P00451 (FA8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Coagulation factor VIII

Alternative name(s):
Antihemophilic factor
Short name=AHF
Procoagulant component

Cleaved into the following 4 chains:

1. Factor VIIIa heavy chain, 200 kDa isoform
2. Factor VIIIa heavy chain, 92 kDa isoform
3. Factor VIII B chain
4. Factor VIIIa light chain

Gene names

Name:	F8
Synonyms:	F8C

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	2351 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	Factor VIII, along with calcium and phospholipid, acts as a cofactor for factor IXa when it converts factor X to the activated form, factor Xa.
Subunit structure	Interacts with vWF. vWF binding is essential for the stabilization of F8 in circulation. Ref.14 Ref.15
Subcellular location	Secreted › extracellular space.
Domain	Domain F5/8 type C 2 is responsible for phospholipid-binding and essential for factor VIII activity.
Post-translational modification	Sulfation on Tyr-1699 is essential for binding vWF.
Involvement in disease	Hemophilia A (HEMA) [MIM:306700]: A disorder of blood coagulation characterized by a permanent tendency to hemorrhage. About 50% of patients have severe hemophilia resulting in frequent spontaneous bleeding into joints, muscles and internal organs. Less severe forms are characterized by bleeding after trauma or surgery. Note: The disease is caused by mutations affecting the gene represented in this entry. Of particular interest for the understanding of the function of F8 is the category of CRM (cross-reacting material) positive patients (approximately 5%) that have considerable amount of F8 in their plasma (at least 30% of normal), but the protein is non-functional; i.e. the F8 activity is much less than the plasma protein level. CRM-reduced is another category of patients in which the F8C antigen and activity are reduced to approximately the same level. Most mutations are CRM negative, and probably affect the folding and stability of the protein. Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.37 Ref.38 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 Ref.60 Ref.61 Ref.62 Ref.63 Ref.64 Ref.65 Ref.66 Ref.67 Ref.68 Ref.69 Ref.70 Ref.71 Ref.72 Ref.73 Ref.74 Ref.75 Ref.76 Ref.77 Ref.78 Ref.79 Ref.80 Ref.81 Ref.82 Ref.83 Ref.84 Ref.86 Ref.87 Ref.88 Ref.89 Ref.90 Ref.91 Ref.92 Ref.93 Ref.94 Ref.95 Ref.96 Ref.97 Ref.98 Ref.99 Ref.100 Ref.101
Pharmaceutical use	Available under the names Kogenate (Bayer) and Recombinate (Baxter and American Home Products). Used to treat hemophilia A.
Sequence similarities	Belongs to the multicopper oxidase family. Contains 3 F5/8 type A domains. Contains 2 F5/8 type C domains. Contains 6 plastocyanin-like domains.
Mass spectrometry	Molecular mass is 1367.6 Da from positions 356 - 378. Determined by ESI. Nonsulfated. Ref.12 Molecular mass is 1407.4 Da from positions 356 - 378. Determined by ESI. Sulfated. Ref.12 Molecular mass is 2975.4 Da from positions 400 - 424. Determined by ESI. Nonsulfated. Ref.12 Molecular mass is 3024 Da from positions 727 - 752. Determined by ESI. Nonsulfated. Ref.12 Molecular mass is 3104 Da from positions 727 - 752. Determined by ESI. Monosulfated. Ref.12 Molecular mass is 3183.5 Da from positions 727 - 752. Determined by ESI. Disulfated. Ref.12 Molecular mass is 3262.5 Da from positions 727 - 752. Determined by ESI. Trisulfated. Ref.12 Molecular mass is 2460.9 Da from positions 1672 - 1692. Determined by ESI. Nonsulfated. Ref.12 Molecular mass is 2540.7 Da from positions 1672 - 1692. Determined by ESI. Sulfated. Ref.12 Molecular mass is 2000.7 Da from positions 1691 - 1708. Determined by ESI. Nonsulfated. Ref.12 Molecular mass is 2080.7 Da from positions 1691 - 1708. Determined by ESI. Sulfated. Ref.12

Ontologies

Keywords
Biological process	Acute phase Blood coagulation Hemostasis
Cellular component	Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Hemophilia
Domain	Repeat Signal
Ligand	Calcium Metal-binding
PTM	Disulfide bond Glycoprotein Sulfation
Technical term	3D-structure Complete proteome Direct protein sequencing Pharmaceutical Reference proteome
Gene Ontology (GO)
Biological_process	acute-phase response Inferred from electronic annotation. Source: UniProtKB-KW blood coagulation, intrinsic pathway Traceable author statement. Source: Reactome cell adhesion Inferred from electronic annotation. Source: InterPro platelet activation Traceable author statement. Source: Reactome platelet degranulation Traceable author statement. Source: Reactome
Cellular_component	extracellular region Non-traceable author statement PubMed 14718574. Source: UniProtKB extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Traceable author statement. Source: Reactome platelet alpha granule lumen Traceable author statement. Source: Reactome
Molecular_function	copper ion binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P00451-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P00451-2)

Also known as: F8B;

The sequence of this isoform differs from the canonical sequence as follows:
     1-8: MQIELSTC → MRIQDPGK
     9-2143: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

Chain

20 – 2351

2332

Coagulation factor VIII

PRO_0000002967

Chain

20 – 1332

1313

Factor VIIIa heavy chain, 200 kDa isoform

PRO_0000002968

Chain

20 – 759

740

Factor VIIIa heavy chain, 92 kDa isoform

PRO_0000002969

Chain

760 – 1332

573

Factor VIII B chain

PRO_0000002970

Chain

1668 – 2351

684

Factor VIIIa light chain

PRO_0000002971

Regions

Domain

20 – 348

329

F5/8 type A 1

Domain

20 – 198

179

Plastocyanin-like 1

Domain

206 – 348

143

Plastocyanin-like 2

Domain

399 – 730

332

F5/8 type A 2

Domain

399 – 573

175

Plastocyanin-like 3

Domain

583 – 730

148

Plastocyanin-like 4

Domain

1713 – 2040

328

F5/8 type A 3

Domain

1713 – 1877

165

Plastocyanin-like 5

Domain

1887 – 2040

154

Plastocyanin-like 6

Domain

2040 – 2188

149

F5/8 type C 1

Domain

2193 – 2345

153

F5/8 type C 2

Region

760 – 1667

908

B

Sites

Site

391 – 392

2

Cleavage; by thrombin

Site

759 – 760

2

Cleavage; by thrombin

Site

1332 – 1333

2

Cleavage (activation)

Site

1667 – 1668

2

Cleavage (activation)

Site

1708 – 1709

2

Cleavage; by thrombin

Amino acid modifications

Modified residue

365

1

Sulfotyrosine Ref.12 Ref.14

Modified residue

737

1

Sulfotyrosine Ref.12

Modified residue

738

1

Sulfotyrosine Ref.12

Modified residue

742

1

Sulfotyrosine Ref.12

Modified residue

1683

1

Sulfotyrosine Ref.12 Ref.14

Modified residue

1699

1

Sulfotyrosine Ref.12 Ref.13 Ref.14

Glycosylation

60

1

N-linked (GlcNAc...) Potential

Glycosylation

258

1

N-linked (GlcNAc...) Potential

Glycosylation

601

1

N-linked (GlcNAc...) Ref.17

Glycosylation

776

1

N-linked (GlcNAc...) Potential

Glycosylation

803

1

N-linked (GlcNAc...) Potential

Glycosylation

847

1

N-linked (GlcNAc...) Potential

Glycosylation

919

1

N-linked (GlcNAc...) Potential

Glycosylation

962

1

N-linked (GlcNAc...) Potential

Glycosylation

982

1

N-linked (GlcNAc...) Potential

Glycosylation

1020

1

N-linked (GlcNAc...) Potential

Glycosylation

1024

1

N-linked (GlcNAc...) Potential

Glycosylation

1074

1

N-linked (GlcNAc...) Potential

Glycosylation

1085

1

N-linked (GlcNAc...) Potential

Glycosylation

1204

1

N-linked (GlcNAc...) Potential

Glycosylation

1274

1

N-linked (GlcNAc...) Potential

Glycosylation

1278

1

N-linked (GlcNAc...) Potential

Glycosylation

1301

1

N-linked (GlcNAc...) Potential

Glycosylation

1319

1

N-linked (GlcNAc...) Potential

Glycosylation

1431

1

N-linked (GlcNAc...) Potential

Glycosylation

1461

1

N-linked (GlcNAc...) Potential

Glycosylation

1829

1

N-linked (GlcNAc...) Potential

Glycosylation

2137

1

N-linked (GlcNAc...) Potential

Disulfide bond

172 ↔ 198

Ref.16

Disulfide bond

267 ↔ 348

Ref.16

Disulfide bond

547 ↔ 573

Ref.16

Disulfide bond

649 ↔ 730

Ref.16

Disulfide bond

1851 ↔ 1877

Ref.16

Disulfide bond

1918 ↔ 1922

Ref.16

Disulfide bond

2040 ↔ 2188

Ref.16

Disulfide bond

2193 ↔ 2345

By similarity

Natural variations

Alternative sequence

1 – 8

8

MQIELSTC → MRIQDPGK in isoform 2.

VSP_042656

Alternative sequence

9 – 2143

2135

Missing in isoform 2.

VSP_042657

Natural variant

19

1

S → R in HEMA. Ref.68

VAR_028447

Natural variant

22

1

R → T in HEMA; severe. Ref.89

VAR_028448

Natural variant

24

1

Y → C in HEMA. Ref.70

VAR_028449

Natural variant

25

1

Y → C in HEMA; mild. Ref.89

VAR_028450

Natural variant

26

1

L → P in HEMA; severe. Ref.89

VAR_028451

Natural variant

26

1

L → R in HEMA; severe. Ref.52 Ref.70 Ref.95

VAR_001045

Natural variant

30

1

E → V in HEMA; mild. Ref.45

VAR_001046

Natural variant

33

1

W → G in HEMA; moderate. Ref.57

VAR_028452

Natural variant

35

1

Y → C in HEMA; mild/severe. Ref.86

VAR_028453

Natural variant

35

1

Y → H in HEMA; severe. Ref.75

VAR_028454

Natural variant

41

1

G → C in HEMA; severe/moderate.

VAR_001047

Natural variant

48

1

R → C in HEMA; severe.

VAR_001048

Natural variant

48

1

R → K in HEMA. Ref.52

VAR_028455

Natural variant

67

1

K → E in HEMA; severe. Ref.92

VAR_028456

Natural variant

67

1

K → N in HEMA. Ref.82

VAR_028457

Natural variant

69

1

L → P in HEMA; moderate-severe. Ref.76

VAR_028458

Natural variant

72

1

E → K in HEMA; moderate. Ref.94

VAR_017330

Natural variant

75

1

D → E in HEMA; moderate. Ref.51

VAR_028459

Natural variant

75

1

D → V.
Corresponds to variant rs1800288 [ dbSNP | Ensembl ].

VAR_001049

Natural variant

75

1

D → Y in HEMA; moderate-severe. Ref.76

VAR_028460

Natural variant

83

1

P → R in HEMA. Ref.100

VAR_065303

Natural variant

84 – 85

2

Missing in HEMA; severe.

VAR_028461

Natural variant

85

1

Missing in HEMA; moderate. Ref.92

VAR_028462

Natural variant

89

1

G → D in HEMA; severe. Ref.52 Ref.78

VAR_001050

Natural variant

89

1

G → V in HEMA; mild. Ref.45

VAR_001051

Natural variant

92

1

G → A in HEMA. Ref.81

VAR_028463

Natural variant

92

1

G → V in HEMA; mild. Ref.45
Corresponds to variant rs28935204 [ dbSNP | Ensembl ].

VAR_028464

Natural variant

97

1

A → P in HEMA. Ref.88

VAR_017331

Natural variant

98

1

E → K in HEMA; severe. Ref.58

VAR_028465

Natural variant

99

1

V → D in HEMA; severe. Ref.52 Ref.78
Corresponds to variant rs28935205 [ dbSNP | Ensembl ].

VAR_001052

Natural variant

101

1

D → G in HEMA; severe. Ref.58

VAR_028466

Natural variant

101

1

D → H in HEMA; severe sporadic. Ref.78

VAR_028467

Natural variant

101

1

D → V in HEMA. Ref.52

VAR_028468

Natural variant

104

1

V → D in HEMA; mild. Ref.45
Corresponds to variant rs28935206 [ dbSNP | Ensembl ].

VAR_001053

Natural variant

108

1

K → T in HEMA; mild. Ref.38
Corresponds to variant rs28935207 [ dbSNP | Ensembl ].

VAR_001054

Natural variant

110

1

M → V in HEMA; moderate. Ref.38
Corresponds to variant rs28936083 [ dbSNP | Ensembl ].

VAR_001055

Natural variant

111

1

A → T in HEMA; severe. Ref.97

VAR_028469

Natural variant

111

1

A → V in HEMA; moderate. Ref.89

VAR_028470

Natural variant

113

1

H → R in HEMA; mild. Ref.49

VAR_028471

Natural variant

113

1

H → Y in HEMA. Ref.70

VAR_028472

Natural variant

117

1

L → F in HEMA; mild. Ref.82

VAR_028473

Natural variant

117

1

L → R in HEMA; severe. Ref.52
Corresponds to variant rs28935208 [ dbSNP | Ensembl ].

VAR_001056

Natural variant

121

1

G → S in HEMA. Ref.70

VAR_028474

Natural variant

129

1

E → V in HEMA; severe. Ref.59

VAR_001057

Natural variant

130

1

G → R in HEMA; severe.

VAR_001058

Natural variant

132

1

E → D in HEMA; severe. Ref.61 Ref.80
Corresponds to variant rs28935209 [ dbSNP | Ensembl ].

VAR_001059

Natural variant

133

1

Y → C in HEMA; mild. Ref.58
Corresponds to variant rs28935210 [ dbSNP | Ensembl ].

VAR_001060

Natural variant

135

1

D → G in HEMA; severe. Ref.52
Corresponds to variant rs28935211 [ dbSNP | Ensembl ].

VAR_001061

Natural variant

135

1

D → Y in HEMA; severe sporadic. Ref.78

VAR_028475

Natural variant

137

1

T → A in HEMA; severe. Ref.82

VAR_028476

Natural variant

137

1

T → I in HEMA; moderate.

VAR_001062

Natural variant

138

1

S → R in HEMA; mild. Ref.89

VAR_028477

Natural variant

141

1

E → K in HEMA; severe familial. Ref.80

VAR_028478

Natural variant

145

1

D → H in HEMA; moderate. Ref.58

VAR_028479

Natural variant

147

1

V → D in HEMA; severe. Ref.93

VAR_028480

Natural variant

155

1

Y → H in HEMA; moderate. Ref.94

VAR_017332

Natural variant

159

1

V → A in HEMA; moderate. Ref.58

VAR_028481

Natural variant

163

1

N → K in HEMA; moderate. Ref.58

VAR_028482

Natural variant

164

1

G → D in HEMA; moderate. Ref.58

VAR_028483

Natural variant

164

1

G → V in HEMA; mild. Ref.45
Corresponds to variant rs28935212 [ dbSNP | Ensembl ].

VAR_001063

Natural variant

165

1

P → S in HEMA; severe.
Corresponds to variant rs28935213 [ dbSNP | Ensembl ].

VAR_001064

Natural variant

172

1

C → W in HEMA. Ref.70 Ref.91

VAR_028484

Natural variant

176

1

S → P in HEMA. Ref.70

VAR_028485

Natural variant

179

1

S → P in HEMA; moderate. Ref.58

VAR_028486

Natural variant

181

1

V → E in HEMA; mild. Ref.94

VAR_017333

Natural variant

181

1

V → M in HEMA; mild/moderate. Ref.45 Ref.51 Ref.58 Ref.70 Ref.83 Ref.92

VAR_001065

Natural variant

185

1

K → T in HEMA; mild.

VAR_001066

Natural variant

186

1

D → G in HEMA; mild. Ref.89

VAR_028487

Natural variant

186

1

D → N in HEMA. Ref.100

VAR_065304

Natural variant

186

1

D → Y in HEMA; severe. Ref.92

VAR_028488

Natural variant

189

1

S → L in HEMA; moderate. Ref.28 Ref.53

VAR_001067

Natural variant

191

1

L → F in HEMA. Ref.101

VAR_065305

Natural variant

193

1

G → R in HEMA; severe familial. Ref.84

VAR_028489

Natural variant

195

1

L → P in HEMA. Ref.100

VAR_065306

Natural variant

198

1

C → G in HEMA; severe. Ref.87

VAR_028490

Natural variant

202

1

S → N in HEMA; mild. Ref.49

VAR_028491

Natural variant

202

1

S → R in HEMA; mild. Ref.69

VAR_008123

Natural variant

214

1

F → V in HEMA. Ref.70

VAR_028492

Natural variant

217

1

L → H in HEMA; moderate. Ref.50

VAR_028493

Natural variant

219

1

A → D in HEMA. Ref.52

VAR_028494

Natural variant

219

1

A → T in HEMA. Ref.70

VAR_028495

Natural variant

220

1

V → G in HEMA; mild. Ref.92

VAR_028496

Natural variant

222

1

D → V in HEMA; moderate.

VAR_001068

Natural variant

223

1

E → K in HEMA; severe. Ref.65

VAR_028497

Natural variant

224

1

G → W in HEMA; moderate.

VAR_001069

Natural variant

252

1

T → I in HEMA; moderate. Ref.96

VAR_028498

Natural variant

253

1

V → F in HEMA; severe. Ref.61

VAR_001070

Natural variant

254

1

N → I in HEMA; severe. Ref.94

VAR_017334

Natural variant

255

1

G → V in HEMA; severe. Ref.79

VAR_015127

Natural variant

261

1

L → P in HEMA. Ref.100

VAR_065307

Natural variant

262

1

P → L in HEMA; moderate. Ref.92

VAR_028499

Natural variant

263

1

G → S in HEMA. Ref.53

VAR_028500

Natural variant

266

1

G → E in HEMA; severe.

VAR_001071

Natural variant

267

1

C → Y in HEMA; moderate. Ref.82

VAR_028501

Natural variant

274

1

W → C in HEMA. Ref.56
Corresponds to variant rs34371500 [ dbSNP | Ensembl ].

VAR_028502

Natural variant

275

1

H → L in HEMA; mild. Ref.49

VAR_028503

Natural variant

278

1

G → R in HEMA; severe. Ref.52

VAR_001072

Natural variant

280

1

G → D in HEMA. Ref.100

VAR_065308

Natural variant

284

1

E → K in HEMA; moderate. Ref.89

VAR_028504

Natural variant

285

1

V → G in HEMA; mild. Ref.38 Ref.49

VAR_001073

Natural variant

291

1

E → G in HEMA; mild. Ref.25

VAR_001074

Natural variant

291

1

E → K in HEMA; mild. Ref.41 Ref.58 Ref.70 Ref.91

VAR_028505

Natural variant

294

1

T → I in HEMA; moderate.

VAR_001075

Natural variant

295

1

F → L in HEMA; moderate. Ref.75

VAR_028506

Natural variant

297

1

V → A in HEMA; mild. Ref.58

VAR_028507

Natural variant

299

1

N → I in HEMA; mild. Ref.48 Ref.50
Corresponds to variant rs28935215 [ dbSNP | Ensembl ].

VAR_001076

Natural variant

301

1

R → C in HEMA; severe/mild. Ref.49 Ref.82 Ref.91 Ref.93

VAR_028508

Natural variant

301

1

R → H in HEMA; severe. Ref.38 Ref.68 Ref.69 Ref.82
Corresponds to variant rs28935216 [ dbSNP | Ensembl ].

VAR_001077

Natural variant

301

1

R → L in HEMA; severe. Ref.52

VAR_001078

Natural variant

302

1

Missing in HEMA. Ref.52

VAR_028509

Natural variant

303

1

A → E in HEMA; mild. Ref.54 Ref.58

VAR_028510

Natural variant

303

1

A → P in HEMA; mild. Ref.55

VAR_028511

Natural variant

307

1

I → S in HEMA; moderate. Ref.75

VAR_028512

Natural variant

308

1

S → L in HEMA; moderate. Ref.47 Ref.54 Ref.68
Corresponds to variant rs28937268 [ dbSNP | Ensembl ].

VAR_001079

Natural variant

312

1

F → S in HEMA; mild/moderate. Ref.38 Ref.58

VAR_001080

Natural variant

314

1

T → A in HEMA; mild. Ref.70
Corresponds to variant rs28937269 [ dbSNP | Ensembl ].

VAR_001081

Natural variant

314

1

T → I in HEMA; moderate. Ref.61

VAR_001082

Natural variant

315

1

A → V in HEMA. Ref.70

VAR_028513

Natural variant

320

1

Missing in HEMA; severe.

VAR_028514

Natural variant

323

1

G → E in HEMA; severe. Ref.79

VAR_015128

Natural variant

326

1

L → P in HEMA. Ref.95

VAR_028515

Natural variant

327

1

L → P in HEMA; severe. Ref.52 Ref.78
Corresponds to variant rs28937270 [ dbSNP | Ensembl ].

VAR_001083

Natural variant

327

1

L → V in HEMA; mild. Ref.89

VAR_028516

Natural variant

329

1

C → F in HEMA. Ref.95

VAR_028517

Natural variant

331

1

I → V in HEMA; mild. Ref.61

VAR_001084

Natural variant

339

1

M → T in HEMA; moderate. Ref.83

VAR_028518

Natural variant

340

1

E → K in HEMA. Ref.70

VAR_028519

Natural variant

345

1

V → A in HEMA. Ref.91

VAR_028520

Natural variant

345

1

V → L in HEMA; severe. Ref.36

VAR_001085

Natural variant

348

1

C → R in HEMA; severe. Ref.36

VAR_001086

Natural variant

348

1

C → S in HEMA; moderate.

VAR_001087

Natural variant

348

1

C → Y in HEMA; mild/severe. Ref.82

VAR_001088

Natural variant

365

1

Y → C in HEMA; mild. Ref.89 Ref.98

VAR_028521

Natural variant

391

1

R → C in HEMA; Okayama; moderate/severe; abolishes the normal cleavage by thrombin. Ref.27 Ref.33 Ref.79 Ref.84

VAR_001089

Natural variant

391

1

R → H in HEMA; Kumamoto; mild/moderate; abolishes the normal cleavage by thrombin. Ref.30 Ref.47 Ref.58 Ref.91 Ref.95
Corresponds to variant rs28935499 [ dbSNP | Ensembl ].

VAR_001090

Natural variant

391

1

R → P in HEMA; severe; abolishes the normal cleavage by thrombin.

VAR_001091

Natural variant

392

1

S → L in HEMA; mild; abolishes normal cleavage by thrombin.
Corresponds to variant rs28933668 [ dbSNP | Ensembl ].

VAR_001092

Natural variant

392

1

S → P in HEMA; mild.
Corresponds to variant rs28933669 [ dbSNP | Ensembl ].

VAR_001093

Natural variant

394

1

A → S in HEMA. Ref.100

VAR_065309

Natural variant

401

1

W → G in HEMA. Ref.95

VAR_028522

Natural variant

405

1

I → F in HEMA. Ref.70

VAR_028523

Natural variant

405

1

I → S in HEMA; severe.
Corresponds to variant rs28933670 [ dbSNP | Ensembl ].

VAR_001094

Natural variant

409

1

E → G in HEMA; severe/moderate. Ref.78
Corresponds to variant rs28933671 [ dbSNP | Ensembl ].

VAR_001095

Natural variant

412

1

W → G in HEMA. Ref.70

VAR_028524

Natural variant

412

1

W → R in HEMA; severe. Ref.92

VAR_028525

Natural variant

427

1

K → I in HEMA; mild. Ref.58

VAR_028526

Natural variant

431

1

L → F in HEMA; moderate.
Corresponds to variant rs28933672 [ dbSNP | Ensembl ].

VAR_001096

Natural variant

431

1

L → S in HEMA; moderate. Ref.89

VAR_028527

Natural variant

437

1

R → P in HEMA; severe. Ref.89

VAR_028528

Natural variant

437

1

R → W in HEMA; mild. Ref.58

VAR_028529

Natural variant

438

1

I → F in HEMA; not severe. Ref.92

VAR_028530

Natural variant

439

1

G → D in HEMA; severe. Ref.92

VAR_028531

Natural variant

439

1

G → S in HEMA; moderate. Ref.94

VAR_017335

Natural variant

439

1

G → V in HEMA; severe. Ref.64 Ref.91

VAR_001097

Natural variant

442

1

Y → C in HEMA. Ref.91

VAR_028532

Natural variant

444

1

K → R in HEMA; severe. Ref.38
Corresponds to variant rs28937272 [ dbSNP | Ensembl ].

VAR_001098

Natural variant

450

1

Y → D in HEMA; severe. Ref.97

VAR_028533

Natural variant

450

1

Y → N in HEMA; mild/moderate. Ref.48 Ref.50 Ref.58
Corresponds to variant rs28937273 [ dbSNP | Ensembl ].

VAR_001099

Natural variant

454

1

T → I in HEMA; mild. Ref.58

VAR_028534

Natural variant

455

1

F → C in HEMA; mild-moderate/severe. Ref.83 Ref.89

VAR_028535

Natural variant

466

1

G → E in HEMA; severe sporadic. Ref.80

VAR_028536

Natural variant

470

1

P → L in HEMA; mild. Ref.58 Ref.91

VAR_028537

Natural variant

470

1

P → R in HEMA; mild. Ref.92

VAR_028538

Natural variant

470

1

P → T in HEMA; mild sporadic. Ref.70 Ref.80 Ref.98

VAR_028539

Natural variant

474

1

G → E in HEMA. Ref.70

VAR_028540

Natural variant

474

1

G → R in HEMA; severe. Ref.61

VAR_001100

Natural variant

474

1

G → V in HEMA. Ref.100

VAR_065310

Natural variant

475

1

E → K in HEMA; moderate. Ref.82

VAR_028541

Natural variant

477

1

G → V in HEMA; moderate. Ref.90

VAR_028542

Natural variant

478

1

D → N in HEMA. Ref.70

VAR_028543

Natural variant

479

1

T → R in HEMA.

VAR_028544

Natural variant

484

1

F → C in HEMA. Ref.70

VAR_028545

Natural variant

488

1

A → G in HEMA; moderate.

VAR_001101

Natural variant

490

1

R → G in HEMA. Ref.70

VAR_028546

Natural variant

492

1

Y → C in HEMA; moderate. Ref.56
Corresponds to variant rs28937275 [ dbSNP | Ensembl ].

VAR_001103

Natural variant

492

1

Y → H in HEMA; mild. Ref.38
Corresponds to variant rs28937274 [ dbSNP | Ensembl ].

VAR_001102

Natural variant

494

1

I → T in HEMA; mild.
Corresponds to variant rs28936968 [ dbSNP | Ensembl ].

VAR_001104

Natural variant

496

1

P → R in HEMA. Ref.100

VAR_065311

Natural variant

498

1

G → R in HEMA; severe/moderate. Ref.56 Ref.61 Ref.70 Ref.78
Corresponds to variant rs28936969 [ dbSNP | Ensembl ].

VAR_001105

Natural variant

503

1

R → H in HEMA. Ref.80
Corresponds to variant rs35383156 [ dbSNP | Ensembl ].

VAR_028547

Natural variant

513

1

G → S in HEMA; moderate. Ref.92

VAR_028548

Natural variant

513

1

G → V in HEMA. Ref.100

VAR_065312

Natural variant

522

1

I → Y in HEMA; requires 2 nucleotide substitutions. Ref.95

VAR_028549

Natural variant

529

1

K → E in HEMA; moderate. Ref.94

VAR_017336

Natural variant

532

1

W → G in HEMA. Ref.91

VAR_028550

Natural variant

540

1

P → T in HEMA. Ref.95

VAR_028551

Natural variant

541

1

T → S in HEMA; mild. Ref.58 Ref.92 Ref.98

VAR_028552

Natural variant

544

1

D → N in HEMA; moderate.
Corresponds to variant rs28937276 [ dbSNP | Ensembl ].

VAR_001106

Natural variant

546

1

R → W in HEMA; mild. Ref.47 Ref.50 Ref.55 Ref.58 Ref.70 Ref.83 Ref.95
Corresponds to variant rs28937277 [ dbSNP | Ensembl ].

VAR_001107

Natural variant

550

1

R → C in HEMA; mild/moderate. Ref.45 Ref.58 Ref.70 Ref.79 Ref.84 Ref.92
Corresponds to variant rs28937278 [ dbSNP | Ensembl ].

VAR_001108

Natural variant

550

1

R → G in HEMA; mild. Ref.62

VAR_001109

Natural variant

550

1

R → H in HEMA; mild/moderate. Ref.54 Ref.55 Ref.56 Ref.58
Corresponds to variant rs28937279 [ dbSNP | Ensembl ].

VAR_001110

Natural variant

553

1

S → P in HEMA; severe. Ref.58

VAR_028553

Natural variant

554

1

S → C in HEMA; moderate. Ref.83

VAR_028554

Natural variant

554

1

S → G in HEMA; mild. Ref.45 Ref.92

VAR_001111

Natural variant

556

1

V → D in HEMA; moderate.

VAR_001112

Natural variant

560

1

R → T in HEMA; mild. Ref.58

VAR_028555

Natural variant

561

1

D → G in HEMA; severe. Ref.38

VAR_028556

Natural variant

561

1

D → H in HEMA. Ref.70

VAR_028557

Natural variant

561

1

D → Y in HEMA; severe. Ref.77 Ref.96

VAR_008967

Natural variant

567

1

I → T in HEMA; mild. Ref.94

VAR_017337

Natural variant

569

1

P → R in HEMA. Ref.100

VAR_065313

Natural variant

577

1

S → F in HEMA; mild. Ref.47

VAR_001113

Natural variant

578

1

V → A in HEMA; mild. Ref.58

VAR_028558

Natural variant

579

1

D → A in HEMA; mild. Ref.82

VAR_028559

Natural variant

579

1

D → H in HEMA; mild. Ref.89

VAR_028560

Natural variant

583

1

N → S in HEMA; mild. Ref.92

VAR_028561

Natural variant

584

1

Q → H in HEMA; mild. Ref.89

VAR_028562

Natural variant

584

1

Q → K in HEMA; moderate.

VAR_001114

Natural variant

584

1

Q → R in HEMA. Ref.70

VAR_028563

Natural variant

585

1

I → R in HEMA; moderate-severe. Ref.76

VAR_028564

Natural variant

585

1

I → T in HEMA; severe/moderate. Ref.70

VAR_001115

Natural variant

586

1

M → V in HEMA; mild. Ref.79

VAR_015129

Natural variant

588

1

D → G in HEMA. Ref.70

VAR_028565

Natural variant

588

1

D → Y in HEMA. Ref.95

VAR_028566

Natural variant

594

1

L → Q in HEMA; mild. Ref.92

VAR_028567

Natural variant

596

1

S → P in HEMA; severe.

VAR_001116

Natural variant

601

1

N → D in HEMA. Ref.70

VAR_028568

Natural variant

601

1

N → K in HEMA. Ref.70

VAR_028569

Natural variant

602

1

R → G in HEMA; mild familial. Ref.70 Ref.80 Ref.98

VAR_028570

Natural variant

603

1

S → I in HEMA.

VAR_001117

Natural variant

603

1

S → R in HEMA; severe. Ref.58 Ref.78

VAR_028571

Natural variant

604

1

W → C in HEMA; severe.

VAR_001118

Natural variant

605

1

Y → H in HEMA. Ref.70

VAR_028572

Natural variant

605

1

Y → S in HEMA; severe.

VAR_001119

Natural variant

609

1

N → I in HEMA; moderate. Ref.92

VAR_028573

Natural variant

612

1

R → C in HEMA; mild/moderate; secretion impaired. Ref.38 Ref.45 Ref.50 Ref.66 Ref.70 Ref.73 Ref.82 Ref.84 Ref.92 Ref.93 Ref.97

VAR_001120

Natural variant

631

1

N → K in HEMA; severe. Ref.59

VAR_001121

Natural variant

631

1

N → S in HEMA.

VAR_001122

Natural variant

633

1

M → I in HEMA; mild. Ref.58

VAR_028574

Natural variant

635

1

S → N in HEMA; mild. Ref.92

VAR_028575

Natural variant

637

1

N → D in HEMA; severe sporadic/moderate. Ref.49 Ref.78

VAR_028576

Natural variant

637

1

N → I in HEMA. Ref.100

VAR_065314

Natural variant

637

1

N → S in HEMA; mild; secretion impaired. Ref.73

VAR_028577

Natural variant

639

1

Y → C in HEMA; moderate. Ref.57

VAR_028578

Natural variant

644

1

L → V in HEMA; mild. Ref.61

VAR_001123

Natural variant

650

1

L → F in HEMA; mild. Ref.89

VAR_028579

Natural variant

653

1

V → A in HEMA; mild. Ref.47

VAR_001124

Natural variant

653

1

V → M in HEMA; severe. Ref.47 Ref.91

VAR_001125

Natural variant

659

1

L → P in HEMA. Ref.52

VAR_028580

Natural variant

663

1

A → V in HEMA; mild.

VAR_001126

Natural variant

664

1

Q → P in HEMA; moderate-severe. Ref.76

VAR_028581

Natural variant

671

1

Missing in HEMA; severe. Ref.47

VAR_001127

Natural variant

677

1

F → L in HEMA; moderate.

VAR_001128

Natural variant

681

1

M → I in HEMA; mild. Ref.89

VAR_028582

Natural variant

682

1

V → F in HEMA. Ref.66

VAR_028583

Natural variant

683

1

Y → C in HEMA; severe. Ref.82 Ref.91 Ref.95

VAR_028584

Natural variant

683

1

Y → N in HEMA; mild. Ref.58

VAR_028585

Natural variant

686

1

T → R in HEMA. Ref.56

VAR_028586

Natural variant

698

1

F → L in HEMA. Ref.82

VAR_028587

Natural variant

699

1

M → T in HEMA; mild. Ref.92

VAR_028588

Natural variant

699

1

M → V in HEMA; severe. Ref.61

VAR_001129

Natural variant

701

1

M → I in HEMA; mild. Ref.92

VAR_028589

Natural variant

705

1

G → V in HEMA; moderate. Ref.50

VAR_028590

Natural variant

710

1

G → W in HEMA. Ref.82

VAR_028591

Natural variant

713

1

N → I in HEMA; mild. Ref.74

VAR_028592

Natural variant

717

1

R → L in HEMA; mild. Ref.54

VAR_028593

Natural variant

717

1

R → W in HEMA; mild. Ref.45 Ref.54 Ref.70 Ref.98

VAR_001130

Natural variant

720

1

G → D in HEMA; severe/moderate. Ref.51 Ref.61

VAR_001131

Natural variant

720

1

G → S in HEMA. Ref.95

VAR_028594

Natural variant

721

1

M → I in HEMA; severe. Ref.92

VAR_028595

Natural variant

721

1

M → L in HEMA; mild. Ref.58

VAR_028596

Natural variant

723

1

A → T in HEMA; moderate. Ref.38 Ref.62

VAR_001132

Natural variant

725

1

L → Q in HEMA; severe. Ref.89

VAR_028597

Natural variant

727

1

V → F in HEMA; severe. Ref.61

VAR_001133

Natural variant

739

1

E → K in HEMA; mild.
Corresponds to variant rs28937285 [ dbSNP | Ensembl ].

VAR_001134

Natural variant

742

1

Y → C in HEMA; mild. Ref.58

VAR_028598

Natural variant

795

1

R → G.
Corresponds to variant rs2228152 [ dbSNP | Ensembl ].

VAR_024380

Natural variant

947

1

P → R in HEMA. Ref.53

VAR_028599

Natural variant

1012

1

V → L in HEMA. Ref.52

VAR_028600

Natural variant

1057

1

E → K in HEMA; moderate. Ref.53
Corresponds to variant rs28933673 [ dbSNP | Ensembl ].

VAR_001135

Natural variant

1066

1

H → Y in HEMA. Ref.95

VAR_028601

Natural variant

1260

1

D → E. Ref.6 Ref.52 Ref.93
Corresponds to variant rs1800291 [ dbSNP | Ensembl ].

VAR_001136

Natural variant

1289

1

K → Q.
Corresponds to variant rs1800292 [ dbSNP | Ensembl ].

VAR_048438

Natural variant

1336

1

Q → K in HEMA. Ref.91

VAR_028602

Natural variant

1460

1

N → K in HEMA. Ref.47

VAR_028603

Natural variant

1481

1

L → P.
Corresponds to variant rs1800294 [ dbSNP | Ensembl ].

VAR_001137

Natural variant

1610

1

A → S in HEMA. Ref.53

VAR_028604

Natural variant

1698

1

I → T in HEMA; mild. Ref.58

VAR_028605

Natural variant

1699

1

Y → C in HEMA; severe.

VAR_001138

Natural variant

1699

1

Y → F in HEMA; moderate. Ref.34 Ref.38
Corresponds to variant rs28935203 [ dbSNP | Ensembl ].

VAR_001139

Natural variant

1701

1

E → K in HEMA; mild. Ref.98

VAR_028606

Natural variant

1705

1

Q → H in HEMA; mild sporadic. Ref.84

VAR_028607

Natural variant

1708

1

R → C in HEMA; East Hartford; severe/moderate/mild; abolishes thrombin cleavage at the light chain. Ref.26 Ref.31 Ref.34 Ref.40 Ref.50 Ref.52 Ref.56 Ref.70 Ref.79 Ref.82 Ref.98

VAR_001140

Natural variant

1708

1

R → H in HEMA; mild; abolishes thrombin cleavage at the light chain. Ref.40 Ref.91
Corresponds to variant rs28937286 [ dbSNP | Ensembl ].

VAR_001141

Natural variant

1714

1

T → S in HEMA; moderate. Ref.90

VAR_028608

Natural variant

1715

1

R → G in HEMA; mild. Ref.43 Ref.58

VAR_001142

Natural variant

1720

1

A → V in HEMA. Ref.100

VAR_065315

Natural variant

1723

1

E → K in HEMA; severe. Ref.37

VAR_001143

Natural variant

1727

1

D → V in HEMA; mild. Ref.89 Ref.98

VAR_028609

Natural variant

1728

1

Y → C in HEMA; moderate. Ref.35

VAR_001144

Natural variant

1740

1

R → G in HEMA; mild. Ref.89

VAR_028610

Natural variant

1751

1

K → Q in HEMA. Ref.70

VAR_028611

Natural variant

1762

1

F → L in HEMA. Ref.100

VAR_065316

Natural variant

1768

1

R → H in HEMA. Ref.95

VAR_028612

Natural variant

1769

1

G → R in HEMA; mild.

VAR_001145

Natural variant

1771

1

L → P in HEMA. Ref.95

VAR_028613

Natural variant

1775

1

L → F in HEMA; mild.

VAR_001147

Natural variant

1775

1

L → V in HEMA; moderate.

VAR_001146

Natural variant

1777

1

L → P in HEMA; moderate. Ref.90

VAR_028614

Natural variant

1779

1

G → E in HEMA; severe/moderate. Ref.76

VAR_001148

Natural variant

1779

1

G → R in HEMA; severe. Ref.58 Ref.92

VAR_028615

Natural variant

1780

1

P → L in HEMA; moderate. Ref.92

VAR_028616

Natural variant

1782

1

I → R in HEMA; severe sporadic. Ref.84

VAR_028617

Natural variant

1788

1

D → H in HEMA; mild. Ref.82

VAR_028618

Natural variant

1791

1

M → T in HEMA; severe. Ref.58 Ref.92

VAR_001149

Natural variant

1798

1

A → P in HEMA; severe. Ref.92

VAR_028619

Natural variant

1799

1

S → H in HEMA; requires 2 nucleotide substitutions.

VAR_028620

Natural variant

1800

1

R → C in HEMA; moderate. Ref.46 Ref.64 Ref.79

VAR_001151

Natural variant

1800

1

R → G in HEMA; mild.

VAR_001152

Natural variant

1800

1

R → H in HEMA; moderate/severe. Ref.38 Ref.57 Ref.58 Ref.59 Ref.70 Ref.92 Ref.95 Ref.97

VAR_001150

Natural variant

1801

1

P → A in HEMA; mild. Ref.58

VAR_028621

Natural variant

1802

1

Y → C in HEMA; moderate. Ref.70 Ref.97

VAR_028622

Natural variant

1803

1

S → Y in HEMA; severe. Ref.38

VAR_001153

Natural variant

1804

1

F → S in HEMA; severe. Ref.94

VAR_017338

Natural variant

1808

1

L → F in HEMA; mild. Ref.45 Ref.49

VAR_001154

Natural variant

1842

1

M → I in HEMA; moderate.
Corresponds to variant rs28933674 [ dbSNP | Ensembl ].

VAR_001155

Natural variant

1844

1

P → S in HEMA; mild.
Corresponds to variant rs28933675 [ dbSNP | Ensembl ].

VAR_001156

Natural variant

1845

1

T → P in HEMA; mild. Ref.42
Corresponds to variant rs28933676 [ dbSNP | Ensembl ].

VAR_001157

Natural variant

1848

1

E → G in HEMA; mild. Ref.92

VAR_028623

Natural variant

1853

1

A → T in HEMA; moderate/severe. Ref.51 Ref.70 Ref.80

VAR_001158

Natural variant

1853

1

A → V in HEMA; mild.
Corresponds to variant rs28933677 [ dbSNP | Ensembl ].

VAR_001159

Natural variant

1858

1

S → C in HEMA; moderate. Ref.89

VAR_028624

Natural variant

1864

1

K → E in HEMA. Ref.70

VAR_028625

Natural variant

1865

1

D → N in HEMA; severe. Ref.52

VAR_001160

Natural variant

1865

1

D → Y in HEMA; severe.

VAR_001161

Natural variant

1867

1

H → P in HEMA; mild. Ref.49

VAR_028626

Natural variant

1867

1

H → R in HEMA; moderate.
Corresponds to variant rs28933679 [ dbSNP | Ensembl ].

VAR_001162

Natural variant

1869

1

G → D in HEMA; severe. Ref.89

VAR_028627

Natural variant

1869

1

G → V in HEMA; severe. Ref.77 Ref.96

VAR_001163

Natural variant

1872

1

G → E in HEMA; severe sporadic. Ref.84

VAR_028628

Natural variant

1873

1

P → R in HEMA; severe. Ref.52
Corresponds to variant rs28933680 [ dbSNP | Ensembl ].

VAR_001164

Natural variant

1875

1

L → P in HEMA. Ref.91

VAR_028629

Natural variant

1876

1

V → L in HEMA; mild. Ref.82

VAR_028630

Natural variant

1877

1

C → R in HEMA. Ref.91

VAR_028631

Natural variant

1877

1

C → Y in HEMA. Ref.101

VAR_065317

Natural variant

1882

1

L → P in HEMA. Ref.70

VAR_028632

Natural variant

1888

1

R → I in HEMA; severe. Ref.51 Ref.70 Ref.98

VAR_001165

Natural variant

1894

1

E → G in HEMA; moderate. Ref.62 Ref.78

VAR_001166

Natural variant

1901

1

I → F in HEMA; mild. Ref.58

VAR_028633

Natural variant

1904

1

E → D in HEMA. Ref.95

VAR_028634

Natural variant

1904

1

E → K in HEMA; severe.
Corresponds to variant rs28933681 [ dbSNP | Ensembl ].

VAR_001167

Natural variant

1907

1

S → C in HEMA; moderate. Ref.92

VAR_028635

Natural variant

1907

1

S → R in HEMA; severe. Ref.92

VAR_028636

Natural variant

1908

1

W → L in HEMA; mild. Ref.57

VAR_028637

Natural variant

1909

1

Y → C in HEMA; moderate. Ref.75

VAR_028638

Natural variant

1939

1

A → T in HEMA; severe. Ref.92

VAR_028639

Natural variant

1939

1

A → V in HEMA; unknown pathological significance. Ref.92

VAR_028640

Natural variant

1941

1

N → D in HEMA; severe/moderate. Ref.35 Ref.38

VAR_001168

Natural variant

1941

1

N → S in HEMA; severe/moderate. Ref.38 Ref.45
Corresponds to variant rs28933682 [ dbSNP | Ensembl ].

VAR_001169

Natural variant

1942

1

G → A in HEMA; moderate. Ref.79

VAR_015130

Natural variant

1945

1

M → V in HEMA; moderate. Ref.93

VAR_028641

Natural variant

1951

1

L → F in HEMA; mild. Ref.54

VAR_028642

Natural variant

1960

1

R → L in HEMA; moderate. Ref.44

VAR_001171

Natural variant

1960

1

R → Q in HEMA; mild/moderate. Ref.41 Ref.49 Ref.56 Ref.58
Corresponds to variant rs28937294 [ dbSNP | Ensembl ].

VAR_001170

Natural variant

1963

1

L → P in HEMA; severe. Ref.79

VAR_015131

Natural variant

1965

1

S → I in HEMA. Ref.91

VAR_028643

Natural variant

1966

1

M → I in HEMA; mild. Ref.55

VAR_028644

Natural variant

1966

1

M → V in HEMA; mild. Ref.98

VAR_028645

Natural variant

1967

1

G → D in HEMA; moderate.
Corresponds to variant rs28937295 [ dbSNP | Ensembl ].

VAR_001172

Natural variant

1968

1

S → R in HEMA; mild. Ref.89

VAR_028646

Natural variant

1971

1

N → T in HEMA. Ref.52

VAR_028647

Natural variant

1973

1

H → L in HEMA; mild. Ref.67 Ref.70

VAR_028648

Natural variant

1979

1

G → V in HEMA; moderate.

VAR_001173

Natural variant

1980

1

H → P in HEMA. Ref.95

VAR_028649

Natural variant

1980

1

H → Y in HEMA; mild.

VAR_001174

Natural variant

1982

1

F → I in HEMA; mild. Ref.92

VAR_028650

Natural variant

1985

1

R → Q in HEMA; mild. Ref.58 Ref.80 Ref.92

VAR_028651

Natural variant

1994

1

L → P in HEMA; moderate. Ref.99

VAR_028652

Natural variant

1998

1

Y → C in HEMA; mild. Ref.89

VAR_028653

Natural variant

2000

1

G → A in HEMA; moderate-severe. Ref.76

VAR_028654

Natural variant

2004

1

T → R in HEMA; sporadic. Ref.80

VAR_028655

Natural variant

2007

1

M → I in HEMA; mild. Ref.58

VAR_028656

Natural variant

2013

1

G → R in HEMA. Ref.101

VAR_065318

Natural variant

2015

1

W → C in HEMA; moderate. Ref.92

VAR_028657

Natural variant

2016

1

R → P in HEMA; severe familial. Ref.84

VAR_028658

Natural variant

2016

1

R → W in HEMA; severe/moderate/mild. Ref.50 Ref.52 Ref.58 Ref.70 Ref.80 Ref.82 Ref.84 Ref.92 Ref.98

VAR_001175

Natural variant

2018

1

E → G in HEMA; moderate. Ref.98

VAR_028659

Natural variant

2022

1

G → D in HEMA; severe. Ref.58

VAR_028660

Natural variant

2028

1

G → R in HEMA. Ref.66

VAR_028661

Natural variant

2030

1

S → N in HEMA; mild. Ref.58

VAR_028662

Natural variant

2035

1

V → A in HEMA. Ref.70

VAR_028663

Natural variant

2036

1

Y → C in HEMA; moderate. Ref.79

VAR_015132

Natural variant

2038

1

N → S in HEMA; mild/moderate. Ref.58 Ref.92

VAR_001176

Natural variant

2040

1

C → Y in HEMA. Ref.70

VAR_028664

Natural variant

2045

1

G → E in HEMA; mild. Ref.82

VAR_028665

Natural variant

2045

1

G → V in HEMA; severe sporadic. Ref.65 Ref.78

VAR_028666

Natural variant

2051

1

I → S in HEMA; severe. Ref.94

VAR_017339

Natural variant

2056

1

I → N in HEMA; severe. Ref.89

VAR_028667

Natural variant

2058

1

A → P in HEMA; moderate. Ref.75

VAR_028668

Natural variant

2065

1

W → R in HEMA; moderate. Ref.45

VAR_001177

Natural variant

2067

1

P → L in HEMA; severe sporadic. Ref.78 Ref.98

VAR_028669

Natural variant

2070

1

A → V in HEMA; mild. Ref.89

VAR_028670

Natural variant

2082

1

S → N in HEMA; severe. Ref.89

VAR_028671

Natural variant

2088

1

S → F in HEMA; severe.

VAR_001178

Natural variant

2093

1

D → G in HEMA; mild.

VAR_001179

Natural variant

2093

1

D → Y in HEMA; severe familial. Ref.80

VAR_028672

Natural variant

2101

1

H → D in HEMA. Ref.100

VAR_065319

Natural variant

2105

1

T → N in HEMA; moderate. Ref.61

VAR_001180

Natural variant

2106

1

Q → E in HEMA; mild. Ref.72

VAR_028673

Natural variant

2106

1

Q → P in HEMA. Ref.100

VAR_065320

Natural variant

2106

1

Q → R in HEMA; mild. Ref.57

VAR_028674

Natural variant

2107

1

G → S in HEMA; severe. Ref.62

VAR_001181

Natural variant

2109

1

R → C in HEMA; mild. Ref.72

VAR_028675

Natural variant

2117

1

I → F in HEMA. Ref.91

VAR_028676

Natural variant

2117

1

I → S in HEMA; mild-moderate; affinity for VWF reduced 8-fold. Ref.71

VAR_028677

Natural variant

2119

1

Q → R in HEMA; moderate. Ref.50

VAR_028678

Natural variant

2120

1

F → C in HEMA. Ref.70

VAR_028679

Natural variant

2120

1

F → L in HEMA; mild.

VAR_001182

Natural variant

2124

1

Y → C in HEMA; mild. Ref.66 Ref.79

VAR_001183

Natural variant

2135

1

R → P in HEMA; severe. Ref.23

VAR_001184

Natural variant

2138

1

S → Y in HEMA; moderate; affinity for VWF reduced 80-fold. Ref.71

VAR_001185

Natural variant

2141

1

T → N in HEMA; severe. Ref.94

VAR_017340

Natural variant

2143

1

M → V in HEMA. Ref.100

VAR_065321

Natural variant

2145

1

F → C in HEMA; mild. Ref.70 Ref.89

VAR_028680

Natural variant

2148

1

N → S in HEMA; moderate. Ref.71

VAR_001186

Natural variant

2157

1

N → D in HEMA; mild. Ref.89

VAR_028681

Natural variant

2162

1

P → L in HEMA; severe. Ref.98

VAR_028682

Natural variant

2169

1

R → C in HEMA; mild. Ref.72 Ref.95

VAR_028683

Natural variant

2169

1

R → H in HEMA; severe/mild; affinity for VWF reducced 3-fold. Ref.38 Ref.45 Ref.49 Ref.53 Ref.56 Ref.64 Ref.66 Ref.68 Ref.70 Ref.71 Ref.76 Ref.80 Ref.84 Ref.92 Ref.95

VAR_001187

Natural variant

2172

1

P → L in HEMA. Ref.100

VAR_065322

Natural variant

2172

1

P → Q in HEMA; moderate. Ref.71

VAR_001188

Natural variant

2172

1

P → R in HEMA; severe. Ref.78 Ref.79

VAR_015133

Natural variant

2173

1

T → A in HEMA; mild. Ref.89

VAR_028684

Natural variant

2173

1

T → I in HEMA; mild. Ref.46

VAR_001189

Natural variant

2174

1

H → D in HEMA. Ref.95

VAR_028685

Natural variant

2178

1

R → C in HEMA; mild/moderate. Ref.45 Ref.47 Ref.49 Ref.56 Ref.70 Ref.72 Ref.82 Ref.83 Ref.93 Ref.95

VAR_001190

Natural variant

2178

1

R → H in HEMA; mild. Ref.95

VAR_001191

Natural variant

2178

1

R → L in HEMA; mild.

VAR_001192

Natural variant

2182

1

R → C in HEMA; severe/moderate. Ref.72 Ref.78 Ref.79 Ref.82 Ref.91 Ref.95

VAR_001193

Natural variant

2182

1

R → H in HEMA; severe/moderate. Ref.60 Ref.64 Ref.66 Ref.70 Ref.80 Ref.82 Ref.84 Ref.98

VAR_001194

Natural variant

2182

1

R → P in HEMA; moderate/severe. Ref.82

VAR_028686

Natural variant

2183

1

M → R in HEMA; moderate. Ref.72

VAR_028687

Natural variant

2183

1

M → V in HEMA; mild. Ref.70

VAR_001195

Natural variant

2185

1

L → S in HEMA; severe. Ref.78

VAR_001196

Natural variant

2185

1

L → W in HEMA. Ref.91

VAR_028688

Natural variant

2192

1

S → I in HEMA; mild. Ref.72 Ref.92

VAR_028689

Natural variant

2193

1

C → G in HEMA. Ref.88

VAR_017341

Natural variant

2196

1

P → R in HEMA.

VAR_028690

Natural variant

2198

1

G → V in HEMA; severe sporadic. Ref.70 Ref.80

VAR_028691

Natural variant

2200

1

E → D in HEMA. Ref.66

VAR_028692

Natural variant

2204

1

I → T in HEMA; mild. Ref.62

VAR_001197

Natural variant

2209

1

I → N in HEMA; moderate.

VAR_001198

Natural variant

2211

1

A → P in HEMA; moderate.

VAR_001199

Natural variant

2220

1

A → P in HEMA; mild. Ref.72

VAR_028693

Natural variant

2223

1

Missing in HEMA; severe/moderate.

VAR_001200

Natural variant

2224

1

P → L in HEMA. Ref.91

VAR_028695

Natural variant

2224

1

Missing in HEMA; moderate. Ref.42

VAR_028694

Natural variant

2228

1

R → G in HEMA; severe. Ref.95

VAR_001201

Natural variant

2228

1

R → L in HEMA; moderate.

VAR_001202

Natural variant

2228

1

R → P in HEMA; moderate-severe. Ref.76

VAR_028696

Natural variant

2228

1

R → Q in HEMA; severe/moderate. Ref.24 Ref.32 Ref.38 Ref.52 Ref.68 Ref.75 Ref.79 Ref.80

VAR_001203

Natural variant

2229

1

L → F in HEMA. Ref.95

VAR_028697

Natural variant

2242

1

V → M. Ref.53

VAR_001204

Natural variant

2248

1

W → C in HEMA; moderate. Ref.45 Ref.66 Ref.70

VAR_001205

Natural variant

2248

1

W → S in HEMA; moderate. Ref.96

VAR_028698

Natural variant

2251

1

V → A in HEMA; mild. Ref.72 Ref.97

VAR_028699

Natural variant

2251

1

V → E in HEMA. Ref.91

VAR_028700

Natural variant

2257

1

M → V. Ref.6 Ref.49 Ref.65
Corresponds to variant rs1800297 [ dbSNP | Ensembl ].

VAR_021356

Natural variant

2262

1

V → VQ in HEMA; moderate. Ref.94

VAR_017342

Natural variant

2264

1

T → A in HEMA. Ref.56

VAR_028701

Natural variant

2265

1

Q → R in HEMA; moderate.

VAR_001206

Natural variant

2279

1

F → C in HEMA; severe sporadic. Ref.65 Ref.78

VAR_028702

Natural variant

2279

1

F → I in HEMA. Ref.66

VAR_028703

Natural variant

2281

1

I → T in HEMA; severe. Ref.49

VAR_028704

Natural variant

2286

1

D → G in HEMA. Ref.100

VAR_065323

Natural variant

2290

1

W → L in HEMA. Ref.91

VAR_028705

Natural variant

2304

1

G → V in HEMA. Ref.56

VAR_028706

Natural variant

2307

1

D → A in HEMA; moderate/mild. Ref.79 Ref.82

VAR_015134

Natural variant

2319

1

P → L in HEMA; mild/severe. Ref.72 Ref.78 Ref.95

VAR_001207

Natural variant

2319

1

P → S in HEMA; mild. Ref.37 Ref.64

VAR_001208

Natural variant

2323

1

R → C in HEMA; severe/moderate; may cause reduced phospholipid binding. Ref.38 Ref.72 Ref.91 Ref.95

VAR_001209

Natural variant

2323

1

R → G in HEMA; moderate. Ref.72

VAR_028707

Natural variant

2323

1

R → H in HEMA; mild; may cause reduced phospholipid binding. Ref.95

VAR_001210

Natural variant

2323

1

R → L in HEMA; mild. Ref.82

VAR_028708

Natural variant

2326

1

R → G in HEMA. Ref.70

VAR_028709

Natural variant

2326

1

R → L in HEMA; severe/moderate; may cause reduced phospholipid binding. Ref.29 Ref.32 Ref.52 Ref.78 Ref.92

VAR_001211

Natural variant

2326

1

R → P in HEMA; severe sporadic. Ref.78 Ref.83

VAR_028710

Natural variant

2326

1

R → Q in HEMA; moderate/mild; may cause reduced phospholipid binding. Ref.22 Ref.68 Ref.72 Ref.93

VAR_001212

Natural variant

2330

1

Q → P in HEMA; severe. Ref.89 Ref.90

VAR_028711

Natural variant

2332

1

W → R in HEMA; severe. Ref.75

VAR_028712

Natural variant

2336

1

I → F in HEMA. Ref.100

VAR_065324

Natural variant

2339

1

R → T in HEMA; moderate. Ref.72

VAR_028713

Natural variant

2344

1

G → C in HEMA; moderate. Ref.77 Ref.96

VAR_008968

Natural variant

2344

1

G → D in HEMA. Ref.101

VAR_065325

Natural variant

2344

1

G → S in HEMA. Ref.52

VAR_028714

Natural variant

2345

1

C → S in HEMA. Ref.95

VAR_028715

Natural variant

2345

1

C → Y in HEMA. Ref.91

VAR_028716

Experimental info

Sequence conflict

768

1

P → R in CAA25619. Ref.2

Sequence conflict

1922

1

C → S in AAA52420. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

2351

Helix Strand Turn

Details...

Turn

2199 – 2201

3

Beta strand

2202 – 2204

3

Helix

2206 – 2208

3

Beta strand

2209 – 2212

4

Beta strand

2215 – 2217

3

Beta strand

2220 – 2222

3

Helix

2224 – 2226

3

Beta strand

2233 – 2235

3

Beta strand

2249 – 2265

17

Beta strand

2267 – 2269

3

Beta strand

2272 – 2289

18

Beta strand

2306 – 2310

5

Beta strand

2312 – 2335

24

Beta strand

2338 – 2346

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 75FB6A2955C74CB0	FASTA	2,351	267,009
	10 20 30 40 50 60 MQIELSTCFF LCLLRFCFSA TRRYYLGAVE LSWDYMQSDL GELPVDARFP PRVPKSFPFN 70 80 90 100 110 120 TSVVYKKTLF VEFTDHLFNI AKPRPPWMGL LGPTIQAEVY DTVVITLKNM ASHPVSLHAV 130 140 150 160 170 180 GVSYWKASEG AEYDDQTSQR EKEDDKVFPG GSHTYVWQVL KENGPMASDP LCLTYSYLSH 190 200 210 220 230 240 VDLVKDLNSG LIGALLVCRE GSLAKEKTQT LHKFILLFAV FDEGKSWHSE TKNSLMQDRD 250 260 270 280 290 300 AASARAWPKM HTVNGYVNRS LPGLIGCHRK SVYWHVIGMG TTPEVHSIFL EGHTFLVRNH 310 320 330 340 350 360 RQASLEISPI TFLTAQTLLM DLGQFLLFCH ISSHQHDGME AYVKVDSCPE EPQLRMKNNE 370 380 390 400 410 420 EAEDYDDDLT DSEMDVVRFD DDNSPSFIQI RSVAKKHPKT WVHYIAAEEE DWDYAPLVLA 430 440 450 460 470 480 PDDRSYKSQY LNNGPQRIGR KYKKVRFMAY TDETFKTREA IQHESGILGP LLYGEVGDTL 490 500 510 520 530 540 LIIFKNQASR PYNIYPHGIT DVRPLYSRRL PKGVKHLKDF PILPGEIFKY KWTVTVEDGP 550 560 570 580 590 600 TKSDPRCLTR YYSSFVNMER DLASGLIGPL LICYKESVDQ RGNQIMSDKR NVILFSVFDE 610 620 630 640 650 660 NRSWYLTENI QRFLPNPAGV QLEDPEFQAS NIMHSINGYV FDSLQLSVCL HEVAYWYILS 670 680 690 700 710 720 IGAQTDFLSV FFSGYTFKHK MVYEDTLTLF PFSGETVFMS MENPGLWILG CHNSDFRNRG 730 740 750 760 770 780 MTALLKVSSC DKNTGDYYED SYEDISAYLL SKNNAIEPRS FSQNSRHPST RQKQFNATTI 790 800 810 820 830 840 PENDIEKTDP WFAHRTPMPK IQNVSSSDLL MLLRQSPTPH GLSLSDLQEA KYETFSDDPS 850 860 870 880 890 900 PGAIDSNNSL SEMTHFRPQL HHSGDMVFTP ESGLQLRLNE KLGTTAATEL KKLDFKVSST 910 920 930 940 950 960 SNNLISTIPS DNLAAGTDNT SSLGPPSMPV HYDSQLDTTL FGKKSSPLTE SGGPLSLSEE 970 980 990 1000 1010 1020 NNDSKLLESG LMNSQESSWG KNVSSTESGR LFKGKRAHGP ALLTKDNALF KVSISLLKTN 1030 1040 1050 1060 1070 1080 KTSNNSATNR KTHIDGPSLL IENSPSVWQN ILESDTEFKK VTPLIHDRML MDKNATALRL 1090 1100 1110 1120 1130 1140 NHMSNKTTSS KNMEMVQQKK EGPIPPDAQN PDMSFFKMLF LPESARWIQR THGKNSLNSG 1150 1160 1170 1180 1190 1200 QGPSPKQLVS LGPEKSVEGQ NFLSEKNKVV VGKGEFTKDV GLKEMVFPSS RNLFLTNLDN 1210 1220 1230 1240 1250 1260 LHENNTHNQE KKIQEEIEKK ETLIQENVVL PQIHTVTGTK NFMKNLFLLS TRQNVEGSYD 1270 1280 1290 1300 1310 1320 GAYAPVLQDF RSLNDSTNRT KKHTAHFSKK GEEENLEGLG NQTKQIVEKY ACTTRISPNT 1330 1340 1350 1360 1370 1380 SQQNFVTQRS KRALKQFRLP LEETELEKRI IVDDTSTQWS KNMKHLTPST LTQIDYNEKE 1390 1400 1410 1420 1430 1440 KGAITQSPLS DCLTRSHSIP QANRSPLPIA KVSSFPSIRP IYLTRVLFQD NSSHLPAASY 1450 1460 1470 1480 1490 1500 RKKDSGVQES SHFLQGAKKN NLSLAILTLE MTGDQREVGS LGTSATNSVT YKKVENTVLP 1510 1520 1530 1540 1550 1560 KPDLPKTSGK VELLPKVHIY QKDLFPTETS NGSPGHLDLV EGSLLQGTEG AIKWNEANRP 1570 1580 1590 1600 1610 1620 GKVPFLRVAT ESSAKTPSKL LDPLAWDNHY GTQIPKEEWK SQEKSPEKTA FKKKDTILSL 1630 1640 1650 1660 1670 1680 NACESNHAIA AINEGQNKPE IEVTWAKQGR TERLCSQNPP VLKRHQREIT RTTLQSDQEE 1690 1700 1710 1720 1730 1740 IDYDDTISVE MKKEDFDIYD EDENQSPRSF QKKTRHYFIA AVERLWDYGM SSSPHVLRNR 1750 1760 1770 1780 1790 1800 AQSGSVPQFK KVVFQEFTDG SFTQPLYRGE LNEHLGLLGP YIRAEVEDNI MVTFRNQASR 1810 1820 1830 1840 1850 1860 PYSFYSSLIS YEEDQRQGAE PRKNFVKPNE TKTYFWKVQH HMAPTKDEFD CKAWAYFSDV 1870 1880 1890 1900 1910 1920 DLEKDVHSGL IGPLLVCHTN TLNPAHGRQV TVQEFALFFT IFDETKSWYF TENMERNCRA 1930 1940 1950 1960 1970 1980 PCNIQMEDPT FKENYRFHAI NGYIMDTLPG LVMAQDQRIR WYLLSMGSNE NIHSIHFSGH 1990 2000 2010 2020 2030 2040 VFTVRKKEEY KMALYNLYPG VFETVEMLPS KAGIWRVECL IGEHLHAGMS TLFLVYSNKC 2050 2060 2070 2080 2090 2100 QTPLGMASGH IRDFQITASG QYGQWAPKLA RLHYSGSINA WSTKEPFSWI KVDLLAPMII 2110 2120 2130 2140 2150 2160 HGIKTQGARQ KFSSLYISQF IIMYSLDGKK WQTYRGNSTG TLMVFFGNVD SSGIKHNIFN 2170 2180 2190 2200 2210 2220 PPIIARYIRL HPTHYSIRST LRMELMGCDL NSCSMPLGME SKAISDAQIT ASSYFTNMFA 2230 2240 2250 2260 2270 2280 TWSPSKARLH LQGRSNAWRP QVNNPKEWLQ VDFQKTMKVT GVTTQGVKSL LTSMYVKEFL 2290 2300 2310 2320 2330 2340 ISSSQDGHQW TLFFQNGKVK VFQGNQDSFT PVVNSLDPPL LTRYLRIHPQ SWVHQIALRM 2350 EVLGCEAQDL Y
	Isoform 2 (F8B) [UniParc]. Checksum: 6C82D4F89E35A376	FASTA	216	24,641
	10 20 30 40 50 60 MRIQDPGKVF FGNVDSSGIK HNIFNPPIIA RYIRLHPTHY SIRSTLRMEL MGCDLNSCSM 70 80 90 100 110 120 PLGMESKAIS DAQITASSYF TNMFATWSPS KARLHLQGRS NAWRPQVNNP KEWLQVDFQK 130 140 150 160 170 180 TMKVTGVTTQ GVKSLLTSMY VKEFLISSSQ DGHQWTLFFQ NGKVKVFQGN QDSFTPVVNS 190 200 210 LDPPLLTRYL RIHPQSWVHQ IALRMEVLGC EAQDLY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of the polypeptide composition of human factor VIII:C and the nucleotide sequence and expression of the human kidney cDNA." Truett M.A., Blacher R., Burke R.L., Caput D., Chu C., Dina D., Hartog K., Kuo C.H., Masiarz F.R., Merryweather J.P., Najarian R., Pachl C., Potter S.J., Puma J., Quiroga M., Rall L.B., Randolph A., Urdea M.S. , Valenzuela P., Dahl H.-H.M., Favalaro J., Hansen J., Nordfang O., Ezban M. DNA 4:333-349(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Expression of active human factor VIII from recombinant DNA clones." Wood W.I., Capon D.J., Simonsen C.C., Eaton D.L., Gitschier J., Keyt B., Seeburg P.H., Smith D.H., Hollingshead P., Wion K.L., Delwart E., Tuddenham E.G.D., Vehar G.A., Lawn R.M. Nature 312:330-337(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"Evidence for a third transcript from the human factor VIII gene." Levinson B., Kenwrick S., Gamel P., Fisher K., Gitschier J. Genomics 14:585-589(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
[4]	"Molecular cloning of a cDNA encoding human antihaemophilic factor." Toole J.J., Knopf J.L., Wozney J.M., Sultzman L.A., Buecker J.L., Pittman D.D., Kaufman R.J., Brown E., Shoemaker C., Orr E.C., Amphlett G.W., Foster W.B., Coe M.L., Knutson G.J., Fass D.N., Hewick R.M. Nature 312:342-347(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]	"Sequence of the exon-containing regions of the human factor VIII gene." Gitschier J., Wood W.I. Hum. Mol. Genet. 1:199-200(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]	SeattleSNPs variation discovery resource Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLU-1260 AND VAL-2257.
[7]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Hippocampus and Kidney.
[8]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[11]	"Factor VIII gene normal intron 20 sequence." de Water N.S., Williams R., Browett P.J. Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2064-2070.
[12]	"Characterization of tyrosine sulfate residues in antihemophilic recombinant factor VIII by liquid chromatography electrospray ionization tandem mass spectrometry and amino acid analysis." Severs J.C., Carnine M., Eguizabal H., Mock K.K. Rapid Commun. Mass Spectrom. 13:1016-1023(1999) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 356-378; 727-752 AND 1672-1708, MASS SPECTROMETRY, SULFATION AT TYR-365; TYR-737; TYR-738; TYR-742; TYR-1683 AND TYR-1699.
[13]	"Sulfation of Tyr1680 of human blood coagulation factor VIII is essential for the interaction of factor VIII with von Willebrand factor." Leyte A., van Schijndel H.B., Niehrs C., Huttner W.B., Verbeet M.P., Mertens K., van Mourik J.A. J. Biol. Chem. 266:740-746(1991) [PubMed] [Europe PMC] [Abstract] Cited for: SULFATION AT TYR-1699.
[14]	"Identification and functional importance of tyrosine sulfate residues within recombinant factor VIII." Pittman D.D., Wang J.H., Kaufman R.J. Biochemistry 31:3315-3325(1992) [PubMed] [Europe PMC] [Abstract] Cited for: SULFATION AT TYR-365; TYR-1683 AND TYR-1699, INTERACTION WITH VWF.
[15]	"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 VWF.
[16]	"Locations of disulfide bonds and free cysteines in the heavy and light chains of recombinant human factor VIII (antihemophilic factor A)." McMullen B.A., Fujikawa K., Davie E.W., Hedner U., Ezban M. Protein Sci. 4:740-746(1995) [PubMed] [Europe PMC] [Abstract] Cited for: DISULFIDE BONDS.
[17]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-601, MASS SPECTROMETRY. Tissue: Plasma.
[18]	"Membrane-binding peptide from the C2 domain of factor VIII forms an amphipathic structure as determined by NMR spectroscopy." Gilbert G.E., Baleja J.D. Biochemistry 34:3022-3031(1995) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 2322-2343.
[19]	"The molecular basis of hemophilia A." Gitschier J. Ann. N. Y. Acad. Sci. 614:89-96(1991) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON MOLECULAR BASIS OF HEMA.
[20]	"Factor VIII gene and hemophilia A." White G.C. II, Shoemaker C.B. Blood 73:1-12(1989) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON MOLECULAR BASIS OF HEMA.
[21]	"Molecular etiology of factor VIII deficiency in hemophilia A." Antonarakis S.E., Kazazian H.H. Jr., Tuddenham E.G.D. Hum. Mutat. 5:1-22(1995) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON MOLECULAR BASIS OF HEMA.
[22]	"Identification of a missense mutation in the factor VIII gene of a mild hemophiliac." Gitschier J., Wood W.I., Shuman M.A., Lawn R.M. Science 232:1415-1416(1986) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HEMA GLN-2326.
[23]	"A novel missense mutation in the factor VIII gene identified by analysis of amplified hemophilia DNA sequences." Levinson B., Janco R.L., Phillips J.A. III, Gitschier J. Nucleic Acids Res. 15:9797-9805(1987) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HEMA PRO-2135.
[24]	"Nonsense and missense mutations in hemophilia A: estimate of the relative mutation rate at CG dinucleotides." Youssoufian H., Antonarakis S.E., Bell W., Griffin A.M., Kazazian H.H. Jr. Am. J. Hum. Genet. 42:718-725(1988) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HEMA GLN-2228.
[25]	"Moderately severe hemophilia A resulting from Glu-->Gly substitution in exon 7 of the factor VIII gene." Youssoufian H., Wong C., Aronis S., Platokoukis H., Kazazian H.H. Jr., Antonarakis S.E. Am. J. Hum. Genet. 42:867-871(1988) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HEMA GLY-291.
[26]	"Purification and characterization of factor VIII 1,689-Cys: a nonfunctional cofactor occurring in a patient with severe hemophilia A." O'Brien D.P., Tuddenham E.G. Blood 73:2117-2122(1989) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HEMA CYS-1708.
[27]	"An arginine to cysteine amino acid substitution at a critical thrombin cleavage site in a dysfunctional factor VIII molecule." Shima M., Ware J., Yoshioka A., Fukui H., Fulcher C.A. Blood 74:1612-1617(1989) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HEMA CYS-391.
[28]	"A novel missense mutation in exon 4 of the factor VIII:C gene resulting in moderately severe hemophilia A." Chan V., Chan T.K., Tong T.M., Todd D. Blood 74:2688-2691(1989) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HEMA LEU-189.
[29]	"Mild hemophilia A resulting from Arg-to-Leu substitution in exon 26 of the factor VIII gene." Inaba H., Fujimaki M., Kazazian H.H. Jr., Antonarakis S.E. Hum. Genet. 81:335-338(1989) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HEMA LEU-2326.
[30]	"Direct characterization of factor VIII in plasma: detection of a mutation altering a thrombin cleavage site (arginine-372-->histidine)." Arai M., Inaba H., Higuchi M., Antonarakis S.E., Kazazian H.H. Jr., Fujimaki M., Hoyer L.W. Proc. Natl. Acad. Sci. U.S.A. 86:4277-4281(1989) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HEMA HIS-391.
[31]	"Characterization of a thrombin cleavage site mutation (Arg 1689 to Cys) in the factor VIII gene of two unrelated patients with cross-reacting material-positive hemophilia A." Arai M., Higuchi M., Antonarakis S.E., Kazazian H.H. Jr., Phillips J.A. III, Janco R.L., Hoyer L.W. Blood 75:384-389(1990) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HEMA CYS-1708.
[32]	"Recurrent mutations and three novel rearrangements in the factor VIII gene of hemophilia A patients of Italian descent." Casula L., Murru S., Pecorara M., Ristaldi M.S., Restagno G., Mancuso G., Morfini M., de Biasi R., Baudo F., Carbonara A. Blood 75:662-670(1990) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA GLN-2228 AND LEU-2326.
[33]	"CRM+ haemophilia A due to a missense mutation (372-->Cys) at the internal heavy chain thrombin cleavage site." Pattinson J.K., McVey J.H., Boon M., Ajani A., Tuddenham E.G. Br. J. Haematol. 75:73-77(1990) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HEMA CYS-391.
[34]	"Characterization of mutations in the factor VIII gene by direct sequencing of amplified genomic DNA." Higuchi M., Wong C., Kochhan L., Olek K., Aronis S., Kasper C.K., Kazazian H.H. Jr., Antonarakis S.E. Genomics 6:65-71(1990) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA PHE-1699 AND CYS-1708.
[35]	"Use of denaturing gradient gel electrophoresis to detect point mutations in the factor VIII gene." Traystman M.D., Higuchi M., Kasper C.K., Antonarakis S.E., Kazazian H.H. Jr. Genomics 6:293-301(1990) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA CYS-1728 AND ASP-1941.
[36]	"Mutations and a polymorphism in the factor VIII gene discovered by denaturing gradient gel electrophoresis." Kogan S., Gitschier J. Proc. Natl. Acad. Sci. U.S.A. 87:2092-2096(1990) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA LEU-345 AND ARG-348.
[37]	"Identification of mutations in two families with sporadic hemophilia A." Paynton C., Sarkar G., Sommer S.S. Hum. Genet. 87:397-400(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA LYS-1723 AND SER-2319.
[38]	"Molecular characterization of severe hemophilia A suggests that about half the mutations are not within the coding regions and splice junctions of the factor VIII gene." Higuchi M., Kazazian H.H. Jr., Kasch L., Warren T.C., McGinniss M.J., Phillips J.A. III, Kasper C., Janco R., Antonarakis S.E. Proc. Natl. Acad. Sci. U.S.A. 88:7405-7409(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA THR-108; VAL-110; GLY-285; HIS-301; SER-312; ARG-444; HIS-492; GLY-561; CYS-612; THR-723; PHE-1699; HIS-1800; TYR-1803; ASP-1941; SER-1941; HIS-2169; GLN-2228 AND CYS-2323.
[39]	"Molecular characterization of mild-to-moderate hemophilia A: detection of the mutation in 25 of 29 patients by denaturing gradient gel electrophoresis." Higuchi M., Antonarakis S.E., Kasch L., Oldenburg J., Economou-Petersen E., Olek K., Arai M., Inaba H., Kazazian H.H. Jr. Proc. Natl. Acad. Sci. U.S.A. 88:8307-8311(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS.
[40]	"Detection and characterisation of two missense mutations at a cleavage site in the factor VIII light chain." Schwaab R., Ludwig M., Kochhan L., Oldenburg J., McVey J.H., Egli H., Brackmann H.H., Olek K. Thromb. Res. 61:225-234(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA CYS-1708 AND HIS-1708.
[41]	"GAA(Glu)272->AAA(Lys) and CGA(Arg)1941->CAA(Gln) in the factor VIII gene in two haemophilia A patients of Czech origin." Krepelova A., Vorlova Z., Acquila M., Mori P. Br. J. Haematol. 81:458-458(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA LYS-291 AND GLN-1960.
[42]	"Detection of mutations in the factor VIII gene using single-stranded conformational polymorphism (SSCP)." Economou E.P., Kazazian H.H. Jr., Antonarakis S.E. Genomics 13:909-911(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA PRO-1845 AND PRO-2224 DEL.
[43]	"Screening for nonsense mutations in patients with severe hemophilia A can provide rapid, direct carrier detection." Reiner A.P., Thompson A.R. Hum. Genet. 89:88-94(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HEMA GLY-1715.
[44]	"A novel mutation (Arg-->Leu in exon 18) in factor VIII gene responsible for moderate hemophilia A." Nafa K., Baudis M., Deburgrave N., Bardin J.M., Sultan Y., Kaplan J.C., Delpech M. Hum. Mutat. 1:77-78(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HEMA LEU-1960.
[45]	"Amino acid substitutions in conserved domains of factor VIII and related proteins: study of patients with mild and moderately severe hemophilia A." Diamond C., Kogan S., Levinson B., Gitschier J. Hum. Mutat. 1:248-257(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA VAL-30; VAL-89; VAL-92; ASP-104; VAL-164; MET-181; CYS-550; GLY-554; CYS-612; TRP-717; PHE-1808; SER-1941; ARG-2065; HIS-2169; CYS-2178 AND CYS-2248.
[46]	"Missense mutations causing mild hemophilia A in Iceland detected by denaturing gradient gel electrophoresis." Jonsdottir S., Diamond C., Levinson B., Magnusson S., Jensson O., Gitschier J. Hum. Mutat. 1:506-508(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA CYS-1800 AND ILE-2173.
[47]	"Spectrum of mutations in CRM-positive and CRM-reduced hemophilia A." McGinniss M.J., Kazazian H.H. Jr., Hoyer L.W., Bi L., Inaba H., Antonarakis S.E. Genomics 15:392-398(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA LEU-308; HIS-391; TRP-546; PHE-577; ALA-653; MET-653; PHE-671 DEL; LYS-1460 AND CYS-2178.
[48]	"Double strand conformation polymorphism (DSCP) detects two point mutations at codon 280 (AAC-->ATC) and at codon 431 (TAC-->AAC) of the blood coagulation factor VIII gene." Pieneman W.C., Reitsma P.H., Briet E. Thromb. Haemost. 69:473-475(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA ILE-299 AND ASN-450.
[49]	"Eleven novel mutations in the factor VIII gene from Brazilian hemophilia A patients." Arruda V.R., Pieneman W.C., Reitsma P.H., Deutz-Terlouw P.P., Annichino-Bizzacchi J.M., Brieet E., Costa F.F. Blood 86:3015-3020(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA ARG-113; ASN-202; LEU-275; GLY-285; CYS-301; ASP-637; PHE-1808; PRO-1867; GLN-1960; HIS-2169; CYS-2178 AND THR-2281, VARIANT VAL-2257.
[50]	"Screening for mutations in haemophilia A patients by multiplex PCR-SSCP, Southern blotting and RNA analysis: the detection of a genetic abnormality in the factor VIII gene in 30 out of 35 patients." Pieneman W.C., Deutz-Terlouw P.P., Reitsma P.H., Brieet E. Br. J. Haematol. 90:442-449(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA HIS-217; ILE-299; ASN-450; TRP-546; CYS-612; VAL-705; CYS-1708; TRP-2016 AND ARG-2119.
[51]	"Detection of mutations in ectopic factor VIII transcripts from nine haemophilia A patients and the correlation with phenotype." Bidichandani S.I., Lanyon W.G., Shiach C.R., Lowe G.D.O., Connor J.M. Hum. Genet. 95:531-538(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA GLU-75; MET-181; ASP-720; THR-1853 AND ILE-1888.
[52]	"Characterization of the factor VIII defect in 147 patients with sporadic hemophilia A: family studies indicate a mutation type-dependent sex ratio of mutation frequencies." Becker J., Schwaab R., Moeller-Taube A., Schwaab U., Schmidt W., Brackmann H.H., Grimm T., Olek K., Oldenburg J. Am. J. Hum. Genet. 58:657-670(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA ARG-26; LYS-48; ASP-89; ASP-99; VAL-101; ARG-117; GLY-135; ASP-219; ARG-278; LEU-301; GLN-302 DEL; PRO-327; PRO-659; LEU-1012; GLU-1260; CYS-1708; ASN-1865; ARG-1873; THR-1971; TRP-2016; GLN-2228; LEU-2326 AND SER-2344.
[53]	"Molecular characterization of haemophilia A in southern Chinese." Chan V., Pang A., Chan T.P.T., Chan V.W.-Y., Chan T.K. Br. J. Haematol. 93:451-456(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA LEU-189; SER-263; ARG-947; LYS-1057; SER-1610 AND HIS-2169, VARIANT MET-2242.
[54]	"Mutations in a subgroup of patients with mild haemophilia A and a familial discrepancy between the one-stage and two-stage factor VIII:C methods." Rudzki Z., Duncan E.M., Casey G.J., Neumann M., Favaloro E.J., Lloyd J.V. Br. J. Haematol. 94:400-406(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA GLU-303; LEU-308; HIS-550; LEU-717; TRP-717 AND PHE-1951.
[55]	"Mutations in the FVIII gene in seven families with mild haemophilia A." Mazurier C., Gaucher C., Jorieux S., Parquet-Gernez A. Br. J. Haematol. 96:426-427(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA PRO-303; TRP-546; HIS-550 AND ILE-1966.
[56]	"Factor VIII gene analysis in Japanese CRM-positive and CRM-reduced haemophilia A patients by single-strand conformation polymorphism." Morichika S., Shima M., Kamisue S., Tanaka I., Imanaka Y., Suzuki H., Shibata H., Pemberton S., Gale K., McVey J., Tuddenham E.G.D., Yoshioka A. Br. J. Haematol. 98:901-906(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA CYS-274; CYS-492; ARG-498; HIS-550; ARG-686; CYS-1708; GLN-1960; HIS-2169; CYS-2178; ALA-2264 AND VAL-2304.
[57]	"Mutational analysis of ectopic factor VIII transcripts from hemophilia A patients: identification of cryptic splice site, exon skipping and novel point mutations." Tavassoli K., Eigel A., Pollmann H., Horst J. Hum. Genet. 100:508-511(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA GLY-33; CYS-639; HIS-1800; LEU-1908 AND ARG-2106.
[58]	"A domain mutations in 65 haemophilia A families and molecular modelling of dysfunctional factor VIII proteins." Liu M., Murphy M.E.P., Thompson A.R. Br. J. Haematol. 103:1051-1060(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA LYS-98; GLY-101; CYS-133; HIS-145; ALA-159; LYS-163; ASP-164; PRO-179; MET-181; LYS-291; ALA-297; GLU-303; SER-312; HIS-391; ILE-427; TRP-437; ASN-450; ILE-454; LEU-470; SER-541; TRP-546; CYS-550; HIS-550; PRO-553; THR-560; ALA-578; ARG-603; ILE-633; ASN-683; LEU-721; CYS-742; THR-1698; GLY-1715; ARG-1779; THR-1791; HIS-1800; ALA-1801; PHE-1901; GLN-1960; GLN-1985; ILE-2007; TRP-2016; ASP-2022; ASN-2030 AND SER-2038.
[59]	"Protein truncation test: detection of severe haemophilia a mutation and analysis of factor VIII transcripts." Maugard C., Tuffery S., Aguilar-Martinez P., Schved J.-F., Gris J.-C., Demaille J., Claustres M. Hum. Mutat. 11:18-22(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA VAL-129; LYS-631 AND HIS-1800.
[60]	"Independent occurrence of the novel Arg2163 to His mutation in the factor VIII gene in three unrelated families with haemophilia A with different phenotypes." Theophilus B.D.M., Enayat M.S., Higuchi M., Kazazian H.H. Jr., Antonarakis S.E., Hill F.G.H. Hum. Mutat. 11:334-334(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HEMA HIS-2182.
[61]	"Fluorescent chemical cleavage of mismatches for efficient screening of the factor VIII gene." Freson K., Peerlinck K., Aguirre T., Arnout J., Vermylen J., Cassiman J.-J., Matthijs G. Hum. Mutat. 11:470-479(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA ASP-132; PHE-253; ILE-314; VAL-331; ARG-474; ARG-498; VAL-644; VAL-699; ASP-720; PHE-727 AND ASN-2105.
[62]	"Identification of four novel mutations in the factor VIII gene: three missense mutations (E1875G, G2088S, I2185T) and a 2-bp deletion (1780delTC)." Tavassoli K., Eigel A., Dworniczak B., Valtseva E., Horst J. Hum. Mutat. Suppl. 1:S260-S262(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA GLY-550; THR-723; GLY-1894; SER-2107 AND THR-2204.
[63]	"Molecular diagnostics of 15 hemophilia A patients: characterization of eight novel mutations in the factor VIII gene, two of which result in exon skipping." Tavassoli K., Eigel A., Wilke K., Pollmann H., Horst J. Hum. Mutat. 12:301-303(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA.
[64]	"Use of denaturing gradient gel blots to screen for point mutations in the factor VIII gene." Laprise S.L., Mak E.K., Killoran K.A., Layman L.C., Gray M.R. Hum. Mutat. 12:393-402(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA VAL-439; CYS-1800; HIS-2169; HIS-2182 AND SER-2319.
[65]	"Precise carrier diagnosis in families with haemophilia A: use of conformation sensitive gel electrophoresis for mutation screening and polymorphism analysis." Williams I.J., Abuzenadah A., Winship P.R., Preston F.E., Dolan G., Wright J., Peake I.R., Goodeve A.C. Thromb. Haemost. 79:723-726(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA LYS-223; VAL-2045 AND CYS-2279, VARIANT VAL-2257.
[66]	"Factor VIII inhibitors in mild and moderate-severity haemophilia A." UK haemophilia centre directors organisation Hay C.R.M., Ludlam C.A., Colvin B.T., Hill F.G.H., Preston F.E., Wasseem N., Bagnall R., Peake I.R., Berntorp E., Mauser Bunschoten E.P., Fijnvandraat K., Kasper C.K., White G., Santagostino E. Thromb. Haemost. 79:762-766(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA CYS-612; PHE-682; ARG-2028; CYS-2124; HIS-2169; HIS-2182; ASP-2200; CYS-2248 AND ILE-2279.
[67]	"Diagnostic importance of the two-stage factor VIII:C assay demonstrated by a case of mild haemophilia associated with His1954-->Leu substitution in the factor VIII A3 domain." Keeling D.M., Sukhu K., Kemball-Cook G., Waseem N., Bagnall R., Lloyd J.V. Br. J. Haematol. 105:1123-1126(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HEMA LEU-1973.
[68]	"Screen of 55 Slovenian haemophilia A patients: identification of 2 novel mutations (S-1R and IVS23+1G-->A) and discussion of mutation spectrum." Strmecki L., Benedik-Dolnicar M., Vouk K., Komel R. Hum. Mutat. 13:413-413(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA ARG-19; HIS-301; LEU-308; HIS-2169; GLN-2228 AND GLN-2326.
[69]	"Mutational-screening in the factor VIII gene resulting in the identification of three novel mutations, one of which is a donor splice mutation." Moeller-Morlang K., Tavassoli K., Eigel A., Pollmann H., Horst J. Hum. Mutat. 13:504-504(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA ARG-202 AND HIS-301.
[70]	"Start of UK confidential haemophilia A database: analysis of 142 patients by solid phase fluorescent chemical cleavage of mismatch." The haemophilia centres Waseem N.H., Bagnall R., Green P.M., Giannelli F. Thromb. Haemost. 81:900-905(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA CYS-24; ARG-26; TYR-113; SER-121; TRP-172; PRO-176; MET-181; VAL-214; THR-219; LYS-291; ALA-314; VAL-315; LYS-340; PHE-405; GLY-412; THR-470; GLU-474; ASN-478; CYS-484; GLY-490; ARG-498; TRP-546; CYS-550; HIS-561; ARG-584; THR-585; GLY-588; ASP-601; LYS-601; GLY-602; HIS-605; CYS-612; TRP-717; CYS-1708; GLN-1751; HIS-1800; CYS-1802; THR-1853; GLU-1864; PRO-1882; ILE-1888; LEU-1973; TRP-2016; ALA-2035; TYR-2040; CYS-2120; CYS-2145; HIS-2169; CYS-2178; HIS-2182; VAL-2183; VAL-2198; CYS-2248 AND GLY-2326.
[71]	"A novel cause of mild/moderate hemophilia A: mutations scattered in the factor VIII C1 domain reduce factor VIII binding to von Willebrand factor." Jacquemin M., Lavend'homme R., Benhida A., Vanzieleghem B., d'Oiron R., Lavergne J.-M., Brackmann H.H., Schwaab R., VandenDriessche T., Chuah M.K.L., Hoylaerts M., Gilles J.G.G., Peerlinck K., Vermylen J., Saint-Remy J.-M.R. Blood 96:958-965(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA SER-2117; TYR-2138; SER-2148; HIS-2169 AND GLN-2172, CHARACTERIZATION OF VARIANTS HEMA SER-2117; TYR-2138 AND HIS-2169.
[72]	"Hemophilic factor VIII C1- and C2-domain missense mutations and their modeling to the 1.5-angstrom human C2-domain crystal structure." Liu M.-L., Shen B.W., Nakaya S., Pratt K.P., Fujikawa K., Davie E.W., Stoddard B.L., Thompson A.R. Blood 96:979-987(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA GLU-2106; CYS-2109; CYS-2169; CYS-2178; CYS-2182; ARG-2183; ILE-2192; PRO-2220; ALA-2251; LEU-2319; CYS-2323; GLY-2323; GLN-2326 AND THR-2339.
[73]	"Intracellular accumulation of factor VIII induced by missense mutations Arg593-->Cys and Asn618-->Ser explains cross-reacting material-reduced haemophilia A." Roelse J.C., De Laaf R.T.M., Timmermans S.M.H., Peters M., Van Mourik J.A., Voorberg J. Br. J. Haematol. 108:241-246(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA CYS-612 AND SER-637, CHARACTERIZATION OF VARIANTS HEMA CYS-612 AND SER-637.
[74]	"Assay discrepancy in mild haemophilia A due to a factor VIII missense mutation (Asn694Ile) in a large Danish family." Schwaab R., Oldenburg J., Kemball-Cook G., Albert T., Juhler C., Hanfland P., Ingerslev J. Br. J. Haematol. 109:523-528(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HEMA ILE-713.
[75]	"Experience of a single Italian center in genetic counseling for hemophilia: from linkage analysis to molecular diagnosis." Tagariello G., Belvini D., Salviato R., Are A., De Biasi E., Goodeve A., Davoli P. Haematologica 85:525-529(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA HIS-35; LEU-295; SER-307; CYS-1909; PRO-2058; GLN-2228 AND ARG-2332.
[76]	"Relationship between factor VIII mutation type and inhibitor development in a cohort of previously untreated patients treated with recombinant factor VIII (Recombinate)." Recombinate PUP study group Goodeve A.C., Williams I., Bray G.L., Peake I.R. Thromb. Haemost. 83:844-848(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA PRO-69; TYR-75; ARG-585; PRO-664; GLU-1779; ALA-2000; HIS-2169 AND PRO-2228.
[77]	"Mutations of the factor VIII gene in Thai hemophilia A patients." Akkarapatumwong V., Oranwiroon S., Pung-amritt P., Treesucon A., Thanootarakul P., Veerakul G., Mahasandana C., Panyim S., Yenchitsomanus P. Hum. Mutat. 15:117-118(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA TYR-561; VAL-1869 AND CYS-2344.
[78]	"Somatic mosaicism in hemophilia A: a fairly common event." Leuer M., Oldenburg J., Lavergne J.-M., Ludwig M., Fregin A., Eigel A., Ljung R., Goodeve A., Peake I., Olek K. Am. J. Hum. Genet. 69:75-87(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA ASP-89; ASP-99; HIS-101; TYR-135; PRO-327; GLY-409; ARG-498; ARG-603; ASP-637; GLY-1894; VAL-2045; LEU-2067; ARG-2172; CYS-2182; SER-2185; CYS-2279; LEU-2319; LEU-2326 AND PRO-2326.
[79]	"Lithuanian haemophilia A and B registry comprising phenotypic and genotypic data." Ivaskevicius V., Jurgutis R., Rost S., Muller A., Schmitt C., Wulff K., Herrmann F.H., Muller C.R., Schwaab R., Oldenburg J. Br. J. Haematol. 112:1062-1070(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA VAL-255; GLU-323; CYS-391; CYS-550; VAL-586; CYS-1708; CYS-1800; ALA-1942; PRO-1963; CYS-2036; CYS-2124; ARG-2172; CYS-2182; GLN-2228 AND ALA-2307.
[80]	"Site and type of mutations in the factor VIII gene in patients and carriers of haemophilia A." Theophilus B.D.M., Enayat M.S., Williams M.D., Hill F.G.H. Haemophilia 7:381-391(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA ASP-132; LYS-141; GLU-466; THR-470; HIS-503; GLY-602; THR-1853; GLN-1985; ARG-2004; TRP-2016; TYR-2093; HIS-2169; HIS-2182; VAL-2198 AND GLN-2228.
[81]	"Mild haemophilia A discovered in a previously multi-operated 73-year-old man: characterization of a new mutation." Bauduer F., Ducout L., Bendriss P., Falaises B., Lavergne J.-M. Haemophilia 7:419-421(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HEMA ALA-92.
[82]	"Molecular pathology of haemophilia A in Turkish patients: identification of 36 independent mutations." Timur A.A., Guergey A., Aktuglu G., Kavakli K., Canatan D., Olek K., Caglayan S.H. Haemophilia 7:475-481(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA ASN-67; PHE-117; ALA-137; TYR-267; CYS-301; HIS-301; TYR-348; LYS-475; ALA-579; CYS-612; CYS-683; LEU-698; TRP-710; CYS-1708; HIS-1788; LEU-1876; TRP-2016; GLU-2045; CYS-2178; CYS-2182; HIS-2182; PRO-2182; ALA-2307 AND LEU-2323.
[83]	"Seven novel and four recurrent point mutations in the factor VIII (F8C) gene." Bogdanova N., Lemcke B., Markoff A., Pollmann H., Dworniczak B., Eigel A., Horst J. Hum. Mutat. 18:546-546(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA MET-181; THR-339; CYS-455; TRP-546; CYS-554; CYS-2178 AND PRO-2326.
[84]	"Rapid hemophilia A molecular diagnosis by a simple DNA sequencing procedure: identification of 14 novel mutations." Vidal F., Farssac E., Altisent C., Puig L., Gallardo D. Thromb. Haemost. 85:580-583(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA ARG-193; CYS-391; CYS-550; CYS-612; HIS-1705; ARG-1782; GLU-1872; TRP-2016; PRO-2016; HIS-2169 AND HIS-2182.
[85]	Erratum Vidal F., Farssac E., Altisent C., Puig L., Gallardo D. Thromb. Haemost. 86:727-727(2001)
[86]	"Skewed X-chromosome inactivation in monochorionic diamniotic twin sisters results in severe and mild hemophilia A." Valleix S., Vinciguerra C., Lavergne J.-M., Leuer M., Delpech M., Negrier C. Blood 100:3034-3036(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HEMA CYS-35.
[87]	"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 HEMA GLY-198.
[88]	"Three novel point mutations causing haemophilia A." Sukarova-Stefanovska E., Zisovski N., Muratovska O., Kostova S., Efremov G.D. Haemophilia 8:715-718(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA PRO-97 AND GLY-2193.
[89]	"The identification and classification of 41 novel mutations in the factor VIII gene (F8C)." Cutler J.A., Mitchell M.J., Smith M.P., Savidge G.F. Hum. Mutat. 19:274-278(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA THR-22; CYS-25; PRO-26; VAL-111; ARG-138; GLY-186; LYS-284; VAL-327; CYS-365; SER-431; PRO-437; CYS-455; HIS-579; HIS-584; PHE-650; ILE-681; GLN-725; VAL-1727; GLY-1740; CYS-1858; ASP-1869; ARG-1968; CYS-1998; ASN-2056; VAL-2070; ASN-2082; CYS-2145; ASP-2157; ALA-2173 AND PRO-2330.
[90]	"Identification of seven novel mutations of F8C by DHPLC." Frusconi S., Passerini I., Girolami F., Masieri M., Linari S., Longo G., Morfini M., Torricelli F. Hum. Mutat. 20:231-232(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA VAL-477; SER-1714; PRO-1777 AND PRO-2330.
[91]	"High throughput mutation screening of the factor VIII gene (F8C) in hemophilia A: 37 novel mutations and genotype-phenotype correlation." Citron M., Godmilow L., Ganguly T., Ganguly A. Hum. Mutat. 20:267-274(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA TRP-172; LYS-291; CYS-301; ALA-345; HIS-391; VAL-439; CYS-442; LEU-470; GLY-532; MET-653; CYS-683; LYS-1336; HIS-1708; PRO-1875; ARG-1877; ILE-1965; PHE-2117; CYS-2182; TRP-2185; LEU-2224; GLU-2251; LEU-2290; CYS-2323 AND TYR-2345.
[92]	"Non-inversion factor VIII mutations in 80 hemophilia A families including 24 with alloimmune responses." Liu M.-L., Nakaya S., Thompson A.R. Thromb. Haemost. 87:273-276(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA GLU-67; 84-ARG-PRO-85 DEL; PRO-85 DEL; MET-181; TYR-186; GLY-220; LEU-262; ARG-412; PHE-438; ASP-439; ARG-470; SER-513; SER-541; CYS-550; GLY-554; SER-583; GLN-594; ILE-609; CYS-612; ASN-635; THR-699; ILE-701; ILE-721; ARG-1779; LEU-1780; THR-1791; PRO-1798; HIS-1800; GLY-1848; ARG-1907; CYS-1907; THR-1939; VAL-1939; ILE-1982; GLN-1985; CYS-2015; TRP-2016; SER-2038; HIS-2169; ILE-2192 AND LEU-2326.
[93]	"11 hemophilia A patients without mutations in the factor VIII encoding gene." Klopp N., Oldenburg J., Uen C., Schneppenheim R., Graw J. Thromb. Haemost. 88:357-360(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA ASP-147; CYS-301; CYS-612; VAL-1945; CYS-2178 AND GLN-2326, VARIANT GLU-1260.
[94]	"Analysis of 18 novel mutations in the factor VIII gene." Bicocchi M.P., Pasino M., Lanza T., Bottini F., Boeri E., Mori P.G., Molinari A.C., Rosano C., Acquila M. Br. J. Haematol. 122:810-817(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA LYS-72; HIS-155; GLU-181; ILE-254; SER-439; GLU-529; THR-567; SER-1804; SER-2051; ASN-2141 AND GLN-2262 INS.
[95]	"Thirty-four novel mutations detected in factor VIII gene by multiplex CSGE: modeling of 13 novel amino acid substitutions." Habart D., Kalabova D., Novotny M., Vorlova Z. J. Thromb. Haemost. 1:773-781(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA ARG-26; PRO-326; PHE-329; HIS-391; GLY-401; TYR-522; THR-540; TRP-546; TYR-588; CYS-683; SER-720; TYR-1066; HIS-1768; PRO-1771; HIS-1800; ASP-1904; PRO-1980; CYS-2169; HIS-2169; ASP-2174; CYS-2178; HIS-2178; CYS-2182; GLY-2228; PHE-2229; LEU-2319; CYS-2323; HIS-2323 AND SER-2345.
[96]	"Genotype and phenotype of haemophilia A in Thai patients." Yenchitsomanus P., Akkarapatumwong V., Pung-Amritt P., Intorasoot S., Thanootarakul P., Oranwiroon S., Veerakul G., Mahasandana C. Haemophilia 9:179-186(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA ILE-252; TYR-561; VAL-1869; SER-2248 AND CYS-2344.
[97]	"Small FVIII gene rearrangements in 18 hemophilia A patients: five novel mutations." Bicocchi M.P., Pasino M., Lanza T., Bottini F., Molinari A.C., Caprino D., Rosano C., Acquila M. Am. J. Hematol. 78:117-122(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA THR-111; ASP-450; CYS-612; HIS-1800; CYS-1802 AND ALA-2251.
[98]	"Mutation analysis in 51 patients with haemophilia A: report of 10 novel mutations and correlations between genotype and clinical phenotype." Hill M., Deam S., Gordon B., Dolan G. Haemophilia 11:133-141(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA CYS-365; THR-470; SER-541; GLY-602; TRP-717; LYS-1701; CYS-1708; VAL-1727; ILE-1888; VAL-1966; TRP-2016; GLY-2018; LEU-2067; LEU-2162 AND HIS-2182.
[99]	"Female haemophilia A heterozygous for a de novo frameshift and a novel missense mutation of factor VIII." Cai X.-H., Wang X.-F., Dai J., Fang Y., Ding Q.-L., Xie F., Wang H.-L. J. Thromb. Haemost. 4:1969-1974(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HEMA PRO-1994.
[100]	"Identification of 31 novel mutations in the F8 gene in Spanish hemophilia A patients: structural analysis of 20 missense mutations suggests new intermolecular binding sites." Vencesla A., Corral-Rodriguez M.A., Baena M., Cornet M., Domenech M., Baiget M., Fuentes-Prior P., Tizzano E.F. Blood 111:3468-3478(2008) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA ARG-83; ASN-186; PRO-195; PRO-261; ASP-280; SER-394; VAL-474; ARG-496; VAL-513; ARG-569; ILE-637; VAL-1720; LEU-1762; ASP-2101; PRO-2106; VAL-2143; LEU-2172; GLY-2286 AND PHE-2336.
[101]	"Identification of factor VIII gene mutations in patients with severe haemophilia A in Venezuela: identification of seven novel mutations." Albanez S., Ruiz-Saez A., Boadas A., De Bosch N., Porco A. Haemophilia 17:913-918(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HEMA PHE-191; TYR-1877; ARG-2013 AND ASP-2344.
+	Additional computationally mapped references.

Web resources

Wikipedia

Factor VIII entry

HAMSters

Factor VIII mutation db

GeneReviews

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M14113 mRNA. Translation: AAA52485.1.
X01179 mRNA. Translation: CAA25619.1.
M90707 mRNA. Translation: AAA58466.1.
K01740 mRNA. Translation: AAA52484.1.
M88648 , M88628, M88629, M88630, M88631, M88632, M88633, M88634, M88635, M88636, M88638, M88639, M88640, M88641, M88642, M88643, M88644, M88645, M88646, M88647 Genomic DNA. Translation: AAA52420.1.
AY769950 Genomic DNA. Translation: AAV85964.1.
AK289947 mRNA. Translation: BAF82636.1.
AK313707 mRNA. Translation: BAG36452.1.
BX470111 , AC109993, BX842559, BX842564, BX890586 Genomic DNA. Translation: CAI41660.1.
BX842564 , AC109993, BX470111, BX842559, BX890586 Genomic DNA. Translation: CAI41666.1.
BX842559 , AC109993, BX470111, BX842564, BX890586 Genomic DNA. Translation: CAI41672.1.
BX890586 , AC109993, BX470111, BX842559, BX842564 Genomic DNA. Translation: CAI43241.1.
BX842559, AC109993 Genomic DNA. Translation: CAO03404.1.
CH471172 Genomic DNA. Translation: EAW72645.1.
BC022513 mRNA. Translation: AAH22513.1.
BC064380 mRNA. Translation: AAH64380.1.
BC098389 mRNA. Translation: AAH98389.1.
BC111967 mRNA. Translation: AAI11968.1.
BC111969 mRNA. Translation: AAI11970.1.
U80228 Genomic DNA. Translation: AAB61261.1.

IPI

IPI00017603.
IPI00925597.

PIR

EZHU. I54318.

RefSeq

NP_000123.1. NM_000132.3.
NP_063916.1. NM_019863.2.

UniGene

Hs.632836.
Hs.654450.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CFG	NMR	-	A	2322-2343	[»]
1D7P	X-ray	1.50	M	2190-2348	[»]
1FAC	NMR	-	A	2322-2342	[»]
1IQD	X-ray	2.00	C	2193-2348	[»]
2R7E	X-ray	3.70	A	19-760	[»]
			B	1582-2351	[»]
3CDZ	X-ray	3.98	A	20-764	[»]
			B	1668-2351	[»]
3HNB	X-ray	1.15	M	2189-2347	[»]
3HNY	X-ray	1.07	M	2189-2347	[»]
3HOB	X-ray	2.07	A/M	2189-2347	[»]

ProteinModelPortal

P00451.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29774N.

IntAct

P00451. 3 interactions.

MINT

MINT-202317.

STRING

9606.ENSP00000353393.

Protein family/group databases

Allergome

9868. Hom s Factor VIII.

PTM databases

GlycoSuiteDB

P00451.

PhosphoSite

P00451.

Polymorphism databases

DMDM

119767.

Proteomic databases

PaxDb

P00451.

PRIDE

P00451.

Protocols and materials databases

DNASU

2157.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000330287; ENSP00000327895; ENSG00000185010.
ENST00000360256; ENSP00000353393; ENSG00000185010.
ENST00000593499; ENSP00000470213; ENSG00000269261.
ENST00000601201; ENSP00000471364; ENSG00000269261.

GeneID

2157.

KEGG

hsa:2157.

UCSC

uc004fmt.3. human.

Organism-specific databases

CTD

2157.

GeneCards

GC0XM154064.

HGNC

HGNC:3546. F8.

HPA

CAB018777.

MIM

134500. phenotype.
300841. gene.
306700. phenotype.

neXtProt

NX_P00451.

Orphanet

169808. Mild hemophilia A.
169805. Moderately severe hemophilia A.
169802. Severe hemophilia A.
177926. Symptomatic form of hemophilia A in female carriers.

PharmGKB

PA27952.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG151351.

HOGENOM

HOG000231686.

HOVERGEN

HBG106657.

InParanoid

P00451.

KO

K03899.

OMA

EDGPTKS.

OrthoDB

EOG40S0DR.

Enzyme and pathway databases

Reactome

REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P00451.

Bgee

P00451.

CleanEx

HS_F8.

Genevestigator

P00451.

GermOnline

ENSG00000185010. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.420. 6 hits.

InterPro

IPR000421. Coagulation_fac_5/8-C_type_dom.
IPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
IPR024715. Factor_5/8.
IPR014707. Factor_8.
IPR008979. Galactose-bd-like.
[Graphical view]

PANTHER

PTHR10127:SF50. PTHR10127:SF50. 1 hit.

Pfam

PF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 2 hits.
PF00754. F5_F8_type_C. 2 hits.
[Graphical view]

PIRSF

PIRSF000354. Factors_V_VIII. 1 hit.

SMART

SM00231. FA58C. 2 hits.
[Graphical view]

SUPFAM

SSF49503. Cupredoxin. 6 hits.
SSF49785. Gal_bind_like. 2 hits.

PROSITE

PS01285. FA58C_1. 2 hits.
PS01286. FA58C_2. 2 hits.
PS50022. FA58C_3. 2 hits.
PS00079. MULTICOPPER_OXIDASE1. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P00451.

ChEMBL

CHEMBL3143.

DrugBank

DB00025. Antihemophilic Factor.
DB00100. Coagulation Factor IX.
DB00055. Drotrecogin alfa.

EvolutionaryTrace

P00451.

GenomeRNAi

2157.

NextBio

8713.

SOURCE

Search...

Entry information

Entry name

FA8_HUMAN

Accession

Primary (citable) accession number: P00451
Secondary accession number(s): Q14286, Q5HY69

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	May 1, 2013
This is version 184 of the entry and version 1 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.