Reviewed, UniProtKB/Swiss-Prot P00740 (FA9_HUMAN)

Names and origin

Protein names

Recommended name:
    Coagulation factor IX
    EC=3.4.21.22
Alternative name(s):
    Christmas factor
    Plasma thromboplastin component
      Short name=PTC
Cleaved into the following 2 chains:
    1- Recommended name:
            Coagulation factor IXa light chain
    2- Recommended name:
            Coagulation factor IXa heavy chain

Gene names

Name:

F9

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	461 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 IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca2+ ions, phospholipids, and factor VIIIa.
Catalytic activity	Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa.
Subunit structure	Heterodimer of a light chain and a heavy chain; disulfide-linked.
Subcellular location	Secreted.
Tissue specificity	Synthesized primarily in the liver and secreted in plasma.
Domain	Calcium binds to the gamma-carboxyglutamic acid (Gla) residues and, with stronger affinity, to another site, beyond the Gla domain.
Post-translational modification	Activated by factor XIa, which excises the activation peptide. The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.
Involvement in disease	Defects in F9 are the cause of recessive X-linked hemophilia B (HEMB) [MIM:306900]; also known as Christmas disease. Ref.9 Ref.11 Ref.32 Ref.35 Ref.36 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42 Ref.43 Ref.44 Ref.45 Ref.46 Ref.47 Ref.48 Ref.49 Ref.50 Ref.51 Ref.52 Ref.53 Ref.54 Ref.55 Ref.56 Ref.57 Ref.58 Ref.60 Ref.61 Ref.62 Ref.63 Ref.64 Ref.65 Ref.68 Ref.69 Ref.70 Mutations in position 43 (Oxford-3, San Dimas) and 46 (Cambridge) prevents cleavage of the propeptide, mutation in position 93 (Alabama) probably fails to bind to cell membranes, mutation in position 191 (Chapel-Hill) or in position 226 (Nagoya OR Hilo) prevent cleavage of the activation peptide.
Pharmaceutical use	Available under the names BeneFix (Baxter and American Home Products). Used to treat hemophilia B.
Miscellaneous	In 1952, one of the earliest researchers of the disease, Dr. R.G. Macfarlane used the patient's surname, Christmas, to refer to the disease and also to refer to the clotting factor which he called the 'Christmas Factor' At the time Stephen Christmas was a 5-year-old boy. He died in 1993 at the age of 46 from acquired immunodeficiency syndrome contracted through treatment with blood products.
Sequence similarities	Belongs to the peptidase S1 family. Contains 2 EGF-like domains. Contains 1 Gla (gamma-carboxy-glutamate) domain. Contains 1 peptidase S1 domain.

Ontologies

Keywords
Biological process	Blood coagulation
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Disease	Disease mutation Hemophilia
Domain	EGF-like domain Repeat Signal
Ligand	Calcium
Molecular function	Hydrolase Protease Serine protease
PTM	Cleavage on pair of basic residues Disulfide bond Gamma-carboxyglutamic acid Glycoprotein Hydroxylation Phosphoprotein Sulfation Zymogen
Technical term	3D-structure Direct protein sequencing Pharmaceutical
Gene Ontology (GO)
Biological process	blood coagulation, extrinsic pathway Inferred from Experiment. Source: Reactome proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from direct assay. Source: HPA extracellular region Non-traceable author statement. Source: UniProtKB nucleus Inferred from direct assay. Source: HPA plasma membrane Inferred from Experiment. Source: Reactome
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase activity Ref.46 Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 28

28

Potential

Propeptide

29 – 46

18

Ref.11

PRO_0000027755

Chain

47 – 461

415

Coagulation factor IX

PRO_0000027756

Chain

47 – 191

145

Coagulation factor IXa light chain

PRO_0000027757

Propeptide

192 – 226

35

Activation peptide

PRO_0000027758

Chain

227 – 461

235

Coagulation factor IXa heavy chain

PRO_0000027759

Regions

Domain

47 – 92

46

Gla

Domain

93 – 129

37

EGF-like 1; calcium-binding Potential

Domain

130 – 171

42

EGF-like 2

Domain

227 – 459

233

Peptidase S1

Sites

Active site

267

1

Charge relay system Ref.15

Active site

315

1

Charge relay system Ref.15

Active site

411

1

Charge relay system Ref.15

Site

191 – 192

2

Cleavage; by factor XIa

Site

226 – 227

2

Cleavage; by factor XIa

Amino acid modifications

Modified residue

53

1

4-carboxyglutamate

Modified residue

54

1

4-carboxyglutamate

Modified residue

61

1

4-carboxyglutamate

Modified residue

63

1

4-carboxyglutamate

Modified residue

66

1

4-carboxyglutamate

Modified residue

67

1

4-carboxyglutamate

Modified residue

72

1

4-carboxyglutamate

Modified residue

73

1

4-carboxyglutamate

Modified residue

76

1

4-carboxyglutamate

Modified residue

79

1

4-carboxyglutamate

Modified residue

82

1

4-carboxyglutamate

Modified residue

86

1

4-carboxyglutamate

Modified residue

110

1

(3R)-3-hydroxyaspartate

Modified residue

114

1

Phosphoserine Ref.22

Modified residue

201

1

Sulfotyrosine

Modified residue

204

1

Phosphoserine

Glycosylation

99

1

O-linked (Glc...)

CAR_000009

Glycosylation

107

1

O-linked (Fuc...)

CAR_000010

Glycosylation

203

1

N-linked (GlcNAc...)

Glycosylation

205

1

O-linked (GalNAc...) Ref.21

Glycosylation

213

1

N-linked (GlcNAc...)

Glycosylation

215

1

O-linked (GalNAc...) Ref.21

Disulfide bond

64 ↔ 69

Disulfide bond

97 ↔ 108

Disulfide bond

102 ↔ 117

Disulfide bond

119 ↔ 128

Disulfide bond

134 ↔ 145

Disulfide bond

141 ↔ 155

Disulfide bond

157 ↔ 170

Disulfide bond

178 ↔ 335

Disulfide bond

252 ↔ 268

Disulfide bond

382 ↔ 396

Disulfide bond

407 ↔ 435

Natural variations

Natural variant

7

1

I → F Ref.42

VAR_006520

Natural variant

17

1

I → N in HEMB; severe; UK 22.

VAR_006521

Natural variant

28

1

C → R in HEMB; moderate; HB130. Ref.69

VAR_006522

Natural variant

28

1

C → Y in HEMB. Ref.69

VAR_017343

Natural variant

30

1

V → I in HEMB. Ref.54

VAR_006523

Natural variant

37

1

A → T in warfarin sensitivity; reduced affinity of the glutamate carboxylase for the factor IX precursor. Ref.59

VAR_017307

Natural variant

43

1

R → L in HEMB; severe; Bendorf, Beuten, Gleiwitz, etc.. Ref.9 Ref.36 Ref.45 Ref.63 Ref.69 Ref.70

VAR_006525

Natural variant

43

1

R → Q in HEMB; severe; San Dimas, Oxford-3, Strasbourg-2, etc.. Ref.9 Ref.36 Ref.45 Ref.63 Ref.69 Ref.70

VAR_006524

Natural variant

43

1

R → W in HEMB; severe; Boxtel, Heiden, Lienen, etc.. Ref.9 Ref.36 Ref.45 Ref.63 Ref.69 Ref.70

VAR_006526

Natural variant

45

1

K → N in HEMB; severe; Seattle E.

VAR_006527

Natural variant

46

1

R → S in HEMB; severe; Cambridge. Ref.63

VAR_006528

Natural variant

46

1

R → T in HEMB; severe. Ref.63

VAR_006529

Natural variant

48

1

N → I in HEMB; severe; Calgary-16.

VAR_006530

Natural variant

49

1

S → P in HEMB.

VAR_006531

Natural variant

52

1

L → S in HEMB; severe; Gla mutant. Ref.69

VAR_017344

Natural variant

53

1

E → A in HEMB; severe; Oxford-B2; Gla mutant.

VAR_006532

Natural variant

54

1

E → G in HEMB; severe; HB151; Gla mutant.

VAR_006533

Natural variant

55

1

F → C in HEMB.

VAR_006534

Natural variant

58

1

G → A in HEMB; severe; Hong Kong-1.

VAR_006535

Natural variant

58

1

G → R in HEMB; severe; Los Angeles-4.

VAR_006536

Natural variant

62 – 63

2

Missing in HEMB; severe.

VAR_006537

Natural variant

66

1

E → V in HEMB; moderate.

VAR_006538

Natural variant

67

1

E → K in HEMB; severe; Nagoya-4; Gla mutant.

VAR_006539

Natural variant

71

1

F → S in HEMB; severe.

VAR_006540

Natural variant

73

1

E → K in HEMB; severe; Seattle-3; Gla mutant. Ref.46 Ref.47

VAR_006541

Natural variant

73

1

E → V in HEMB; severe; Chongqing; Gla mutant. Ref.46 Ref.47

VAR_006542

Natural variant

75

1

R → Q in HEMB; mild. Ref.42

VAR_017308

Natural variant

79

1

E → D in HEMB. Ref.42

VAR_017309

Natural variant

84

1

T → R in HEMB. Ref.70

VAR_017345

Natural variant

91

1

Y → C in HEMB; moderate.

VAR_006543

Natural variant

93

1

D → G in HEMB; moderate; Alabama. Ref.37

VAR_006544

Natural variant

96

1

Q → P in HEMB; severe; New London.

VAR_006545

Natural variant

97

1

C → S in HEMB.

VAR_006546

Natural variant

101

1

P → R in HEMB.

VAR_006547

Natural variant

102

1

C → R in HEMB; severe; Basel.

VAR_006548

Natural variant

106

1

G → D in HEMB. Ref.46 Ref.63 Ref.69

VAR_017346

Natural variant

106

1

G → S in HEMB; mild; Durham. Ref.46 Ref.63 Ref.69

VAR_006549

Natural variant

108

1

C → S in HEMB.

VAR_006550

Natural variant

110

1

D → N in HEMB; severe; Oxford-D1. Ref.54

VAR_006551

Natural variant

112

1

I → S in HEMB.

VAR_006552

Natural variant

113

1

N → K in HEMB; mild. Ref.60

VAR_006553

Natural variant

115

1

Y → C in HEMB; severe. Ref.63

VAR_006554

Natural variant

119

1

C → F in HEMB; severe. Ref.62

VAR_006555

Natural variant

119

1

C → R in HEMB; Iran. Ref.62

VAR_006556

Natural variant

124

1

E → K in HEMB. Ref.69

VAR_017347

Natural variant

125

1

G → E in HEMB. Ref.70

VAR_006557

Natural variant

125

1

G → R in HEMB. Ref.70

VAR_017348

Natural variant

125

1

G → V in HEMB. Ref.70

VAR_006558

Natural variant

129 – 130

2

Missing in HEMB. Ref.54

VAR_006559

Natural variant

134

1

C → Y in HEMB. Ref.69

VAR_017349

Natural variant

136

1

I → T in HEMB; mild.

VAR_006560

Natural variant

139

1

G → D in HEMB; severe.

VAR_006561

Natural variant

139

1

G → S in HEMB.

VAR_006562

Natural variant

155

1

C → F in HEMB; severe. Ref.63

VAR_006563

Natural variant

160

1

G → E in HEMB; mild. Ref.54

VAR_006564

Natural variant

167

1

Q → H in HEMB; mild.

VAR_006565

Natural variant

169

1

S → C in HEMB. Ref.68

VAR_017350

Natural variant

170

1

C → F in HEMB. Ref.54 Ref.70

VAR_017351

Natural variant

178

1

C → R in HEMB.

VAR_006566

Natural variant

178

1

C → W in HEMB; severe.

VAR_006567

Natural variant

191

1

R → C in HEMB; moderate; Albuquerque, Cardiff-1, etc.. Ref.35 Ref.43 Ref.55

VAR_006569

Natural variant

191

1

R → H in HEMB; moderate; Chapel-Hill, Chicago-2, etc.. Ref.35 Ref.43 Ref.55

VAR_006568

Natural variant

194

1

T → A: dbSNP rs6048. Ref.3 Ref.4 Ref.5 Ref.66

VAR_011773

Natural variant

226

1

R → G in HEMB; severe; Madrid. Ref.11 Ref.40 Ref.49 Ref.55 Ref.69

VAR_006571

Natural variant

226

1

R → Q in HEMB; severe; Hilo and Novara. Ref.11 Ref.40 Ref.49 Ref.55 Ref.69

VAR_006572

Natural variant

226

1

R → W in HEMB; severe; Nagoya-1, Dernbach, Deventer, Idaho, etc.. Ref.11 Ref.40 Ref.49 Ref.55 Ref.69

VAR_006570

Natural variant

227

1

V → D in HEMB; mild. Ref.49

VAR_006573

Natural variant

227

1

V → F in HEMB; Milano. Ref.49

VAR_017310

Natural variant

228

1

V → F in HEMB; severe; Kashihara. Ref.44 Ref.48

VAR_017311

Natural variant

228

1

V → L in HEMB; mild; Cardiff-2. Ref.44 Ref.48

VAR_006574

Natural variant

241

1

Q → H in HEMB. Ref.69

VAR_006575

Natural variant

241

1

Q → K in HEMB. Ref.69

VAR_017352

Natural variant

252

1

C → S in HEMB; severe; this is the mutation in the index case of the disease, Stephen Christmas. Ref.53 Ref.69

VAR_017312

Natural variant

252

1

C → Y in HEMB. Ref.53 Ref.69

VAR_017353

Natural variant

253

1

G → E in HEMB; severe. Ref.54

VAR_006576

Natural variant

253

1

G → R in HEMB; severe; Luanda. Ref.54

VAR_006577

Natural variant

265

1

A → T in HEMB; mild.

VAR_006578

Natural variant

268

1

C → W in HEMB; moderate. Ref.42

VAR_017313

Natural variant

279

1

A → T in HEMB; mild. Ref.42 Ref.55

VAR_006579

Natural variant

283

1

N → D in HEMB; severe.

VAR_006580

Natural variant

286

1

Missing in HEMB; severe.

VAR_006581

Natural variant

291

1

E → V in HEMB; Monschau. Ref.52

VAR_017314

Natural variant

294

1

R → G in HEMB; severe. Ref.46 Ref.52 Ref.54 Ref.57 Ref.69

VAR_006582

Natural variant

294

1

R → Q in HEMB; mild to moderate; Dreihacken, Penafiel and Seattle-4. Ref.46 Ref.52 Ref.54 Ref.57 Ref.69

VAR_006583

Natural variant

302

1

H → R in HEMB. Ref.70

VAR_006584

Natural variant

306

1

N → S in HEMB; mild. Ref.42

VAR_017315

Natural variant

316

1

I → F in HEMB. Ref.69

VAR_006585

Natural variant

318

1

L → R in HEMB. Ref.69

VAR_017354

Natural variant

321

1

L → Q in HEMB; severe.

VAR_006586

Natural variant

333

1

P → H in HEMB; severe. Ref.68

VAR_006587

Natural variant

333

1

P → T in HEMB. Ref.68

VAR_017355

Natural variant

342

1

T → K in HEMB; mild. Ref.42 Ref.60 Ref.70

VAR_006588

Natural variant

342

1

T → M in HEMB; moderate. Ref.42 Ref.60 Ref.70

VAR_006589

Natural variant

344

1

I → L in HEMB. Ref.70

VAR_017356

Natural variant

351

1

G → D in HEMB.

VAR_006590

Natural variant

356

1

W → C in HEMB; severe.

VAR_006591

Natural variant

357

1

G → E in HEMB; severe; Amagasaki. Ref.42 Ref.50

VAR_006592

Natural variant

357

1

G → R in HEMB. Ref.42 Ref.50

VAR_017316

Natural variant

362

1

K → E in HEMB; moderate.

VAR_006593

Natural variant

363

1

G → W in HEMB.

VAR_006594

Natural variant

366

1

A → D in HEMB.

VAR_006595

Natural variant

379

1

R → G in HEMB; moderate. Ref.54 Ref.55 Ref.63 Ref.69

VAR_006596

Natural variant

379

1

R → Q in HEMB; severe; Iceland-1, London and Sesimbra. Ref.54 Ref.55 Ref.63 Ref.69

VAR_006597

Natural variant

382

1

C → Y in HEMB.

VAR_006598

Natural variant

383

1

L → F in HEMB. Ref.69

VAR_017358

Natural variant

383

1

L → I in HEMB. Ref.69

VAR_017357

Natural variant

387

1

K → E in HEMB; mild. Ref.63

VAR_006599

Natural variant

390

1

I → F in HEMB; severe. Ref.54

VAR_006600

Natural variant

394

1

M → K in HEMB.

VAR_006601

Natural variant

395

1

F → I in HEMB. Ref.69 Ref.70

VAR_017359

Natural variant

395

1

F → L in HEMB. Ref.69 Ref.70

VAR_017360

Natural variant

396

1

C → F in HEMB. Ref.69

VAR_017361

Natural variant

396

1

C → S in HEMB; severe. Ref.69

VAR_006602

Natural variant

397

1

A → P in HEMB; mild; Hong Kong-11. Ref.61

VAR_017317

Natural variant

404

1

R → T in HEMB.

VAR_006603

Natural variant

407

1

C → R in HEMB. Ref.69

VAR_017362

Natural variant

407

1

C → S in HEMB; severe. Ref.69

VAR_006604

Natural variant

410

1

D → H in HEMB; Mechtal. Ref.52 Ref.54

VAR_017318

Natural variant

411

1

S → G in HEMB; Varel. Ref.52

VAR_017320

Natural variant

411

1

S → I in HEMB; Schmallenberg. Ref.52

VAR_017319

Natural variant

412

1

G → E in HEMB. Ref.69

VAR_017363

Natural variant

413

1

G → R in HEMB; moderate to severe. Ref.57 Ref.60

VAR_006605

Natural variant

414

1

P → T in HEMB; Bergamo. Ref.49 Ref.70

VAR_017321

Natural variant

419

1

V → E in HEMB; moderately severe. Ref.55 Ref.56

VAR_006606

Natural variant

424

1

F → V in HEMB. Ref.60

VAR_006607

Natural variant

426

1

T → P in HEMB; severe; Barcelos. Ref.54

VAR_006608

Natural variant

430

1

S → T in HEMB. Ref.54

VAR_006609

Natural variant

431

1

W → G in HEMB.

VAR_006610

Natural variant

431

1

W → R in HEMB; moderate.

VAR_006611

Natural variant

432

1

G → S in HEMB; severe. Ref.63

VAR_006612

Natural variant

432

1

G → V in HEMB; severe. Ref.63

VAR_006613

Natural variant

433

1

E → A in HEMB.

VAR_006614

Natural variant

433

1

E → K in HEMB.

VAR_006615

Natural variant

435

1

C → Y in HEMB. Ref.70

VAR_017364

Natural variant

436

1

A → V in HEMB; moderately severe; Niigata. Ref.39

VAR_006616

Natural variant

442

1

G → E in HEMB. Ref.41 Ref.70

VAR_017365

Natural variant

442

1

G → R in HEMB; severe; Angers. Ref.41 Ref.70

VAR_017322

Natural variant

443

1

I → T in HEMB; moderately severe; Long Beach, Los Angeles and Vancouver. Ref.38 Ref.51

VAR_017323

Natural variant

445

1

T → TIYT in HEMB; severe; Lousada.

