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VWF

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Summary

VWF (von Willebrand factor, HGNC:12726) is a protein-coding gene on chromosome 12p13.31, encoding von Willebrand factor (P04275). 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.

This gene encodes a glycoprotein involved in hemostasis. The encoded preproprotein is proteolytically processed following assembly into large multimeric complexes. These complexes function in the adhesion of platelets to sites of vascular injury and the transport of various proteins in the blood. Mutations in this gene result in von Willebrand disease, an inherited bleeding disorder. An unprocessed pseudogene has been found on chromosome 22.

Source: NCBI Gene 7450 — RefSeq curated summary.

At a glance

  • Gene–disease (curated): hereditary von Willebrand disease (Definitive, ClinGen) — +7 more curated relationships
  • GWAS associations: 34
  • Clinical variants (ClinVar): 2,115 total — 246 pathogenic, 201 likely-pathogenic
  • Phenotypes (HPO): 23
  • Druggable target: yes
  • MANE Select transcript: NM_000552

Identifiers

Gene identifiers

FieldValue
HGNC IDHGNC:12726
Approved symbolVWF
Namevon Willebrand factor
Location12p13.31
Locus typegene with protein product
StatusApproved
Ensembl geneENSG00000110799
Ensembl biotypeprotein_coding
OMIM613160
Entrez7450

Gene structure

Transcript identifiers

Ensembl transcripts: 11 — 4 protein_coding_CDS_not_defined, 3 protein_coding, 2 nonsense_mediated_decay, 2 retained_intron

ENST00000261405, ENST00000321023, ENST00000538563, ENST00000538635, ENST00000539641, ENST00000540192, ENST00000545906, ENST00000612016, ENST00000621700, ENST00000895679, ENST00000895680

RefSeq mRNA: 1 — MANE Select: NM_000552 NM_000552

CCDS: CCDS8539

Canonical transcript exons

ENST00000261405 — 52 exons

ExonStartEnd
ENSE0000086686459681275968167
ENSE0000086686759761115976260
ENSE0000086686959831505983254
ENSE0000086687359938625994203
ENSE0000086687459944155994607
ENSE0000093696760525436052783
ENSE0000093696860467236046817
ENSE0000093696960442916044451
ENSE0000093697060363886036491
ENSE0000093697160346886034826
ENSE0000093697260314446031578
ENSE0000093697360293426029488
ENSE0000093697460259066026046
ENSE0000093697660236316023787
ENSE0000093698360134816013645
ENSE0000118449661244216124670
ENSE0000126157959715995971709
ENSE0000126160359850455985119
ENSE0000126160959855635985665
ENSE0000126163659960025996222
ENSE0000128962459674865967602
ENSE0000129343759497865949883
ENSE0000130738759518445951883
ENSE0000130918559817865981991
ENSE0000131281959534965953594
ENSE0000131453559488775949203
ENSE0000131639459692115969391
ENSE0000132664159523915952519
ENSE0000132874559918195992018
ENSE0000160327160160896016232
ENSE0000162228660116176011794
ENSE0000164005160736196073741
ENSE0000164016360578496058044
ENSE0000164525360642466064384
ENSE0000164633760165166016656
ENSE0000165628060723316072442
ENSE0000167458460651376065273
ENSE0000167617160954606095584
ENSE0000167696360167546016870
ENSE0000167924860219006022035
ENSE0000167991560629546063054
ENSE0000168272060753356075551
ENSE0000170003960712976071343
ENSE0000172707460568576057072
ENSE0000173150460255806025693
ENSE0000174906860183656019743
ENSE0000176124160120876012130
ENSE0000179272260227406022898
ENSE0000350775061231426123196
ENSE0000357245061211746121338
ENSE0000358650161103746110582
ENSE0000368888461108666110968

Expression profiles

Bgee: expression breadth ubiquitous, 289 present calls, max score 99.38.

FANTOM5 (CAGE): breadth broad, TPM avg 19.7218 / max 1788.9565, expressed in 375 samples.

FANTOM5 promoters (7 alternative TSS)

Promoter IDTPM avgSamples expressed
1290528.4236290
1290485.4538339
1290502.8578277
1290511.7076254
1290490.9414236
1290530.2943145
1290470.043214

Top tissues by expression

305 total, by Bgee expression score (0-100, higher = more expressed):

TissueAnatomy IDExpression scoreQuality
urethraUBERON:000005799.38gold quality
tendon of biceps brachiiUBERON:000818899.20gold quality
apex of heartUBERON:000209899.11gold quality
right lungUBERON:000216799.09gold quality
omental fat padUBERON:001041499.01gold quality
adipose tissue of abdominal regionUBERON:000780898.99gold quality
peritoneumUBERON:000235898.98gold quality
upper lobe of left lungUBERON:000895298.88gold quality
upper lobe of lungUBERON:000894898.80gold quality
pericardiumUBERON:000240798.76gold quality
heart left ventricleUBERON:000208498.51gold quality
cardiac ventricleUBERON:000208298.50gold quality
adipose tissueUBERON:000101398.42gold quality
subcutaneous adipose tissueUBERON:000219098.42gold quality
right atrium auricular regionUBERON:000663198.41gold quality
lower lobe of lungUBERON:000894998.39gold quality
cardiac atriumUBERON:000208198.36gold quality
saphenous veinUBERON:000731898.35gold quality
veinUBERON:000163898.25gold quality
lungUBERON:000204898.23gold quality
vena cavaUBERON:000408797.96gold quality
heartUBERON:000094897.82gold quality
heart right ventricleUBERON:000208097.75gold quality
connective tissueUBERON:000238497.73gold quality
penisUBERON:000098997.60gold quality
left uterine tubeUBERON:000130397.56gold quality
ectocervixUBERON:001224997.55gold quality
mucosa of stomachUBERON:000119997.51gold quality
right coronary arteryUBERON:000162597.47gold quality
myocardiumUBERON:000234997.41gold quality

Single-cell (SCXA)

Detected in 25 experiment(s), a significant marker in 24.

ExperimentMarker?Max mean expression
E-GEOD-135922yes8291.65
E-MTAB-6308yes3899.79
E-HCAD-15yes3410.24
E-ANND-2yes2357.33
E-CURD-126yes2309.92
E-MTAB-11268yes2084.82
E-GEOD-134144yes1829.66
E-MTAB-6678yes1819.89
E-MTAB-8410yes1344.88
E-MTAB-8381yes1256.54
E-HCAD-11yes1231.85
E-HCAD-36yes1104.56
E-MTAB-8322yes1067.41
E-MTAB-10287yes836.17
E-CURD-6yes144.35

Regulation

Is transcription factor: no

Upstream regulators (CollecTRI, top): BMAL1, CLOCK, ERG, ETS1, ETS2, GATA2, GATA6, IRF6, NFIC, NFIL3, NFKB1, POU1F1, POU2F1, RELA, YY1

miRNA regulators (miRDB)

12 targeting VWF, top 30 by miRDB confidence (max_score; target_count = how many genes the miRNA targets in total — lower means more specific):

miRNAMax scoreAvg scoremiRNA target_count
HSA-MIR-6759-5P99.9966.54785
HSA-MIR-450B-5P99.9271.483175
HSA-MIR-443799.5265.291266
HSA-MIR-3190-5P98.8764.891345
HSA-MIR-2467-3P98.6567.181969
HSA-MIR-446898.0166.851187
HSA-MIR-197297.6767.381172
HSA-MIR-227897.3066.191130
HSA-MIR-429696.3563.551233
HSA-MIR-426596.1864.68557
HSA-MIR-432296.1864.85539
HSA-MIR-6796-5P95.3766.081120

Literature-anchored findings (GeneRIF, showing 40)

  • Ser968Thr mutation in the A3 domain leads to defective binding to collagen and bleeding tendency. (PMID:11583318)
  • Our findings highlight a newly recognized role of circulating VWF in the initiation of platelet adhesion (PMID:11756664)
  • Incubation of a recombinant provWF (rpvWF) preparation with canine and human vWF-deficient plasma induced a time-dependent decrease in provWF antigen and an increase in vWFpp antigen without changing total vWF antigen or collagen-binding activity. (PMID:11776313)
  • 4 mutations, at C509, V551, R552 and R611 lead to decreased binding to heparin in plasma and rVWF. No heparin-binding defect was found with different type 2 VWF mutants, at positions G561, E596, I662, R543, R545, V553, R578 or L697. (PMID:11776314)
  • VWF with a unique multimeric structure plays a pivotal role in hemostasis and pathological intravascular thrombosis by contributing to platelet function and blood coagulation through its multiple adhesive functions for platelet membrane receptors. (PMID:11843285)
  • VWF has roles in hemostasis, platelet adhesion, and inflammation. (PMID:11843287)
  • Mutations in particular domains of VWF correlate with specific subtypes of type 2 von Willebrand disease depending on how they affect its post-translational processing, multimerization, secretion, or binding. (PMID:11843298)
  • In several genetic subtypes of VWF disease, the F8/VWF ratio increases as VWF synthesis is reduced. It remains 1 when VWF clearance increases. A high F8/VWF ratio & a low VWF level may indicate a true genetic defect, possibly a null allele. (PMID:11859851)
  • vWF and tPAag but not thrombomodulin in the present population are independent markers of atherosclerosis. (PMID:11864703)
  • Elevation of vWF in plasma was associated with neuropathic foot ulceration, linking endothelial dysfunction to foot ulceration (PMID:11869299)
  • Shear-dependent morphology of von Willebrand factor bound to immobilized collagen (PMID:11877281)
  • raised vWf in breast cancer seems likely to be independent of the acute phase response (PMID:11914659)
  • Arg 1715 is not essential in the function but it is necessary for maintaining the conformation recognized by MoAb 9 specific for the GPIIb/IIIa-binding domain of VWF. (PMID:11920243)
  • Identification of the regulatory elements of the human von Willebrand factor for binding to platelet GPIb (PMID:11943773)
  • REVIEW: current knowledge on the role of vWF in primary hemostasis is reviewed. (PMID:11992236)
  • role in the preservation of factor VIII in the circulation is investigated by administration of human VWF and pro-VWF in murine and dog models of vWD. (PMID:11992244)
  • the ability of VWF pseudogranules, which are secretagogue responsive, to recruit membrane proteins (PMID:12006654)
  • Site-directed mutagenesis of platelet glycoprotein Ib alpha demonstrates residues crucial for botrocetin-mediated VWF binding. (PMID:12036871)
  • Endothelial VWF recruits platelets to atherosclerosis-prone sites in response to hypercholesterolemia. Hypercholesterolemia primes platelets for recruitment via VWF, GPIb alpha, and P-selectin before lesions are detectable. (PMID:12036879)
  • Binding of VFW to the modulator, snake venom protein bitiscetin, has been defined at a distinct site in the A1 domain of VWF spanning over alpha4a, alpha5 helices and the loop between alpha5 and beta6 close to the botrocetin- and mAb NMC-4-binding sites. (PMID:12069583)
  • the rGPIa/IIa-collagen interaction dominates the adhesion of rGPIa/IIa-Ib alpha-liposomes to the collagen surface at low shear rates; the rGPIa/IIa-collagen and rGPIb alpha-VWF interactions synergistically support liposome adhesion at high shear rates. (PMID:12070018)
  • Factor VIIa induces release of von Willebrand factor from human umbilical vein endothelial cells by a tyrosine kinase dependent pathway. (PMID:12083486)
  • REVIEW: Control of VWF multimer size by VWF-cleaving protease and thrombospondin-1 and role in arterial thrombosis. (PMID:12163004)
  • structures of the glycoprotein Ibalpha amino-terminal domain and its complex with the VWF domain A1 are presented (PMID:12183630)
  • Expression in uterine leiomyoma (PMID:12215337)
  • PKA-mediated phosphorylation of GPIbbeta at Ser(166) negatively regulates VWF binding to GPIb-IX and is one of the mechanisms by which PKA mediates platelet inhibition (PMID:12361948)
  • The mucin-like macroglycopeptide region of glycoprotein Ibalpha is required for cell adhesion to immobilized von Willebrand factor (VWF) under flow but not for static VWF binding. (PMID:12362242)
  • Polymorphisms in the von Willebrand factor gene are not associated with proliferative retinopathy in non-insulin-dependent diabetes mellitus. Two polymorphisms (-1793G/C and Thr789Ala) in the von Willebrand factor gene with PDR. (PMID:12381897)
  • impaired thrombus generation in type 2B VWD ascribed to the critical function of larger VWF multimers in the proper spatial growth of mural thrombi under high shear rate conditions. (PMID:12393671)
  • gentic variant demonstrates that a normal consensus sequence for VWF propeptide cleavage and efficient cleavage are required in vivo for normal FVIII binding capacity of VWF (PMID:12393698)
  • Interaction between von Willebrand factor and glycoprotein Ib activates Src kinase in human platelets. (PMID:12393736)
  • Calcium-regulated secretion of von Willebrand factor in vascular endothelial cells. (PMID:12445472)
  • The binding site of the A3 domain of von Willebrand factor was located at its hydrophobic ‘front’ surface. (PMID:12447349)
  • studies demonstrating that fluid shear stress rather than shear rate controls platelet activation show for the first time the ability of hydrodynamic forces to induce VWF aggregation in suspension, that may control cell adhesion rates in circulation (PMID:12456504)
  • inhibition of promoter activation by nuclear factor Y transcription factor (PMID:12511565)
  • Enhanced interaction of 2B-rVWF with GPIb, without engagement of alphaIIbbeta3, is sufficient to induce shear-induced platelet aggregation, but does not lead to stable thrombus formation. (PMID:12543870)
  • REVEIW: structural and functional properties of VWF domains; their interaction with glycoprotein Ibalpha, and their role in platelet activation and thrombus formation (PMID:12579041)
  • Surface characteristics of the collagen-binding site of the A3 domain were ellicited using 22 point mutations as a mapping tool; docking studies suggested possible engagements of a collagen triple helix interacting with A3 (PMID:12582178)
  • the strongest linkage signal (LOD =3.46, p = 0.00003) for vWF was found on chromosome 9q34 at the DNA marker D9S290, where the ABO gene is located (PMID:12624629)
  • data demonstrate residues D1323(560) and G1324(561) being critical for vWF-A1 mediated platelet aggregation (PMID:12646253)

