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P04275 (VWF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 197. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
von Willebrand factor

Short name=vWF

Cleaved into the following chain:

  1. von Willebrand antigen 2
    Alternative name(s):
    von Willebrand antigen II
Gene names
Name:VWF
Synonyms:F8VWF
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2813 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 structure

Multimeric. Interacts with F8. Ref.19 Ref.22

Subcellular location

Secreted. Secretedextracellular spaceextracellular matrix. Note: Localized to storage granules. Ref.19

Tissue specificity

Plasma.

Domain

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

Post-translational modification

All cysteine residues are involved in intrachain or interchain disulfide bonds.

N- and O-glycosylated. Ref.21 Ref.26

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.60 Ref.61

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42 Ref.43 Ref.44 Ref.45 Ref.46 Ref.47 Ref.48 Ref.49 Ref.50 Ref.51 Ref.54 Ref.55 Ref.56 Ref.57 Ref.58 Ref.59 Ref.62 Ref.65

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.52 Ref.53 Ref.60

Sequence similarities

Contains 1 CTCK (C-terminal cystine knot-like) domain.

Contains 4 TIL (trypsin inhibitory-like) domains.

Contains 3 VWFA domains.

Contains 3 VWFC domains.

Contains 4 VWFD domains.

Sequence caution

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

Ontologies

Keywords
   Biological processBlood coagulation
Cell adhesion
Hemostasis
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
von Willebrand disease
   DomainRepeat
Signal
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Isopeptide bond
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Inferred from mutant phenotype PubMed 16409464. Source: UniProtKB

blood coagulation, intrinsic pathway

Traceable author statement. Source: Reactome

cell adhesion

Inferred from direct assay PubMed 10764791. Source: UniProtKB

cell-substrate adhesion

Inferred from direct assay PubMed 9079671. Source: UniProtKB

extracellular matrix organization

Traceable author statement. Source: Reactome

hemostasis

Inferred from mutant phenotype Ref.60. Source: UniProtKB

liver development

Inferred from electronic annotation. Source: Ensembl

placenta development

Inferred from electronic annotation. Source: Ensembl

platelet activation

Inferred from direct assay PubMed 8565074. Source: UniProtKB

platelet degranulation

Traceable author statement. Source: Reactome

protein homooligomerization

Inferred from direct assay PubMed 8874190. Source: UniProtKB

response to wounding

Traceable author statement PubMed 15029268. Source: UniProtKB

   Cellular_componentWeibel-Palade body

Inferred from direct assay PubMed 3082891PubMed 3087627. Source: UniProtKB

endoplasmic reticulum

Inferred from direct assay PubMed 6754744. Source: UniProtKB

external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

extracellular matrix

Inferred from direct assay PubMed 6754744. Source: UniProtKB

extracellular region

Inferred from direct assay Ref.60. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

platelet alpha granule

Non-traceable author statement PubMed 9759493. Source: UniProtKB

platelet alpha granule lumen

Traceable author statement. Source: Reactome

proteinaceous extracellular matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionchaperone binding

Inferred from direct assay Ref.60. Source: UniProtKB

collagen binding

Inferred from direct assay PubMed 2056120. Source: UniProtKB

glycoprotein binding

Inferred from direct assay PubMed 16409464. Source: UniProtKB

identical protein binding

Inferred from physical interaction PubMed 21857647. Source: IntAct

immunoglobulin binding

Inferred from direct assay PubMed 3121636. Source: UniProtKB

integrin binding

Inferred from physical interaction PubMed 9079671. Source: UniProtKB

protease binding

Inferred from physical interaction PubMed 12775718. Source: UniProtKB

protein N-terminus binding

Inferred from physical interaction PubMed 7721887. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 11943773PubMed 16912226PubMed 2839553PubMed 7756647. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay Ref.60. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Ref.7
Chain23 – 763741von Willebrand antigen 2
PRO_0000022682
Chain764 – 28132050von Willebrand factor
PRO_0000022683

