Reviewed, UniProtKB/Swiss-Prot P04275 (VWF_HUMAN)

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	2813 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Secreted › extracellular space › extracellular 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 process	Blood coagulation Cell adhesion Hemostasis
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Polymorphism
Disease	Disease mutation von Willebrand disease
Domain	Repeat Signal
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Isopeptide bond Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cell-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 component	Weibel-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 function	chaperone 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
ADAMTS13	Q76LX8	2	EBI-981819,EBI-981764
GP1BA	P07359	2	EBI-981819,EBI-297082

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Ref.6

Chain

23 – 763

741

von Willebrand antigen 2

PRO_0000022682

Chain

764 – 2813

2050

von Willebrand factor

PRO_0000022683

Regions

Domain

34 – 240

207

VWFD 1

Domain

295 – 348

54

TIL 1

Domain

387 – 598

212

VWFD 2

Domain

652 – 707

56

TIL 2

Domain

776 – 827

52

TIL 3

Domain

866 – 1074

209

VWFD 3

Domain

1146 – 1196

51

TIL 4

Domain

1277 – 1453

177

VWFA 1; binding site for platelet glycoprotein Ib

Domain

1498 – 1665

168

VWFA 2

Domain

1691 – 1871

181

VWFA 3; main binding site for collagens type I and III

Domain

1949 – 2153

205

VWFD 4

Domain

2255 – 2328

74

VWFC 1

Domain

2429 – 2495

67

VWFC 2

Domain

2580 – 2645

66

VWFC 3

Domain

2724 – 2812

89

CTCK

Region

764 – 787

24

Amino-terminal

Region

788 – 833

46

E1

Region

826 – 853

28

CX

Region

2216 – 2261

46

E2

Motif

2507 – 2509

3

Cell attachment site

Amino acid modifications

Glycosylation

99

1

N-linked (GlcNAc...) Potential

Glycosylation

156

1

N-linked (GlcNAc...) Potential

Glycosylation

211

1

N-linked (GlcNAc...) Potential

Glycosylation

666

1

N-linked (GlcNAc...) Potential

Glycosylation

857

1

N-linked (GlcNAc...)

Glycosylation

1147

1

N-linked (GlcNAc...); atypical

Glycosylation

1231

1

N-linked (GlcNAc...)

Glycosylation

1248

1

O-linked (GalNAc...) Probable

Glycosylation

1255

1

O-linked (GalNAc...) Probable

Glycosylation

1256

1

O-linked (GalNAc...) Probable

Glycosylation

1263

1

O-linked (GalNAc...) Probable Ref.7

Glycosylation

1468

1

O-linked (GalNAc...) Probable

Glycosylation

1477

1

O-linked (GalNAc...) Probable

Glycosylation

1486

1

O-linked (GalNAc...) Probable

Glycosylation

1487

1

O-linked (GalNAc...) Probable

Glycosylation

1515

1

N-linked (GlcNAc...) Ref.22

Glycosylation

1574

1

N-linked (GlcNAc...)

Glycosylation

1679

1

O-linked (GalNAc...) Probable

Glycosylation

2223

1

N-linked (GlcNAc...)

Glycosylation

2290

1

N-linked (GlcNAc...)

Glycosylation

2298

1

O-linked (GalNAc...) Probable

Glycosylation

2357

1

N-linked (GlcNAc...)

Glycosylation

2400

1

N-linked (GlcNAc...)

Glycosylation

2546

1

N-linked (GlcNAc...) Ref.24

Glycosylation

2585

1

N-linked (GlcNAc...)

Glycosylation

2790

1

N-linked (GlcNAc...)

Disulfide bond

767 ↔ 808

Ref.19

Disulfide bond

776 ↔ 804

Ref.19

Disulfide bond

810 ↔ 821

Ref.19

Disulfide bond

867 ↔ 996

Ref.19

Disulfide bond

889 ↔ 1031

Ref.19

Disulfide bond

898 ↔ 993

Ref.19

Disulfide bond

914 ↔ 921

Ref.19

Disulfide bond

1060 ↔ 1084

Ref.19

Disulfide bond

1071 ↔ 1111

Ref.19

Disulfide bond

1089 ↔ 1091

Ref.19

Disulfide bond

1126 ↔ 1130

Ref.19

Disulfide bond

1149 ↔ 1169

Ref.19

Disulfide bond

1153 ↔ 1165

Ref.19

Disulfide bond

1196 ↔ 1199

Ref.19

Disulfide bond

1234 ↔ 1237

Ref.19

Disulfide bond

1272 ↔ 1458

Ref.19

Disulfide bond

1669 ↔ 1670

Ref.19

Disulfide bond

1686 ↔ 1872

Ref.19

Disulfide bond

1879 ↔ 1904

Ref.19

Disulfide bond

1899 ↔ 1940

Or C-1899 with C-1942 Ref.19

Disulfide bond

1927 ↔ 2088

Ref.19

Disulfide bond

1950 ↔ 2085

Ref.19

Disulfide bond

1972 ↔ 2123

Ref.19

Disulfide bond

1993 ↔ 2001

Ref.19

Disulfide bond

2724 ↔ 2774

By similarity

Disulfide bond

2739 ↔ 2788

By similarity

Disulfide bond

2750 ↔ 2804

By similarity

Disulfide bond

2754 ↔ 2806

By similarity

Disulfide bond

? ↔ 2811

By similarity

Cross-link

1720

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.23

Natural variations

Natural variant

273

1

R → W in VWD; type I/III; defect in secretion and formation of multimers. Ref.58

VAR_010242

Natural variant

318

1

N → K: dbSNP rs1800387.

VAR_057023

Natural variant

377

1

W → C in VWD; type III. Ref.51

VAR_005782

Natural variant

484

1

H → R: dbSNP rs1800378. Ref.3

VAR_024553

Natural variant

528

1

N → S in VWD; type IIC. Ref.52

VAR_005783

Natural variant

550

1

G → R in VWD; type IIC. Ref.56

VAR_005784

Natural variant

740

1

M → I: dbSNP rs16932374.

VAR_057024

Natural variant

788

1

C → Y in VWD; type II.

VAR_009141

Natural variant

789

1

T → A: dbSNP rs1063856.

VAR_005785

Natural variant

791

1

T → M in Normandy-1. Ref.36

VAR_005786

Natural variant

816

1

R → W in Normandy-2. Ref.31

VAR_005787

Natural variant

852

1

R → Q: dbSNP rs216321.

VAR_005788

Natural variant

854

1

R → Q in Normandy-3. Ref.31

VAR_005789

Natural variant

857

1

N → D

VAR_005790

Natural variant

885

1

F → S: dbSNP rs11064002.

VAR_057025

Natural variant

1060

1

C → R in VWD; type IIN. Ref.59

VAR_028446

Natural variant

1266

1

P → L in VWD; type I. Ref.47

VAR_005791

Natural variant

1268

1

H → D in VWD; type IIB. Ref.46

VAR_005792

Natural variant

1272

1

C → R in VWD; type IIA. Ref.40

VAR_005793

Natural variant

1306

1

R → W in VWD; type IIB. Ref.33 Ref.34 Ref.38 Ref.39

VAR_005794

Natural variant

1308

1

R → C in VWD; type IIB. Ref.32 Ref.33 Ref.34 Ref.39

VAR_005795

Natural variant

1313

1

W → C in VWD; type IIB. Ref.35

VAR_005796

Natural variant

1314

1

V → L in VWD; type IIB. Ref.39

VAR_005797

Natural variant

1316

1

V → M in VWD; type IIB. Ref.34 Ref.37 Ref.38

VAR_005798

Natural variant

1318

1

V → L in VWD; type IIB. Ref.39

VAR_005799

Natural variant

1324

1

G → S in VWD; type IIB. Ref.42

VAR_005800

Natural variant

1341

1

R → Q in VWD; type IIB. Ref.34

VAR_005801

Natural variant

1374

1

R → C in VWD. Ref.53

VAR_005802

Natural variant

1374

1

R → H in VWD. Ref.53 Ref.54

VAR_005803

Natural variant

1381

1

A → T: dbSNP rs216311.

VAR_005804

Natural variant

1399

1

R → H: dbSNP rs216312. Ref.34

VAR_005805

Natural variant

1460

1

L → V in VWD; type IIB. Ref.48

VAR_005806

Natural variant

1461

1

A → V in VWD; type IIB. Ref.55

VAR_005807

Natural variant

1472

1

H → D: dbSNP rs1800383. Ref.7 Ref.12

VAR_029656

Natural variant

1514

1

F → C in VWD; type IIA. Ref.44

VAR_005808

Natural variant

1540

1

L → P in VWD; type IIA. Ref.49

VAR_005809

Natural variant

1565

1

V → L: dbSNP rs1800385.

VAR_014630

Natural variant

1570

1

Y → C in a breast cancer sample; somatic mutation. Ref.60

VAR_036276

Natural variant

1584

1

Y → C: dbSNP rs1800386. Ref.45

VAR_005810

Natural variant

1597

1

R → G in VWD; type IIA. Ref.45

VAR_005811

Natural variant

1597

1

R → Q in VWD; type IIA. Ref.43

VAR_005812

Natural variant

1597

1

R → W in VWD; type IIA. Ref.29

VAR_005813

Natural variant

1607

1

V → D in VWD; type IIA. Ref.29

VAR_005814

Natural variant

1609

1

G → R in VWD; type IIA. Ref.43 Ref.45

VAR_005815

Natural variant

1613

1

S → P in VWD; type IIA. Ref.33

VAR_005816

Natural variant

1628

1

I → T in VWD; type IIA. Ref.30 Ref.38 Ref.49

VAR_005817

Natural variant

1638

1

E → K in VWD; type IIA. Ref.41

VAR_005818

Natural variant

1648

1

P → S in VWD; type IIA. Ref.38

VAR_005819

Natural variant

1665

1

V → E in VWD; type IIA. Ref.43

VAR_005820

Natural variant

2063

1

P → S in VWD; type III.

VAR_009142

Natural variant

2178

1

A → S: dbSNP rs34230288.

VAR_057026

Natural variant

2185

1

R → Q: dbSNP rs2229446.

VAR_057027

Natural variant

2362

1

C → F in VWD; type III.

VAR_009143

Natural variant

2546

1

N → Y in VWD; type III.

VAR_009144

Natural variant

2705

1

G → R: dbSNP rs7962217.

VAR_057028

Natural variant

2739

1

C → Y in VWD; type III. Ref.50

VAR_005821

Natural variant

2773

1

C → R in VWD; type IID. Ref.57

VAR_005822

Experimental info

Sequence conflict

471

1

I → V in CAA27972. Ref.1

Sequence conflict

471

1

I → V in CAA27765. Ref.3

Sequence conflict

770

1

P → H in AAB59512. Ref.8

Sequence conflict

804

1

C → S AA sequence Ref.7

Sequence conflict

804

1

C → S in AAB59512. Ref.8

Sequence conflict

804

1

C → S Ref.10

Sequence conflict

1914

1

S → T in CAA27972. Ref.1

Sequence conflict

2168

1

C → S AA sequence Ref.7

Secondary structure

1

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2813

Helix Strand Turn

Details...

Beta strand

1274 – 1283

10

Helix

1290 – 1305

16

Beta strand

1313 – 1329

17

Helix

1337 – 1345

9

Helix

1357 – 1366

10

Beta strand

1369 – 1371

3

Beta strand

1377 – 1386

10

Helix

1391 – 1394

4

Helix

1397 – 1406

10

Beta strand

1409 – 1417

9

Helix

1422 – 1431

10

Beta strand

1438 – 1442

5

Helix

1443 – 1445

3

Helix

1446 – 1460

15

Beta strand

1690 – 1697

8

Beta strand

1699 – 1702

4

Helix

1705 – 1720

16

Beta strand

1727 – 1738

12

Beta strand

1740 – 1743

4

Helix

1751 – 1759

9

Helix

1770 – 1782

13

Turn

1784 – 1787

4

Beta strand

1792 – 1800

9

Helix

1809 – 1817

9

Beta strand

1820 – 1829

10

Helix

1833 – 1839

7

Helix

1841 – 1847

7

Beta strand

1849 – 1853

5

Helix

1856 – 1862

7

Helix

1866 – 1871

6

Sequences

	Sequence		Length	Mass (Da)
	P04275-1 [UniParc]. Last modified July 1, 1993. Version 2. Checksum: 4B98F8EA3C082DCC	FASTA	2,813	309,299
	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

References

	« Hide 'large scale' referencesShow '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. , 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

EMBLGenBankDDBJ

X04385 mRNA. Translation: CAA27972.1.
M25865 , M25828, M25829, M25830, M25831, M25832, M25833, M25834, M25835, M25836, M25837, M25838, M25839, M25840, M25841, M25842, M25843, M25844, M25845, M25846, M25847, M25848, M25849, M25850, M25851, M25852, M25853, M25854, M25855, M25856, M25857, M25858, M25859, M25860, M25861, M25862, M25863, M25864 Genomic DNA. Translation: AAB59458.1.
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.

IPI

IPI00023014.

PIR

VWHU. A34480.

RefSeq

NP_000543.2.

UniGene

Hs.440848

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AO3	X-ray	2.20	A/B	1686-1872	[»]
1ATZ	X-ray	1.80	A/B	1685-1873	[»]
1AUQ	X-ray	2.30	A	1261-1468	[»]
1FE8	X-ray	2.03	A/B/C	1683-1874	[»]
1FNS	X-ray	2.00	A	1271-1465	[»]
1IJB	X-ray	1.80	A	1263-1464	[»]
1IJK	X-ray	2.60	A	1263-1464	[»]
1M10	X-ray	3.10	A	1261-1468	[»]
1OAK	X-ray	2.20	A	1271-1465	[»]
1SQ0	X-ray	2.60	A	1260-1472	[»]
1U0N	X-ray	2.95	A	1261-1468	[»]
1UEX	X-ray	2.85	C	1260-1468	[»]
2ADF	X-ray	1.90	A	1683-1874	[»]
3GXB	X-ray	1.90	A/B	1495-1671	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P04275. 2 interactions.

STRING

P04275.

Protein family/group databases

MEROPS

I08.950.
I08.954.

PTM databases

GlycoSuiteDB

P04275.

PhosphoSite

P04275.

Proteomic databases

PRIDE

P04275.

Genome annotation databases

Ensembl

ENST00000261405; ENSP00000261405; ENSG00000110799; Homo sapiens. [Genome view]
ENST00000321023; ENSP00000316900; ENSG00000110799; Homo sapiens. [Genome view]
ENST00000453974; ENSP00000391464; ENSG00000110799; Homo sapiens. [Genome view]

GeneID

7450.

KEGG

hsa:7450.

UCSC

uc001qnn.1. human.

Organism-specific databases

CTD

7450.

GeneCards

GC12M005917.

H-InvDB

HIX0010356.

HGNC

HGNC:12726. VWF.

HPA

CAB001694.
HPA001815.
HPA002082.

MIM

193400. gene+phenotype.
277480. phenotype.

Orphanet

903. 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.

PharmGKB

PA37337.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P04275.

HOVERGEN

P04275.

Enzyme and pathway databases

Reactome

REACT_13552. Integrin cell surface interactions.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P04275.

Bgee

P04275.

CleanEx

HS_VWF.

Genevestigator

P04275.

GermOnline

ENSG00000110799. Homo sapiens.

Family and domain databases

InterPro

IPR014853. 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]

Pfam

PF08742. C8. 4 hits.
PF01826. TIL. 3 hits.
PF00092. VWA. 3 hits.
PF00093. VWC. 3 hits.
PF00094. VWD. 4 hits.
[Graphical view]

PIRSF

PIRSF002495. VWF. 1 hit.

SMART

SM00041. CT. 1 hit.
SM00327. VWA. 3 hits.
SM00214. VWC. 5 hits.
SM00216. VWD. 4 hits.
[Graphical view]

PROSITE

PS01185. CTCK_1. 1 hit.
PS01225. CTCK_2. 1 hit.
PS50234. VWFA. 3 hits.
PS01208. VWFC_1. 3 hits.
PS50184. VWFC_2. 3 hits.
PS51233. VWFD. 4 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00025. Antihemophilic Factor.

NextBio

29172.

SOURCE

Search...

Entry information

Entry name

VWF_HUMAN

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.