Cross-species orthologs

3 orthologs

OrganismSymbolGene ID
danio_reriovwfENSDARG00000077231
mus_musculusVwfENSMUSG00000001930
rattus_norvegicusVwfENSRNOG00000019689

Paralogs (19): CHRDL2 (ENSG00000054938), CHRD (ENSG00000090539), CHRDL1 (ENSG00000101938), TECTA (ENSG00000109927), MUC5B (ENSG00000117983), KCP (ENSG00000135253), ZAN (ENSG00000146839), CRIM1 (ENSG00000150938), BMPER (ENSG00000164619), OTOGL (ENSG00000165899), VWCE (ENSG00000167992), VWC2L (ENSG00000174453), MUC6 (ENSG00000184956), OTOG (ENSG00000188162), VWC2 (ENSG00000188730), MUC2 (ENSG00000198788), MUC19 (ENSG00000205592), MUC5AC (ENSG00000215182), FCGBP (ENSG00000275395)

Protein

Protein identifiers

von Willebrand factor — P04275 (reviewed: P04275)

All UniProt accessions (2): P04275, I3L4K4

UniProt curated annotations — full annotation on UniProt →

Function. 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.

Subunit / interactions. Multimeric. Interacts with F8.

Subcellular location. Secreted. Extracellular space. Extracellular matrix.

Tissue specificity. Plasma.

Post-translational modifications. All cysteine residues are involved in intrachain or interchain disulfide bonds. N- and O-glycosylated.

Disease relevance. 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. The disease is caused by variants affecting the gene represented in this entry. 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. The disease is caused by variants affecting the gene represented in this entry. 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. The disease is caused by variants affecting the gene represented in this entry.

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

Isoforms (2)

UniProt IDNamesCanonical?
P04275-11yes
P04275-22

RefSeq proteins (1): NP_000543* (*=MANE)

Domains & families (InterPro)

IDNameType
IPR001007VWF_domDomain
IPR001846VWF_type-DDomain
IPR002035VWF_ADomain
IPR002919TIL_domDomain
IPR006207Cys_knot_CDomain
IPR014853VWF/SSPO/ZAN-like_Cys-rich_domDomain
IPR032361VWA_N2Domain
IPR036084Ser_inhib-like_sfHomologous_superfamily
IPR036465vWFA_dom_sfHomologous_superfamily
IPR037578Von_Willebrand_factorFamily
IPR050780Mucin_vWF_Thrombospondin_sfFamily
IPR058753TIL_OTOGL_MucinDomain

Pfam: PF00092, PF00093, PF00094, PF01826, PF08742, PF16164, PF23244, PF25962

UniProt features (351 total): strand 120, sequence variant 60, helix 59, disulfide bond 34, glycosylation site 26, turn 20, domain 15, sequence conflict 4, region of interest 4, splice variant 3, chain 2, mutagenesis site 2, signal peptide 1, short sequence motif 1

Structure

Experimental structures (PDB)

48 structures, top 30 by resolution.

PDBMethodResolution (Å)
5BV8X-RAY DIFFRACTION1.59
7EOWX-RAY DIFFRACTION1.6
3ZQKX-RAY DIFFRACTION1.7
1ATZX-RAY DIFFRACTION1.8
1IJBX-RAY DIFFRACTION1.8
2ADFX-RAY DIFFRACTION1.9
3GXBX-RAY DIFFRACTION1.9
3PPVX-RAY DIFFRACTION1.9
3PPWX-RAY DIFFRACTION1.9
3PPXX-RAY DIFFRACTION1.91
1FNSX-RAY DIFFRACTION2
3PPYX-RAY DIFFRACTION2
1FE8X-RAY DIFFRACTION2.03
4C2AX-RAY DIFFRACTION2.08
7F49X-RAY DIFFRACTION2.09
1AO3X-RAY DIFFRACTION2.2
1OAKX-RAY DIFFRACTION2.2
4C29X-RAY DIFFRACTION2.2
1AUQX-RAY DIFFRACTION2.3
3HXOX-RAY DIFFRACTION2.4
6N29X-RAY DIFFRACTION2.5
1IJKX-RAY DIFFRACTION2.6
1SQ0X-RAY DIFFRACTION2.6
3HXQX-RAY DIFFRACTION2.69
4C2BX-RAY DIFFRACTION2.8
4DMUX-RAY DIFFRACTION2.8
1UEXX-RAY DIFFRACTION2.85
7WPPELECTRON MICROSCOPY2.85
7KWOELECTRON MICROSCOPY2.9
1U0NX-RAY DIFFRACTION2.95

Predicted structure (AlphaFold)

No AlphaFold model available for P04275 — AlphaFold DB does not currently provide models for proteins above ~3000 aa.

Antibody-complex structures (SAbDab): 5 — 1FE8, 1FNS, 1OAK, 2ADF, 7EOW

Functional residue map

Curated UniProt residues grouped by drug-discovery relevance — catalytic, ligand-binding, modification, and mutation-validated positions. Source: UniProtKB sequence features.

Disulfide bonds (34): 35–162, 57–200, 388–524, 410–559, 432–440, 767–808, 776–804, 810–821, 867–996, 889–1031, 898–993, 914–921, 1060–1084, 1071–1111, 1089–1091, 1126–1130, 1149–1169, 1153–1165, 1196–1199, 1234–1237 …

Glycosylation sites (26): 99, 156, 211, 666, 857, 1147, 1231, 1248, 1255, 1256, 1263, 1468, 1477, 1486, 1487, 1515, 1574, 1679, 2223, 2290 …

Mutagenesis-validated functional residues (2):

PositionPhenotype
1149reduced secretion and increased intracellular retention. similar phenotype; when associated with s-1169.
1169reduced secretion and increased intracellular retention. similar phenotype; when associated with r-1149.