Regions

Domain34 – 240207VWFD 1
Domain295 – 34854TIL 1
Domain387 – 598212VWFD 2
Domain652 – 70756TIL 2
Domain776 – 82752TIL 3
Domain866 – 1074209VWFD 3
Domain1146 – 119651TIL 4
Domain1277 – 1453177VWFA 1; binding site for platelet glycoprotein Ib
Domain1498 – 1665168VWFA 2
Domain1691 – 1871181VWFA 3; main binding site for collagens type I and III
Domain1949 – 2153205VWFD 4
Domain2255 – 232874VWFC 1
Domain2429 – 249567VWFC 2
Domain2580 – 264566VWFC 3
Domain2724 – 281289CTCK
Region764 – 78724Amino-terminal
Region788 – 83346E1
Region826 – 85328CX
Region2216 – 226146E2
Motif2507 – 25093Cell attachment site

Amino acid modifications

Glycosylation991N-linked (GlcNAc...) Potential
Glycosylation1561N-linked (GlcNAc...) Potential
Glycosylation2111N-linked (GlcNAc...) Potential
Glycosylation6661N-linked (GlcNAc...) Potential
Glycosylation8571N-linked (GlcNAc...)
Glycosylation11471N-linked (GlcNAc...); atypical
Glycosylation12311N-linked (GlcNAc...)
Glycosylation12481O-linked (GalNAc...) Probable
Glycosylation12551O-linked (GalNAc...) Probable
Glycosylation12561O-linked (GalNAc...) Probable
Glycosylation12631O-linked (GalNAc...) Probable Ref.8
Glycosylation14681O-linked (GalNAc...) Probable
Glycosylation14771O-linked (GalNAc...) Probable
Glycosylation14861O-linked (GalNAc...) Probable
Glycosylation14871O-linked (GalNAc...) Probable
Glycosylation15151N-linked (GlcNAc...) (complex) Ref.23 Ref.26
Glycosylation15741N-linked (GlcNAc...)
Glycosylation16791O-linked (GalNAc...) Probable
Glycosylation22231N-linked (GlcNAc...)
Glycosylation22901N-linked (GlcNAc...)
Glycosylation22981O-linked (GalNAc...) Probable
Glycosylation23571N-linked (GlcNAc...)
Glycosylation24001N-linked (GlcNAc...)
Glycosylation25461N-linked (GlcNAc...) Ref.25
Glycosylation25851N-linked (GlcNAc...)
Glycosylation27901N-linked (GlcNAc...)
Disulfide bond767 ↔ 808 Ref.20
Disulfide bond776 ↔ 804 Ref.20
Disulfide bond810 ↔ 821 Ref.20
Disulfide bond867 ↔ 996 Ref.20
Disulfide bond889 ↔ 1031 Ref.20
Disulfide bond898 ↔ 993 Ref.20
Disulfide bond914 ↔ 921 Ref.20
Disulfide bond1060 ↔ 1084 Ref.20
Disulfide bond1071 ↔ 1111 Ref.20
Disulfide bond1089 ↔ 1091 Ref.20
Disulfide bond1126 ↔ 1130 Ref.20
Disulfide bond1149 ↔ 1169 Ref.20
Disulfide bond1153 ↔ 1165 Ref.20
Disulfide bond1196 ↔ 1199 Ref.20
Disulfide bond1234 ↔ 1237 Ref.20
Disulfide bond1272 ↔ 1458 Ref.20
Disulfide bond1669 ↔ 1670 Ref.20
Disulfide bond1686 ↔ 1872 Ref.20
Disulfide bond1879 ↔ 1904 Ref.20
Disulfide bond1899 ↔ 1940Or C-1899 with C-1942 Ref.20
Disulfide bond1927 ↔ 2088 Ref.20
Disulfide bond1950 ↔ 2085 Ref.20
Disulfide bond1972 ↔ 2123 Ref.20
Disulfide bond1993 ↔ 2001 Ref.20
Disulfide bond2724 ↔ 2774 By similarity
Disulfide bond2739 ↔ 2788 By similarity
Disulfide bond2750 ↔ 2804 By similarity
Disulfide bond2754 ↔ 2806 By similarity
Disulfide bond? ↔ 2811 By similarity
Cross-link1720Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.24

Natural variations

Natural variant2731R → W in VWD1 and VWD3; defect in secretion and formation of multimers. Ref.60
Corresponds to variant rs61753997 [ dbSNP | Ensembl ].
VAR_010242
Natural variant3181N → K.
Corresponds to variant rs1800387 [ dbSNP | Ensembl ].
VAR_057023
Natural variant3771W → C in VWD3. Ref.53
VAR_005782
Natural variant4711V → I. Ref.2
Corresponds to variant rs1800377 [ dbSNP | Ensembl ].
VAR_060591
Natural variant4841H → R. Ref.4
Corresponds to variant rs1800378 [ dbSNP | Ensembl ].
VAR_024553
Natural variant5281N → S in VWD2. Ref.54
VAR_005783
Natural variant5501G → R in VWD2. Ref.58
VAR_005784
Natural variant7401M → I.
Corresponds to variant rs16932374 [ dbSNP | Ensembl ].
VAR_057024
Natural variant7881C → Y in VWD2.
VAR_009141
Natural variant7891T → A. Ref.9
Corresponds to variant rs1063856 [ dbSNP | Ensembl ].
VAR_005785
Natural variant7911T → M in VWD2; Normandy type. Ref.38
VAR_005786
Natural variant8161R → W in VWD2; Normandy type. Ref.33
VAR_005787
Natural variant8521Q → R. Ref.1 Ref.2 Ref.4 Ref.8 Ref.9 Ref.11
Corresponds to variant rs216321 [ dbSNP | Ensembl ].
VAR_005788
Natural variant8541R → Q in VWD2; Normandy type. Ref.33
Corresponds to variant rs41276738 [ dbSNP | Ensembl ].
VAR_005789
Natural variant8571N → D.
VAR_005790
Natural variant8851F → S.
Corresponds to variant rs11064002 [ dbSNP | Ensembl ].
VAR_057025
Natural variant10601C → R in VWD2. Ref.62
VAR_028446
Natural variant11491C → R in VWD1; reduced secretion of homodimers and heterodimers with wild type VWD and increased degradation by the proteasome. Ref.61
VAR_064925
Natural variant12661P → L in VWD2. Ref.49
VAR_005791
Natural variant12681H → D in VWD2. Ref.48
VAR_005792
Natural variant12721C → F in VWD2; subtype 2A. Ref.65
VAR_067340
Natural variant12721C → R in VWD2. Ref.42
VAR_005793
Natural variant13061R → W in VWD2. Ref.35 Ref.36 Ref.40 Ref.41
VAR_005794
Natural variant13081R → C in VWD2. Ref.34 Ref.35 Ref.36 Ref.41
VAR_005795
Natural variant13131W → C in VWD2. Ref.37
VAR_005796
Natural variant13141V → L in VWD2. Ref.41
VAR_005797
Natural variant13161V → M in VWD2. Ref.36 Ref.39 Ref.40
VAR_005798
Natural variant13181V → L in VWD2. Ref.41
VAR_005799
Natural variant13241G → S in VWD2. Ref.44
VAR_005800
Natural variant13411R → Q in VWD2. Ref.36
VAR_005801
Natural variant13741R → C in VWD2. Ref.55
VAR_005802
Natural variant13741R → H in VWD2. Ref.55 Ref.56
VAR_005803
Natural variant13811T → A. Ref.1 Ref.2 Ref.4 Ref.8 Ref.9 Ref.11 Ref.12 Ref.13
Corresponds to variant rs216311 [ dbSNP | Ensembl ].
VAR_005804
Natural variant13991R → H. Ref.36
Corresponds to variant rs216312 [ dbSNP | Ensembl ].
VAR_005805
Natural variant14601L → V in VWD2. Ref.50
VAR_005806
Natural variant14611A → V in VWD2. Ref.57
VAR_005807
Natural variant14721D → H. Ref.1 Ref.2 Ref.12
Corresponds to variant rs1800383 [ dbSNP | Ensembl ].
VAR_029656
Natural variant15141F → C in VWD2. Ref.46
VAR_005808
Natural variant15401L → P in VWD2. Ref.51
VAR_005809
Natural variant15651V → L.
Corresponds to variant rs1800385 [ dbSNP | Ensembl ].
VAR_014630
Natural variant15701Y → C in a breast cancer sample; somatic mutation. Ref.64
VAR_036276
Natural variant15841Y → C Exhibits increased in susceptibility to proteolysis by ADAMTS13. Ref.47 Ref.63
Corresponds to variant rs1800386 [ dbSNP | Ensembl ].
VAR_005810
Natural variant15971R → G in VWD2. Ref.47
VAR_005811
Natural variant15971R → Q in VWD2. Ref.45
VAR_005812
Natural variant15971R → W in VWD2. Ref.31
VAR_005813
Natural variant16071V → D in VWD2. Ref.31
VAR_005814
Natural variant16091G → R in VWD2. Ref.45 Ref.47
VAR_005815
Natural variant16131S → P in VWD2. Ref.35
VAR_005816
Natural variant16281I → T in VWD2. Ref.32 Ref.40 Ref.51
VAR_005817
Natural variant16381E → K in VWD2. Ref.43
VAR_005818
Natural variant16481P → S in VWD2. Ref.40
VAR_005819
Natural variant16651V → E in VWD2. Ref.45
VAR_005820
Natural variant20631P → S in VWD3.
Corresponds to variant rs61750615 [ dbSNP | Ensembl ].
VAR_009142
Natural variant21781A → S.
Corresponds to variant rs34230288 [ dbSNP | Ensembl ].
VAR_057026
Natural variant21851R → Q.
Corresponds to variant rs2229446 [ dbSNP | Ensembl ].
VAR_057027
Natural variant23621C → F in VWD3.
VAR_009143
Natural variant25461N → Y in VWD3.
VAR_009144
Natural variant27051G → R.
Corresponds to variant rs7962217 [ dbSNP | Ensembl ].
VAR_057028
Natural variant27391C → Y in VWD3. Ref.52
VAR_005821
Natural variant27731C → R in VWD2. Ref.59
VAR_005822

