in TTP. Ref.3 Ref.23 Ref.33
Corresponds to variant rs121908470 [ dbSNP | Ensembl ].
VAR_027114
Natural variant2031S → P in TTP. Ref.26
Corresponds to variant rs281875298 [ dbSNP | Ensembl ].
VAR_067773
Natural variant2321L → Q in TTP. Ref.20
Corresponds to variant rs281875292 [ dbSNP | Ensembl ].
VAR_067774
Natural variant2341H → Q in TTP. Ref.32
Corresponds to variant rs281875304 [ dbSNP | Ensembl ].
VAR_027115
Natural variant2351D → H in TTP. Ref.22
Corresponds to variant rs281875337 [ dbSNP | Ensembl ].
VAR_067775
Natural variant2501A → V in TTP; mild effect on protein secretion; strong reduction of proteolytic activity. Ref.25
Corresponds to variant rs121908478 [ dbSNP | Ensembl ].
VAR_027116
Natural variant2631S → C in TTP. Ref.20 Ref.33
Corresponds to variant rs281875293 [ dbSNP | Ensembl ].
VAR_067776
Natural variant2681R → P in TTP; affects protein secretion. Ref.19 Ref.26
Corresponds to variant rs121908477 [ dbSNP | Ensembl ].
VAR_027117
Natural variant3041Y → C in TTP. Ref.36
Corresponds to variant rs281875285 [ dbSNP | Ensembl ].
VAR_067777
Natural variant3111C → Y in TTP. Ref.22
Corresponds to variant rs281875336 [ dbSNP | Ensembl ].
VAR_067778
Natural variant3391T → R. Ref.36
Corresponds to variant rs149517360 [ dbSNP | Ensembl ].
VAR_067779
Natural variant3471C → S in TTP. Ref.33
Corresponds to variant rs281875294 [ dbSNP | Ensembl ].
VAR_067780
Natural variant3491R → C in TTP. Ref.36
Corresponds to variant rs281875288 [ dbSNP | Ensembl ].
VAR_067781
Natural variant3531P → L in TTP. Ref.20 Ref.22 Ref.33
Corresponds to variant rs281875338 [ dbSNP | Ensembl ].
VAR_067782
Natural variant3901W → C in TTP. Ref.27
Corresponds to variant rs281875306 [ dbSNP | Ensembl ].
VAR_027118
Natural variant3981R → H in TTP. Ref.3
Corresponds to variant rs121908471 [ dbSNP | Ensembl ].
VAR_027119
Natural variant4481Q → E Does not affect protein secretion; normal proteolytic activity. Ref.3 Ref.5 Ref.7 Ref.19 Ref.23 Ref.24 Ref.29 Ref.34 Ref.36
Corresponds to variant rs2301612 [ dbSNP | Ensembl ].
VAR_027120
Natural variant4561Q → H. Ref.5
Corresponds to variant rs36220239 [ dbSNP | Ensembl ].
VAR_027162
Natural variant4571P → L. Ref.5 Ref.22
Corresponds to variant rs36220240 [ dbSNP | Ensembl ].
VAR_027163
Natural variant4751P → S. Ref.19
Corresponds to variant rs11575933 [ dbSNP | Ensembl ].
VAR_027121
Natural variant5071R → Q in TTP. Ref.26 Ref.33
Corresponds to variant rs281875296 [ dbSNP | Ensembl ].
VAR_067783
Natural variant5081C → Y in TTP; impairs protein secretion. Ref.19
Corresponds to variant rs281875305 [ dbSNP | Ensembl ].
VAR_027122
Natural variant5251G → D in TTP. Ref.36
Corresponds to variant rs281875286 [ dbSNP | Ensembl ].
VAR_067784
Natural variant5281R → G in TTP. Ref.3
Corresponds to variant rs121908473 [ dbSNP | Ensembl ].
VAR_027123
Natural variant5961A → V in TTP. Ref.26
Corresponds to variant rs281875299 [ dbSNP | Ensembl ].
VAR_067785
Natural variant6061A → P in TTP. Ref.36
Corresponds to variant rs281875290 [ dbSNP | Ensembl ].
VAR_067786
Natural variant6181P → A. Ref.3 Ref.5 Ref.29 Ref.36
Corresponds to variant rs28647808 [ dbSNP | Ensembl ].
VAR_027124
Natural variant6251R → H. Ref.3 Ref.5
Corresponds to variant rs36090624 [ dbSNP | Ensembl ].
VAR_027125
Natural variant6581Y → C in TTP. Ref.38
Corresponds to variant rs281875335 [ dbSNP | Ensembl ].
VAR_067787
Natural variant6711P → L in TTP. Ref.33
Corresponds to variant rs281875295 [ dbSNP | Ensembl ].
VAR_067788
Natural variant6731I → F in TTP; impairs protein secretion. Ref.24
Corresponds to variant rs281875307 [ dbSNP | Ensembl ].
VAR_027126
Natural variant6921R → C in TTP. Ref.3
Corresponds to variant rs121908475 [ dbSNP | Ensembl ].
VAR_027127
Natural variant7321A → V. Ref.3 Ref.21 Ref.29
Corresponds to variant rs41314453 [ dbSNP | Ensembl ].
VAR_027128
Natural variant7401E → K. Ref.5
Corresponds to variant rs36221451 [ dbSNP | Ensembl ].
VAR_027164
Natural variant7581C → R in TTP. Ref.26
Corresponds to variant rs281875300 [ dbSNP | Ensembl ].
VAR_067789
Natural variant9001A → V. Ref.2 Ref.3 Ref.5
Corresponds to variant rs685523 [ dbSNP | Ensembl ].
VAR_027129
Natural variant9031S → L. Ref.28 Ref.32
Corresponds to variant rs78977446 [ dbSNP | Ensembl ].
VAR_027130
Natural variant9081C → S in TTP. Ref.26
Corresponds to variant rs281875301 [ dbSNP | Ensembl ].
VAR_067790
Natural variant9081C → Y in TTP; impairs protein secretion. Ref.24
Corresponds to variant rs281875301 [ dbSNP | Ensembl ].
VAR_027131
Natural variant9511C → G in TTP. Ref.3
Corresponds to variant rs121908468 [ dbSNP | Ensembl ].
VAR_027132
Natural variant977 – 9793CAR → W in TTP.
VAR_067791
Natural variant9821G → R. Ref.5
Corresponds to variant rs36222275 [ dbSNP | Ensembl ].
VAR_027165
Natural variant10241C → G in TTP. Ref.3
Corresponds to variant rs121908472 [ dbSNP | Ensembl ].
VAR_027133
Natural variant10331A → T. Ref.3 Ref.5
Corresponds to variant rs28503257 [ dbSNP | Ensembl ].
VAR_027134
Natural variant10601R → W in TTP; affects protein secretion; the mutant protein has reduced protease activity. Ref.31 Ref.33 Ref.34
Corresponds to variant rs142572218 [ dbSNP | Ensembl ].
VAR_067792
Natural variant10951R → W in a patient with thrombotic thrombocytopenic purpura. Ref.28
VAR_027135
Natural variant11231R → C in TTP; impairs protein secretion; the mutant protein has reduced protease activity. Ref.24 Ref.34
Corresponds to variant rs281875340 [ dbSNP | Ensembl ].
VAR_027136
Natural variant12131C → Y in TTP. Ref.3
Corresponds to variant rs121908474 [ dbSNP | Ensembl ].
VAR_027137
Natural variant12191R → W in TTP; affects protein secretion; the mutant protein has reduced protease activity. Ref.34
Corresponds to variant rs281875339 [ dbSNP | Ensembl ].
VAR_067793
Natural variant12261T → I. Ref.5
Corresponds to variant rs36222894 [ dbSNP | Ensembl ].
VAR_027166
Natural variant12391G → V in TTP; impairs protein secretion. Ref.30
Corresponds to variant rs281875303 [ dbSNP | Ensembl ].
VAR_027138
Natural variant13141S → L Found in a patient with hemolytic uremic syndrome. Ref.39
Corresponds to variant rs142060916 [ dbSNP | Ensembl ].
VAR_067794
Natural variant13361R → W in TTP; impairs protein secretion and proteolytic activity. Ref.21 Ref.29
Corresponds to variant rs281875308 [ dbSNP | Ensembl ].
VAR_027139

Experimental info

Mutagenesis711R → K: Abolishes pro-domain removal but no loss of proteolytic activity; when associated with D-73. Ref.12
Mutagenesis731R → D: Abolishes pro-domain removal but no loss of proteolytic activity; when associated with K-71. Ref.12
Mutagenesis831E → A: No change in calcium dependence for proteolysis. Ref.16
Mutagenesis1731D → A: No change in calcium dependence for proteolysis. Ref.16
Mutagenesis1841E → A: Dramatically reduced affinity for calcium. Ref.16
Mutagenesis1871D → A: Dramatically reduced affinity for calcium. Ref.16
Mutagenesis2121E → A: Dramatically reduced affinity for calcium. Ref.16
Mutagenesis3991S → A: No effect on cleavage of VWF and little change in secretion of ADAMTS13. Abolishes secretion of ADAMTS13; when associated with A-698. Ref.15
Mutagenesis6981S → A: No effect on cleavage of VWF and greatly reduced secretion of ADAMTS13. Abolishes secretion of ADAMTS13; when associated with A-399. Ref.15
Mutagenesis7571S → A: No effect on cleavage of VWF and little change in secretion of ADAMTS13. Ref.15
Mutagenesis9071S → 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. Ref.15
Mutagenesis9651S → 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. Ref.15
Mutagenesis10271S → 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. Ref.15
Mutagenesis10871S → 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. Ref.15
Sequence conflict1011E → R AA sequence Ref.1

Secondary structure

......................................................................... 1427
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: A2103AFABC1A4445

FASTA1,427153,604
        10         20         30         40         50         60 
MHQRHPRARC PPLCVAGILA CGFLLGCWGP SHFQQSCLQA LEPQAVSSYL SPGAPLKGRP 

        70         80         90        100        110        120 
PSPGFQRQRQ RQRRAAGGIL HLELLVAVGP DVFQAHQEDT ERYVLTNLNI GAELLRDPSL 

       130        140        150        160        170        180 
GAQFRVHLVK MVILTEPEGA PNITANLTSS LLSVCGWSQT INPEDDTDPG HADLVLYITR 

       190        200        210        220        230        240 
FDLELPDGNR QVRGVTQLGG ACSPTWSCLI TEDTGFDLGV TIAHEIGHSF GLEHDGAPGS 

       250        260        270        280        290        300 
GCGPSGHVMA SDGAAPRAGL AWSPCSRRQL LSLLSAGRAR CVWDPPRPQP GSAGHPPDAQ 

       310        320        330        340        350        360 
PGLYYSANEQ CRVAFGPKAV ACTFAREHLD MCQALSCHTD PLDQSSCSRL LVPLLDGTEC 

       370        380        390        400        410        420 
GVEKWCSKGR CRSLVELTPI AAVHGRWSSW GPRSPCSRSC GGGVVTRRRQ CNNPRPAFGG 

       430        440        450        460        470        480 
RACVGADLQA EMCNTQACEK TQLEFMSQQC ARTDGQPLRS SPGGASFYHW GAAVPHSQGD 

       490        500        510        520        530        540 
ALCRHMCRAI GESFIMKRGD SFLDGTRCMP SGPREDGTLS LCVSGSCRTF GCDGRMDSQQ 

       550        560        570        580        590        600 
VWDRCQVCGG DNSTCSPRKG SFTAGRAREY VTFLTVTPNL TSVYIANHRP LFTHLAVRIG 

       610        620        630        640        650        660 
GRYVVAGKMS ISPNTTYPSL LEDGRVEYRV ALTEDRLPRL EEIRIWGPLQ EDADIQVYRR 

       670        680        690        700        710        720 
YGEEYGNLTR PDITFTYFQP KPRQAWVWAA VRGPCSVSCG AGLRWVNYSC LDQARKELVE 

       730        740        750        760        770        780 
TVQCQGSQQP PAWPEACVLE PCPPYWAVGD FGPCSASCGG GLRERPVRCV EAQGSLLKTL 

       790        800        810        820        830        840 
PPARCRAGAQ QPAVALETCN PQPCPARWEV SEPSSCTSAG GAGLALENET CVPGADGLEA 

       850        860        870        880        890        900 
PVTEGPGSVD EKLPAPEPCV GMSCPPGWGH LDATSAGEKA PSPWGSIRTG AQAAHVWTPA 

       910        920        930        940        950        960 
AGSCSVSCGR GLMELRFLCM DSALRVPVQE ELCGLASKPG SRREVCQAVP CPARWQYKLA 

       970        980        990       1000       1010       1020 
ACSVSCGRGV VRRILYCARA HGEDDGEEIL LDTQCQGLPR PEPQEACSLE PCPPRWKVMS 

      1030       1040       1050       1060       1070       1080 
LGPCSASCGL GTARRSVACV QLDQGQDVEV DEAACAALVR PEASVPCLIA DCTYRWHVGT 

      1090       1100       1110       1120       1130       1140 
WMECSVSCGD GIQRRRDTCL GPQAQAPVPA DFCQHLPKPV TVRGCWAGPC VGQGTPSLVP 

      1150       1160       1170       1180       1190       1200 
HEEAAAPGRT TATPAGASLE WSQARGLLFS PAPQPRRLLP GPQENSVQSS ACGRQHLEPT 

      1210       1220       1230       1240       1250       1260 
GTIDMRGPGQ ADCAVAIGRP LGEVVTLRVL ESSLNCSAGD MLLLWGRLTW RKMCRKLLDM 

      1270       1280       1290       1300       1310       1320 
TFSSKTNTLV VRQRCGRPGG GVLLRYGSQL APETFYRECD MQLFGPWGEI VSPSLSPATS 

      1330       1340       1350       1360       1370       1380 
NAGGCRLFIN VAPHARIAIH ALATNMGAGT EGANASYILI RDTHSLRTTA FHGQQVLYWE 

      1390       1400       1410       1420 
SESSQAEMEF SEGFLKAQAS LRGQYWTLQS WVPEMQDPQS WKGKEGT 

« Hide

Isoform 2 [UniParc].

Checksum: AE4C713AE5B64DFC
Show »

FASTA1,371147,804
Isoform 3 [UniParc].

Checksum: 0BFBEF4C3D58B2C2
Show »

FASTA1,340144,517

References

« Hide 'large scale' references
[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]"Mutations in a member of the ADAMTS gene family cause thrombotic thrombocytopenic purpura."
Levy G.G., Nichols W.C., Lian E.C., Foroud T., McClintick J.N., McGee B.M., Yang A.Y., Siemieniak D.R., Stark K.R., Gruppo R., Sarode R., Shurin S.B., Chandrasekaran V., Stabler S.P., Sabio H., Bouhassira E.E., Upshaw J.D. Jr., Ginsburg D., Tsai H.-M.
Nature 413:488-494(2001) [PubMed] [Europe PMC] [Abstract]
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]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.
[6]"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. expand/collapse author list , 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].
[7]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 275-1427, VARIANT GLU-448.
[8]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1191-1427.
Tissue: Testis.
[9]"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.
[10]"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.
[11]"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.
[12]"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.
[13]"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.
[14]"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.
[15]"O-fucosylation is required for ADAMTS13 secretion."
Ricketts L.M., Dlugosz M., Luther K.B., Haltiwanger R.S., Majerus E.M.
J. Biol. Chem. 282:17014-17023(2007) [PubMed] [Europe PMC] [Abstract]
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.
[16]"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.
[17]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-667 AND ASN-707.
[18]"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.
[19]"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.
[20]"von Willebrand factor cleaving protease and ADAMTS13 mutations in childhood TTP."
Schneppenheim R., Budde U., Oyen F., Angerhaus D., Aumann V., Drewke E., Hassenpflug W., Haberle J., Kentouche K., Kohne E., Kurnik K., Mueller-Wiefel D., Obser T., Santer R., Sykora K.W.
Blood 101:1845-1850(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS TTP GLN-232; CYS-263 AND LEU-353.
[21]"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.
[22]"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.
[23]"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.
[24]"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.
[25]"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.
[26]"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.
[27]"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.
[28]"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.
[29]"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.
[30]"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.
[31]"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.
[32]"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.
[33]"A common origin of the 4143insA ADAMTS13 mutation."
Schneppenheim R., Kremer Hovinga J.A., Becker T., Budde U., Karpman D., Brockhaus W., Hrachovinova I., Korczowski B., Oyen F., Rittich S., von Rosen J., Tjonnfjord G.E., Pimanda J.E., Wienker T.F., Lammle B.
Thromb. Haemost. 96:3-6(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS TTP ILE-196; CYS-263; SER-347; LEU-353; GLN-507; LEU-671 AND TRP-1060.
[34]"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., Gastoldi S., Nosari S., Monteferrante G., Ruggeri Z.M., Bresin E., Scheiflinger F., Rossi E., Martinez C., Coppo R., Remuzzi G., Noris M.
Thromb. Haemost. 96:454-464(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS TTP TRP-1060; CYS-1123 AND TRP-1219, CHARACTERIZATION OF VARIANTS TTP TRP-1060; CYS-1123 AND TRP-1219, VARIANT GLU-448.
[35]"A first case of congenital TTP on the African continent due to a new homozygous mutation in the catalytic domain of ADAMTS13."
Meyer S.C., Jeddi R., Meddeb B., Gouider E., Lammle B., Kremer Hovinga J.A.
Ann. Hematol. 87:663-666(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT TTP PHE-119.
[36]"Pregnancy-induced thrombocytopenia and TTP, and the risk of fetal death, in Upshaw-Schulman syndrome: a series of 15 pregnancies in 9 genotyped patients."
Fujimura Y., Matsumoto M., Kokame K., Isonishi A., Soejima K., Akiyama N., Tomiyama J., Natori K., Kuranishi Y., Imamura Y., Inoue N., Higasa S., Seike M., Kozuka T., Hara M., Wada H., Murata M., Ikeda Y., Miyata T., George J.N.
Br. J. Haematol. 144:742-754(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS TTP THR-178; TRP-193; CYS-304; CYS-349; ASP-525 AND PRO-606, VARIANTS ARG-339; GLU-448 AND ALA-618.
[37]"The first deletion mutation in the TSP1-6 repeat domain of ADAMTS13 in a family with inherited thrombotic thrombocytopenic purpura."
Palla R., Lavoretano S., Lombardi R., Garagiola I., Karimi M., Afrasiabi A., Ramzi M., De Cristofaro R., Peyvandi F.
Haematologica 94:289-293(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT TTP 977-CYS--ARG-979 DELINS TRP.
[38]"A novel homozygous missense ADAMTS13 mutation Y658C in a patient with recurrent thrombotic thrombocytopenic purpura."
Lee S.H., Park J.H., Park S.K., Lee E.H., Choi J.I., Visentin G.P., Park T.S., Oh S.H., Kim S.R.
Ann. Clin. Lab. Sci. 41:273-276(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT TTP CYS-658.
[39]"ADAMTS13 gene mutations in children with hemolytic uremic syndrome."
Choi H.S., Cheong H.I., Kim N.K., Oh D., Park H.W.
Yonsei Med. J. 52:530-534(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LEU-1314.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
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.
AY358118 mRNA. Translation: AAQ88485.1. Different initiation.
AL136809 mRNA. Translation: CAB66743.1. Different initiation.
CCDSCCDS6970.1. [Q76LX8-1]
CCDS6971.1. [Q76LX8-3]
CCDS6972.1. [Q76LX8-2]
RefSeqNP_620594.1. NM_139025.4. [Q76LX8-1]
NP_620595.1. NM_139026.4. [Q76LX8-3]
NP_620596.2. NM_139027.4. [Q76LX8-2]
UniGeneHs.131433.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3GHMX-ray2.60A287-685[»]
3GHNX-ray2.80A287-685[»]
3VN4X-ray2.80A287-685[»]
ProteinModelPortalQ76LX8.
SMRQ76LX8. Positions 82-682.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116274. 1 interaction.
DIPDIP-36050N.
IntActQ76LX8. 1 interaction.
MINTMINT-4713142.
STRING9606.ENSP00000360997.

Chemistry

ChEMBLCHEMBL2346492.

Protein family/group databases

MEROPSM12.241.

PTM databases

PhosphoSiteQ76LX8.

Polymorphism databases

DMDM74749836.

Proteomic databases

PaxDbQ76LX8.
PRIDEQ76LX8.

Protocols and materials databases

DNASU11093.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000355699; ENSP00000347927; ENSG00000160323. [Q76LX8-2]
ENST00000356589; ENSP00000348997; ENSG00000160323. [Q76LX8-3]
ENST00000371910; ENSP00000360978; ENSG00000160323.
ENST00000371929; ENSP00000360997; ENSG00000160323. [Q76LX8-1]
ENST00000562382; ENSP00000454450; ENSG00000260099.
ENST00000562694; ENSP00000457843; ENSG00000260099. [Q76LX8-3]
ENST00000563979; ENSP00000456186; ENSG00000260099. [Q76LX8-1]
ENST00000568644; ENSP00000457774; ENSG00000260099. [Q76LX8-2]
GeneID11093.
KEGGhsa:11093.
UCSCuc004cdt.1. human. [Q76LX8-2]
uc004cdu.1. human. [Q76LX8-3]
uc004cdv.4. human. [Q76LX8-1]

Organism-specific databases

CTD11093.
GeneCardsGC09P136279.
HGNCHGNC:1366. ADAMTS13.
HPAHPA042014.
HPA042844.
MIM274150. phenotype.
604134. gene.
neXtProtNX_Q76LX8.
Orphanet93583. Congenital thrombotic thrombocytopenic purpura due to ADAMTS-13 deficiency.
PharmGKBPA24539.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG239882.
HOGENOMHOG000231627.
HOVERGENHBG080358.
InParanoidQ76LX8.
KOK08627.
OMACDMQLFG.
PhylomeDBQ76LX8.
TreeFamTF313537.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressQ76LX8.
BgeeQ76LX8.
CleanExHS_ADAMTS13.
GenevestigatorQ76LX8.

Family and domain databases

Gene3D3.40.390.10. 1 hit.
InterProIPR000859. CUB_dom.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
PfamPF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 5 hits.
[Graphical view]
PRINTSPR01857. ADAMTSFAMILY.
SMARTSM00209. TSP1. 7 hits.
[Graphical view]
SUPFAMSSF49854. SSF49854. 2 hits.
SSF82895. SSF82895. 5 hits.
PROSITEPS50215. ADAM_MEPRO. 1 hit.
PS50092. TSP1. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ76LX8.
GeneWikiADAMTS13.
GenomeRNAi11093.
NextBio42166.
PROQ76LX8.
SOURCESearch...

Entry information

Entry nameATS13_HUMAN
AccessionPrimary (citable) accession number: Q76LX8
Secondary accession number(s): Q6UY16 expand/collapse secondary AC list , Q710F6, Q711T8, Q96L37, Q9H0G3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: July 19, 2004
Last modified: July 9, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM