P04275 (VWF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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.19 Ref.22
Subcellular location	Secreted. Secreted › extracellular space › extracellular 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
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.59 Ref.60 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.30 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.53 Ref.54 Ref.55 Ref.56 Ref.57 Ref.58 Ref.61 Ref.64 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.51 Ref.52 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.
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 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 Reference proteome
Gene Ontology (GO)
Biological_process	blood coagulation, intrinsic pathway Traceable author statement. Source: Reactome cell-substrate adhesion Inferred from direct assay PubMed 9079671. Source: UniProtKB liver development Inferred from electronic annotation. Source: Compara placenta development Inferred from electronic annotation. Source: Compara 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
Cellular_component	Weibel-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: Compara extracellular matrix Inferred from direct assay PubMed 6754744. Source: UniProtKB extracellular region Inferred from direct assay Ref.59. Source: UniProtKB platelet alpha granule lumen Traceable author statement. Source: Reactome proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	chaperone binding Inferred from direct assay Ref.59. Source: UniProtKB collagen binding Inferred from direct assay PubMed 2056120. Source: UniProtKB glycoprotein binding Inferred from direct assay PubMed 16409464. Source: UniProtKB immunoglobulin binding Inferred from direct assay PubMed 3121636. Source: UniProtKB protease binding Inferred from direct assay PubMed 15824096. Source: MGI protein homodimerization activity Inferred from direct assay Ref.59. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ADAMTS13	Q76LX8	5	EBI-981819,EBI-981764
GP1BA	P07359	2	EBI-981819,EBI-297082
OPTN	Q96CV9	2	EBI-981819,EBI-748974

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Ref.7

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.8

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.23

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.25

Glycosylation

2585

1

N-linked (GlcNAc...)

Glycosylation

2790

1

N-linked (GlcNAc...)

Disulfide bond

767 ↔ 808

Ref.20

Disulfide bond

776 ↔ 804

Ref.20

Disulfide bond

810 ↔ 821

Ref.20

Disulfide bond

867 ↔ 996

Ref.20

Disulfide bond

889 ↔ 1031

Ref.20

Disulfide bond

898 ↔ 993

Ref.20

Disulfide bond

914 ↔ 921

Ref.20

Disulfide bond

1060 ↔ 1084

Ref.20

Disulfide bond

1071 ↔ 1111

Ref.20

Disulfide bond

1089 ↔ 1091

Ref.20

Disulfide bond

1126 ↔ 1130

Ref.20

Disulfide bond

1149 ↔ 1169

Ref.20

Disulfide bond

1153 ↔ 1165

Ref.20

Disulfide bond

1196 ↔ 1199

Ref.20

Disulfide bond

1234 ↔ 1237

Ref.20

Disulfide bond

1272 ↔ 1458

Ref.20

Disulfide bond

1669 ↔ 1670

Ref.20

Disulfide bond

1686 ↔ 1872

Ref.20

Disulfide bond

1879 ↔ 1904

Ref.20

Disulfide bond

1899 ↔ 1940

Or C-1899 with C-1942 Ref.20

Disulfide bond

1927 ↔ 2088

Ref.20

Disulfide bond

1950 ↔ 2085

Ref.20

Disulfide bond

1972 ↔ 2123

Ref.20

Disulfide bond

1993 ↔ 2001

Ref.20

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.24

Natural variations

Natural variant

273

1

R → W in VWD1 and VWD3; defect in secretion and formation of multimers. Ref.59

VAR_010242

Natural variant

318

1

N → K.
Corresponds to variant rs1800387 [ dbSNP | Ensembl ].

VAR_057023

Natural variant

377

1

W → C in VWD3. Ref.52

VAR_005782

Natural variant

471

1

V → I. Ref.2
Corresponds to variant rs1800377 [ dbSNP | Ensembl ].

VAR_060591

Natural variant

484

1

H → R. Ref.4
Corresponds to variant rs1800378 [ dbSNP | Ensembl ].

VAR_024553

Natural variant

528

1

N → S in VWD2. Ref.53

VAR_005783

Natural variant

550

1

G → R in VWD2. Ref.57

VAR_005784

Natural variant

740

1

M → I.
Corresponds to variant rs16932374 [ dbSNP | Ensembl ].

VAR_057024

Natural variant

788

1

C → Y in VWD2.

VAR_009141

Natural variant

789

1

T → A. Ref.9
Corresponds to variant rs1063856 [ dbSNP | Ensembl ].

VAR_005785

Natural variant

791

1

T → M in VWD2; Normandy type. Ref.37

VAR_005786

Natural variant

816

1

R → W in VWD2; Normandy type. Ref.32

VAR_005787

Natural variant

852

1

Q → R. Ref.1 Ref.2 Ref.4 Ref.8 Ref.9 Ref.11
Corresponds to variant rs216321 [ dbSNP | Ensembl ].

VAR_005788

Natural variant

854

1

R → Q in VWD2; Normandy type. Ref.32
Corresponds to variant rs41276738 [ dbSNP | Ensembl ].

VAR_005789

Natural variant

857

1

N → D.

VAR_005790

Natural variant

885

1

F → S.
Corresponds to variant rs11064002 [ dbSNP | Ensembl ].

VAR_057025

Natural variant

1060

1

C → R in VWD2. Ref.61

VAR_028446

Natural variant

1149

1

C → R in VWD1; reduced secretion of homodimers and heterodimers with wild type VWD and increased degradation by the proteasome. Ref.60

VAR_064925

Natural variant

1266

1

P → L in VWD2. Ref.48

VAR_005791

Natural variant

1268

1

H → D in VWD2. Ref.47

VAR_005792

Natural variant

1272

1

C → F in VWD2; subtype 2A. Ref.64

VAR_067340

Natural variant

1272

1

C → R in VWD2. Ref.41

VAR_005793

Natural variant

1306

1

R → W in VWD2. Ref.34 Ref.35 Ref.39 Ref.40

VAR_005794

Natural variant

1308

1

R → C in VWD2. Ref.33 Ref.34 Ref.35 Ref.40

VAR_005795

Natural variant

1313

1

W → C in VWD2. Ref.36

VAR_005796

Natural variant

1314

1

V → L in VWD2. Ref.40

VAR_005797

Natural variant

1316

1

V → M in VWD2. Ref.35 Ref.38 Ref.39

VAR_005798

Natural variant

1318

1

V → L in VWD2. Ref.40

VAR_005799

Natural variant

1324

1

G → S in VWD2. Ref.43

VAR_005800

Natural variant

1341

1

R → Q in VWD2. Ref.35

VAR_005801

Natural variant

1374

1

R → C in VWD2. Ref.54

VAR_005802

Natural variant

1374

1

R → H in VWD2. Ref.54 Ref.55

VAR_005803

Natural variant

1381

1

T → 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 variant

1399

1

R → H. Ref.35
Corresponds to variant rs216312 [ dbSNP | Ensembl ].

VAR_005805

Natural variant

1460

1

L → V in VWD2. Ref.49

VAR_005806

Natural variant

1461

1

A → V in VWD2. Ref.56

VAR_005807

Natural variant

1472

1

D → H. Ref.1 Ref.2 Ref.12
Corresponds to variant rs1800383 [ dbSNP | Ensembl ].

VAR_029656

Natural variant

1514

1

F → C in VWD2. Ref.45

VAR_005808

Natural variant

1540

1

L → P in VWD2. Ref.50

VAR_005809

Natural variant

1565

1

V → L.
Corresponds to variant rs1800385 [ dbSNP | Ensembl ].

VAR_014630

Natural variant

1570

1

Y → C in a breast cancer sample; somatic mutation. Ref.63

VAR_036276

Natural variant

1584

1

Y → C Exhibits increased in susceptibility to proteolysis by ADAMTS13. Ref.46 Ref.62
Corresponds to variant rs1800386 [ dbSNP | Ensembl ].

VAR_005810

Natural variant

1597

1

R → G in VWD2. Ref.46

VAR_005811

Natural variant

1597

1

R → Q in VWD2. Ref.44

VAR_005812

Natural variant

1597

1

R → W in VWD2. Ref.30

VAR_005813

Natural variant

1607

1

V → D in VWD2. Ref.30

VAR_005814

Natural variant

1609

1

G → R in VWD2. Ref.44 Ref.46

VAR_005815

Natural variant

1613

1

S → P in VWD2. Ref.34

VAR_005816

Natural variant

1628

1

I → T in VWD2. Ref.31 Ref.39 Ref.50

VAR_005817

Natural variant

1638

1

E → K in VWD2. Ref.42

VAR_005818

Natural variant

1648

1

P → S in VWD2. Ref.39

VAR_005819

Natural variant

1665

1

V → E in VWD2. Ref.44

VAR_005820

Natural variant

2063

1

P → S in VWD3.

VAR_009142

Natural variant

2178

1

A → S.
Corresponds to variant rs34230288 [ dbSNP | Ensembl ].

VAR_057026

Natural variant

2185

1

R → Q.
Corresponds to variant rs2229446 [ dbSNP | Ensembl ].

VAR_057027

Natural variant

2362

1

C → F in VWD3.

VAR_009143

Natural variant

2546

1

N → Y in VWD3.

VAR_009144

Natural variant

2705

1

G → R.
Corresponds to variant rs7962217 [ dbSNP | Ensembl ].

VAR_057028

Natural variant

2739

1

C → Y in VWD3. Ref.51

VAR_005821

Natural variant

2773

1

C → R in VWD2. Ref.58

VAR_005822

Experimental info

Mutagenesis

1149

1

C → R: Reduced secretion and increased intracellular retention. Similar phenotype; when associated with S-1169. Ref.60

Mutagenesis

1169

1

C → S: Reduced secretion and increased intracellular retention. Similar phenotype; when associated with R-1149. Ref.60

Sequence conflict

770

1

P → H in AAB59512. Ref.9

Sequence conflict

804

1

C → S AA sequence Ref.8

Sequence conflict

804

1

C → S in AAB59512. Ref.9

Sequence conflict

1914

1

S → T in CAA27972. Ref.1

Sequence conflict

2168

1

C → S AA sequence Ref.8

Secondary structure

1

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2813

Helix Strand Turn

Details...

Beta strand

1267 – 1269

3

Beta strand

1276 – 1283

8

Helix

1290 – 1305

16

Turn

1307 – 1310

4

Beta strand

1313 – 1329

17

Helix

1337 – 1345

9

Helix

1357 – 1367

11

Beta strand

1369 – 1371

3

Beta strand

1377 – 1385

9

Helix

1391 – 1393

3

Helix

1394 – 1396

3

Helix

1397 – 1406

10

Beta strand

1409 – 1417

9

Helix

1422 – 1431

10

Beta strand

1432 – 1434

3

Beta strand

1438 – 1442

5

Helix

1443 – 1445

3

Helix

1446 – 1460

15

Beta strand

1498 – 1504

7

Turn

1507 – 1509

3

Helix

1511 – 1527

17

Beta strand

1534 – 1550

17

Helix

1558 – 1567

10

Helix

1578 – 1587

10

Turn

1588 – 1590

3

Helix

1592 – 1594

3

Helix

1595 – 1599

5

Beta strand

1602 – 1608

7

Beta strand

1623 – 1631

9

Helix

1636 – 1643

8

Beta strand

1649 – 1652

4

Turn

1654 – 1656

3

Helix

1657 – 1670

14

Beta strand

1690 – 1697

8

Beta strand

1699 – 1702

4

Helix

1704 – 1720

17

Beta strand

1727 – 1743

17

Beta strand

1745 – 1747

3

Helix

1751 – 1759

9

Helix

1770 – 1782

13

Helix

1784 – 1786

3

Beta strand

1792 – 1800

9

Helix

1809 – 1817

9

Beta strand

1820 – 1831

12

Helix

1833 – 1839

7

Helix

1841 – 1847

7

Beta strand

1849 – 1853

5

Helix

1856 – 1862

7

Beta strand

1863 – 1865

3

Helix

1866 – 1870

5

Sequences

	Sequence		Length	Mass (Da)
	P04275 [UniParc]. Last modified January 11, 2011. Version 4. Checksum: D5C1C78360917C29	FASTA	2,813	309,265
	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

References

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[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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Liver.
[26]	"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.
[27]	"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.
[28]	"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.
[29]	"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.
[30]	"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.
[31]	"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.
[32]	"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.
[33]	"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.
[34]	"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.
[35]	"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.
[36]	"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.
[37]	"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.
[38]	"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.
[39]	"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.
[40]	"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.
[41]	"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.
[42]	"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.
[43]	"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.
[44]	"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.
[45]	"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.
[46]	"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.
[47]	"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.
[48]	"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.
[49]	"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.
[50]	"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.
[51]	"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.
[52]	"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.
[53]	"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.
[54]	"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.
[55]	"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.
[56]	"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.
[57]	"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.
[58]	"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.
[59]	"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.
[60]	"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.
[61]	"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.
[62]	"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.
[63]	"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] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-1570.
[64]	"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

GeneReviews

Wikipedia

Von Willebrand factor entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X04385 mRNA. Translation: CAA27972.1.
M25865 , M25828, M25829, M25830, M25831, M25832, M25833, M25834, M25835, M25836, M25837, M25838, M25839, M25840, M25841, M25842, M25843, M25844, M25845, M25846, M25847, M25848, M25849, M25850, M25851, M25852, M25853, M25854, M25855, M25856, M25857, M25858, M25859, M25860, M25861, M25862, M25863, M25864 Genomic DNA. Translation: AAB59458.1.
AC005845 Genomic DNA. No translation available.
AC005846 Genomic DNA. No translation available.
AC005904 Genomic DNA. No translation available.
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.

IPI

IPI00023014.

PIR

VWHU. A34480.

RefSeq

NP_000543.2. NM_000552.3.

UniGene

Hs.440848.

3D structure databases

PDBe
RCSB PDB
PDBj

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	1260-1471	[»]
1U0N	X-ray	2.95	A	1261-1468	[»]
1UEX	X-ray	2.85	C	1260-1468	[»]
2ADF	X-ray	1.90	A	1683-1874	[»]
3GXB	X-ray	1.90	A/B	1495-1671	[»]
3HXO	X-ray	2.40	A	1260-1468	[»]
3HXQ	X-ray	2.69	A	1260-1468	[»]
3PPV	X-ray	1.90	A	1488-1675	[»]
3PPW	X-ray	1.90	A	1488-1675	[»]
3PPX	X-ray	1.91	A	1488-1675	[»]
3PPY	X-ray	2.00	A	1488-1675	[»]
3ZQK	X-ray	1.70	A/B/C	1478-1674	[»]
4DMU	X-ray	2.80	B/D/F/H/J/L	1683-1874	[»]

ProteinModelPortal

P04275.

SMR

P04275. Positions 1261-1468, 1495-1671, 1685-1873.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29667N.

IntAct

P04275. 46 interactions.

MINT

MINT-244925.

STRING

9606.ENSP00000261405.

Protein family/group databases

MEROPS

I08.950.

PTM databases

GlycoSuiteDB

P04275.

PhosphoSite

P04275.

Polymorphism databases

DMDM

269849730.

Proteomic databases

PaxDb

P04275.

PRIDE

P04275.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000261405; ENSP00000261405; ENSG00000110799.

GeneID

7450.

KEGG

hsa:7450.

UCSC

uc001qnn.1. human.

Organism-specific databases

CTD

7450.

GeneCards

GC12M006058.

H-InvDB

HIX0010356.
HIX0171640.

HGNC

HGNC:12726. VWF.

HPA

CAB001694.
HPA001815.
HPA002082.

MIM

193400. phenotype.
277480. phenotype.
613160. gene.
613554. phenotype.

neXtProt

NX_P04275.

Orphanet

166078. Von Willebrand disease type 1.
166084. Von Willebrand disease type 2A.
166087. Von Willebrand disease type 2B.
166090. Von Willebrand disease type 2M.
166093. Von Willebrand disease type 2N.
166096. Von Willebrand disease type 3.

PharmGKB

PA37337.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG12793.

HOGENOM

HOG000169747.

HOVERGEN

HBG004380.

InParanoid

P04275.

KO

K03900.

OMA

ECCGRCL.

OrthoDB

EOG44TP6X.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P04275.

Bgee

P04275.

CleanEx

HS_VWF.

Genevestigator

P04275.

GermOnline

ENSG00000110799. Homo sapiens.

Family and domain databases

Gene3D

3.40.50.410. 3 hits.

InterPro

IPR006207. Cys_knot_C.
IPR002919. TIL_dom.
IPR014853. Unchr_dom_Cys-rich.
IPR012011. VWF.
IPR002035. VWF_A.
IPR001007. VWF_C.
IPR001846. VWF_type-D.
[Graphical view]

Pfam

PF08742. C8. 4 hits.
PF01826. TIL. 5 hits.
PF00092. VWA. 3 hits.
PF00093. VWC. 2 hits.
PF00094. VWD. 4 hits.
[Graphical view]

PIRSF

PIRSF002495. VWF. 1 hit.

SMART

SM00832. C8. 4 hits.
SM00041. CT. 1 hit.
SM00327. VWA. 3 hits.
SM00214. VWC. 5 hits.
SM00216. VWD. 4 hits.
[Graphical view]

SUPFAM

SSF57567. Cysrich_TIL. 5 hits.

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

ChiTaRS

VWF. human.

DrugBank

DB00025. Antihemophilic Factor.

EvolutionaryTrace

P04275.

GenomeRNAi

7450.

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:	January 11, 2011
Last modified:	May 29, 2013
This is version 185 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.