Experimental info

Mutagenesis11491C → R: Reduced secretion and increased intracellular retention. Similar phenotype; when associated with S-1169. Ref.61
Mutagenesis11691C → S: Reduced secretion and increased intracellular retention. Similar phenotype; when associated with R-1149. Ref.61
Sequence conflict7701P → H in AAB59512. Ref.9
Sequence conflict8041C → S AA sequence Ref.8
Sequence conflict8041C → S in AAB59512. Ref.9
Sequence conflict19141S → T in CAA27972. Ref.1
Sequence conflict21681C → S AA sequence Ref.8

Secondary structure

............................................................................................................. 2813
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04275 [UniParc].

Last modified January 11, 2011. Version 4.
Checksum: D5C1C78360917C29

FASTA2,813309,265
        10         20         30         40         50         60 
MIPARFAGVL LALALILPGT LCAEGTRGRS STARCSLFGS DFVNTFDGSM YSFAGYCSYL 

        70         80         90        100        110        120 
LAGGCQKRSF SIIGDFQNGK RVSLSVYLGE FFDIHLFVNG TVTQGDQRVS MPYASKGLYL 

       130        140        150        160        170        180 
ETEAGYYKLS GEAYGFVARI DGSGNFQVLL SDRYFNKTCG LCGNFNIFAE DDFMTQEGTL 

       190        200        210        220        230        240 
TSDPYDFANS WALSSGEQWC ERASPPSSSC NISSGEMQKG LWEQCQLLKS TSVFARCHPL 

       250        260        270        280        290        300 
VDPEPFVALC EKTLCECAGG LECACPALLE YARTCAQEGM VLYGWTDHSA CSPVCPAGME 

       310        320        330        340        350        360 
YRQCVSPCAR TCQSLHINEM CQERCVDGCS CPEGQLLDEG LCVESTECPC VHSGKRYPPG 

       370        380        390        400        410        420 
TSLSRDCNTC ICRNSQWICS NEECPGECLV TGQSHFKSFD NRYFTFSGIC QYLLARDCQD 

       430        440        450        460        470        480 
HSFSIVIETV QCADDRDAVC TRSVTVRLPG LHNSLVKLKH GAGVAMDGQD VQLPLLKGDL 

       490        500        510        520        530        540 
RIQHTVTASV RLSYGEDLQM DWDGRGRLLV KLSPVYAGKT CGLCGNYNGN QGDDFLTPSG 

       550        560        570        580        590        600 
LAEPRVEDFG NAWKLHGDCQ DLQKQHSDPC ALNPRMTRFS EEACAVLTSP TFEACHRAVS 

       610        620        630        640        650        660 
PLPYLRNCRY DVCSCSDGRE CLCGALASYA AACAGRGVRV AWREPGRCEL NCPKGQVYLQ 

       670        680        690        700        710        720 
CGTPCNLTCR SLSYPDEECN EACLEGCFCP PGLYMDERGD CVPKAQCPCY YDGEIFQPED 

       730        740        750        760        770        780 
IFSDHHTMCY CEDGFMHCTM SGVPGSLLPD AVLSSPLSHR SKRSLSCRPP MVKLVCPADN 

       790        800        810        820        830        840 
LRAEGLECTK TCQNYDLECM SMGCVSGCLC PPGMVRHENR CVALERCPCF HQGKEYAPGE 

       850        860        870        880        890        900 
TVKIGCNTCV CQDRKWNCTD HVCDATCSTI GMAHYLTFDG LKYLFPGECQ YVLVQDYCGS 

       910        920        930        940        950        960 
NPGTFRILVG NKGCSHPSVK CKKRVTILVE GGEIELFDGE VNVKRPMKDE THFEVVESGR 

       970        980        990       1000       1010       1020 
YIILLLGKAL SVVWDRHLSI SVVLKQTYQE KVCGLCGNFD GIQNNDLTSS NLQVEEDPVD 

      1030       1040       1050       1060       1070       1080 
FGNSWKVSSQ CADTRKVPLD SSPATCHNNI MKQTMVDSSC RILTSDVFQD CNKLVDPEPY 

      1090       1100       1110       1120       1130       1140 
LDVCIYDTCS CESIGDCACF CDTIAAYAHV CAQHGKVVTW RTATLCPQSC EERNLRENGY 

      1150       1160       1170       1180       1190       1200 
ECEWRYNSCA PACQVTCQHP EPLACPVQCV EGCHAHCPPG KILDELLQTC VDPEDCPVCE 

      1210       1220       1230       1240       1250       1260 
VAGRRFASGK KVTLNPSDPE HCQICHCDVV NLTCEACQEP GGLVVPPTDA PVSPTTLYVE 

      1270       1280       1290       1300       1310       1320 
DISEPPLHDF YCSRLLDLVF LLDGSSRLSE AEFEVLKAFV VDMMERLRIS QKWVRVAVVE 

      1330       1340       1350       1360       1370       1380 
YHDGSHAYIG LKDRKRPSEL RRIASQVKYA GSQVASTSEV LKYTLFQIFS KIDRPEASRI 

      1390       1400       1410       1420       1430       1440 
TLLLMASQEP QRMSRNFVRY VQGLKKKKVI VIPVGIGPHA NLKQIRLIEK QAPENKAFVL 

      1450       1460       1470       1480       1490       1500 
SSVDELEQQR DEIVSYLCDL APEAPPPTLP PDMAQVTVGP GLLGVSTLGP KRNSMVLDVA 

      1510       1520       1530       1540       1550       1560 
FVLEGSDKIG EADFNRSKEF MEEVIQRMDV GQDSIHVTVL QYSYMVTVEY PFSEAQSKGD 

      1570       1580       1590       1600       1610       1620 
ILQRVREIRY QGGNRTNTGL ALRYLSDHSF LVSQGDREQA PNLVYMVTGN PASDEIKRLP 

      1630       1640       1650       1660       1670       1680 
GDIQVVPIGV GPNANVQELE RIGWPNAPIL IQDFETLPRE APDLVLQRCC SGEGLQIPTL 

      1690       1700       1710       1720       1730       1740 
SPAPDCSQPL DVILLLDGSS SFPASYFDEM KSFAKAFISK ANIGPRLTQV SVLQYGSITT 

      1750       1760       1770       1780       1790       1800 
IDVPWNVVPE KAHLLSLVDV MQREGGPSQI GDALGFAVRY LTSEMHGARP GASKAVVILV 

      1810       1820       1830       1840       1850       1860 
TDVSVDSVDA AADAARSNRV TVFPIGIGDR YDAAQLRILA GPAGDSNVVK LQRIEDLPTM 

      1870       1880       1890       1900       1910       1920 
VTLGNSFLHK LCSGFVRICM DEDGNEKRPG DVWTLPDQCH TVTCQPDGQT LLKSHRVNCD 

      1930       1940       1950       1960       1970       1980 
RGLRPSCPNS QSPVKVEETC GCRWTCPCVC TGSSTRHIVT FDGQNFKLTG SCSYVLFQNK 

      1990       2000       2010       2020       2030       2040 
EQDLEVILHN GACSPGARQG CMKSIEVKHS ALSVELHSDM EVTVNGRLVS VPYVGGNMEV 

      2050       2060       2070       2080       2090       2100 
NVYGAIMHEV RFNHLGHIFT FTPQNNEFQL QLSPKTFASK TYGLCGICDE NGANDFMLRD 

      2110       2120       2130       2140       2150       2160 
GTVTTDWKTL VQEWTVQRPG QTCQPILEEQ CLVPDSSHCQ VLLLPLFAEC HKVLAPATFY 

      2170       2180       2190       2200       2210       2220 
AICQQDSCHQ EQVCEVIASY AHLCRTNGVC VDWRTPDFCA MSCPPSLVYN HCEHGCPRHC 

      2230       2240       2250       2260       2270       2280 
DGNVSSCGDH PSEGCFCPPD KVMLEGSCVP EEACTQCIGE DGVQHQFLEA WVPDHQPCQI 

      2290       2300       2310       2320       2330       2340 
CTCLSGRKVN CTTQPCPTAK APTCGLCEVA RLRQNADQCC PEYECVCDPV SCDLPPVPHC 

      2350       2360       2370       2380       2390       2400 
ERGLQPTLTN PGECRPNFTC ACRKEECKRV SPPSCPPHRL PTLRKTQCCD EYECACNCVN 

      2410       2420       2430       2440       2450       2460 
STVSCPLGYL ASTATNDCGC TTTTCLPDKV CVHRSTIYPV GQFWEEGCDV CTCTDMEDAV 

      2470       2480       2490       2500       2510       2520 
MGLRVAQCSQ KPCEDSCRSG FTYVLHEGEC CGRCLPSACE VVTGSPRGDS QSSWKSVGSQ 

      2530       2540       2550       2560       2570       2580 
WASPENPCLI NECVRVKEEV FIQQRNVSCP QLEVPVCPSG FQLSCKTSAC CPSCRCERME 

      2590       2600       2610       2620       2630       2640 
ACMLNGTVIG PGKTVMIDVC TTCRCMVQVG VISGFKLECR KTTCNPCPLG YKEENNTGEC 

      2650       2660       2670       2680       2690       2700 
CGRCLPTACT IQLRGGQIMT LKRDETLQDG CDTHFCKVNE RGEYFWEKRV TGCPPFDEHK 

      2710       2720       2730       2740       2750       2760 
CLAEGGKIMK IPGTCCDTCE EPECNDITAR LQYVKVGSCK SEVEVDIHYC QGKCASKAMY 

      2770       2780       2790       2800       2810 
SIDINDVQDQ CSCCSPTRTE PMQVALHCTN GSVVYHEVLN AMECKCSPRK CSK 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of pre-pro-von Willebrand factor cDNA."
Bonthron D., Orr E.C., Mitsock L.M., Ginsburg D., Handin R.I., Orkin S.H.
Nucleic Acids Res. 14:7125-7128(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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. expand/collapse author list , 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]"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, VARIANTS ARG-484; ARG-852 AND ALA-1381.
[5]Erratum
Verweij C.L., Diergaarde P.J., Hart M., Pannekoek H.
EMBO J. 5:3074-3074(1986)
[6]"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.
[7]"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, PROTEIN SEQUENCE OF 23-56.
Tissue: Umbilical vein endothelial cell.
[8]"Amino acid sequence of human von Willebrand factor."
Titani K., Kumar S., Takio K., Ericsson L.H., Wade R.D., Ashida K., Walsh K.A., Chopek M.W., Sadler J.E., Fujikawa K.
Biochemistry 25:3171-3184(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 764-2813, VARIANTS ARG-852 AND ALA-1381.
[9]"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, VARIANTS ALA-789; ARG-852 AND ALA-1381.
[10]"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.
[11]"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, VARIANTS ARG-852 AND ALA-1381.
[12]"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.
[13]"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, VARIANT ALA-1381.
[14]"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.
[15]"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.
[16]Lynch D.C.
Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[17]"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.
[18]"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.
[19]"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.
[20]"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.
[21]"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.
[22]"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.
[23]"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.
[24]"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.
[25]"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.
[26]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-1515.
[27]"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.
[28]"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.
[29]"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.
[30]"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.
[31]"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.
[32]"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.
[33]"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.
[34]"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.
[35]"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.
[36]"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.
[37]"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.
[38]"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.
[39]"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.
[40]"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.
[41]"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.
[42]"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.
[43]"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.
[44]"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.
[45]"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.
[46]"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.
[47]"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.
[48]"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.
[49]"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.
[50]"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.
[51]"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.
[52]"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.
[53]"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.
[54]"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.
[55]"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.
[56]"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.
[57]"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.
[58]"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.
[59]"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.
[60]"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.
[61]"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.
[62]"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.
[63]"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.
[64]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-1570.
[65]"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.
+Additional computationally mapped references.

Web resources

vWF

von Willebrand factor (vWF) mutation db

Wikipedia

Von Willebrand factor entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X04385 mRNA. Translation: CAA27972.1.
M25865 expand/collapse EMBL AC list , 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.
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.
CCDSCCDS8539.1.
PIRVWHU. A34480.
RefSeqNP_000543.2. NM_000552.3.
UniGeneHs.440848.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP04275.
SMRP04275. Positions 1261-1468, 1495-1671, 1685-1873, 2721-2813.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113289. 15 interactions.
DIPDIP-29667N.
IntActP04275. 48 interactions.
MINTMINT-244925.
STRING9606.ENSP00000261405.

Chemistry

ChEMBLCHEMBL2021748.
DrugBankDB00025. Antihemophilic Factor.

Protein family/group databases

MEROPSI08.950.

PTM databases

PhosphoSiteP04275.
UniCarbKBP04275.

Polymorphism databases

DMDM317373549.

Proteomic databases

PaxDbP04275.
PRIDEP04275.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261405; ENSP00000261405; ENSG00000110799.
GeneID7450.
KEGGhsa:7450.
UCSCuc001qnn.1. human.

Organism-specific databases

CTD7450.
GeneCardsGC12M006058.
GeneReviewsVWF.
H-InvDBHIX0010356.
HIX0171640.
HGNCHGNC:12726. VWF.
HPACAB001694.
HPA001815.
HPA002082.
MIM193400. phenotype.
277480. phenotype.
613160. gene.
613554. phenotype.
neXtProtNX_P04275.
Orphanet166078. 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.
PharmGKBPA37337.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000169747.
HOVERGENHBG004380.
InParanoidP04275.
KOK03900.
OMAECCGRCL.
OrthoDBEOG73V6J9.
PhylomeDBP04275.
TreeFamTF300299.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_118779. Extracellular matrix organization.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP04275.
BgeeP04275.
CleanExHS_VWF.
GenevestigatorP04275.

Family and domain databases

Gene3D3.40.50.410. 3 hits.
InterProIPR006207. 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]
PfamPF08742. C8. 4 hits.
PF01826. TIL. 5 hits.
PF00092. VWA. 3 hits.
PF00093. VWC. 2 hits.
PF00094. VWD. 4 hits.
[Graphical view]
PIRSFPIRSF002495. VWF. 1 hit.
SMARTSM00832. C8. 4 hits.
SM00041. CT. 1 hit.
SM00327. VWA. 3 hits.
SM00214. VWC. 5 hits.
SM00216. VWD. 4 hits.
[Graphical view]
SUPFAMSSF53300. SSF53300. 3 hits.
SSF57567. SSF57567. 5 hits.
PROSITEPS01185. 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]
ProtoNetSearch...

Other

ChiTaRSVWF. human.
EvolutionaryTraceP04275.
GeneWikiVon_Willebrand_factor.
GenomeRNAi7450.
NextBio29172.
PROP04275.
SOURCESearch...

Entry information

Entry nameVWF_HUMAN
AccessionPrimary (citable) accession number: P04275
Secondary accession number(s): Q99806
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 197 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM