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P04275

- VWF_HUMAN

UniProt

P04275 - VWF_HUMAN

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Protein

von Willebrand factor

Gene

VWF

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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 homodimerization activity Source: UniProtKB
  9. 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
Complete GO annotation...

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-KW
  9. Weibel-Palade body Source: UniProtKB
Complete GO annotation...

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

BgeeiP04275.
CleanExiHS_VWF.
ExpressionAtlasiP04275. baseline and differential.
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 766-864, 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.
GeneTreeiENSGT00760000118896.
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. 1 hit.
[Graphical view]
PIRSFiPIRSF002495. VWF. 1 hit.
SMARTiSM00832. C8. 4 hits.
SM00041. CT. 1 hit.
SM00327. VWA. 3 hits.
SM00214. VWC. 5 hits.
SM00216. VWD. 1 hit.
[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

        10         20         30         40         50
MIPARFAGVL LALALILPGT LCAEGTRGRS STARCSLFGS DFVNTFDGSM
60 70 80 90 100
YSFAGYCSYL LAGGCQKRSF SIIGDFQNGK RVSLSVYLGE FFDIHLFVNG
110 120 130 140 150
TVTQGDQRVS MPYASKGLYL ETEAGYYKLS GEAYGFVARI DGSGNFQVLL
160 170 180 190 200
SDRYFNKTCG LCGNFNIFAE DDFMTQEGTL TSDPYDFANS WALSSGEQWC
210 220 230 240 250
ERASPPSSSC NISSGEMQKG LWEQCQLLKS TSVFARCHPL VDPEPFVALC
260 270 280 290 300
EKTLCECAGG LECACPALLE YARTCAQEGM VLYGWTDHSA CSPVCPAGME
310 320 330 340 350
YRQCVSPCAR TCQSLHINEM CQERCVDGCS CPEGQLLDEG LCVESTECPC
360 370 380 390 400
VHSGKRYPPG TSLSRDCNTC ICRNSQWICS NEECPGECLV TGQSHFKSFD
410 420 430 440 450
NRYFTFSGIC QYLLARDCQD HSFSIVIETV QCADDRDAVC TRSVTVRLPG
460 470 480 490 500
LHNSLVKLKH GAGVAMDGQD VQLPLLKGDL RIQHTVTASV RLSYGEDLQM
510 520 530 540 550
DWDGRGRLLV KLSPVYAGKT CGLCGNYNGN QGDDFLTPSG LAEPRVEDFG
560 570 580 590 600
NAWKLHGDCQ DLQKQHSDPC ALNPRMTRFS EEACAVLTSP TFEACHRAVS
610 620 630 640 650
PLPYLRNCRY DVCSCSDGRE CLCGALASYA AACAGRGVRV AWREPGRCEL
660 670 680 690 700
NCPKGQVYLQ CGTPCNLTCR SLSYPDEECN EACLEGCFCP PGLYMDERGD
710 720 730 740 750
CVPKAQCPCY YDGEIFQPED IFSDHHTMCY CEDGFMHCTM SGVPGSLLPD
760 770 780 790 800
AVLSSPLSHR SKRSLSCRPP MVKLVCPADN LRAEGLECTK TCQNYDLECM
810 820 830 840 850
SMGCVSGCLC PPGMVRHENR CVALERCPCF HQGKEYAPGE TVKIGCNTCV
860 870 880 890 900
CQDRKWNCTD HVCDATCSTI GMAHYLTFDG LKYLFPGECQ YVLVQDYCGS
910 920 930 940 950
NPGTFRILVG NKGCSHPSVK CKKRVTILVE GGEIELFDGE VNVKRPMKDE
960 970 980 990 1000
THFEVVESGR YIILLLGKAL SVVWDRHLSI SVVLKQTYQE KVCGLCGNFD
1010 1020 1030 1040 1050
GIQNNDLTSS NLQVEEDPVD FGNSWKVSSQ CADTRKVPLD SSPATCHNNI
1060 1070 1080 1090 1100
MKQTMVDSSC RILTSDVFQD CNKLVDPEPY LDVCIYDTCS CESIGDCACF
1110 1120 1130 1140 1150
CDTIAAYAHV CAQHGKVVTW RTATLCPQSC EERNLRENGY ECEWRYNSCA
1160 1170 1180 1190 1200
PACQVTCQHP EPLACPVQCV EGCHAHCPPG KILDELLQTC VDPEDCPVCE
1210 1220 1230 1240 1250
VAGRRFASGK KVTLNPSDPE HCQICHCDVV NLTCEACQEP GGLVVPPTDA
1260 1270 1280 1290 1300
PVSPTTLYVE DISEPPLHDF YCSRLLDLVF LLDGSSRLSE AEFEVLKAFV
1310 1320 1330 1340 1350
VDMMERLRIS QKWVRVAVVE YHDGSHAYIG LKDRKRPSEL RRIASQVKYA
1360 1370 1380 1390 1400
GSQVASTSEV LKYTLFQIFS KIDRPEASRI TLLLMASQEP QRMSRNFVRY
1410 1420 1430 1440 1450
VQGLKKKKVI VIPVGIGPHA NLKQIRLIEK QAPENKAFVL SSVDELEQQR