Function

Pathways and Gene Ontology

Reactome pathways

26 pathways

IDPathway
R-HSA-114608Platelet degranulation
R-HSA-216083Integrin cell surface interactions
R-HSA-354192Integrin signaling
R-HSA-354194GRB2:SOS provides linkage to MAPK signaling for Integrins
R-HSA-372708p130Cas linkage to MAPK signaling for integrins
R-HSA-430116GP1b-IX-V activation signalling
R-HSA-5674135MAP2K and MAPK activation
R-HSA-6802946Signaling by moderate kinase activity BRAF mutants
R-HSA-6802948Signaling by high-kinase activity BRAF mutants
R-HSA-6802952Signaling by BRAF and RAF1 fusions
R-HSA-6802955Paradoxical activation of RAF signaling by kinase inactive BRAF
R-HSA-75892Platelet Adhesion to exposed collagen
R-HSA-76009Platelet Aggregation (Plug Formation)
R-HSA-9649948Signaling downstream of RAS mutants
R-HSA-9656223Signaling by RAF1 mutants
R-HSA-9672391Defective F8 cleavage by thrombin
R-HSA-9672393Defective F8 binding to von Willebrand factor
R-HSA-9769735Initiation of coagulation cascade
R-HSA-9769739Regulation of clotting cascade
R-HSA-9769743Amplification and propagation of coagulation cascade
R-HSA-9845619Enhanced cleavage of VWF variant by ADAMTS13
R-HSA-9845620Enhanced binding of GP1BA variant to VWF multimer:collagen
R-HSA-9845621Defective VWF cleavage by ADAMTS13 variant
R-HSA-9845622Defective VWF binding to collagen type I
R-HSA-9846298Defective binding of VWF variant to GPIb:IX:V
R-HSA-140837

MSigDB gene sets: 310 (showing top): MODULE_52, GOCC_SECRETORY_GRANULE, REACTOME_PLATELET_AGGREGATION_PLUG_FORMATION, REACTOME_PLATELET_ACTIVATION_SIGNALING_AND_AGGREGATION, GOBP_PLATELET_ACTIVATION, MODULE_128, AREB6_01, MCBRYAN_PUBERTAL_TGFB1_TARGETS_DN, PATIL_LIVER_CANCER, GOBP_WOUND_HEALING, REACTOME_P130CAS_LINKAGE_TO_MAPK_SIGNALING_FOR_INTEGRINS, MODULE_118, PICCALUGA_ANGIOIMMUNOBLASTIC_LYMPHOMA_UP, INAMURA_LUNG_CANCER_SCC_DN, REACTOME_GRB2_SOS_PROVIDES_LINKAGE_TO_MAPK_SIGNALING_FOR_INTEGRINS

GO Biological Process (7): cell adhesion (GO:0007155), blood coagulation (GO:0007596), hemostasis (GO:0007599), response to wounding (GO:0009611), platelet activation (GO:0030168), cell-substrate adhesion (GO:0031589), positive regulation of intracellular signal transduction (GO:1902533)

GO Molecular Function (8): protease binding (GO:0002020), integrin binding (GO:0005178), extracellular matrix structural constituent (GO:0005201), collagen binding (GO:0005518), immunoglobulin binding (GO:0019865), identical protein binding (GO:0042802), protein-folding chaperone binding (GO:0051087), protein binding (GO:0005515)

GO Cellular Component (9): extracellular region (GO:0005576), obsolete extracellular space (GO:0005615), endoplasmic reticulum (GO:0005783), extracellular matrix (GO:0031012), platelet alpha granule (GO:0031091), platelet alpha granule lumen (GO:0031093), Weibel-Palade body (GO:0033093), extracellular exosome (GO:0070062), cell periphery (GO:0071944)

Reactome top-level categories

Rollup of top-12 pathways:

CategoryPathways
Oncogenic MAPK signaling5
Coagulation pathway3
Integrin signaling2
Platelet activation, signaling and aggregation2
Defective factor VIII causes hemophilia A2
Response to elevated platelet cytosolic Ca2+1
Extracellular matrix organization1
Signal Transduction1
Platelet Aggregation (Plug Formation)1
RAF/MAP kinase cascade1
Hemostasis1
Signaling by RAS mutants1

GO top-level categories

Rollup of top GO terms by namespace:

CategoryTerms
protein-containing complex binding3
protein binding2
cellular anatomical structure2
secretory granule2
cellular process1
hemostasis1
wound healing1
coagulation1
regulation of body fluid levels1
response to stress1
cell activation1
blood coagulation1
cell adhesion1
positive regulation of signal transduction1
intracellular signal transduction1
regulation of intracellular signal transduction1
enzyme binding1
signaling receptor binding1
cell adhesion molecule binding1
structural molecule activity1
extracellular matrix1
binding1
cytoplasm1
endomembrane system1
intracellular membrane-bounded organelle1
external encapsulating structure1
platelet alpha granule1
secretory granule lumen1
clathrin-coated vesicle1
extracellular vesicle1

Protein interactions and networks

STRING

5048 interactions, top by confidence (×1000):

Protein AProtein BPartner UniProtScore
VWFF8P00451999
VWFGP1BAP07359999
VWFITGA2BP08514999
VWFSELPP16109999
VWFFN1P02751998
VWFGP6Q9HCN6997
VWFADAMTS13Q76LX8991
VWFITGB3P05106984
VWFGP1BBP13224983
VWFF3P13726980
VWFGP9P14770977
VWFVTNP01141964
VWFCXCL8P10145962
VWFGP5P40197959
VWFPLATP00750931

IntAct

110 interactions, top by confidence:

ABTypeScore
VWFVWFpsi-mi:“MI:0407”(direct interaction)0.870
VWFVWFpsi-mi:“MI:0195”(covalent binding)0.870
ADAMTS13VWFpsi-mi:“MI:0570”(protein cleavage)0.790
VWFADAMTS13psi-mi:“MI:0570”(protein cleavage)0.790
ADAMTS13VWFpsi-mi:“MI:0407”(direct interaction)0.790

