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Reviewed, UniProtKB/Swiss-Prot P04275 (VWF_HUMAN)

Last modified October 13, 2009. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    von Willebrand factor
      Short name=vWF
Cleaved into the following chain:
    1- Recommended name:
            von Willebrand antigen 2
        Alternative name(s):
            von Willebrand antigen II
Gene names
Name: VWF
Synonyms: F8VWF
OrganismHomo sapiens (Human) [Complete 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.18 Ref.21

Subcellular location

Secreted. Secretedextracellular spaceextracellular matrix. Note: Localized to storage granules. Ref.18

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.20 Ref.22 Ref.24

Involvement in disease

Defects in VWF are associated with various forms of von Willebrand disease (VWD) [MIM:193400, 277480]. VWD is characterized by frequent bleeding (gingival, minor skin quantitative lacerations, menorrhagia, etc.). Type I VWD is associated with a deficiency of VWF; type II by normal to decreased plasma level of VWF; type III by a virtual absence of VWF. There are subtypes (A to H) of type II VWD; for example: type IIA is characterized by the absence of VWF high molecular weight multimers in plasma. Ref.29 Ref.30 Ref.32 Ref.33 Ref.34 Ref.35 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.52 Ref.53 Ref.54 Ref.55 Ref.56 Ref.57 Ref.58 Ref.59

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.

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
Gene Ontology (GO)
   Biological processcell-substrate adhesion

Inferred from direct assay. Source: UniProtKB

platelet activation

Inferred from direct assay. Source: UniProtKB

protein homooligomerization

Inferred from direct assay. Source: UniProtKB

   Cellular componentWeibel-Palade body

Inferred from direct assay. Source: UniProtKB

endoplasmic reticulum

Inferred from direct assay. Source: UniProtKB

platelet alpha granule

Non-traceable author statement. Source: UniProtKB

proteinaceous extracellular matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionchaperone binding Ref.58

Inferred from direct assay. Source: UniProtKB

collagen binding

Inferred from direct assay. Source: UniProtKB

glycoprotein binding

Inferred from direct assay. Source: UniProtKB

immunoglobulin binding

Inferred from direct assay. Source: UniProtKB

integrin binding

Inferred from physical interaction. Source: UniProtKB

protease binding

Inferred from physical interaction. Source: UniProtKB

protein N-terminus binding

Inferred from physical interaction. Source: UniProtKB

protein homodimerization activity Ref.58

Inferred from direct assay. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ADAMTS13Q76LX82EBI-981819,EBI-981764
GP1BAP073592EBI-981819,EBI-297082

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Ref.6
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.7
Glycosylation14681O-linked (GalNAc...) Probable
Glycosylation14771O-linked (GalNAc...) Probable
Glycosylation14861O-linked (GalNAc...) Probable
Glycosylation14871O-linked (GalNAc...) Probable
Glycosylation15151N-linked (GlcNAc...) Ref.22
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.24
Glycosylation25851N-linked (GlcNAc...)
Glycosylation27901N-linked (GlcNAc...)
Disulfide bond767 ↔ 808 Ref.19
Disulfide bond776 ↔ 804 Ref.19
Disulfide bond810 ↔ 821 Ref.19
Disulfide bond867 ↔ 996 Ref.19
Disulfide bond889 ↔ 1031 Ref.19
Disulfide bond898 ↔ 993 Ref.19
Disulfide bond914 ↔ 921 Ref.19
Disulfide bond1060 ↔ 1084 Ref.19
Disulfide bond1071 ↔ 1111 Ref.19
Disulfide bond1089 ↔ 1091 Ref.19
Disulfide bond1126 ↔ 1130 Ref.19
Disulfide bond1149 ↔ 1169 Ref.19
Disulfide bond1153 ↔ 1165 Ref.19
Disulfide bond1196 ↔ 1199 Ref.19
Disulfide bond1234 ↔ 1237 Ref.19
Disulfide bond1272 ↔ 1458 Ref.19
Disulfide bond1669 ↔ 1670 Ref.19
Disulfide bond1686 ↔ 1872 Ref.19
Disulfide bond1879 ↔ 1904 Ref.19
Disulfide bond1899 ↔ 1940Or C-1899 with C-1942 Ref.19
Disulfide bond1927 ↔ 2088 Ref.19
Disulfide bond1950 ↔ 2085 Ref.19
Disulfide bond1972 ↔ 2123 Ref.19
Disulfide bond1993 ↔ 2001 Ref.19
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.23

Natural variations

Natural variant2731R → W in VWD; type I/III; defect in secretion and formation of multimers. Ref.58
VAR_010242
Natural variant3181N → K: dbSNP rs1800387.
VAR_057023
Natural variant3771W → C in VWD; type III. Ref.51
VAR_005782
Natural variant4841H → R: dbSNP rs1800378. Ref.3
VAR_024553
Natural variant5281N → S in VWD; type IIC. Ref.52
VAR_005783
Natural variant5501G → R in VWD; type IIC. Ref.56
VAR_005784
Natural variant7401M → I: dbSNP rs16932374.
VAR_057024
Natural variant7881C → Y in VWD; type II.
VAR_009141
Natural variant7891T → A: dbSNP rs1063856.
VAR_005785
Natural variant7911T → M in Normandy-1. Ref.36
VAR_005786
Natural variant8161R → W in Normandy-2. Ref.31
VAR_005787
Natural variant8521R → Q: dbSNP rs216321.
VAR_005788
Natural variant8541R → Q in Normandy-3. Ref.31
VAR_005789
Natural variant8571N → D
VAR_005790
Natural variant8851F → S: dbSNP rs11064002.
VAR_057025
Natural variant10601C → R in VWD; type IIN. Ref.59
VAR_028446
Natural variant12661P → L in VWD; type I. Ref.47
VAR_005791
Natural variant12681H → D in VWD; type IIB. Ref.46
VAR_005792
Natural variant12721C → R in VWD; type IIA. Ref.40
VAR_005793
Natural variant13061R → W in VWD; type IIB. Ref.33 Ref.34 Ref.38 Ref.39
VAR_005794
Natural variant13081R → C in VWD; type IIB. Ref.32 Ref.33 Ref.34 Ref.39
VAR_005795
Natural variant13131W → C in VWD; type IIB. Ref.35
VAR_005796
Natural variant13141V → L in VWD; type IIB. Ref.39
VAR_005797
Natural variant13161V → M in VWD; type IIB. Ref.34 Ref.37 Ref.38
VAR_005798
Natural variant13181V → L in VWD; type IIB. Ref.39
VAR_005799
Natural variant13241G → S in VWD; type IIB. Ref.42
VAR_005800
Natural variant13411R → Q in VWD; type IIB. Ref.34
VAR_005801
Natural variant13741R → C in VWD. Ref.53
VAR_005802
Natural variant13741R → H in VWD. Ref.53 Ref.54
VAR_005803
Natural variant13811A → T: dbSNP rs216311.
VAR_005804
Natural variant13991R → H: dbSNP rs216312. Ref.34
VAR_005805
Natural variant14601L → V in VWD; type IIB. Ref.48
VAR_005806
Natural variant14611A → V in VWD; type IIB. Ref.55
VAR_005807
Natural variant14721H → D: dbSNP rs1800383. Ref.7 Ref.12
VAR_029656
Natural variant15141F → C in VWD; type IIA. Ref.44
VAR_005808
Natural variant15401L → P in VWD; type IIA. Ref.49
VAR_005809
Natural variant15651V → L: dbSNP rs1800385.
VAR_014630
Natural variant15701Y → C in a breast cancer sample; somatic mutation. Ref.60
VAR_036276
Natural variant15841Y → C: dbSNP rs1800386. Ref.45
VAR_005810
Natural variant15971R → G in VWD; type IIA. Ref.45
VAR_005811
Natural variant15971R → Q in VWD; type IIA. Ref.43
VAR_005812
Natural variant15971R → W in VWD; type IIA. Ref.29
VAR_005813
Natural variant16071V → D in VWD; type IIA. Ref.29
VAR_005814
Natural variant16091G → R in VWD; type IIA. Ref.43 Ref.45
VAR_005815
Natural variant16131S → P in VWD; type IIA. Ref.33
VAR_005816
Natural variant16281I → T in VWD; type IIA. Ref.30 Ref.38 Ref.49
VAR_005817
Natural variant16381E → K in VWD; type IIA. Ref.41
VAR_005818
Natural variant16481P → S in VWD; type IIA. Ref.38
VAR_005819
Natural variant16651V → E in VWD; type IIA. Ref.43
VAR_005820
Natural variant20631P → S in VWD; type III.
VAR_009142
Natural variant21781A → S: dbSNP rs34230288.
VAR_057026
Natural variant21851R → Q: dbSNP rs2229446.
VAR_057027
Natural variant23621C → F in VWD; type III.
VAR_009143
Natural variant25461N → Y in VWD; type III.
VAR_009144
Natural variant27051G → R: dbSNP rs7962217.
VAR_057028
Natural variant27391C → Y in VWD; type III. Ref.50
VAR_005821
Natural variant27731C → R in VWD; type IID. Ref.57
VAR_005822

Experimental info

Sequence conflict4711I → V in CAA27972. Ref.1
Sequence conflict4711I → V in CAA27765. Ref.3
Sequence conflict7701P → H in AAB59512. Ref.8
Sequence conflict8041C → S AA sequence Ref.7
Sequence conflict8041C → S in AAB59512. Ref.8
Sequence conflict8041C → S Ref.10
Sequence conflict19141S → T in CAA27972. Ref.1
Sequence conflict21681C → S AA sequence Ref.7

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P04275-1 [UniParc].

Last modified July 1, 1993. Version 2.
Checksum: 4B98F8EA3C082DCC

FASTA2,813309,299
        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 IQLPLLKGDL 

       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 CRDRKWNCTD 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 
ALLLMASQEP QRMSRNFVRY VQGLKKKKVI VIPVGIGPHA NLKQIRLIEK QAPENKAFVL 

      1450       1460       1470       1480       1490       1500 
SSVDELEQQR DEIVSYLCDL APEAPPPTLP PHMAQVTVGP 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: 3489923] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 2584182] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"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: 3019665] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1400, VARIANT ARG-484.
[4]Erratum
Verweij C.L., Diergaarde P.J., Hart M., Pannekoek H.
EMBO J. 5:3074-3074(1986)
[5]"The human von Willebrand factor gene. Structure of the 5' region."
Bonthron D., Orkin S.H.
Eur. J. Biochem. 171:51-57(1988) [PubMed: 2828057] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-177.
[6]"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: 3495266] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-120, PROTEIN SEQUENCE OF 23-56.
Tissue: Umbilical vein endothelial cell.
[7]"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: 3524673] [Abstract]
Cited for: PROTEIN SEQUENCE OF 764-2813, VARIANT ASP-1472.
[8]"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: 2864688] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 764-873 AND 1289-2813.
[9]"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: 12665801] [Abstract]
Cited for: PROTEIN SEQUENCE OF 764-782.
Tissue: Platelet.
[10]"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: 3488076] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 781-1424.
[11]"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: 1988024] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 990-1947.
[12]"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: 9373253] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1236-1476, VARIANT ASP-1472.
[13]"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: 3874428] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2621-2813.
[14]"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: 3873280] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2731-2813.
[15]Lynch D.C.
Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[16]"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: 3875078] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2731-2813.
[17]"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: 3496594] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2731-2813.
[18]"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: 10961880] [Abstract]
Cited for: SUBUNIT, SUBCELLULAR LOCATION.
[19]"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: 3502076] [Abstract]
Cited for: DISULFIDE BONDS.
[20]"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: 3089784] [Abstract]
Cited for: STRUCTURE OF CARBOHYDRATES.
[21]"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: 9218428] [Abstract]
Cited for: INTERACTION WITH F8.
[22]"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: 14760718] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1515, MASS SPECTROMETRY.
Tissue: Plasma.
[23]"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: 17370265] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-1720, MASS SPECTROMETRY.
[24]"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: 19159218] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2546, MASS SPECTROMETRY.
Tissue: Liver.
[25]"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: 9553097] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1261-1468.
[26]"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: 9331419] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1685-1873.
[27]"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: 9312128] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1686-1872.
[28]"von Willebrand factor, platelets and endothelial cell interactions."
Ruggeri Z.M.
J. Thromb. Haemost. 1:1335-1342(2003) [PubMed: 12871266] [Abstract]
Cited for: REVIEW.
[29]"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: 2786201] [Abstract]
Cited for: VARIANTS VWD TRP-1597 AND ASP-1607.
[30]"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: 1673047] [Abstract]
Cited for: VARIANT VWD THR-1628.
[31]"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: 1832934] [Abstract]
Cited for: VARIANTS NORMANDY-2 TRP-816 AND NORMANDY-3 GLN-854.
[32]"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: 1761120] [Abstract]
Cited for: VARIANT VWD CYS-1308.
[33]"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: 2010538] [Abstract]
Cited for: VARIANTS VWD TRP-1306; CYS-1308 AND PRO-1613.
[34]"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: 1672694] [Abstract]
Cited for: VARIANTS VWD TRP-1306; CYS-1308; MET-1316 AND GLN-1341, VARIANT HIS-1399.
[35]"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: 2011604] [Abstract]
Cited for: VARIANT VWD CYS-1313.
[36]"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: 1906179] [Abstract]
Cited for: VARIANT NORMANDY-1 MET-791.
[37]"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: 1729889] [Abstract]
Cited for: VARIANT VWD MET-1316.
[38]"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: 1420817] [Abstract]
Cited for: VARIANTS VWD TRP-1306; MET-1316; THR-1628 AND SER-1648.
[39]"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: 1419803] [Abstract]
Cited for: VARIANTS VWD TRP-1306; CYS-1308; LEU-1314 AND LEU-1318.
[40]"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: 1419804] [Abstract]
Cited for: VARIANT VWD ARG-1272.
[41]"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: 1429668] [Abstract]
Cited for: VARIANT VWD LYS-1638.
[42]"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: 1409710] [Abstract]
Cited for: VARIANT VWD SER-1324.
[43]"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: 8338947] [Abstract]
Cited for: VARIANTS VWD GLN-1597; ARG-1609 AND GLU-1665.
[44]"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: 8435341] [Abstract]
Cited for: VARIANT VWD CYS-1514.
[45]"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: 8348943] [Abstract]
Cited for: VARIANTS VWD GLY-1597 AND ARG-1609, VARIANT CYS-1584.
[46]"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: 8376405] [Abstract]
Cited for: VARIANT VWD ASP-1268.
[47]"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: 8486782] [Abstract]
Cited for: VARIANT VWD LEU-1266.
[48]"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: 8123843] [Abstract]
Cited for: VARIANT VWD VAL-1460.
[49]"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: 8123844] [Abstract]
Cited for: VARIANTS VWD PRO-1540 AND THR-1628.
[50]"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: 8088787] [Abstract]
Cited for: VARIANT VWD TYR-2739.
[51]"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: 7989040] [Abstract]
Cited for: VARIANT VWD CYS-377.
[52]"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: 8011991] [Abstract]
Cited for: VARIANT VWD SER-528.
[53]"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: 7620154] [Abstract]
Cited for: VARIANTS VWD CYS-1374 AND HIS-1374.
[54]"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: 7734373] [Abstract]
Cited for: VARIANT VWD HIS-1374.
[55]"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: 8547152] [Abstract]
Cited for: VARIANT VWD VAL-1461.
[56]"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: 7789955] [Abstract]
Cited for: VARIANT VWD ARG-550.
[57]"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: 8622978] [Abstract]
Cited for: VARIANT VWD ARG-2773.
[58]"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: 10887119] [Abstract]
Cited for: VARIANT VWD TRP-273.
[59]"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: 12406074] [Abstract]
Cited for: VARIANT VWD ARG-1060.
[60]"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: 16959974] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-1570.
+Additional computationally mapped references.

Web resources

vWF

von Willebrand factor (vWF) mutation db

GeneReviews
Wikipedia

Von Willebrand factor entry

Cross-references

Sequence databases

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.
X04146 mRNA. Translation: CAA27765.1.
X06828, X06829 Genomic DNA. Translation: CAA29985.1. Sequence problems.
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.
IPIIPI00023014.
PIRVWHU. A34480.
RefSeqNP_000543.2.
UniGeneHs.440848

3D structure databases

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-ray2.60A1260-1472[»]
1U0NX-ray2.95A1261-1468[»]
1UEXX-ray2.85C1260-1468[»]
2ADFX-ray1.90A1683-1874[»]
3GXBX-ray1.90A/B1495-1671[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP04275. 2 interactions.
STRINGP04275.

Protein family/group databases

MEROPSI08.950.
I08.954.

PTM databases

GlycoSuiteDBP04275.
PhosphoSiteP04275.

Proteomic databases

PRIDEP04275.

Genome annotation databases

EnsemblENST00000261405; ENSP00000261405; ENSG00000110799; Homo sapiens. [Genome view]
ENST00000321023; ENSP00000316900; ENSG00000110799; Homo sapiens. [Genome view]
ENST00000453974; ENSP00000391464; ENSG00000110799; Homo sapiens. [Genome view]
GeneID7450.
KEGGhsa:7450.
UCSCuc001qnn.1. human.

Organism-specific databases

CTD7450.
GeneCardsGC12M005917.
H-InvDBHIX0010356.
HGNCHGNC:12726. VWF.
HPACAB001694.
HPA001815.
HPA002082.
MIM193400. gene+phenotype.
277480. phenotype.
Orphanet903. Von Willebrand disease.
166078. Von Willebrand disease, type 1.
166081. Von Willebrand disease, type 2.
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

HOGENOMP04275.
HOVERGENP04275.

Enzyme and pathway databases

ReactomeREACT_13552. Integrin cell surface interactions.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP04275.
BgeeP04275.
CleanExHS_VWF.
GenevestigatorP04275.
GermOnlineENSG00000110799. Homo sapiens.

Family and domain databases

InterProIPR014853. Conserved-cysteine-rich_domain.
IPR006207. Cys_knot_C.
IPR018453. Prot_Inh_CR_TIL_sg.
IPR001846. von_Willebrand_fac_D.
IPR012011. VWF.
IPR002035. VWF_A.
IPR001007. VWF_C.
[Graphical view]
PfamPF08742. C8. 4 hits.
PF01826. TIL. 3 hits.
PF00092. VWA. 3 hits.
PF00093. VWC. 3 hits.
PF00094. VWD. 4 hits.
[Graphical view]
PIRSFPIRSF002495. VWF. 1 hit.
SMARTSM00041. CT. 1 hit.
SM00327. VWA. 3 hits.
SM00214. VWC. 5 hits.
SM00216. VWD. 4 hits.
[Graphical view]
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 Resources

DrugBankDB00025. Antihemophilic Factor.
NextBio29172.
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: July 1, 1993
Last modified: October 13, 2009
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 12

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents