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P04275

- VWF_HUMAN

UniProt

P04275 - VWF_HUMAN

Protein

von Willebrand factor

Gene

VWF

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 199 (01 Oct 2014)
      Sequence version 4 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    Important in the maintenance of hemostasis, it promotes adhesion of platelets to the sites of vascular injury by forming a molecular bridge between sub-endothelial collagen matrix and platelet-surface receptor complex GPIb-IX-V. Also acts as a chaperone for coagulation factor VIII, delivering it to the site of injury, stabilizing its heterodimeric structure and protecting it from premature clearance from plasma.

    GO - Molecular functioni

    1. chaperone binding Source: UniProtKB
    2. collagen binding Source: UniProtKB
    3. glycoprotein binding Source: UniProtKB
    4. identical protein binding Source: IntAct
    5. immunoglobulin binding Source: UniProtKB
    6. integrin binding Source: UniProtKB
    7. protease binding Source: UniProtKB
    8. protein binding Source: UniProtKB
    9. protein homodimerization activity Source: UniProtKB
    10. protein N-terminus binding Source: UniProtKB

    GO - Biological processi

    1. blood coagulation Source: UniProtKB
    2. blood coagulation, intrinsic pathway Source: Reactome
    3. cell adhesion Source: UniProtKB
    4. cell-substrate adhesion Source: UniProtKB
    5. extracellular matrix organization Source: Reactome
    6. hemostasis Source: UniProtKB
    7. liver development Source: Ensembl
    8. placenta development Source: Ensembl
    9. platelet activation Source: UniProtKB
    10. platelet degranulation Source: Reactome
    11. protein homooligomerization Source: UniProtKB
    12. response to wounding Source: UniProtKB

    Keywords - Biological processi

    Blood coagulation, Cell adhesion, Hemostasis

    Enzyme and pathway databases

    ReactomeiREACT_1230. Platelet Adhesion to exposed collagen.
    REACT_13552. Integrin cell surface interactions.
    REACT_15381. p130Cas linkage to MAPK signaling for integrins.
    REACT_15523. Integrin alphaIIb beta3 signaling.
    REACT_23847. GP1b-IX-V activation signalling.
    REACT_326. Intrinsic Pathway.

    Protein family/group databases

    MEROPSiI08.950.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    von Willebrand factor
    Short name:
    vWF
    Cleaved into the following chain:
    Alternative name(s):
    von Willebrand antigen II
    Gene namesi
    Name:VWF
    Synonyms:F8VWF
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:12726. VWF.

    Subcellular locationi

    Secreted 1 Publication. Secretedextracellular spaceextracellular matrix 1 Publication
    Note: Localized to storage granules.

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB
    2. external side of plasma membrane Source: Ensembl
    3. extracellular matrix Source: UniProtKB
    4. extracellular region Source: UniProtKB
    5. extracellular vesicular exosome Source: UniProt
    6. platelet alpha granule Source: UniProtKB
    7. platelet alpha granule lumen Source: Reactome
    8. proteinaceous extracellular matrix Source: UniProtKB-SubCell
    9. Weibel-Palade body Source: UniProtKB

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    von Willebrand disease 1 (VWD1) [MIM:193400]: A common hemorrhagic disorder due to defects in von Willebrand factor protein and resulting in impaired platelet aggregation. Von Willebrand disease type 1 is characterized by partial quantitative deficiency of circulating von Willebrand factor, that is otherwise structurally and functionally normal. Clinical manifestations are mucocutaneous bleeding, such as epistaxis and menorrhagia, and prolonged bleeding after surgery or trauma.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti273 – 2731R → W in VWD1 and VWD3; defect in secretion and formation of multimers. 1 Publication
    Corresponds to variant rs61753997 [ dbSNP | Ensembl ].
    VAR_010242
    Natural varianti1149 – 11491C → R in VWD1; reduced secretion of homodimers and heterodimers with wild type VWD and increased degradation by the proteasome. 1 Publication
    VAR_064925
    von Willebrand disease 2 (VWD2) [MIM:613554]: A hemorrhagic disorder due to defects in von Willebrand factor protein and resulting in altered platelet aggregation. Von Willebrand disease type 2 is characterized by qualitative deficiency and functional anomalies of von Willebrand factor. It is divided in different subtypes including 2A, 2B, 2M and 2N (Normandy variant). The mutant VWF protein in types 2A, 2B and 2M are defective in their platelet-dependent function, whereas the mutant protein in type 2N is defective in its ability to bind factor VIII. Clinical manifestations are mucocutaneous bleeding, such as epistaxis and menorrhagia, and prolonged bleeding after surgery or trauma.29 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti528 – 5281N → S in VWD2. 1 Publication
    VAR_005783
    Natural varianti550 – 5501G → R in VWD2. 1 Publication
    VAR_005784
    Natural varianti788 – 7881C → Y in VWD2.
    VAR_009141
    Natural varianti791 – 7911T → M in VWD2; Normandy type. 1 Publication
    VAR_005786
    Natural varianti816 – 8161R → W in VWD2; Normandy type. 1 Publication
    VAR_005787
    Natural varianti854 – 8541R → Q in VWD2; Normandy type. 1 Publication
    Corresponds to variant rs41276738 [ dbSNP | Ensembl ].
    VAR_005789
    Natural varianti1060 – 10601C → R in VWD2. 1 Publication
    VAR_028446
    Natural varianti1266 – 12661P → L in VWD2. 1 Publication
    VAR_005791
    Natural varianti1268 – 12681H → D in VWD2. 1 Publication
    VAR_005792
    Natural varianti1272 – 12721C → F in VWD2; subtype 2A. 1 Publication
    VAR_067340
    Natural varianti1272 – 12721C → R in VWD2. 1 Publication
    VAR_005793
    Natural varianti1306 – 13061R → W in VWD2. 4 Publications
    VAR_005794
    Natural varianti1308 – 13081R → C in VWD2. 4 Publications
    VAR_005795
    Natural varianti1313 – 13131W → C in VWD2. 1 Publication
    VAR_005796
    Natural varianti1314 – 13141V → L in VWD2. 1 Publication
    VAR_005797
    Natural varianti1316 – 13161V → M in VWD2. 3 Publications
    VAR_005798
    Natural varianti1318 – 13181V → L in VWD2. 1 Publication
    VAR_005799
    Natural varianti1324 – 13241G → S in VWD2. 1 Publication
    VAR_005800
    Natural varianti1341 – 13411R → Q in VWD2. 1 Publication
    VAR_005801
    Natural varianti1374 – 13741R → C in VWD2. 1 Publication
    VAR_005802
    Natural varianti1374 – 13741R → H in VWD2. 2 Publications
    VAR_005803
    Natural varianti1460 – 14601L → V in VWD2. 1 Publication
    VAR_005806
    Natural varianti1461 – 14611A → V in VWD2. 1 Publication
    VAR_005807
    Natural varianti1514 – 15141F → C in VWD2. 1 Publication
    VAR_005808
    Natural varianti1540 – 15401L → P in VWD2. 1 Publication
    VAR_005809
    Natural varianti1597 – 15971R → G in VWD2. 1 Publication
    VAR_005811
    Natural varianti1597 – 15971R → Q in VWD2. 1 Publication
    VAR_005812
    Natural varianti1597 – 15971R → W in VWD2. 1 Publication
    VAR_005813
    Natural varianti1607 – 16071V → D in VWD2. 1 Publication
    VAR_005814
    Natural varianti1609 – 16091G → R in VWD2. 2 Publications
    VAR_005815
    Natural varianti1613 – 16131S → P in VWD2. 1 Publication
    VAR_005816
    Natural varianti1628 – 16281I → T in VWD2. 3 Publications
    VAR_005817
    Natural varianti1638 – 16381E → K in VWD2. 1 Publication
    VAR_005818
    Natural varianti1648 – 16481P → S in VWD2. 1 Publication
    VAR_005819
    Natural varianti1665 – 16651V → E in VWD2. 1 Publication
    VAR_005820
    Natural varianti2773 – 27731C → R in VWD2. 1 Publication
    VAR_005822
    von Willebrand disease 3 (VWD3) [MIM:277480]: A severe hemorrhagic disorder due to a total or near total absence of von Willebrand factor in the plasma and cellular compartments, also leading to a profound deficiency of plasmatic factor VIII. Bleeding usually starts in infancy and can include epistaxis, recurrent mucocutaneous bleeding, excessive bleeding after minor trauma, and hemarthroses.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti273 – 2731R → W in VWD1 and VWD3; defect in secretion and formation of multimers. 1 Publication
    Corresponds to variant rs61753997 [ dbSNP | Ensembl ].
    VAR_010242
    Natural varianti377 – 3771W → C in VWD3. 1 Publication
    VAR_005782
    Natural varianti2063 – 20631P → S in VWD3.
    Corresponds to variant rs61750615 [ dbSNP | Ensembl ].
    VAR_009142
    Natural varianti2362 – 23621C → F in VWD3.
    VAR_009143
    Natural varianti2546 – 25461N → Y in VWD3.
    VAR_009144
    Natural varianti2739 – 27391C → Y in VWD3. 1 Publication
    VAR_005821

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1149 – 11491C → R: Reduced secretion and increased intracellular retention. Similar phenotype; when associated with S-1169. 1 Publication
    Mutagenesisi1169 – 11691C → S: Reduced secretion and increased intracellular retention. Similar phenotype; when associated with R-1149. 1 Publication

    Keywords - Diseasei

    Disease mutation, von Willebrand disease

    Organism-specific databases

    MIMi193400. phenotype.
    277480. phenotype.
    613554. phenotype.
    Orphaneti166078. Von Willebrand disease type 1.
    166084. Von Willebrand disease type 2A.
    166087. Von Willebrand disease type 2B.
    166090. Von Willebrand disease type 2M.
    166093. Von Willebrand disease type 2N.
    166096. Von Willebrand disease type 3.
    PharmGKBiPA37337.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 22221 PublicationAdd
    BLAST
    Chaini23 – 763741von Willebrand antigen 2PRO_0000022682Add
    BLAST
    Chaini764 – 28132050von Willebrand factorPRO_0000022683Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi? ↔ 2811By similarity
    Glycosylationi99 – 991N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi156 – 1561N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi211 – 2111N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi666 – 6661N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi767 ↔ 8081 Publication
    Disulfide bondi776 ↔ 8041 Publication
    Disulfide bondi810 ↔ 8211 Publication
    Glycosylationi857 – 8571N-linked (GlcNAc...)
    Disulfide bondi867 ↔ 9961 Publication
    Disulfide bondi889 ↔ 10311 Publication
    Disulfide bondi898 ↔ 9931 Publication
    Disulfide bondi914 ↔ 9211 Publication
    Disulfide bondi1060 ↔ 10841 Publication
    Disulfide bondi1071 ↔ 11111 Publication
    Disulfide bondi1089 ↔ 10911 Publication
    Disulfide bondi1126 ↔ 11301 Publication
    Glycosylationi1147 – 11471N-linked (GlcNAc...); atypical
    Disulfide bondi1149 ↔ 11691 Publication
    Disulfide bondi1153 ↔ 11651 Publication
    Disulfide bondi1196 ↔ 11991 Publication
    Glycosylationi1231 – 12311N-linked (GlcNAc...)
    Disulfide bondi1234 ↔ 12371 Publication
    Glycosylationi1248 – 12481O-linked (GalNAc...)Curated
    Glycosylationi1255 – 12551O-linked (GalNAc...)Curated
    Glycosylationi1256 – 12561O-linked (GalNAc...)Curated
    Glycosylationi1263 – 12631O-linked (GalNAc...)1 Publication
    Disulfide bondi1272 ↔ 14581 Publication
    Glycosylationi1468 – 14681O-linked (GalNAc...)Curated
    Glycosylationi1477 – 14771O-linked (GalNAc...)Curated
    Glycosylationi1486 – 14861O-linked (GalNAc...)Curated
    Glycosylationi1487 – 14871O-linked (GalNAc...)Curated
    Glycosylationi1515 – 15151N-linked (GlcNAc...) (complex)2 Publications
    Glycosylationi1574 – 15741N-linked (GlcNAc...)
    Disulfide bondi1669 ↔ 16701 Publication
    Glycosylationi1679 – 16791O-linked (GalNAc...)Curated
    Disulfide bondi1686 ↔ 18721 Publication
    Cross-linki1720 – 1720Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Disulfide bondi1879 ↔ 19041 Publication
    Disulfide bondi1899 ↔ 1940Or C-1899 with C-19421 PublicationPROSITE-ProRule annotation
    Disulfide bondi1927 ↔ 20881 Publication
    Disulfide bondi1950 ↔ 20851 Publication
    Disulfide bondi1972 ↔ 21231 Publication
    Disulfide bondi1993 ↔ 20011 Publication
    Glycosylationi2223 – 22231N-linked (GlcNAc...)
    Glycosylationi2290 – 22901N-linked (GlcNAc...)
    Glycosylationi2298 – 22981O-linked (GalNAc...)Curated
    Glycosylationi2357 – 23571N-linked (GlcNAc...)
    Glycosylationi2400 – 24001N-linked (GlcNAc...)
    Glycosylationi2546 – 25461N-linked (GlcNAc...)1 Publication
    Glycosylationi2585 – 25851N-linked (GlcNAc...)
    Disulfide bondi2724 ↔ 2774By similarity
    Disulfide bondi2739 ↔ 2788By similarity
    Disulfide bondi2750 ↔ 2804By similarity
    Disulfide bondi2754 ↔ 2806By similarity
    Glycosylationi2790 – 27901N-linked (GlcNAc...)

    Post-translational modificationi

    All cysteine residues are involved in intrachain or interchain disulfide bonds.
    N- and O-glycosylated.3 Publications

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Isopeptide bond, Ubl conjugation

    Proteomic databases

    PaxDbiP04275.
    PRIDEiP04275.

    PTM databases

    PhosphoSiteiP04275.
    UniCarbKBiP04275.

    Expressioni

    Tissue specificityi

    Plasma.

    Gene expression databases

    ArrayExpressiP04275.
    BgeeiP04275.
    CleanExiHS_VWF.
    GenevestigatoriP04275.

    Organism-specific databases

    HPAiCAB001694.
    HPA001815.
    HPA002082.

    Interactioni

    Subunit structurei

    Multimeric. Interacts with F8.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself15EBI-981819,EBI-981819
    ADAMTS13Q76LX85EBI-981819,EBI-981764
    GP1BAP073592EBI-981819,EBI-297082
    OPTNQ96CV92EBI-981819,EBI-748974

    Protein-protein interaction databases

    BioGridi113289. 15 interactions.
    DIPiDIP-29667N.
    IntActiP04275. 49 interactions.
    MINTiMINT-244925.
    STRINGi9606.ENSP00000261405.

    Structurei

    Secondary structure

    1
    2813
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi767 – 7693
    Beta strandi771 – 7744
    Turni781 – 7866
    Turni792 – 7943
    Beta strandi795 – 7973
    Beta strandi804 – 8096
    Beta strandi814 – 8174
    Beta strandi820 – 8234
    Helixi824 – 8263
    Beta strandi829 – 8335
    Beta strandi841 – 8444
    Beta strandi847 – 8526
    Beta strandi855 – 8584
    Beta strandi1267 – 12693
    Turni1270 – 12734
    Beta strandi1276 – 12838
    Beta strandi1285 – 12884
    Helixi1290 – 130516
    Turni1307 – 13104
    Beta strandi1313 – 132917
    Helixi1337 – 13459
    Helixi1357 – 136711
    Beta strandi1369 – 13713
    Beta strandi1377 – 13859
    Helixi1391 – 13933
    Helixi1394 – 13963
    Helixi1397 – 140610
    Beta strandi1409 – 14179
    Helixi1422 – 143110
    Helixi1433 – 14353
    Beta strandi1438 – 14425
    Helixi1443 – 14453
    Helixi1446 – 146015
    Beta strandi1498 – 15047
    Turni1507 – 15093
    Helixi1511 – 152717
    Beta strandi1534 – 155017
    Helixi1558 – 156710
    Helixi1578 – 158710
    Turni1588 – 15903
    Helixi1592 – 15943
    Helixi1595 – 15995
    Beta strandi1602 – 16087
    Beta strandi1623 – 16319
    Helixi1636 – 16438
    Beta strandi1649 – 16524
    Turni1654 – 16563
    Helixi1657 – 167014
    Beta strandi1690 – 16978
    Beta strandi1699 – 17024
    Helixi1704 – 172017
    Beta strandi1727 – 174317
    Beta strandi1745 – 17473
    Helixi1751 – 17599
    Helixi1770 – 178213
    Helixi1784 – 17863
    Beta strandi1792 – 18009
    Helixi1809 – 18179
    Beta strandi1820 – 183112
    Helixi1833 – 18397
    Helixi1841 – 18477
    Beta strandi1849 – 18535
    Helixi1856 – 18627
    Beta strandi1863 – 18653
    Helixi1866 – 18705
    Beta strandi2728 – 27325
    Beta strandi2739 – 27435
    Beta strandi2745 – 27495
    Beta strandi2756 – 27616
    Turni2762 – 27654
    Beta strandi2766 – 278722
    Beta strandi2793 – 28019
    Beta strandi2804 – 28096

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AO3X-ray2.20A/B1686-1872[»]
    1ATZX-ray1.80A/B1685-1873[»]
    1AUQX-ray2.30A1261-1468[»]
    1FE8X-ray2.03A/B/C1683-1874[»]
    1FNSX-ray2.00A1271-1465[»]
    1IJBX-ray1.80A1263-1464[»]
    1IJKX-ray2.60A1263-1464[»]
    1M10X-ray3.10A1261-1468[»]
    1OAKX-ray2.20A1271-1465[»]
    1SQ0X-ray2.60A1259-1471[»]
    1U0NX-ray2.95A1261-1468[»]
    1UEXX-ray2.85C1260-1468[»]
    2ADFX-ray1.90A1683-1874[»]
    2MHPNMR-A766-864[»]
    2MHQNMR-A766-864[»]
    3GXBX-ray1.90A/B1495-1671[»]
    3HXOX-ray2.40A1260-1468[»]
    3HXQX-ray2.69A1260-1468[»]
    3PPVX-ray1.90A1488-1674[»]
    3PPWX-ray1.90A1488-1674[»]
    3PPXX-ray1.91A1488-1674[»]
    3PPYX-ray2.00A1488-1674[»]
    3ZQKX-ray1.70A/B/C1478-1674[»]
    4C29X-ray2.20A/B1264-1471[»]
    4C2AX-ray2.08A1264-1471[»]
    4C2BX-ray2.80A/C/E/G1264-1471[»]
    4DMUX-ray2.80B/D/F/H/J/L1683-1874[»]
    4NT5X-ray3.28A2721-2813[»]
    ProteinModelPortaliP04275.
    SMRiP04275. Positions 1261-1468, 1495-1671, 1685-1873, 2721-2813.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04275.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini34 – 240207VWFD 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini295 – 34854TIL 1Add
    BLAST
    Domaini387 – 598212VWFD 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini652 – 70756TIL 2Add
    BLAST
    Domaini776 – 82752TIL 3Add
    BLAST
    Domaini866 – 1074209VWFD 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini1146 – 119651TIL 4Add
    BLAST
    Domaini1277 – 1453177VWFA 1; binding site for platelet glycoprotein IbPROSITE-ProRule annotationAdd
    BLAST
    Domaini1498 – 1665168VWFA 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1691 – 1871181VWFA 3; main binding site for collagens type I and IIIPROSITE-ProRule annotationAdd
    BLAST
    Domaini1949 – 2153205VWFD 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini2255 – 232874VWFC 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini2429 – 249567VWFC 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini2580 – 264566VWFC 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini2724 – 281289CTCKPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni764 – 78724Amino-terminalAdd
    BLAST
    Regioni788 – 83346E1Add
    BLAST
    Regioni826 – 85328CXAdd
    BLAST
    Regioni2216 – 226146E2Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi2507 – 25093Cell attachment site

    Domaini

    The von Willebrand antigen 2 is required for multimerization of vWF and for its targeting to storage granules.

    Sequence similaritiesi

    Contains 1 CTCK (C-terminal cystine knot-like) domain.PROSITE-ProRule annotation
    Contains 3 VWFA domains.PROSITE-ProRule annotation
    Contains 3 VWFC domains.PROSITE-ProRule annotation
    Contains 4 VWFD domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG12793.
    HOGENOMiHOG000169747.
    HOVERGENiHBG004380.
    InParanoidiP04275.
    KOiK03900.
    OMAiECCGRCL.
    OrthoDBiEOG73V6J9.
    PhylomeDBiP04275.
    TreeFamiTF300299.

    Family and domain databases

    Gene3Di3.40.50.410. 3 hits.
    InterProiIPR006207. Cys_knot_C.
    IPR002919. TIL_dom.
    IPR014853. Unchr_dom_Cys-rich.
    IPR012011. VWF.
    IPR002035. VWF_A.
    IPR001007. VWF_C.
    IPR001846. VWF_type-D.
    [Graphical view]
    PfamiPF08742. C8. 4 hits.
    PF01826. TIL. 5 hits.
    PF00092. VWA. 3 hits.
    PF00093. VWC. 2 hits.
    PF00094. VWD. 4 hits.
    [Graphical view]
    PIRSFiPIRSF002495. VWF. 1 hit.
    SMARTiSM00832. C8. 4 hits.
    SM00041. CT. 1 hit.
    SM00327. VWA. 3 hits.
    SM00214. VWC. 5 hits.
    SM00216. VWD. 4 hits.
    [Graphical view]
    SUPFAMiSSF53300. SSF53300. 3 hits.
    SSF57567. SSF57567. 5 hits.
    PROSITEiPS01185. CTCK_1. 1 hit.
    PS01225. CTCK_2. 1 hit.
    PS50234. VWFA. 3 hits.
    PS01208. VWFC_1. 3 hits.
    PS50184. VWFC_2. 3 hits.
    PS51233. VWFD. 4 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P04275-1) [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

    MIPARFAGVL LALALILPGT LCAEGTRGRS STARCSLFGS DFVNTFDGSM     50
    YSFAGYCSYL LAGGCQKRSF SIIGDFQNGK RVSLSVYLGE FFDIHLFVNG 100
    TVTQGDQRVS MPYASKGLYL ETEAGYYKLS GEAYGFVARI DGSGNFQVLL 150
    SDRYFNKTCG LCGNFNIFAE DDFMTQEGTL TSDPYDFANS WALSSGEQWC 200
    ERASPPSSSC NISSGEMQKG LWEQCQLLKS TSVFARCHPL VDPEPFVALC 250
    EKTLCECAGG LECACPALLE YARTCAQEGM VLYGWTDHSA CSPVCPAGME 300
    YRQCVSPCAR TCQSLHINEM CQERCVDGCS CPEGQLLDEG LCVESTECPC 350
    VHSGKRYPPG TSLSRDCNTC ICRNSQWICS NEECPGECLV TGQSHFKSFD 400
    NRYFTFSGIC QYLLARDCQD HSFSIVIETV QCADDRDAVC TRSVTVRLPG 450
    LHNSLVKLKH GAGVAMDGQD VQLPLLKGDL RIQHTVTASV RLSYGEDLQM 500
    DWDGRGRLLV KLSPVYAGKT CGLCGNYNGN QGDDFLTPSG LAEPRVEDFG 550
    NAWKLHGDCQ DLQKQHSDPC ALNPRMTRFS EEACAVLTSP TFEACHRAVS 600
    PLPYLRNCRY DVCSCSDGRE CLCGALASYA AACAGRGVRV AWREPGRCEL 650
    NCPKGQVYLQ CGTPCNLTCR SLSYPDEECN EACLEGCFCP PGLYMDERGD 700
    CVPKAQCPCY YDGEIFQPED IFSDHHTMCY CEDGFMHCTM SGVPGSLLPD 750
    AVLSSPLSHR SKRSLSCRPP MVKLVCPADN LRAEGLECTK TCQNYDLECM 800
    SMGCVSGCLC PPGMVRHENR CVALERCPCF HQGKEYAPGE TVKIGCNTCV 850
    CQDRKWNCTD HVCDATCSTI GMAHYLTFDG LKYLFPGECQ YVLVQDYCGS 900
    NPGTFRILVG NKGCSHPSVK CKKRVTILVE GGEIELFDGE VNVKRPMKDE 950
    THFEVVESGR YIILLLGKAL SVVWDRHLSI SVVLKQTYQE KVCGLCGNFD 1000
    GIQNNDLTSS NLQVEEDPVD FGNSWKVSSQ CADTRKVPLD SSPATCHNNI 1050
    MKQTMVDSSC RILTSDVFQD CNKLVDPEPY LDVCIYDTCS CESIGDCACF 1100
    CDTIAAYAHV CAQHGKVVTW RTATLCPQSC EERNLRENGY ECEWRYNSCA 1150
    PACQVTCQHP EPLACPVQCV EGCHAHCPPG KILDELLQTC VDPEDCPVCE 1200
    VAGRRFASGK KVTLNPSDPE HCQICHCDVV NLTCEACQEP GGLVVPPTDA 1250
    PVSPTTLYVE DISEPPLHDF YCSRLLDLVF LLDGSSRLSE AEFEVLKAFV 1300
    VDMMERLRIS QKWVRVAVVE YHDGSHAYIG LKDRKRPSEL RRIASQVKYA 1350
    GSQVASTSEV LKYTLFQIFS KIDRPEASRI TLLLMASQEP QRMSRNFVRY 1400
    VQGLKKKKVI VIPVGIGPHA NLKQIRLIEK QAPENKAFVL SSVDELEQQR 1450
    DEIVSYLCDL APEAPPPTLP PDMAQVTVGP GLLGVSTLGP KRNSMVLDVA 1500
    FVLEGSDKIG EADFNRSKEF MEEVIQRMDV GQDSIHVTVL QYSYMVTVEY 1550
    PFSEAQSKGD ILQRVREIRY QGGNRTNTGL ALRYLSDHSF LVSQGDREQA 1600
    PNLVYMVTGN PASDEIKRLP GDIQVVPIGV GPNANVQELE RIGWPNAPIL 1650
    IQDFETLPRE APDLVLQRCC SGEGLQIPTL SPAPDCSQPL DVILLLDGSS 1700
    SFPASYFDEM KSFAKAFISK ANIGPRLTQV SVLQYGSITT IDVPWNVVPE 1750
    KAHLLSLVDV MQREGGPSQI GDALGFAVRY LTSEMHGARP GASKAVVILV 1800
    TDVSVDSVDA AADAARSNRV TVFPIGIGDR YDAAQLRILA GPAGDSNVVK 1850
    LQRIEDLPTM VTLGNSFLHK LCSGFVRICM DEDGNEKRPG DVWTLPDQCH 1900
    TVTCQPDGQT LLKSHRVNCD RGLRPSCPNS QSPVKVEETC GCRWTCPCVC 1950
    TGSSTRHIVT FDGQNFKLTG SCSYVLFQNK EQDLEVILHN GACSPGARQG 2000
    CMKSIEVKHS ALSVELHSDM EVTVNGRLVS VPYVGGNMEV NVYGAIMHEV 2050
    RFNHLGHIFT FTPQNNEFQL QLSPKTFASK TYGLCGICDE NGANDFMLRD 2100
    GTVTTDWKTL VQEWTVQRPG QTCQPILEEQ CLVPDSSHCQ VLLLPLFAEC 2150
    HKVLAPATFY AICQQDSCHQ EQVCEVIASY AHLCRTNGVC VDWRTPDFCA 2200
    MSCPPSLVYN HCEHGCPRHC DGNVSSCGDH PSEGCFCPPD KVMLEGSCVP 2250
    EEACTQCIGE DGVQHQFLEA WVPDHQPCQI CTCLSGRKVN CTTQPCPTAK 2300
    APTCGLCEVA RLRQNADQCC PEYECVCDPV SCDLPPVPHC ERGLQPTLTN 2350
    PGECRPNFTC ACRKEECKRV SPPSCPPHRL PTLRKTQCCD EYECACNCVN 2400
    STVSCPLGYL ASTATNDCGC TTTTCLPDKV CVHRSTIYPV GQFWEEGCDV 2450
    CTCTDMEDAV MGLRVAQCSQ KPCEDSCRSG FTYVLHEGEC CGRCLPSACE 2500
    VVTGSPRGDS QSSWKSVGSQ WASPENPCLI NECVRVKEEV FIQQRNVSCP 2550
    QLEVPVCPSG FQLSCKTSAC CPSCRCERME ACMLNGTVIG PGKTVMIDVC 2600
    TTCRCMVQVG VISGFKLECR KTTCNPCPLG YKEENNTGEC CGRCLPTACT 2650
    IQLRGGQIMT LKRDETLQDG CDTHFCKVNE RGEYFWEKRV TGCPPFDEHK 2700
    CLAEGGKIMK IPGTCCDTCE EPECNDITAR LQYVKVGSCK SEVEVDIHYC 2750
    QGKCASKAMY SIDINDVQDQ CSCCSPTRTE PMQVALHCTN GSVVYHEVLN 2800
    AMECKCSPRK CSK 2813
    Length:2,813
    Mass (Da):309,265
    Last modified:January 11, 2011 - v4
    Checksum:iD5C1C78360917C29
    GO
    Isoform 2 (identifier: P04275-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-18: MIPARFAGVLLALALILP → MGAQDEEEGIQDLDGLLVFDKIVEVTLLNLPWYNEETEGQRGEMTAPKSPRAKIR
         220-314: GLWEQCQLLK...VSPCARTCQS → EEPECNDITA...KCSPRKCSKI
         315-2813: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:351
    Mass (Da):38,745
    Checksum:iA8236A7126BC6BB5
    GO

    Sequence cautioni

    The sequence AAB59512.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti770 – 7701P → H in AAB59512. (PubMed:2864688)Curated
    Sequence conflicti804 – 8041C → S AA sequence (PubMed:3524673)Curated
    Sequence conflicti804 – 8041C → S in AAB59512. (PubMed:2864688)Curated
    Sequence conflicti1914 – 19141S → T in CAA27972. (PubMed:3489923)Curated
    Sequence conflicti2168 – 21681C → S AA sequence (PubMed:3524673)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti273 – 2731R → W in VWD1 and VWD3; defect in secretion and formation of multimers. 1 Publication
    Corresponds to variant rs61753997 [ dbSNP | Ensembl ].
    VAR_010242
    Natural varianti318 – 3181N → K.
    Corresponds to variant rs1800387 [ dbSNP | Ensembl ].
    VAR_057023
    Natural varianti377 – 3771W → C in VWD3. 1 Publication
    VAR_005782
    Natural varianti471 – 4711V → I.1 Publication
    Corresponds to variant rs1800377 [ dbSNP | Ensembl ].
    VAR_060591
    Natural varianti484 – 4841H → R.1 Publication
    Corresponds to variant rs1800378 [ dbSNP | Ensembl ].
    VAR_024553
    Natural varianti528 – 5281N → S in VWD2. 1 Publication
    VAR_005783
    Natural varianti550 – 5501G → R in VWD2. 1 Publication
    VAR_005784
    Natural varianti740 – 7401M → I.
    Corresponds to variant rs16932374 [ dbSNP | Ensembl ].
    VAR_057024
    Natural varianti788 – 7881C → Y in VWD2.
    VAR_009141
    Natural varianti789 – 7891T → A.1 Publication
    Corresponds to variant rs1063856 [ dbSNP | Ensembl ].
    VAR_005785
    Natural varianti791 – 7911T → M in VWD2; Normandy type. 1 Publication
    VAR_005786
    Natural varianti816 – 8161R → W in VWD2; Normandy type. 1 Publication
    VAR_005787
    Natural varianti852 – 8521Q → R.6 Publications
    Corresponds to variant rs216321 [ dbSNP | Ensembl ].
    VAR_005788
    Natural varianti854 – 8541R → Q in VWD2; Normandy type. 1 Publication
    Corresponds to variant rs41276738 [ dbSNP | Ensembl ].
    VAR_005789
    Natural varianti857 – 8571N → D.
    VAR_005790
    Natural varianti885 – 8851F → S.
    Corresponds to variant rs11064002 [ dbSNP | Ensembl ].
    VAR_057025
    Natural varianti1060 – 10601C → R in VWD2. 1 Publication
    VAR_028446
    Natural varianti1149 – 11491C → R in VWD1; reduced secretion of homodimers and heterodimers with wild type VWD and increased degradation by the proteasome. 1 Publication
    VAR_064925
    Natural varianti1266 – 12661P → L in VWD2. 1 Publication
    VAR_005791
    Natural varianti1268 – 12681H → D in VWD2. 1 Publication
    VAR_005792
    Natural varianti1272 – 12721C → F in VWD2; subtype 2A. 1 Publication
    VAR_067340
    Natural varianti1272 – 12721C → R in VWD2. 1 Publication
    VAR_005793
    Natural varianti1306 – 13061R → W in VWD2. 4 Publications
    VAR_005794
    Natural varianti1308 – 13081R → C in VWD2. 4 Publications
    VAR_005795
    Natural varianti1313 – 13131W → C in VWD2. 1 Publication
    VAR_005796
    Natural varianti1314 – 13141V → L in VWD2. 1 Publication
    VAR_005797
    Natural varianti1316 – 13161V → M in VWD2. 3 Publications
    VAR_005798
    Natural varianti1318 – 13181V → L in VWD2. 1 Publication
    VAR_005799
    Natural varianti1324 – 13241G → S in VWD2. 1 Publication
    VAR_005800
    Natural varianti1341 – 13411R → Q in VWD2. 1 Publication
    VAR_005801
    Natural varianti1374 – 13741R → C in VWD2. 1 Publication
    VAR_005802
    Natural varianti1374 – 13741R → H in VWD2. 2 Publications
    VAR_005803
    Natural varianti1381 – 13811T → A.8 Publications
    Corresponds to variant rs216311 [ dbSNP | Ensembl ].
    VAR_005804
    Natural varianti1399 – 13991R → H.1 Publication
    Corresponds to variant rs216312 [ dbSNP | Ensembl ].
    VAR_005805
    Natural varianti1460 – 14601L → V in VWD2. 1 Publication
    VAR_005806
    Natural varianti1461 – 14611A → V in VWD2. 1 Publication
    VAR_005807
    Natural varianti1472 – 14721D → H.3 Publications
    Corresponds to variant rs1800383 [ dbSNP | Ensembl ].
    VAR_029656
    Natural varianti1514 – 15141F → C in VWD2. 1 Publication
    VAR_005808
    Natural varianti1540 – 15401L → P in VWD2. 1 Publication
    VAR_005809
    Natural varianti1565 – 15651V → L.
    Corresponds to variant rs1800385 [ dbSNP | Ensembl ].
    VAR_014630
    Natural varianti1570 – 15701Y → C in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036276
    Natural varianti1584 – 15841Y → C Exhibits increased in susceptibility to proteolysis by ADAMTS13. 2 Publications
    Corresponds to variant rs1800386 [ dbSNP | Ensembl ].
    VAR_005810
    Natural varianti1597 – 15971R → G in VWD2. 1 Publication
    VAR_005811
    Natural varianti1597 – 15971R → Q in VWD2. 1 Publication
    VAR_005812
    Natural varianti1597 – 15971R → W in VWD2. 1 Publication
    VAR_005813
    Natural varianti1607 – 16071V → D in VWD2. 1 Publication
    VAR_005814
    Natural varianti1609 – 16091G → R in VWD2. 2 Publications
    VAR_005815
    Natural varianti1613 – 16131S → P in VWD2. 1 Publication
    VAR_005816
    Natural varianti1628 – 16281I → T in VWD2. 3 Publications
    VAR_005817
    Natural varianti1638 – 16381E → K in VWD2. 1 Publication
    VAR_005818
    Natural varianti1648 – 16481P → S in VWD2. 1 Publication
    VAR_005819
    Natural varianti1665 – 16651V → E in VWD2. 1 Publication
    VAR_005820
    Natural varianti2063 – 20631P → S in VWD3.
    Corresponds to variant rs61750615 [ dbSNP | Ensembl ].
    VAR_009142
    Natural varianti2178 – 21781A → S.
    Corresponds to variant rs34230288 [ dbSNP | Ensembl ].
    VAR_057026
    Natural varianti2185 – 21851R → Q.
    Corresponds to variant rs2229446 [ dbSNP | Ensembl ].
    VAR_057027
    Natural varianti2362 – 23621C → F in VWD3.
    VAR_009143
    Natural varianti2546 – 25461N → Y in VWD3.
    VAR_009144
    Natural varianti2705 – 27051G → R.
    Corresponds to variant rs7962217 [ dbSNP | Ensembl ].
    VAR_057028
    Natural varianti2739 – 27391C → Y in VWD3. 1 Publication
    VAR_005821
    Natural varianti2773 – 27731C → R in VWD2. 1 Publication
    VAR_005822

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1818MIPAR…ALILP → MGAQDEEEGIQDLDGLLVFD KIVEVTLLNLPWYNEETEGQ RGEMTAPKSPRAKIR in isoform 2. 1 PublicationVSP_056527Add
    BLAST
    Alternative sequencei220 – 31495GLWEQ…RTCQS → EEPECNDITARLQYVKVGSC KSEVEVDIHYCQGKCASKAM YSIDINDVQDQCSCCSPTRT EPMQVALHCTNGSVVYHEVL NAMECKCSPRKCSKI in isoform 2. 1 PublicationVSP_056528Add
    BLAST
    Alternative sequencei315 – 28132499Missing in isoform 2. 1 PublicationVSP_056529Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04385 mRNA. Translation: CAA27972.1.
    M25865
    , M25828, M25829, M25830, M25831, M25832, M25833, M25834, M25835, M25836, M25837, M25838, M25839, M25840, M25841, M25842, M25843, M25844, M25845, M25846, M25847, M25848, M25849, M25850, M25851, M25852, M25853, M25854, M25855, M25856, M25857, M25858, M25859, M25860, M25861, M25862, M25863, M25864 Genomic DNA. Translation: AAB59458.1.
    AC005845 Genomic DNA. No translation available.
    AC005846 Genomic DNA. No translation available.
    AC005904 Genomic DNA. No translation available.
    CH471116 Genomic DNA. Translation: EAW88817.1.
    BC022258 mRNA. Translation: AAH22258.1.
    X04146 mRNA. Translation: CAA27765.1.
    X06828, X06829 Genomic DNA. Translation: CAA29985.1.
    M17588 mRNA. Translation: AAA65940.1.
    M10321 mRNA. Translation: AAB59512.1. Sequence problems.
    M60675 Genomic DNA. Translation: AAA61295.1.
    U81237 mRNA. Translation: AAB39987.1.
    K03028 mRNA. Translation: AAA61293.1.
    X02672 mRNA. Translation: CAA26503.1.
    M16946, M16945 Genomic DNA. Translation: AAA61294.1.
    CCDSiCCDS8539.1.
    PIRiA34480. VWHU.
    RefSeqiNP_000543.2. NM_000552.3.
    UniGeneiHs.440848.

    Genome annotation databases

    EnsembliENST00000261405; ENSP00000261405; ENSG00000110799.
    ENST00000572068; ENSP00000461318; ENSG00000110799.
    GeneIDi7450.
    KEGGihsa:7450.
    UCSCiuc001qnn.1. human.

    Polymorphism databases

    DMDMi317373549.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    vWF

    von Willebrand factor (vWF) mutation db

    Wikipedia

    Von Willebrand factor entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04385 mRNA. Translation: CAA27972.1 .
    M25865
    , M25828 , M25829 , M25830 , M25831 , M25832 , M25833 , M25834 , M25835 , M25836 , M25837 , M25838 , M25839 , M25840 , M25841 , M25842 , M25843 , M25844 , M25845 , M25846 , M25847 , M25848 , M25849 , M25850 , M25851 , M25852 , M25853 , M25854 , M25855 , M25856 , M25857 , M25858 , M25859 , M25860 , M25861 , M25862 , M25863 , M25864 Genomic DNA. Translation: AAB59458.1 .
    AC005845 Genomic DNA. No translation available.
    AC005846 Genomic DNA. No translation available.
    AC005904 Genomic DNA. No translation available.
    CH471116 Genomic DNA. Translation: EAW88817.1 .
    BC022258 mRNA. Translation: AAH22258.1 .
    X04146 mRNA. Translation: CAA27765.1 .
    X06828 , X06829 Genomic DNA. Translation: CAA29985.1 .
    M17588 mRNA. Translation: AAA65940.1 .
    M10321 mRNA. Translation: AAB59512.1 . Sequence problems.
    M60675 Genomic DNA. Translation: AAA61295.1 .
    U81237 mRNA. Translation: AAB39987.1 .
    K03028 mRNA. Translation: AAA61293.1 .
    X02672 mRNA. Translation: CAA26503.1 .
    M16946 , M16945 Genomic DNA. Translation: AAA61294.1 .
    CCDSi CCDS8539.1.
    PIRi A34480. VWHU.
    RefSeqi NP_000543.2. NM_000552.3.
    UniGenei Hs.440848.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AO3 X-ray 2.20 A/B 1686-1872 [» ]
    1ATZ X-ray 1.80 A/B 1685-1873 [» ]
    1AUQ X-ray 2.30 A 1261-1468 [» ]
    1FE8 X-ray 2.03 A/B/C 1683-1874 [» ]
    1FNS X-ray 2.00 A 1271-1465 [» ]
    1IJB X-ray 1.80 A 1263-1464 [» ]
    1IJK X-ray 2.60 A 1263-1464 [» ]
    1M10 X-ray 3.10 A 1261-1468 [» ]
    1OAK X-ray 2.20 A 1271-1465 [» ]
    1SQ0 X-ray 2.60 A 1259-1471 [» ]
    1U0N X-ray 2.95 A 1261-1468 [» ]
    1UEX X-ray 2.85 C 1260-1468 [» ]
    2ADF X-ray 1.90 A 1683-1874 [» ]
    2MHP NMR - A 766-864 [» ]
    2MHQ NMR - A 766-864 [» ]
    3GXB X-ray 1.90 A/B 1495-1671 [» ]
    3HXO X-ray 2.40 A 1260-1468 [» ]
    3HXQ X-ray 2.69 A 1260-1468 [» ]
    3PPV X-ray 1.90 A 1488-1674 [» ]
    3PPW X-ray 1.90 A 1488-1674 [» ]
    3PPX X-ray 1.91 A 1488-1674 [» ]
    3PPY X-ray 2.00 A 1488-1674 [» ]
    3ZQK X-ray 1.70 A/B/C 1478-1674 [» ]
    4C29 X-ray 2.20 A/B 1264-1471 [» ]
    4C2A X-ray 2.08 A 1264-1471 [» ]
    4C2B X-ray 2.80 A/C/E/G 1264-1471 [» ]
    4DMU X-ray 2.80 B/D/F/H/J/L 1683-1874 [» ]
    4NT5 X-ray 3.28 A 2721-2813 [» ]
    ProteinModelPortali P04275.
    SMRi P04275. Positions 1261-1468, 1495-1671, 1685-1873, 2721-2813.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113289. 15 interactions.
    DIPi DIP-29667N.
    IntActi P04275. 49 interactions.
    MINTi MINT-244925.
    STRINGi 9606.ENSP00000261405.

    Chemistry

    ChEMBLi CHEMBL2021748.
    DrugBanki DB00025. Antihemophilic Factor.

    Protein family/group databases

    MEROPSi I08.950.

    PTM databases

    PhosphoSitei P04275.
    UniCarbKBi P04275.

    Polymorphism databases

    DMDMi 317373549.

    Proteomic databases

    PaxDbi P04275.
    PRIDEi P04275.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261405 ; ENSP00000261405 ; ENSG00000110799 .
    ENST00000572068 ; ENSP00000461318 ; ENSG00000110799 .
    GeneIDi 7450.
    KEGGi hsa:7450.
    UCSCi uc001qnn.1. human.

    Organism-specific databases

    CTDi 7450.
    GeneCardsi GC12M006058.
    GeneReviewsi VWF.
    H-InvDB HIX0010356.
    HIX0171640.
    HGNCi HGNC:12726. VWF.
    HPAi CAB001694.
    HPA001815.
    HPA002082.
    MIMi 193400. phenotype.
    277480. phenotype.
    613160. gene.
    613554. phenotype.
    neXtProti NX_P04275.
    Orphaneti 166078. Von Willebrand disease type 1.
    166084. Von Willebrand disease type 2A.
    166087. Von Willebrand disease type 2B.
    166090. Von Willebrand disease type 2M.
    166093. Von Willebrand disease type 2N.
    166096. Von Willebrand disease type 3.
    PharmGKBi PA37337.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOGENOMi HOG000169747.
    HOVERGENi HBG004380.
    InParanoidi P04275.
    KOi K03900.
    OMAi ECCGRCL.
    OrthoDBi EOG73V6J9.
    PhylomeDBi P04275.
    TreeFami TF300299.

    Enzyme and pathway databases

    Reactomei REACT_1230. Platelet Adhesion to exposed collagen.
    REACT_13552. Integrin cell surface interactions.
    REACT_15381. p130Cas linkage to MAPK signaling for integrins.
    REACT_15523. Integrin alphaIIb beta3 signaling.
    REACT_23847. GP1b-IX-V activation signalling.
    REACT_326. Intrinsic Pathway.

    Miscellaneous databases

    ChiTaRSi VWF. human.
    EvolutionaryTracei P04275.
    GeneWikii Von_Willebrand_factor.
    GenomeRNAii 7450.
    NextBioi 29172.
    PROi P04275.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P04275.
    Bgeei P04275.
    CleanExi HS_VWF.
    Genevestigatori P04275.

    Family and domain databases

    Gene3Di 3.40.50.410. 3 hits.
    InterProi IPR006207. Cys_knot_C.
    IPR002919. TIL_dom.
    IPR014853. Unchr_dom_Cys-rich.
    IPR012011. VWF.
    IPR002035. VWF_A.
    IPR001007. VWF_C.
    IPR001846. VWF_type-D.
    [Graphical view ]
    Pfami PF08742. C8. 4 hits.
    PF01826. TIL. 5 hits.
    PF00092. VWA. 3 hits.
    PF00093. VWC. 2 hits.
    PF00094. VWD. 4 hits.
    [Graphical view ]
    PIRSFi PIRSF002495. VWF. 1 hit.
    SMARTi SM00832. C8. 4 hits.
    SM00041. CT. 1 hit.
    SM00327. VWA. 3 hits.
    SM00214. VWC. 5 hits.
    SM00216. VWD. 4 hits.
    [Graphical view ]
    SUPFAMi SSF53300. SSF53300. 3 hits.
    SSF57567. SSF57567. 5 hits.
    PROSITEi PS01185. CTCK_1. 1 hit.
    PS01225. CTCK_2. 1 hit.
    PS50234. VWFA. 3 hits.
    PS01208. VWFC_1. 3 hits.
    PS50184. VWFC_2. 3 hits.
    PS51233. VWFD. 4 hits.
    [Graphical view ]
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    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ARG-852; ALA-1381 AND HIS-1472.
    2. "Structure of the gene for human von Willebrand factor."
      Mancuso D.J., Tuley E.A., Westfield L.A., Worrall N.K., Shelton-Inloes B.B., Sorace J.M., Alevy Y.G., Sadler J.E.
      J. Biol. Chem. 264:19514-19527(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ILE-471; ARG-852; ALA-1381 AND HIS-1472.
    3. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Lung.
    6. "Full-length von Willebrand factor (vWF) cDNA encodes a highly repetitive protein considerably larger than the mature vWF subunit."
      Verweij C.L., Diergaarde P.J., Hart M., Pannekoek H.
      EMBO J. 5:1839-1847(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1400 (ISOFORM 1), VARIANTS ARG-484; ARG-852 AND ALA-1381.
    7. Erratum
      Verweij C.L., Diergaarde P.J., Hart M., Pannekoek H.
      EMBO J. 5:3074-3074(1986)
    8. "The human von Willebrand factor gene. Structure of the 5' region."
      Bonthron D., Orkin S.H.
      Eur. J. Biochem. 171:51-57(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-178.
    9. "Evolution of human von Willebrand factor: cDNA sequence polymorphisms, repeated domains, and relationship to von Willebrand antigen II."
      Shelton-Inloes B.B., Broze G.J. Jr., Miletich J.P., Sadler J.E.
      Biochem. Biophys. Res. Commun. 144:657-665(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-120 (ISOFORM 1), PROTEIN SEQUENCE OF 23-56.
      Tissue: Umbilical vein endothelial cell.
    10. Cited for: PROTEIN SEQUENCE OF 764-2813, VARIANTS ARG-852 AND ALA-1381.
    11. "Cloning and characterization of two cDNAs coding for human von Willebrand factor."
      Sadler J.E., Shelton-Inloes B.B., Sorace J.M., Harlan J.M., Titani K., Davie E.W.
      Proc. Natl. Acad. Sci. U.S.A. 82:6394-6398(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 744-873 AND 1289-2813 (ISOFORM 1), VARIANTS ALA-789; ARG-852 AND ALA-1381.
    12. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 764-782.
      Tissue: Platelet.
    13. "cDNA sequences for human von Willebrand factor reveal five types of repeated domains and five possible protein sequence polymorphisms."
      Shelton-Inloes B.B., Titani K., Sadler J.E.
      Biochemistry 25:3164-3171(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 781-1424 (ISOFORM 1), VARIANTS ARG-852 AND ALA-1381.
    14. "Human von Willebrand factor gene and pseudogene: structural analysis and differentiation by polymerase chain reaction."
      Mancuso D.J., Tuley E.A., Westfield L.A., Lester-Mancuso T.L., Le Beau M.M., Sorace J.M., Sadler J.E.
      Biochemistry 30:253-269(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 990-1947, VARIANTS ALA-1381 AND HIS-1472.
    15. "Activation of human platelets by the membrane-expressed A1 domain of von Willebrand factor."
      Schulte am Esch J. II, Cruz M.A., Siegel J.B., Anrather J., Robson S.C.
      Blood 90:4425-4437(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1236-1476 (ISOFORM 1), VARIANT ALA-1381.
    16. "Human von Willebrand factor (vWF): isolation of complementary DNA (cDNA) clones and chromosomal localization."
      Ginsburg D., Handin R.I., Bonthron D.T., Donlon T.A., Bruns G.A.P., Latt S.A., Orkin S.H.
      Science 228:1401-1406(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2621-2813 (ISOFORM 1).
    17. "Molecular cloning of cDNA for human von Willebrand factor: authentication by a new method."
      Lynch D.C., Zimmerman T.S., Collins C.J., Brown M., Morin M.J., Ling E.H., Livingston D.M.
      Cell 41:49-56(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2731-2813 (ISOFORM 1).
    18. Lynch D.C.
      Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    19. "Construction of cDNA coding for human von Willebrand factor using antibody probes for colony-screening and mapping of the chromosomal gene."
      Verweij C.L., de Vries C.J.M., Distel B., van Zonneveld A.-J., Geurts van Kessel A., van Mourik J.A., Pannekoek H.
      Nucleic Acids Res. 13:4699-4717(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2731-2813 (ISOFORM 1).
    20. "Molecular cloning of the human gene for von Willebrand factor and identification of the transcription initiation site."
      Collins C.J., Underdahl J.P., Levene R.B., Ravera C.P., Morin M.J., Dombalagian M.J., Ricca G., Livingston D.M., Lynch D.C.
      Proc. Natl. Acad. Sci. U.S.A. 84:4393-4397(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2731-2813.
    21. "von Willebrand factor storage and multimerization: 2 independent intracellular processes."
      Haberichter S.L., Fahs S.A., Montgomery R.R.
      Blood 96:1808-1815(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, SUBCELLULAR LOCATION.
    22. "Identification of disulfide-bridged substructures within human von Willebrand factor."
      Marti T., Rosselet S.J., Titani K., Walsh K.A.
      Biochemistry 26:8099-8109(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BONDS.
    23. "Primary structure of a new tetraantennary glycan of the N-acetyllactosaminic type isolated from human factor VIII/von Willebrand factor."
      Samor B., Michalski J.C., Debray H., Mazurier C., Goudemand M., van Halbeek H., Vliegenthart J.F.G., Montreuil J.
      Eur. J. Biochem. 158:295-298(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE OF CARBOHYDRATES.
    24. "The acidic region of the factor VIII light chain and the C2 domain together form the high affinity binding site for von Willebrand factor."
      Saenko E.L., Scandella D.
      J. Biol. Chem. 272:18007-18014(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH F8.
    25. "Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
      Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
      Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1515.
      Tissue: Plasma.
    26. "Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
      Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
      Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-1720.
      Tissue: Mammary cancer.
    27. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2546.
      Tissue: Liver.
    28. Cited for: GLYCOSYLATION AT ASN-1515.
    29. "Crystal structure of the von Willebrand factor A1 domain and implications for the binding of platelet glycoprotein Ib."
      Emsley J., Cruz M., Handin R., Liddington R.
      J. Biol. Chem. 273:10396-10401(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1261-1468.
    30. "Crystal structure of the A3 domain of human von Willebrand factor: implications for collagen binding."
      Huizinga E.G., Martijn van der Plas R., Kroon J., Sixma J.J., Gros P.
      Structure 5:1147-1156(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1685-1873.
    31. "The von Willebrand factor A3 domain does not contain a metal ion-dependent adhesion site motif."
      Bienkowska J., Cruz M., Atiemo A., Handin R., Liddington R.
      J. Biol. Chem. 272:25162-25167(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1686-1872.
    32. "von Willebrand factor, platelets and endothelial cell interactions."
      Ruggeri Z.M.
      J. Thromb. Haemost. 1:1335-1342(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    33. "Molecular basis of human von Willebrand disease: analysis of platelet von Willebrand factor mRNA."
      Ginsburg D., Konkle B.A., Gill J.C., Montgomery R.R., Bockenstedt P.L., Johnson T.A., Yang A.Y.
      Proc. Natl. Acad. Sci. U.S.A. 86:3723-3727(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS VWD2 TRP-1597 AND ASP-1607.
    34. "Analysis of the relationship of von Willebrand disease (vWD) and hereditary hemorrhagic telangiectasia and identification of a potential type IIA vWD mutation (IIe865 to Thr)."
      Iannuzzi M.C., Hidaka N., Boehnke M., Bruck M.E., Hanna W.T., Collins F.S., Ginsburg D.
      Am. J. Hum. Genet. 48:757-763(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VWD2 THR-1628.
    35. "Identification of two point mutations in the von Willebrand factor gene of three families with the 'Normandy' variant of von Willebrand disease."
      Gaucher C., Mercier B., Jorieux S., Oufkir D., Mazurier C.
      Br. J. Haematol. 78:506-514(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS VWD2 TRP-816 AND GLN-854.
    36. "An Arg545-->Cys545 substitution mutation of the von Willebrand factor in type IIB von Willebrand's disease."
      Donner M., Andersson A.-M., Kristoffersson A.-C., Nilsson I.M., Dahlback B., Holmberg L.
      Eur. J. Haematol. 47:342-345(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VWD2 CYS-1308.
    37. "Molecular basis of von Willebrand disease type IIB. Candidate mutations cluster in one disulfide loop between proposed platelet glycoprotein Ib binding sequences."
      Randi A.M., Rabinowitz I., Mancuso D.J., Mannucci P.M., Sadler J.E.
      J. Clin. Invest. 87:1220-1226(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS VWD2 TRP-1306; CYS-1308 AND PRO-1613.
    38. "The molecular defect in type IIB von Willebrand disease. Identification of four potential missense mutations within the putative GpIb binding domain."
      Cooney K.A., Nichols W.C., Bruck M.E., Bahou W.F., Shapiro A.D., Bowie E.J.W., Gralnick H.R., Ginsburg D.
      J. Clin. Invest. 87:1227-1233(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS VWD2 TRP-1306; CYS-1308; MET-1316 AND GLN-1341, VARIANT HIS-1399.
    39. "Identification of a point mutation in type IIB von Willebrand disease illustrating the regulation of von Willebrand factor affinity for the platelet membrane glycoprotein Ib-IX receptor."
      Ware J., Dent J.A., Azuma H., Sugimoto M., Kyrle P.A., Yoshioka A., Ruggeri Z.M.
      Proc. Natl. Acad. Sci. U.S.A. 88:2946-2950(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VWD2 CYS-1313.
    40. "Expression of von Willebrand factor 'Normandy': an autosomal mutation that mimics hemophilia A."
      Tuley E.A., Gaucher C., Jorieux S., Worrall N.K., Sadler J.E., Mazurier C.
      Proc. Natl. Acad. Sci. U.S.A. 88:6377-6381(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VWD2 MET-791.
    41. "Germ-line mosaicism for a valine-to-methionine substitution at residue 553 in the glycoprotein Ib-binding domain of von Willebrand factor, causing type IIB von Willebrand disease."
      Murray E.W., Giles A.R., Lillicrap D.
      Am. J. Hum. Genet. 50:199-207(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VWD2 MET-1316.
    42. "Molecular study of von Willebrand disease: identification of potential mutations in patients with type IIA and type IIB."
      Pietu G., Ribba A.S., de Paillette L., Cherel G., Lavergne J.-M., Bahnak B.R., Meyer D.
      Blood Coagul. Fibrinolysis 3:415-421(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS VWD2 TRP-1306; MET-1316; THR-1628 AND SER-1648.
    43. "Type IIB von Willebrand's disease: gene mutations and clinical presentation in nine families from Denmark, Germany and Sweden."
      Donner M., Kristoffersson A.-C., Lenk H., Scheibel E., Dahlback B., Nilsson I.M., Holmberg L.
      Br. J. Haematol. 82:58-65(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS VWD2 TRP-1306; CYS-1308; LEU-1314 AND LEU-1318.
    44. "Defects in type IIA von Willebrand disease: a cysteine 509 to arginine substitution in the mature von Willebrand factor disrupts a disulphide loop involved in the interaction with platelet glycoprotein Ib-IX."
      Lavergne J.-M., de Paillette L., Bahnak B.R., Ribba A.-S., Fressinaud E., Meyer D., Pietu G.
      Br. J. Haematol. 82:66-72(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VWD2 ARG-1272.
    45. "Characterization of recombinant von Willebrand factor corresponding to mutations in type IIA and type IIB von Willebrand disease."
      Ribba A.S., Voorberg J., Meyer D., Pannekoek H., Pietu G.
      J. Biol. Chem. 267:23209-23215(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VWD2 LYS-1638.
    46. "von Willebrand disease type B: a missense mutation selectively abolishes ristocetin-induced von Willebrand factor binding to platelet glycoprotein Ib."
      Rabinowitz I., Tuley E.A., Mancuso D.J., Randi A.M., Firkin B.G., Howard M.A., Sadler J.E.
      Proc. Natl. Acad. Sci. U.S.A. 89:9846-9849(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VWD2 SER-1324.
    47. "Identification of three candidate mutations causing type IIA von Willebrand disease using a rapid, nonradioactive, allele-specific hybridization method."
      Inbal A., Englender T., Kornbrot N., Randi A.M., Castaman G., Mannucci P.M., Sadler J.E.
      Blood 82:830-836(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS VWD2 GLN-1597; ARG-1609 AND GLU-1665.
    48. "Substitution of cysteine for phenylalanine 751 in mature von Willebrand factor is a novel candidate mutation in a family with type IIA von Willebrand disease."
      Gaucher C., Hanss M., Dechavanne M., Mazurier C.
      Br. J. Haematol. 83:94-99(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VWD2 CYS-1514.
    49. "Two new candidate mutations in type IIA von Willebrand's disease (Arg834-->Gly, Gly846-->Arg) and one polymorphism (Tyr821-->Cys) in the A2 region of the von Willebrand factor."
      Donner M., Kristoffersson A.C., Berntorp E., Scheibel E., Thorsen S., Dahlback B., Nilsson I.M., Holmberg L.
      Eur. J. Haematol. 51:38-44(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS VWD2 GLY-1597 AND ARG-1609, VARIANT CYS-1584.
    50. "Type IIB mutation His-505-->Asp implicates a new segment in the control of von Willebrand factor binding to platelet glycoprotein Ib."
      Rabinowitz I., Randi A.M., Shindler K.S., Tuley E.A., Rustagi P.K., Sadler J.E.
      J. Biol. Chem. 268:20497-20501(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VWD2 ASP-1268.
    51. "von Willebrand factor mutation enhancing interaction with platelets in patients with normal multimeric structure."
      Holmberg L., Dent J.A., Schneppenheim R., Budde U., Ware J., Ruggeri Z.M.
      J. Clin. Invest. 91:2169-2177(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VWD2 LEU-1266.
    52. "Leu 697-->Val mutation in mature von Willebrand factor is responsible for type IIB von Willebrand disease."
      Hilbert L., Gaucher C., de Romeuf C., Horellou M.H., Vink T., Mazurier C.
      Blood 83:1542-1550(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VWD2 VAL-1460.
    53. "Characterization of Leu777Pro and Ile865Thr type IIA von Willebrand disease mutations."
      Lyons S.E., Cooney K.A., Bockenstedt P., Ginsburg D.
      Blood 83:1551-1557(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS VWD2 PRO-1540 AND THR-1628.
    54. "Characterization of the von Willebrand factor gene (VWF) in von Willebrand disease type III patients from 24 families of Swedish and Finnish origin."
      Zhang Z.P., Blombaeck M., Egberg N., Falk G., Anvret M.
      Genomics 21:188-193(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VWD3 TYR-2739.
    55. "Genetic heterogeneity of severe von Willebrand disease type III in the German population."
      Schneppenheim R., Krey S., Bergmann F., Bock D., Budde U., Lange M., Linde R., Mittler U., Meili E., Mertes G., Olek K., Plendl H., Simeoni E.
      Hum. Genet. 94:640-652(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VWD3 CYS-377.
    56. "Investigation of type IIC von Willebrand disease."
      Uno H., Nishida N., Ishizaki J., Suzuki M., Nishikubo T., Miyata S., Takahashi Y., Yoshioka A., Tsuda K.
      Int. J. Hematol. 59:219-225(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VWD2 SER-528.
    57. "Identification of two mutations (Arg611Cys and Arg611His) in the A1 loop of von Willebrand factor (vWF) responsible for type 2 von Willebrand disease with decreased platelet-dependent function of vWF."
      Hilbert L., Gaucher C., Mazurier C.
      Blood 86:1010-1018(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS VWD2 CYS-1374 AND HIS-1374.
    58. "A novel candidate mutation (Arg611-->His) in type I 'platelet discordant' von Willebrand's disease with desmopressin-induced thrombocytopenia."
      Castaman G., Eikenboom C.J.C., Rodeghiero F., Briet K., Reitsma P.H.
      Br. J. Haematol. 89:656-658(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VWD2 HIS-1374.
    59. "Effects of different amino-acid substitutions in the leucine 694-proline 708 segment of recombinant von Willebrand factor."
      Hilbert L., Gaucher C., Mazurier C.
      Br. J. Haematol. 91:983-990(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VWD2 VAL-1461.
    60. "Identification of a candidate missense mutation in a family with von Willebrand disease type IIC."
      Schneppenheim R., Thomas K.B., Krey S., Budde U., Jessat U., Sutor A.H., Zeiger B.
      Hum. Genet. 95:681-686(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VWD2 ARG-550.
    61. "Defective dimerization of von Willebrand factor subunits due to a Cys-> Arg mutation in type IID von Willebrand disease."
      Schneppenheim R., Brassard J., Krey S., Budde U., Kunicki T.J., Holmberg L., Ware J., Ruggeri Z.M.
      Proc. Natl. Acad. Sci. U.S.A. 93:3581-3586(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VWD2 ARG-2773.
    62. "A novel von Willebrand disease-causing mutation (Arg273Trp) in the von Willebrand factor propeptide that results in defective multimerization and secretion."
      Allen S., Abuzenadah A.M., Hinks J., Blagg J.L., Gursel T., Ingerslev J., Goodeve A.C., Peake I.R., Daly M.E.
      Blood 96:560-568(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VWD1 TRP-273, VARIANT VWD3 TRP-273.
    63. "Type 1 von Willebrand disease mutation Cys1149Arg causes intracellular retention and degradation of heterodimers: a possible general mechanism for dominant mutations of oligomeric proteins."
      Bodo I., Katsumi A., Tuley E.A., Eikenboom J.C., Dong Z., Sadler J.E.
      Blood 98:2973-2979(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VWD1 ARG-1149, MUTAGENESIS OF CYS-1149 AND CYS-1169.
    64. "Factor VIII deficiency not induced by FVIII gene mutation in a female first cousin of two brothers with haemophilia A."
      Mazurier C., Parquet-Gernez A., Gaucher C., Lavergne J.-M., Goudemand J.
      Br. J. Haematol. 119:390-392(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VWD2 ARG-1060.
    65. "The prevalence of the cysteine1584 variant of von Willebrand factor is increased in type 1 von Willebrand disease: co-segregation with increased susceptibility to ADAMTS13 proteolysis but not clinical phenotype."
      Bowen D.J., Collins P.W., Lester W., Cumming A.M., Keeney S., Grundy P., Enayat S.M., Bolton-Maggs P.H., Keeling D.M., Khair K., Tait R.C., Wilde J.T., Pasi K.J., Hill F.G.
      Br. J. Haematol. 128:830-836(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CYS-1584.
    66. Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-1570.
    67. "C1272F: a novel type 2A von Willebrand's disease mutation in A1 domain; its clinical significance."
      Woods A.I., Sanchez-Luceros A., Kempfer A.C., Powazniak Y., Calderazzo Pereyra J.C., Blanco A.N., Meschengieser S.S., Lazzari M.A.
      Haemophilia 18:112-116(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VWD2 PHE-1272.

    Entry informationi

    Entry nameiVWF_HUMAN
    AccessioniPrimary (citable) accession number: P04275
    Secondary accession number(s): Q8TCE8, Q99806
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 20, 1987
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 199 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3