BioGRID (46): P4HB (Affinity Capture-Western), P4HB (Reconstituted Complex), VWF (Reconstituted Complex), VWF (Reconstituted Complex), VWF (Far Western), VWF (Synthetic Lethality), VWF (Co-crystal Structure), CKAP4 (Proximity Label-MS), VWF (Proximity Label-MS), COL1A1 (Co-fractionation), COL1A1 (Reconstituted Complex), HIST3H3 (Proximity Label-MS), VWF (Two-hybrid), VWF (Co-localization), F8 (Reconstituted Complex)

ESM2 similar proteins: A0A292G9J6, A1A5Y0, A2VCU8, A6QR11, F7A4A7, O00187, O55225, O57472, O95450, P04275, P57110, P59511, P79331, P80012, P98088, P98089, Q02817, Q13219, Q28295, Q28833, Q2VWQ2, Q3ZCN5, Q4VC17, Q5R3Z7, Q60519, Q61220, Q62635, Q62918, Q62919, Q6PZE0, Q6W4X9, Q6ZRI0, Q7ZXL5, Q80T03, Q80Z19, Q86XX4, Q8CIZ8, Q8CJ69, Q8N8U9, Q8R4K8

Diamond homologs: A2VEC9, A6QNY1, B3EWZ3, B3EWZ8, C0HL12, C5IAW9, D3YXG0, D3ZTD8, F1LW30, O08721, O08722, O08747, O14514, O15072, O55225, O60241, O60242, O75173, O88783, O95185, O95450, P04275, P07358, P07996, P27918, P35441, P35442, P35448, P55314, P57110, P58397, P58459, P59384, P79331, P80012, P97857, P98088, P98092, P98160, P98164

SIGNOR signaling

16 interactions.

AEffectBMechanism
ADAMTS13“down-regulates activity”VWFcleavage
VWF“up-regulates activity”F8binding
FGG“down-regulates activity”VWFbinding
ERG“up-regulates quantity by expression”VWF“transcriptional regulation”
ETS1“up-regulates quantity by expression”VWF“transcriptional regulation”
VWF“up-regulates activity”“GPIb-IX-V complex”binding
VWF“up-regulates activity”“AIIB/b3 integrin”binding
“Blood vessel damage”up-regulatesVWF
Platelet_alpha_granule_formationup-regulatesVWF
VWF“up-regulates quantity by stabilization”F8
NBEAL2up-regulatesVWF
FAM20C“up-regulates activity”VWFphosphorylation
CLOCK/BMAL1“down-regulates quantity by repression”VWF“transcriptional regulation”
ARNTL“down-regulates quantity by repression”VWF“transcriptional regulation”
PCSK6“up-regulates activity”VWFcleavage
FURIN“up-regulates activity”VWFcleavage

Enriched among interaction partners

Reactome pathways and GO biological processes over-represented among this gene’s 45 IntAct physical interaction partners (hypergeometric vs the genome-wide background, BH-FDR, gene-set size 15–500, ranked by fold). A functional readout of the neighbourhood — distinct from this gene’s own memberships above, and biased toward well-studied / hub proteins, so read it as themes rather than proof.

GO biological processes:

GO termPartnersFoldFDR
blood coagulation536.2×7e-05

Disease & clinical

Clinical variants and AI predictions

ClinVar

2115 variants total. Per-class counts are floors (≥ shown; pagination cap):

ClassificationCount (floor)
Pathogenic246
Likely pathogenic201
Uncertain significance986
Likely benign209
Benign100

Top pathogenic / likely-pathogenic (30)

Variant IDHGVSClassification
100171NM_000552.5(VWF):c.100C>T (p.Arg34Ter)Pathogenic
100172NM_000552.5(VWF):c.1093C>T (p.Arg365Ter)Pathogenic
100173NM_000552.5(VWF):c.1109+2T>CPathogenic
100175NM_000552.5(VWF):c.1117C>T (p.Arg373Ter)Pathogenic
100179NM_000552.5(VWF):c.1309_1326del (p.Asp437_Arg442del)Pathogenic
100198NM_000552.5(VWF):c.1930G>T (p.Glu644Ter)Pathogenic
100201NM_000552.5(VWF):c.2072del (p.Pro691fs)Pathogenic
100202NM_000552.5(VWF):c.2116C>T (p.Gln706Ter)Pathogenic
100203NM_000552.5(VWF):c.2124_2125del (p.Cys709fs)Pathogenic
100217NM_000552.5(VWF):c.2363G>A (p.Cys788Tyr)Pathogenic
100231NM_000552.5(VWF):c.2635G>A (p.Asp879Asn)Pathogenic
100237NM_000552.5(VWF):c.276dup (p.Asp93Ter)Pathogenic
100238NM_000552.5(VWF):c.276del (p.Phe92fs)Pathogenic
100248NM_000552.5(VWF):c.3179G>A (p.Cys1060Tyr)Pathogenic
100257NM_000552.5(VWF):c.3379+1G>APathogenic
100261NM_000552.5(VWF):c.3389G>T (p.Cys1130Phe)Pathogenic
100262NM_000552.5(VWF):c.3430T>G (p.Trp1144Gly)Pathogenic
100267NM_000552.5(VWF):c.3538+1G>APathogenic
100269NM_000552.5(VWF):c.3568T>C (p.Cys1190Arg)Pathogenic
100281NM_000552.5(VWF):c.3802C>G (p.His1268Asp)Pathogenic
100292NM_000552.5(VWF):c.3853T>C (p.Ser1285Pro)Pathogenic
100295NM_000552.5(VWF):c.3877T>C (p.Phe1293Leu)Pathogenic
100300NM_000552.5(VWF):c.3917G>A (p.Arg1306Gln)Pathogenic
100301NM_000552.5(VWF):c.3917G>T (p.Arg1306Leu)Pathogenic
100302NM_000552.5(VWF):c.3920T>C (p.Leu1307Pro)Pathogenic
100305NM_000552.5(VWF):c.3925A>G (p.Ile1309Val)Pathogenic
100307NM_000552.5(VWF):c.3931C>T (p.Gln1311Ter)Pathogenic
100308NM_000552.5(VWF):c.3940G>T (p.Val1314Phe)Pathogenic
100309NM_000552.5(VWF):c.3941T>A (p.Val1314Asp)Pathogenic
100313NM_000552.5(VWF):c.3971G>C (p.Gly1324Ala)Pathogenic

SpliceAI

9513 predictions. Top by Δscore:

VariantEffectΔscore
12:5949199:TTGCC:Tacceptor_gain1.0000
12:5949200:TGCC:Tacceptor_gain1.0000
12:5949202:CC:Cacceptor_gain1.0000
12:5949203:CC:Cacceptor_gain1.0000
12:5949204:C:CCacceptor_gain1.0000
12:5949204:CTGCA:Cacceptor_loss1.0000
12:5949782:TTACC:Tdonor_loss1.0000
12:5949783:TA:Tdonor_loss1.0000
12:5949784:A:AGdonor_loss1.0000
12:5949881:CAC:Cacceptor_gain1.0000
12:5949881:CACCT:Cacceptor_loss1.0000
12:5949885:T:Cacceptor_loss1.0000
12:5952387:TCA:Tdonor_loss1.0000
12:5952388:CAC:Cdonor_loss1.0000
12:5952389:A:ACdonor_gain1.0000
12:5952389:AC:Adonor_loss1.0000
12:5952389:ACT:Adonor_gain1.0000
12:5952389:ACTC:Adonor_gain1.0000
12:5952389:ACTCC:Adonor_gain1.0000
12:5952390:C:CTdonor_gain1.0000
12:5952390:CT:Cdonor_gain1.0000
12:5952390:CTC:Cdonor_gain1.0000
12:5952390:CTCC:Cdonor_gain1.0000
12:5952390:CTCCC:Cdonor_gain1.0000
12:5952392:C:CAdonor_gain1.0000
12:5952460:T:Adonor_gain1.0000
12:5952515:TCACG:Tacceptor_gain1.0000
12:5952516:CACG:Cacceptor_gain1.0000
12:5952516:CACGC:Cacceptor_gain1.0000
12:5952517:ACG:Aacceptor_gain1.0000

AlphaMissense

18569 scored. Top likely-pathogenic:

VariantProtein changeam_pathogenicity
12:5993881:C:AW2193C0.999
12:5993881:C:GW2193C0.999
12:6056876:C:AW642C0.999
12:6056876:C:GW642C0.999
12:6057027:A:CF592C0.998
12:6034805:C:AW856C0.997
12:6034805:C:GW856C0.997
12:6011780:C:AW1893C0.996
12:6011780:C:GW1893C0.996
12:5976216:C:AW2444C0.995
12:5976216:C:GW2444C0.995
12:6023650:C:AW1120C0.995
12:6023650:C:GW1120C0.995
12:6062981:C:AW502C0.995
12:6062981:C:GW502C0.995
12:6065236:G:CS398R0.995
12:6065236:G:TS398R0.995
12:6065238:T:GS398R0.995
12:6071322:C:AW377C0.995
12:6071322:C:GW377C0.995
12:5993883:A:GW2193R0.994
12:5993883:A:TW2193R0.994
12:6025939:C:AW1025C0.994
12:6025939:C:GW1025C0.994
12:6065268:A:GC388R0.994
12:6075354:C:AW285C0.994
12:6075354:C:GW285C0.994
12:6034807:A:GW856R0.993
12:6034807:A:TW856R0.993
12:6056917:A:CY629D0.993

dbSNP variants (sampled 300 via entrez): RS1000028897 (12:6027415 G>A), RS1000045175 (12:6071085 C>T), RS1000049175 (12:6108209 G>A,T), RS1000052675 (12:5956136 C>A,T), RS1000093133 (12:5963830 G>A), RS1000104996 (12:5962762 G>A), RS1000120896 (12:6107184 G>A), RS1000122141 (12:6115779 C>A,G,T), RS1000122849 (12:6059111 G>A), RS1000153122 (12:6000521 T>TAG), RS1000163249 (12:5969970 G>A,C), RS1000185974 (12:5995939 G>A,C), RS1000188180 (12:6121746 C>T), RS1000199831 (12:5958809 A>G), RS1000207282 (12:6083190 T>C)

Disease associations

OMIM: gene MIM:613160 | disease phenotypes: MIM:193400, MIM:277480, MIM:613554, MIM:300049, MIM:134500, MIM:306700

GenCC curated gene-disease

DiseaseClassificationInheritance
von Willebrand disease 2DefinitiveAutosomal dominant
von Willebrand disease 1StrongAutosomal dominant
von Willebrand disease 3StrongAutosomal recessive
von Willebrand disease type 2ASupportiveAutosomal dominant
von Willebrand disease type 2BSupportiveAutosomal dominant
von Willebrand disease type 2MSupportiveAutosomal dominant
von Willebrand disease type 2NSupportiveAutosomal recessive

ClinGen Gene-Disease Validity (2)

Expert-panel classifications — Definitive > Strong > Moderate > Limited > Disputed > Refuted.

DiseaseClassificationInheritance
hereditary von Willebrand diseaseDefinitiveAD
von Willebrand disease type 2BDefinitiveAD

Mondo (12): von Willebrand disease 1 (MONDO:0008668), von Willebrand disease 3 (MONDO:0010191), von Willebrand disease 2 (MONDO:0013304), hereditary von Willebrand disease (MONDO:0019565), von Willebrand disease type 2A (MONDO:0015628), von Willebrand disease type 2N (MONDO:0015631), thrombocytopenia (MONDO:0002049), von Willebrand disease (hereditary or acquired) (MONDO:0024574), von Willebrand disease type 2B (MONDO:0015629), von Willebrand disease type 2M (MONDO:0015630), heterotopia, periventricular, X-linked dominant (MONDO:0010233), hemophilia A (MONDO:0010602)

Orphanet (11): Von Willebrand disease type 1 (Orphanet:166078), Von Willebrand disease type 2 (Orphanet:166081), Von Willebrand disease type 3 (Orphanet:166096), Von Willebrand disease (Orphanet:903), Von Willebrand disease type 2A (Orphanet:166084), Von Willebrand disease type 2N (Orphanet:166093), Von Willebrand disease type 2B (Orphanet:166087), Von Willebrand disease type 2M (Orphanet:166090), Nodular neuronal heterotopia (Orphanet:2149), Ehlers-Danlos syndrome with periventricular heterotopia (Orphanet:82004), Hemophilia A (Orphanet:98878)

HPO phenotypes

23 total (23 of 23 shown, HPO-id order):

HPOTerm
HP:0000006Autosomal dominant inheritance
HP:0000007Autosomal recessive inheritance
HP:0000132Menorrhagia
HP:0000421Epistaxis
HP:0000471Gastrointestinal angiodysplasia
HP:0000978Bruising susceptibility
HP:0001634Mitral valve prolapse
HP:0001650Aortic valve stenosis
HP:0001873Thrombocytopenia
HP:0001892Abnormal bleeding
HP:0001934Persistent bleeding after trauma
HP:0002239Gastrointestinal hemorrhage
HP:0003010Prolonged bleeding time
HP:0003125Reduced factor VIII activity
HP:0003540Impaired platelet aggregation
HP:0003828Variable expressivity
HP:0003829Typified by incomplete penetrance
HP:0004846Prolonged bleeding after surgery
HP:0005261Joint hemorrhage
HP:0005542Prolonged whole-blood clotting time
HP:0006298Prolonged bleeding after dental extraction
HP:0008330Reduced von Willebrand factor activity
HP:0012147Reduced quantity of Von Willebrand factor

GWAS associations

34 associations (top):

StudyTraitp-value
GCST000626_2Factor VIII levels4.000000e-09
GCST000627_4vWF levels2.000000e-32
GCST001335_20Mean platelet volume2.000000e-21
GCST001337_34Platelet count4.000000e-11
GCST001793_3Coagulation factor levels6.000000e-07
GCST001793_5Coagulation factor levels5.000000e-16
GCST003210_2Low vWF levels5.000000e-22
GCST003383_12Platelet count2.000000e-07
GCST004598_2vWF levels in ischaemic stroke and hyperhomocysteinaemia5.000000e-06
GCST004599_105Mean platelet volume7.000000e-15
GCST007445_15Factor VIII levels8.000000e-07
GCST007445_18Factor VIII levels2.000000e-15
GCST007445_25Factor VIII levels2.000000e-15
GCST007445_36Factor VIII levels2.000000e-24
GCST007445_37Factor VIII levels4.000000e-24
GCST007445_51Factor VIII levels2.000000e-11
GCST007445_54Factor VIII levels3.000000e-18
GCST007445_6Factor VIII levels3.000000e-19
GCST007445_61Factor VIII levels8.000000e-12
GCST007446_16vWF levels8.000000e-27
GCST007446_18vWF levels9.000000e-43
GCST007446_23vWF levels2.000000e-89
GCST007446_25vWF levels2.000000e-89
GCST007446_30vWF levels1.000000e-82
GCST007446_32vWF levels6.000000e-83
GCST007446_73vWF levels2.000000e-27
GCST007446_75vWF levels1.000000e-42
GCST008514_18Peginterferon alfa-2a treatment response in chronic hepatitis B infection5.000000e-06
GCST009030_18Venous thromboembolism4.000000e-13
GCST012083_3Response to tofacitinib treatment in psoriasis (herpes zoster)1.000000e-06

EFO canonical traits (3, from GWAS)

EFO IDTrait name
EFO:0004630factor VIII measurement
EFO:0004309platelet count
EFO:0010103response to peginterferon alfa-2a

MeSH disease descriptors (7)

DescriptorNameTree numbers
D006467Hemophilia AC15.378.100.100.500; C15.378.100.141.500; C15.378.463.500; C16.320.099.500
D013921ThrombocytopeniaC15.378.140.855; C15.378.243.937
D056725von Willebrand Disease, Type 1C15.378.100.100.900.100; C15.378.100.141.900.100; C15.378.463.920.100; C16.320.099.920.100
D056728von Willebrand Disease, Type 2C15.378.100.100.900.200; C15.378.100.141.900.200; C15.378.463.920.200; C16.320.099.920.200
D056729von Willebrand Disease, Type 3C15.378.100.100.900.300; C15.378.100.141.900.300; C15.378.463.920.300; C16.320.099.920.300
D014842von Willebrand DiseasesC15.378.100.100.900; C15.378.100.141.900; C15.378.140.900; C15.378.463.920; C16.320.099.920
C531844Von willebrand factor, deficiency (supp.)

Drugs & pharmacology

Drug and pharmacology data

Is drug target: yes

ChEMBL targets (1): CHEMBL2021748 (SINGLE PROTEIN)

PharmGKB: 1 entry (VIP=true, CPIC=false)

CTD chemical–gene interactions

81 total (human), top 30 by PubMed support.

ChemicalActions (top 5)PubMed papers
Benzo(a)pyreneincreases mutagenesis, affects methylation, decreases expression, increases methylation5
Air Pollutantsaffects expression, increases abundance, increases expression4
sodium arseniteincreases expression3
Deamino Arginine Vasopressinincreases activity, increases secretion3
Estradiolaffects cotreatment, decreases expression, increases expression3
Ethinyl Estradiolaffects cotreatment, increases expression, decreases expression3
Particulate Matteraffects expression, increases abundance, increases expression3
mercuric bromidedecreases expression, affects cotreatment2
Arsenicaffects methylation, decreases expression, increases abundance2
Cadmiumincreases secretion, affects expression, affects response to substance, increases expression2
Cisplatinaffects expression, increases expression2
Cocaineincreases expression2
Methylprednisoloneincreases expression, decreases expression2
Phenylmercuric Acetateaffects cotreatment, decreases expression2
Tamoxifenincreases expression2
Aflatoxin B1decreases methylation, increases expression2
Cadmium Chlorideaffects binding, increases reaction, increases expression, affects reaction2
2,4,6-tribromophenolincreases expression1
methylmercuric chloridedecreases expression1
lasiocarpinedecreases expression1
triphenyl phosphateaffects expression1
bisphenol Aincreases expression1
sodium arsenatedecreases expression, increases abundance1
nylestrioldecreases expression1
11-nor-delta(9)-tetrahydrocannabinol-9-carboxylic acidaffects methylation, increases abundance1
tetrabromobisphenol Aincreases expression1
benzo(e)pyrenedecreases methylation1
aflatoxin B2decreases methylation1
Gestodeneaffects cotreatment, increases expression1
piceindecreases expression, decreases reaction1

ChEMBL screening assays

17 unique, capped per target: 17 binding

Representative assays (with source publication via chembl_document):

Assay IDTypeDescriptionSource paper
CHEMBL2026118BindingInhibition of GPIbalpha-vWF binding assessed as inhibition of ristocetin-induced platelet agglutination at 100 uM after 2 mins by static agglutination assayInhibition of platelet adhesion by peptidomimetics mimicking the interactive β-hairpin of glycoprotein Ibα. — Bioorg Med Chem Lett

Clinical trials (associated diseases)

302 trials via MONDO — disease-level, not drug-specific.

TrialPhaseStatusTitle
NCT00168090PHASE4COMPLETEDStudy of Safety and Efficacy of Antihemophilic Factor/Von Willebrand Factor Complex in Surgical Subjects With Von Willebrand Disease (vWD)
NCT00555555PHASE4ACTIVE_NOT_RECRUITINGEfficacy of Alphanate FVIII/VWF Concentrate in Type 3 Von Willebrand Patients
NCT02472665PHASE4WITHDRAWNEfficacy and Safety of Fanhdi®, a High-purity Von Willebrand Containing FVIII Concentrate, in Pediatric Patients With Von Willebrand Disease
NCT02552576PHASE4COMPLETEDStudy of Voncento® in Subjects With Von Willebrand Disease
NCT00039858PHASE4COMPLETEDEvaluation of Argatroban Injection in Pediatric Patients Requiring Anticoagulant Alternatives to Heparin
NCT00239733PHASE4TERMINATEDAnti-D for Treating Thrombocytopenia in Adults Infected With Hepatitis C Virus With or Without HIV Co-Infection
NCT00907478PHASE4COMPLETEDStudy on Bone Marrow Morphology in Adults Receiving Romiplostim for Treatment of Thrombocytopenia Associated With Immune Thrombocytopenia Purpura (ITP)
NCT01727401PHASE4TERMINATEDThromboprophylaxis of Venous Thromboembolism in Acutely-ill Medical Inpatients With Thrombocytopenia
NCT02032134PHASE4TERMINATEDProtocol for the Infusion of Buffy Coat-derived Cryopreserved Platelets in Patients With Severe Thrombocytopenia
NCT02267993PHASE4COMPLETEDEfficacy and Safety of rhTPO for the Treatment of Thrombocytopenia After Chemotherapy in AML Patients
NCT03633019PHASE4UNKNOWNHigh-dose Use of rhTPO in CIT Patients
NCT03688191PHASE4UNKNOWNStudy of Sirolimus in CTD-TP in China
NCT04906083PHASE4UNKNOWNAvatrombopag in Patients With End-stage Liver Disease and Thrombocytopenia
NCT05217719PHASE4UNKNOWNEffects of Recombinant Human Thrombopoietin on Platelet Levels in ICU Patients
NCT05255003PHASE4RECRUITINGSTrategies for Anticoagulation in Patients With thRombocytopenia and Cancer-associated Thrombosis
NCT05382013PHASE4UNKNOWNEfficacy and Safety of Avatrombopag for Treating TCP in HBV-ACLF Patients Receiving ALSS Treatment
NCT05944458PHASE4COMPLETEDEfficacy of Intravenous N-Acetylcysteine in Preventing Linezolid-Induced Thrombocytopenia in Critically Ill Patients
NCT06562738PHASE4RECRUITINGClinical Study on Efficacy and Safety of Hetrombopag in the Preoperative Patients of Thrombocytopenia
NCT06998524PHASE3RECRUITINGA Study to Assess the Efficacy and Safety of Emicizumab in Participants With Type 3 Von Willebrand Disease
NCT00387192PHASE3TERMINATEDA Study With OPTIVATE® in People With Von Willebrand Disease
NCT00404300PHASE3TERMINATEDOptivate in People With Von Willebrand Disease Undergoing Surgery
NCT01213446PHASE3COMPLETEDStudy of Biostate® in Children With Von Willebrand Disease
NCT01224808PHASE3COMPLETEDExtension Study of Biostate in Subjects With Von Willebrand Disease
NCT01410227PHASE3COMPLETEDPharmacokinetics, Safety and Efficacy of Recombinant Von Willebrand Factor (rVWF) in the Treatment of Bleeding Episodes in Von Willebrand Disease (VWD)
NCT02246881PHASE3COMPLETEDA Study to Compare the Pharmacokinetics and Safety of Current Factor VIII Concentrate and Optivate® in Haemophilia A.
NCT02283268PHASE3COMPLETEDRecombinant Von Willebrand Factor in Subjects With Severe Von Willebrand Disease Undergoing Surgery
NCT02606045PHASE3TERMINATEDMinimize Menorrhagia in Women With Von Willebrand Disease
NCT02932618PHASE3COMPLETEDA Study of Recombinant Von Willebrand Factor (rVWF) With or Without ADVATE in Children With Severe Von Willebrand Disease (VWD)
NCT02973087PHASE3COMPLETEDrVWF IN PROPHYLAXIS
NCT03879135PHASE3COMPLETEDA Study of Recombinant Von Willebrand Factor (rVWF) in Pediatric and Adult Participants With Severe Von Willebrand Disease (VWD)
NCT04052698PHASE3COMPLETEDClinical Study to Investigate the Efficacy and Safety of Wilate During Prophylaxis in Previously Treated Patients With VWD
NCT04344860PHASE3COMPLETEDPrevent Postpartum Hemorrhage in Women With Von Willebrand Disease: The VWD-WOMAN Trial
NCT04953884PHASE3COMPLETEDEfficacy, PK, Immunogenicity and Safety of Wilate in Severe Von Willebrand Disease (VWD) Patients <6 Years of Age
NCT05582993PHASE3RECRUITINGA Study of Vonicog Alfa (rVWF) in Children With Severe Von Willebrand Disease (vWD)
NCT06205095PHASE3RECRUITINGA Pilot Crossover Trial of Prophylactic Wilate Compared to Placebo for Heavy Menstrual Bleeding in Patients with VWD
NCT07115004PHASE3RECRUITINGStudy to Evaluate Subcutaneous (SC) VGA039 in Patients With Von Willebrand Disease (VWD)
NCT07129343PHASE3RECRUITINGA Study of Recombinant Von Willebrand Factor (rVWF) in Chinese Participants With Von Willebrand Disease (vWD)
NCT00037791PHASE3COMPLETEDSafety and Efficacy of (PN-152,243)/PN-196,444 in the Prevention of Thrombocytopenia
NCT00039910PHASE3COMPLETEDSafety and Efficacy of (PN-152,243)/PN-196,444 in the Prevention of Thrombocytopenia
NCT00073580PHASE3COMPLETEDAngiomax in Patients With HIT/HITTS Type II Undergoing Off-Pump Coronary Artery Bypass Grafting (CABG) (CHOOSE)

About this page

Generated deterministically by Sugi Atlas from primary biomedical databases via BioBTree. Every record on this page traces to a primary source.

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Sources 78

This page pulls from 78 datasets indexed by BioBTree:

alphafoldalphamissenseantibodybgeebgee_evidencebindingdbbiogrid_interactionbrendabrenda_kineticsccdscellosauruschembl_activitychembl_assaychembl_documentchembl_moleculechembl_targetciviccivic_evidenceclingen_dosageclingen_gene_validityclinical_trialsclinvarcollectrictd_gene_interactiondbsnpdepmapdiamond_similarityefoensemblentrezesm2_similarityexonfantom5_genefantom5_promotergenccgenerifgogoparentgtopdbgwasgwas_studyhgnchpointactinterprointogenjasparmeshmimmirdbmondomsigdborphanetorthologparalogpdbpfampharmgkb_clinicalpharmgkb_genepharmgkb_guidelinepharmgkb_variantpubchempubchem_activitypubchem_assaypubmedreactomereactomeparentrefseqrhearnacentralscxa_expressionscxa_gene_experimentsignorspliceaistring_interactiontranscriptufeatureuniprot