VAR_006617

Natural variant

449

1

R → Q in HEMB; mild. Ref.55 Ref.70

VAR_006618

Natural variant

449

1

R → W in HEMB; mild. Ref.55 Ref.70

VAR_006619

Natural variant

450

1

Y → C in HEMB; severe. Ref.54 Ref.63

VAR_006620

Natural variant

453

1

W → R in HEMB. Ref.42

VAR_017324

Natural variant

454

1

I → T in HEMB; Italy. Ref.62

VAR_006621

Natural variant

461

1

T → P: dbSNP rs4149751. Ref.6

VAR_014308

Secondary structure

1

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461

Helix Strand Turn

Details...

Beta strand

50 – 52

3

Helix

60 – 64

5

Helix

71 – 75

5

Beta strand

78 – 80

3

Helix

81 – 90

10

Turn

96 – 99

4

Beta strand

107 – 111

5

Beta strand

114 – 118

5

Helix

136 – 140

5

Beta strand

142 – 147

6

Beta strand

153 – 156

4

Beta strand

161 – 163

3

Beta strand

167 – 172

6

Beta strand

174 – 176

3

Beta strand

241 – 248

8

Beta strand

252 – 258

7

Beta strand

261 – 264

4

Helix

266 – 268

3

Beta strand

276 – 280

5

Beta strand

282 – 286

5

Beta strand

292 – 301

10

Turn

307 – 309

3

Beta strand

310 – 312

3

Beta strand

317 – 323

7

Helix

339 – 346

8

Beta strand

349 – 356

8

Beta strand

358 – 360

3

Beta strand

370 – 376

7

Helix

379 – 385

7

Beta strand

394 – 398

5

Beta strand

414 – 421

8

Beta strand

423 – 436

14

Beta strand

442 – 446

5

Helix

447 – 449

3

Helix

451 – 458

8

Sequences

	Sequence		Length	Mass (Da)
	P00740-1 [UniParc]. Last modified June 7, 2005. Version 2. Checksum: C4720C1234477EF5	FASTA	461	51,778
	10 20 30 40 50 60 MQRVNMIMAE SPGLITICLL GYLLSAECTV FLDHENANKI LNRPKRYNSG KLEEFVQGNL 70 80 90 100 110 120 ERECMEEKCS FEEAREVFEN TERTTEFWKQ YVDGDQCESN PCLNGGSCKD DINSYECWCP 130 140 150 160 170 180 FGFEGKNCEL DVTCNIKNGR CEQFCKNSAD NKVVCSCTEG YRLAENQKSC EPAVPFPCGR 190 200 210 220 230 240 VSVSQTSKLT RAETVFPDVD YVNSTEAETI LDNITQSTQS FNDFTRVVGG EDAKPGQFPW 250 260 270 280 290 300 QVVLNGKVDA FCGGSIVNEK WIVTAAHCVE TGVKITVVAG EHNIEETEHT EQKRNVIRII 310 320 330 340 350 360 PHHNYNAAIN KYNHDIALLE LDEPLVLNSY VTPICIADKE YTNIFLKFGS GYVSGWGRVF 370 380 390 400 410 420 HKGRSALVLQ YLRVPLVDRA TCLRSTKFTI YNNMFCAGFH EGGRDSCQGD SGGPHVTEVE 430 440 450 460 GTSFLTGIIS WGEECAMKGK YGIYTKVSRY VNWIKEKTKL T

References

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[1]	"Isolation and characterization of a cDNA coding for human factor IX." Kurachi K., Davie E.W. Proc. Natl. Acad. Sci. U.S.A. 79:6461-6464(1982) [PubMed: 6959130] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Isolation of a human anti-haemophilic factor IX cDNA clone using a unique 52-base synthetic oligonucleotide probe deduced from the amino acid sequence of bovine factor IX." Jaye M., de la Salle H., Schamber F., Balland A., Kohli V., Findeli A., Tolstoshev P., Lecocq J.-P. Nucleic Acids Res. 11:2325-2335(1983) [PubMed: 6687940] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[3]	"The gene structure of human anti-haemophilic factor IX." Anson D.S., Choo K.H., Rees D.J.G., Giannelli F., Gould K.G., Huddleston J.A., Brownlee G.G. EMBO J. 3:1053-1060(1984) [PubMed: 6329734] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-194.
[4]	"Nucleotide sequence of the gene for human factor IX (antihemophilic factor B)." Yoshitake S., Schach B.G., Foster D.C., Davie E.W., Kurachi K. Biochemistry 24:3736-3750(1985) [PubMed: 2994716] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-194.
[5]	"Evidence for a prevalent dimorphism in the activation peptide of human coagulation factor IX." McGraw R.A., Davis L.M., Noyes C.M., Lundblad R.L., Roberts H.R., Graham J.B., Stafford D.W. Proc. Natl. Acad. Sci. U.S.A. 82:2847-2851(1985) [PubMed: 3857619] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-194.
[6]	SeattleSNPs variation discovery resource Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PRO-461.
[7]	"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: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[9]	"The Arg-4 mutant factor IX Strasbourg 2 shows a delayed activation by factor XIa." de la Salle C., Charmantier J.L., Ravanat C., Ohlmann P., Hartmann M.L., Schuhler S., Bischoff R., Ebel C., Roecklin D., Balland A. Nouv. Rev. Fr. Hematol. 35:473-480(1993) [PubMed: 8295821] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 30-84, VARIANT HEMB GLN-43.
[10]	"Isolation and characterization of human factor IX cDNA: identification of Taq I polymorphism and regional assignment." Jagadeeswaran P., Lavelle D.E., Kaul R., Mohandas T., Warren S.T. Somat. Cell Mol. Genet. 10:465-473(1984) [PubMed: 6089357] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 36-326. Tissue: Liver.
[11]	"Blood clotting factor IX BM Nagoya. Substitution of arginine 180 by tryptophan and its activation by alpha-chymotrypsin and rat mast cell chymase." Suehiro K., Kawabata S., Miyata T., Takeya H., Takamatsu J., Ogata K., Kamiya T., Saito H., Niho Y., Iwanaga S. J. Biol. Chem. 264:21257-21265(1989) [PubMed: 2592373] [Abstract] Cited for: PROTEIN SEQUENCE OF 47-461, VARIANT HEMB TRP-226.
[12]	"Genomic amplification with transcript sequencing." Stoflet E.S., Koeberl D.D., Sarkar G., Sommer S.S. Science 239:491-494(1988) [PubMed: 3340835] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 290-359.
[13]	"A deletion located in the 3' non translated part of the factor IX gene responsible for mild haemophilia B." de la Salle C., Charmantier J.L., Baas M.-J., Schwartz A., Wiesel M.L., Grunebaum L., Cazenave J.-P. Thromb. Haemost. 70:370-371(1993) [PubMed: 8236150] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 444-461.
[14]	"The occurrence of beta-hydroxyaspartic acid in the vitamin K-dependent blood coagulation zymogens." McMullen B.A., Fujikawa K., Kisiel W. Biochem. Biophys. Res. Commun. 115:8-14(1983) [PubMed: 6688526] [Abstract] Cited for: HYDROXYLATION AT ASP-110.
[15]	"Activation of human factor IX (Christmas factor)." di Scipio R.G., Kurachi K., Davie E.W. J. Clin. Invest. 61:1528-1538(1978) [PubMed: 659613] [Abstract] Cited for: PROTEOLYTIC PROCESSING, ACTIVE SITE.
[16]	"Derivatives of blood coagulation factor IX contain a high affinity Ca2+-binding site that lacks gamma-carboxyglutamic acid." Morita T., Isaacs B.S., Esmon C.T., Johnson A.E. J. Biol. Chem. 259:5698-5704(1984) [PubMed: 6425296] [Abstract] Cited for: CALCIUM-BINDING DATA.
[17]	Erratum Morita T., Isaacs B.S., Esmon C.T., Johnson A.E. J. Biol. Chem. 260:2583-2583(1985)
[18]	"Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z." Nishimura H., Kawabata S., Kisiel W., Hase S., Ikenaka T., Takao T., Shimonishi Y., Iwanaga S. J. Biol. Chem. 264:20320-20325(1989) [PubMed: 2511201] [Abstract] Cited for: STRUCTURE OF CARBOHYDRATE ON SER-99.
[19]	"A new trisaccharide sugar chain linked to a serine residue in the first EGF-like domain of clotting factors VII and IX and protein Z." Iwanaga S., Nishimura H., Kawabata S., Kisiel W., Hase S., Ikenaka T. Adv. Exp. Med. Biol. 281:121-131(1990) [PubMed: 2129367] [Abstract] Cited for: STRUCTURE OF CARBOHYDRATE ON SER-99.
[20]	"Human factor IX has a tetrasaccharide O-glycosidically linked to serine 61 through the fucose residue." Nishimura H., Takao T., Hase S., Shimonishi Y., Iwanaga S. J. Biol. Chem. 267:17520-17525(1992) [PubMed: 1517205] [Abstract] Cited for: STRUCTURE OF CARBOHYDRATE ON SER-107.
[21]	"Activation peptide of human factor IX has oligosaccharides O-glycosidically linked to threonine residues at 159 and 169." Agarwala K.L., Kawabata S., Takao T., Murata H., Shimonishi Y., Nishimura H., Iwanaga S. Biochemistry 33:5167-5171(1994) [PubMed: 8172892] [Abstract] Cited for: GLYCOSYLATION AT THR-205 AND THR-215.
[22]	"Partial phosphorylation of serine-68 in EGF-1 of human factor IX." Harris R.J., Papac D.I., Truong L., Smith K.J. (In) Proceedings of XIth international conference on methods in protein structure analysis, pp.50-50, Annecy (1996) Cited for: PHOSPHORYLATION AT SER-114.
[23]	"Posttranslational modifications of recombinant myotube-synthesized human factor IX." Arruda V.R., Hagstrom J.N., Deitch J., Heiman-Patterson T., Camire R.M., Chu K., Fields P.A., Herzog R.W., Couto L.B., Larson P.J., High K.A. Blood 97:130-138(2001) [PubMed: 11133752] [Abstract] Cited for: POST-TRANSLATIONAL MODIFICATIONS.
[24]	"Structure of the metal-free gamma-carboxyglutamic acid-rich membrane binding region of factor IX by two-dimensional NMR spectroscopy." Freedman S.J., Furie B.C., Furie B., Baleja J.D. J. Biol. Chem. 270:7980-7987(1995) [PubMed: 7713897] [Abstract] Cited for: STRUCTURE BY NMR OF 47-93.
[25]	"Structure of the calcium ion-bound gamma-carboxyglutamic acid-rich domain of factor IX." Freedman S.J., Furie B.C., Furie B., Baleja J.D. Biochemistry 34:12126-12137(1995) [PubMed: 7547952] [Abstract] Cited for: STRUCTURE BY NMR OF 47-93.
[26]	"Identification of the phospholipid binding site in the vitamin K-dependent blood coagulation protein factor IX." Freedman S.J., Blostein M.D., Baleja J.D., Jacobs M., Furie B.C., Furie B. J. Biol. Chem. 271:16227-16236(1996) [PubMed: 8663165] [Abstract] Cited for: STRUCTURE BY NMR OF 47-93.
[27]	"Refinement of the NMR solution structure of the gamma-carboxyglutamic acid domain of coagulation factor IX using molecular dynamics simulation with initial Ca2+ positions determined by a genetic algorithm." Li L., Darden T.A., Freedman S.J., Furie B.C., Furie B., Baleja J.D., Smith H., Hiskey R.G., Pedersen L.G. Biochemistry 36:2132-2138(1997) [PubMed: 9047312] [Abstract] Cited for: STRUCTURE BY NMR OF 47-93.
[28]	"Sequence-specific 1H NMR assignments, secondary structure, and location of the calcium binding site in the first epidermal growth factor like domain of blood coagulation factor IX." Huang L.H., Cheng H., Pardi A., Tam J.P., Sweeney W.V. Biochemistry 30:7402-7409(1991) [PubMed: 1854745] [Abstract] Cited for: STRUCTURE BY NMR OF 91-133.
[29]	"The three-dimensional structure of the first EGF-like module of human factor IX: comparison with EGF and TGF-alpha." Baron M., Norman D.G., Harvey T.S., Handford P.A., Mayhew M., Tse A.G.D., Brownlee G.G., Campbell I.D.C. Protein Sci. 1:81-90(1992) [PubMed: 1304885] [Abstract] Cited for: STRUCTURE BY NMR OF 92-130.
[30]	"The structure of a Ca(2+)-binding epidermal growth factor-like domain: its role in protein-protein interactions." Rao Z., Handford P., Mayhew M., Knott V., Brownlee G.G., Stuart D. Cell 82:131-141(1995) [PubMed: 7606779] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 92-130.
[31]	"Coagulation factor IXa: the relaxed conformation of Tyr99 blocks substrate binding." Hopfner K.-P., Lang A., Karcher A., Sichler K., Kopetzki E., Brandstetter H., Huber R., Bode W., Engh R.A. Structure 7:989-996(1999) [PubMed: 10467148] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 133-461.
[32]	"Molecular pathology of haemophilia B." Green P.M., Bentley D.R., Mibashan R.S., Nilsson I.M., Giannelli F. EMBO J. 8:1067-1072(1989) [PubMed: 2743975] [Abstract] Cited for: MOLECULAR PATHOLOGY OF HEMB B.
[33]	"Assessing the underlying pattern of human germline mutations: lessons from the factor IX gene." Sommer S.S. FASEB J. 6:2767-2774(1992) [PubMed: 1634040] [Abstract] Cited for: REVIEW ON HEMB VARIANTS.
[34]	"Haemophilia B: database of point mutations and short additions and deletions -- fourth edition, 1993." Giannelli F., Green P.M., High K.A., Sommer S., Poon M.-C., Ludwig M., Schwaab R., Reitsma P.H., Goossens M., Yoshioka A., Brownlee G.G. Nucleic Acids Res. 21:3075-3087(1993) [PubMed: 8392713] [Abstract] Cited for: REVIEW ON HEMB VARIANTS.
[35]	"Identification of the molecular defect in factor IX Chapel Hill: substitution of histidine for arginine at position 145." Noyes C.M., Griffith M.J., Roberts H.R., Lundblad R.L. Proc. Natl. Acad. Sci. U.S.A. 80:4200-4202(1983) [PubMed: 6603618] [Abstract] Cited for: VARIANT HEMB HIS-191.
[36]	"Defective propeptide processing of blood clotting factor IX caused by mutation of arginine to glutamine at position -4." Bentley A.K., Rees D.J., Rizza C., Brownlee G.G. Cell 45:343-348(1986) [PubMed: 3009023] [Abstract] Cited for: VARIANT HEMB GLN-43.
[37]	"Factor IXAlabama: a point mutation in a clotting protein results in hemophilia B." Davis L.M., McGraw R.A., Ware J.L., Roberts H.R., Stafford D.W. Blood 69:140-143(1987) [PubMed: 3790720] [Abstract] Cited for: VARIANT HEMB GLY-93.
[38]	"Genetic defect responsible for the dysfunctional protein: factor IX (Long Beach)." Ware J., Davis L., Frazier D., Bajaj S.P., Stafford D.W. Blood 72:820-822(1988) [PubMed: 3401602] [Abstract] Cited for: VARIANT HEMB THR-443.
[39]	"Blood clotting factor IX Niigata: substitution of alanine-390 by valine in the catalytic domain." Sugimoto M., Miyata T., Kawabata S., Yoshioka A., Fukui H., Takahashi H., Iwanaga S. J. Biochem. 104:878-880(1988) [PubMed: 3243764] [Abstract] Cited for: VARIANT HEMB VAL-436.
[40]	"Functional consequences of an arginine180 to glutamine mutation in factor IX Hilo." Monroe D.M., McCord D.M., Huang M.N., High K.A., Lundblad R.L., Kasper C.K., Roberts H.R. Blood 73:1540-1544(1989) [PubMed: 2713493] [Abstract] Cited for: VARIANT HEMB GLN-226.
[41]	"Mutations in the catalytic domain of human coagulation factor IX: rapid characterization by direct genomic sequencing of DNA fragments displaying an altered melting behavior." Attree O., Vidaud D., Vidaud M., Amselem S., Lavergne J.-M., Goossens M. Genomics 4:266-272(1989) [PubMed: 2714791] [Abstract] Cited for: VARIANT HEMB ARG-442.
[42]	"Functionally important regions of the factor IX gene have a low rate of polymorphism and a high rate of mutation in the dinucleotide CpG." Koeberl D.D., Bottema C.D., Buerstedde J.-M., Sommer S.S. Am. J. Hum. Genet. 45:448-457(1989) [PubMed: 2773937] [Abstract] Cited for: VARIANTS HEMB GLN-75; ASP-79; TRP-268; THR-279; SER-306; MET-342; ARG-357 AND ARG-453, VARIANT PHE-7.
[43]	"Factor IX Cardiff: a variant factor IX protein that shows abnormal activation is caused by an arginine to cysteine substitution at position 145." Liddell M.B., Peake I.R., Taylor S.A., Lillicrap D.P., Giddings J.C., Bloom A.L. Br. J. Haematol. 72:556-560(1989) [PubMed: 2775660] [Abstract] Cited for: VARIANT HEMB CYS-191.
[44]	"Blood clotting factor IX Kashihara: amino acid substitution of valine-182 by phenylalanine." Sakai T., Yoshioka A., Yamamoto K., Niinomi K., Fujimura Y., Fukui H., Miyata T., Iwanaga S. J. Biochem. 105:756-759(1989) [PubMed: 2753873] [Abstract] Cited for: VARIANT HEMB PHE-228.
[45]	"Factor IX San Dimas. Substitution of glutamine for Arg-4 in the propeptide leads to incomplete gamma-carboxylation and altered phospholipid binding properties." Ware J., Diuguid D.L., Liebman H.A., Rabiet M.J., Kasper C.K., Furie B.C., Furie B., Stafford D.W. J. Biol. Chem. 264:11401-11406(1989) [PubMed: 2738071] [Abstract] Cited for: VARIANT HEMB GLN-43.
[46]	"Three point mutations in the factor IX genes of five hemophilia B patients. Identification strategy using localization by altered epitopes in their hemophilic proteins." Chen S.H., Thompson A.R., Zhang M., Scott C.R. J. Clin. Invest. 84:113-118(1989) [PubMed: 2472424] [Abstract] Cited for: VARIANTS HEMB LYS-73; SER-106 AND GLN-294.
[47]	"Factor IX Chongqing: a new mutation in the calcium-binding domain of factor IX resulting in severe hemophilia B." Wang N.S., Zhang M., Thompson A.R., Chen S.H. Thromb. Haemost. 63:24-26(1990) [PubMed: 2339358] [Abstract] Cited for: VARIANT HEMB VAL-73.
[48]	"A mutation adjacent to the beta cleavage site of factor IX (valine 182 to leucine) results in mild haemophilia Bm." Taylor S.A., Liddell M.B., Peake I.R., Bloom A.L., Lillicrap D.P. Br. J. Haematol. 75:217-221(1990) [PubMed: 2372509] [Abstract] Cited for: VARIANT HEMB LEU-228.
[49]	"Mutations in hemophilia Bm occur at the Arg180-Val activation site or in the catalytic domain of factor IX." Bertina R.M., van der Linden I.K., Mannucci P.M., Reinalda-Poot H.H., Cupers R., Poort S.R., Reitsma P.H. J. Biol. Chem. 265:10876-10883(1990) [PubMed: 2162822] [Abstract] Cited for: VARIANTS HEMB GLN-226; TRP-226; PHE-227 AND THR-414.
[50]	"Factor IX Amagasaki: a new mutation in the catalytic domain resulting in the loss of both coagulant and esterase activities." Miyata T., Sakai T., Sugimoto M., Naka H., Yamamoto K., Yoshioka A., Fukui H., Mitsui K., Kamiya K., Umeyama H., Iwanaga S. Biochemistry 30:11286-11291(1991) [PubMed: 1958666] [Abstract] Cited for: VARIANT HEMB GLU-357.
[51]	"Isoleucine-397 is changed to threonine in two females with hemophilia B." Sarkar G., Cassady J.D., Pyeritz R.E., Gilchrist G.S., Sommer S.S. Nucleic Acids Res. 19:1165-1165(1991) [PubMed: 1902289] [Abstract] Cited for: VARIANT HEMB THR-443.
[52]	"Hemophilia B caused by five different nondeletion mutations in the protease domain of factor IX." Ludwig M., Sabharwal A.K., Brackmann H.H., Olek K., Smith K.J., Birktoft J.J., Bajaj S.P. Blood 79:1225-1232(1992) [PubMed: 1346975] [Abstract] Cited for: VARIANTS HEMB VAL-291; GLN-294; HIS-410; GLY-411 AND ILE-411.
[53]	"Characterization of the original Christmas disease mutation (cysteine 206-->serine): from clinical recognition to molecular pathogenesis." Taylor S.A., Duffin J., Cameron C., Teitel J., Garvey B., Lillicrap D.P. Thromb. Haemost. 67:63-65(1992) [PubMed: 1615485] [Abstract] Cited for: VARIANT HEMB SER-252.
[54]	"Single-strand conformation polymorphism (SSCP) analysis of the molecular pathology of hemophilia B." David D., Rosa H.A.V., Pemberton S., Diniz M.J., Campos M., Lavinha J. Hum. Mutat. 2:355-361(1993) [PubMed: 8257988] [Abstract] Cited for: VARIANTS HEMB ARG-253; GLN-294; GLN-379; PRO-426 AND ILE-TYR-THR-445 INS.
[55]	"Factor IX gene mutations causing haemophilia B: comparison of SSC screening versus systematic DNA sequencing and diagnostic applications." Aguilar-Martinez P., Romey M.-C., Schved J.-F., Gris J.-C., Demaille J., Claustres M. Hum. Genet. 94:287-290(1994) [PubMed: 8076946] [Abstract] Cited for: VARIANTS HEMB HIS-191; GLY-226; THR-279; GLN-379; GLU-419 AND GLN-449.
[56]	"A novel mutation (Val-373 to Glu) in the catalytic domain of factor IX, resulting in moderately/severe hemophilia B in a southern French patient." Aguilar-Martinez P., Romey M.-C., Gris J.-C., Schved J.-F., Demaille J., Claustres M. Hum. Mutat. 3:156-158(1994) [PubMed: 8199596] [Abstract] Cited for: VARIANT HEMB GLU-419.
[57]	"Identification of mutations in four hemophilia B patients of Turkish origin, including a novel deletion of base 6411." Caglayan S.H., Vielhaber E., Guersel T., Aktuglu G., Sommer S.S. Hum. Mutat. 4:163-165(1994) [PubMed: 7981722] [Abstract] Cited for: VARIANTS HEMB GLN-294 AND ARG-413.
[58]	"Twenty-five novel mutations of the factor IX gene in haemophilia B." Wulff K., Schroeder W., Wehnert M., Herrmann F.H. Hum. Mutat. 6:346-348(1995) [PubMed: 8680410] [Abstract] Cited for: VARIANTS HEMB.
[59]	"A mutation in the propeptide of factor IX leads to warfarin sensitivity by a novel mechanism." Chu K., Wu S.M., Stanley T., Stafford D.W., High K.A. J. Clin. Invest. 98:1619-1625(1996) [PubMed: 8833911] [Abstract] Cited for: VARIANT WARFARIN SENSITIVITY THR-37.
[60]	"Mutations associated with hemophilia B in Turkish patients." Caglayan S.H., Goekmen Y., Aktuglu G., Guergey A., Sommer S.S. Hum. Mutat. 10:76-79(1997) [PubMed: 9222764] [Abstract] Cited for: VARIANTS HEMB LYS-113; MET-342; ARG-413 AND VAL-424.
[61]	"Hemophilia B in a female carrier due to skewed inactivation of the normal X-chromosome." Chan V., Chan V.W.Y., Yip B., Chim C.S., Chan T.K. Am. J. Hematol. 58:72-76(1998) [PubMed: 9590153] [Abstract] Cited for: VARIANT HEMB PRO-397.
[62]	"Five novel factor IX mutations in unrelated hemophilia B patients." David D., Moreira I., Morais S., de Deus G. Hum. Mutat. Suppl. 1:S301-S303(1998) [PubMed: 9452115] [Abstract] Cited for: VARIANTS HEMB ARG-119 AND THR-454.
[63]	"Germline mutations in Peruvian patients with hemophilia B: pattern of mutation in Amerindians is similar to the putative endogenous germline pattern." Heit J.A., Thorland E.C., Ketterling R.P., Lind T.J., Daniels T.M., Zapata R.E., Ordonez S.M., Kasper C.K., Sommer S.S. Hum. Mutat. 11:372-376(1998) [PubMed: 9600455] [Abstract] Cited for: VARIANTS HEMB GLN-43; TRP-43; THR-46; SER-106; CYS-115; PHE-155; GLN-379; GLU-387; VAL-432 AND CYS-450.
[64]	"Molecular analysis of hemophilia B in Poland: 12 novel mutations of the factor IX gene." Wulff K., Bykowska K., Lopaciuk S., Herrmann F.H. Acta Biochim. Pol. 46:721-726(1999) [PubMed: 10698280] [Abstract] Cited for: VARIANTS HEMB.
[65]	"Identification of twenty-one new mutations in the factor IX gene by SSCP analysis." Montejo J.M., Magallon M., Tizzano E., Solera J. Hum. Mutat. 13:160-165(1999) [PubMed: 10094553] [Abstract] Cited for: VARIANTS HEMB.
[66]	"Characterization of single-nucleotide polymorphisms in coding regions of human genes." Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S. Nat. Genet. 22:231-238(1999) [PubMed: 10391209] [Abstract] Cited for: VARIANT ALA-194.
[67]	Erratum Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S. Nat. Genet. 23:373-373(1999)
[68]	"Factor IX gene sequencing by a simple and sensitive 15-hour procedure for haemophilia B diagnosis: identification of two novel mutations." Vidal F., Farssac E., Altisent C., Puig L., Gallardo D. Br. J. Haematol. 111:549-551(2000) [PubMed: 11122099] [Abstract] Cited for: VARIANTS HEMB CYS-169 AND THR-333.
[69]	"Molecular pathology of haemophilia B in Turkish patients: identification of a large deletion and 33 independent point mutations." Onay U.V., Kavakli K., Kilinc Y., Gurgey A., Aktuglu G., Kemahli S., Ozbek U., Caglayan S.H. Br. J. Haematol. 120:656-659(2003) [PubMed: 12588353] [Abstract] Cited for: VARIANTS HEMB TYR-28; LEU-43; GLN-43; SER-52; ASP-106; LYS-124; TYR-134; GLN-226; GLY-226; TRP-226; LYS-241; TYR-252; GLN-294; PHE-316; ARG-318; GLY-379; ILE-383; PHE-383; ILE-395; PHE-396; ARG-407 AND GLU-412.
[70]	"Molecular analyses in hemophilia B families: identification of six new mutations in the factor IX gene." Espinos C., Casana P., Haya S., Cid A.R., Aznar J.A. Haematologica 88:235-236(2003) [PubMed: 12604421] [Abstract] Cited for: VARIANTS HEMB TRP-43; ARG-84; ARG-125; VAL-125; PHE-170; ARG-302; MET-342; LEU-344; LEU-395; THR-414; TYR-435; GLU-442 AND TRP-449.
+	Additional computationally mapped references.

Web resources

Wikipedia

Factor IX entry

HAEMB

Hemophilia B mutation database

GeneReviews

SeattleSNPs

BeneFix

Clinical information on BeneFix

Protein Spotlight

The Christmas Factor - Issue 41 of December 2003

Cross-references

Sequence databases

EMBLGenBankDDBJ

J00136 mRNA. Translation: AAA98726.1.
J00137 mRNA. Translation: AAA52763.1.
K02053 , K02048, K02049, K02051, K02052 Genomic DNA. Translation: AAA56822.1.
K02402 Genomic DNA. Translation: AAB59620.1.
M11309 mRNA. Translation: AAA52023.1.
AL033403 Genomic DNA. Translation: CAI42103.1.
AF536327 Genomic DNA. Translation: AAM96188.1.
BC109214 mRNA. Translation: AAI09215.1.
BC109215 mRNA. Translation: AAI09216.1.
S68634 Genomic DNA. Translation: AAB29758.1.
M35672 mRNA. Translation: AAA51981.1.
M19063 Genomic DNA. Translation: AAA52456.1.
S66752 Genomic DNA. Translation: AAB28588.1.

IPI

IPI00296176.

PIR

KFHU. A00922.

RefSeq

NP_000124.1.

UniGene

Hs.522798

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CFH	NMR	-	A	47-93	[»]
1CFI	NMR	-	A	47-93	[»]
1EDM	X-ray	1.50	B/C	92-130	[»]
1IXA	NMR	-	A	92-130	[»]
1MGX	NMR	-	A	47-93	[»]
1NL0	X-ray	2.20	G	47-91	[»]
1RFN	X-ray	2.80	A	227-461	[»]
			B	133-188	[»]

SMR

P00740. Positions 47-191.

ModBase

Search...

Protein family/group databases

MEROPS

S01.214.

PTM databases

GlycoSuiteDB

P00740.

PhosphoSite

P00740.

Proteomic databases

PeptideAtlas

P00740.

PRIDE

P00740.

Genome annotation databases

Ensembl

ENSG00000101981. Homo sapiens. [Contig view]

GeneID

2158.

KEGG

hsa:2158.

NMPDR

fig|9606.3.peg.33470.

Organism-specific databases

GeneCards

GC0XP138440.

H-InvDB

HIX0056112.

HGNC

HGNC:3551. F9.

HPA

HPA000254.

MIM

300746. gene.
306900. phenotype.

Orphanet

448. Hemophilia.
98879. Hemophilia B.

PharmGKB

PA24978.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P00740.

HOVERGEN

P00740.

OMA

P00740. RPKRYNS.

Enzyme and pathway databases

BRENDA

3.4.21.22. 247.

Reactome

REACT_1069. Post-translational protein modification.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P00740.

Bgee

P00740.

CleanEx

HS_F9.

GermOnline

ENSG00000101981. Homo sapiens.

Family and domain databases

InterPro

IPR002383. Coagulation_factor_Gla.
IPR006209. EGF.
IPR006210. EGF-like.
IPR013032. EGF-like_reg_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_CS.
IPR001438. EGF_2.
IPR000742. EGF_3.
IPR001881. EGF_Ca_bd.
IPR018097. EGF_Ca_bd_CS.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]

Pfam

PF00008. EGF. 2 hits.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]

PIRSF

PIRSF001143. Factor_X. 1 hit.

PRINTS

PR00722. CHYMOTRYPSIN.
PR00010. EGFBLOOD.
PR00001. GLABLOOD.

SMART

SM00181. EGF. 1 hit.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]

PROSITE

PS00010. ASX_HYDROXYL. 1 hit.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 1 hit.
PS01187. EGF_CA. 1 hit.
PS00011. GLA_1. 1 hit.
PS50998. GLA_2. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

BindingDB

P00740.

DrugBank

DB00025. Antihemophilic Factor.
DB00100. Coagulation Factor IX.
DB01109. Heparin.
DB00170. Menadione.

NextBio

8719.

PMAP-CutDB

P00740.

SOURCE

Search...

Entry information

Entry name

FA9_HUMAN

Accession

Primary (citable) accession number: P00740
Secondary accession number(s): Q5JYJ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	June 7, 2005
Last modified:	June 16, 2009
This is version 149 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)