1460 1470 1480 1490 1500
DEIVSYLCDL APEAPPPTLP PDMAQVTVGP GLLGVSTLGP KRNSMVLDVA
1510 1520 1530 1540 1550
FVLEGSDKIG EADFNRSKEF MEEVIQRMDV GQDSIHVTVL QYSYMVTVEY
1560 1570 1580 1590 1600
PFSEAQSKGD ILQRVREIRY QGGNRTNTGL ALRYLSDHSF LVSQGDREQA
1610 1620 1630 1640 1650
PNLVYMVTGN PASDEIKRLP GDIQVVPIGV GPNANVQELE RIGWPNAPIL
1660 1670 1680 1690 1700
IQDFETLPRE APDLVLQRCC SGEGLQIPTL SPAPDCSQPL DVILLLDGSS
1710 1720 1730 1740 1750
SFPASYFDEM KSFAKAFISK ANIGPRLTQV SVLQYGSITT IDVPWNVVPE
1760 1770 1780 1790 1800
KAHLLSLVDV MQREGGPSQI GDALGFAVRY LTSEMHGARP GASKAVVILV
1810 1820 1830 1840 1850
TDVSVDSVDA AADAARSNRV TVFPIGIGDR YDAAQLRILA GPAGDSNVVK
1860 1870 1880 1890 1900
LQRIEDLPTM VTLGNSFLHK LCSGFVRICM DEDGNEKRPG DVWTLPDQCH
1910 1920 1930 1940 1950
TVTCQPDGQT LLKSHRVNCD RGLRPSCPNS QSPVKVEETC GCRWTCPCVC
1960 1970 1980 1990 2000
TGSSTRHIVT FDGQNFKLTG SCSYVLFQNK EQDLEVILHN GACSPGARQG
2010 2020 2030 2040 2050
CMKSIEVKHS ALSVELHSDM EVTVNGRLVS VPYVGGNMEV NVYGAIMHEV
2060 2070 2080 2090 2100
RFNHLGHIFT FTPQNNEFQL QLSPKTFASK TYGLCGICDE NGANDFMLRD
2110 2120 2130 2140 2150
GTVTTDWKTL VQEWTVQRPG QTCQPILEEQ CLVPDSSHCQ VLLLPLFAEC
2160 2170 2180 2190 2200
HKVLAPATFY AICQQDSCHQ EQVCEVIASY AHLCRTNGVC VDWRTPDFCA
2210 2220 2230 2240 2250
MSCPPSLVYN HCEHGCPRHC DGNVSSCGDH PSEGCFCPPD KVMLEGSCVP
2260 2270 2280 2290 2300
EEACTQCIGE DGVQHQFLEA WVPDHQPCQI CTCLSGRKVN CTTQPCPTAK
2310 2320 2330 2340 2350
APTCGLCEVA RLRQNADQCC PEYECVCDPV SCDLPPVPHC ERGLQPTLTN
2360 2370 2380 2390 2400
PGECRPNFTC ACRKEECKRV SPPSCPPHRL PTLRKTQCCD EYECACNCVN
2410 2420 2430 2440 2450
STVSCPLGYL ASTATNDCGC TTTTCLPDKV CVHRSTIYPV GQFWEEGCDV
2460 2470 2480 2490 2500
CTCTDMEDAV MGLRVAQCSQ KPCEDSCRSG FTYVLHEGEC CGRCLPSACE
2510 2520 2530 2540 2550
VVTGSPRGDS QSSWKSVGSQ WASPENPCLI NECVRVKEEV FIQQRNVSCP
2560 2570 2580 2590 2600
QLEVPVCPSG FQLSCKTSAC CPSCRCERME ACMLNGTVIG PGKTVMIDVC
2610 2620 2630 2640 2650
TTCRCMVQVG VISGFKLECR KTTCNPCPLG YKEENNTGEC CGRCLPTACT
2660 2670 2680 2690 2700
IQLRGGQIMT LKRDETLQDG CDTHFCKVNE RGEYFWEKRV TGCPPFDEHK
2710 2720 2730 2740 2750
CLAEGGKIMK IPGTCCDTCE EPECNDITAR LQYVKVGSCK SEVEVDIHYC
2760 2770 2780 2790 2800
QGKCASKAMY SIDINDVQDQ CSCCSPTRTE PMQVALHCTN GSVVYHEVLN
2810
AMECKCSPRK CSK
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. [P04275-1]
PIRiA34480. VWHU.
RefSeqiNP_000543.2. NM_000552.3.
UniGeneiHs.440848.

Genome annotation databases

EnsembliENST00000261405; ENSP00000261405; ENSG00000110799. [P04275-1]
GeneIDi7450.
KEGGihsa:7450.
UCSCiuc001qnn.1. human. [P04275-1]

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. [P04275-1 ]
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 766-864, 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 . [P04275-1 ]
GeneIDi 7450.
KEGGi hsa:7450.
UCSCi uc001qnn.1. human. [P04275-1 ]

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.
GeneTreei ENSGT00760000118896.
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

Bgeei P04275.
CleanExi HS_VWF.
ExpressionAtlasi P04275. baseline and differential.
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. 1 hit.
[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. 1 hit.
[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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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 29, 2014
This is version 200 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