P00740 (FA9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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. Coagulation factor IXa light chain
2. Coagulation factor IXa heavy chain

Gene names

Name:

F9

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	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	Hemophilia B (HEMB) [MIM:306900]: An X-linked blood coagulation disorder characterized by a permanent tendency to hemorrhage, due to factor IX deficiency. It is phenotypically similar to hemophilia A, but patients present with fewer symptoms. Many patients are asymptomatic until the hemostatic system is stressed by surgery or trauma. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12 Ref.14 Ref.35 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42 Ref.43 Ref.44 Ref.45 Ref.46 Ref.47 Ref.48 Ref.49 Ref.50 Ref.51 Ref.52 Ref.53 Ref.54 Ref.55 Ref.56 Ref.57 Ref.58 Ref.59 Ref.60 Ref.61 Ref.63 Ref.64 Ref.65 Ref.66 Ref.67 Ref.68 Ref.71 Ref.72 Ref.73 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. Thrombophilia, X-linked, due to factor IX defect (THPH8) [MIM:300807]: A hemostatic disorder characterized by a tendency to thrombosis. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.74
Pharmaceutical use	Available under the name 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 Hemostasis
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Disease	Disease mutation Hemophilia Thrombophilia
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 Complete proteome Direct protein sequencing Pharmaceutical Reference proteome
Gene Ontology (GO)
Biological_process	blood coagulation, extrinsic pathway Traceable author statement. Source: Reactome blood coagulation, intrinsic pathway Traceable author statement. Source: Reactome peptidyl-glutamic acid carboxylation Traceable author statement. Source: Reactome post-translational protein modification Traceable author statement. Source: Reactome proteolysis Traceable author statement. Source: Reactome
Cellular_component	Golgi lumen Traceable author statement. Source: Reactome endoplasmic reticulum lumen Traceable author statement. Source: Reactome extracellular region Non-traceable author statement PubMed 14718574. Source: UniProtKB plasma membrane Traceable author statement. Source: Reactome
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro serine-type endopeptidase activity Traceable author statement Ref.49. 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

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.18

Active site

315

1

Charge relay system Ref.18

Active site

411

1

Charge relay system Ref.18

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.25

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.24

Glycosylation

213

1

N-linked (GlcNAc...)

Glycosylation

215

1

O-linked (GalNAc...) Ref.24

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.45

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.

VAR_006522

Natural variant

28

1

C → Y in HEMB. Ref.72

VAR_017343

Natural variant

30

1

V → I in HEMB.

VAR_006523

Natural variant

37

1

A → T in warfarin sensitivity; reduced affinity of the glutamate carboxylase for the factor IX precursor. Ref.62

VAR_017307

Natural variant

43

1

R → L in HEMB; severe; Bendorf, Beuten, Gleiwitz, etc.. Ref.72

VAR_006525

Natural variant

43

1

R → Q in HEMB; severe; San Dimas, Oxford-3, Strasbourg-2, etc.. Ref.12 Ref.39 Ref.48 Ref.66 Ref.72

VAR_006524

Natural variant

43

1

R → W in HEMB; severe; Boxtel, Heiden, Lienen, etc.. Ref.66 Ref.73

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.

VAR_006528

Natural variant

46

1

R → T in HEMB; severe. Ref.66

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.72

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.49

VAR_006541

Natural variant

73

1

E → V in HEMB; severe; Chongqing; Gla mutant. Ref.50

VAR_006542

Natural variant

75

1

R → Q in HEMB; mild. Ref.45

VAR_017308

Natural variant

79

1

E → D in HEMB. Ref.45

VAR_017309

Natural variant

84

1

T → R in HEMB. Ref.73

VAR_017345

Natural variant

91

1

Y → C in HEMB; moderate.

VAR_006543

Natural variant

93

1

D → G in HEMB; moderate; Alabama. Ref.40

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.72

VAR_017346

Natural variant

106

1

G → S in HEMB; mild; Durham. Ref.49 Ref.66

VAR_006549

Natural variant

108

1

C → S in HEMB.

VAR_006550

Natural variant

110

1

D → N in HEMB; severe; Oxford-D1.

VAR_006551

Natural variant

112

1

I → S in HEMB.

VAR_006552

Natural variant

113

1

N → K in HEMB; mild. Ref.63

VAR_006553

Natural variant

115

1

Y → C in HEMB; severe. Ref.66

VAR_006554

Natural variant

119

1

C → F in HEMB; severe.

VAR_006555

Natural variant

119

1

C → R in HEMB; Iran. Ref.65

VAR_006556

Natural variant

124

1

E → K in HEMB. Ref.72

VAR_017347

Natural variant

125

1

G → E in HEMB.

VAR_006557

Natural variant

125

1

G → R in HEMB. Ref.73

VAR_017348

Natural variant

125

1

G → V in HEMB. Ref.73

VAR_006558

Natural variant

129 – 130

2

Missing in HEMB.

VAR_006559

Natural variant

134

1

C → Y in HEMB. Ref.72

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.66

VAR_006563

Natural variant

160

1

G → E in HEMB; mild.

VAR_006564

Natural variant

167

1

Q → H in HEMB; mild.

VAR_006565

Natural variant

169

1

S → C in HEMB. Ref.71

VAR_017350

Natural variant

170

1

C → F in HEMB. Ref.73

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.46

VAR_006569

Natural variant

191

1

R → H in HEMB; moderate; Chapel-Hill, Chicago-2, etc.. Ref.38 Ref.58

VAR_006568

Natural variant

194

1

T → A. Ref.3 Ref.4 Ref.5 Ref.69
Corresponds to variant rs6048 [ dbSNP | Ensembl ].

VAR_011773

Natural variant

226

1

R → G in HEMB; severe; Madrid. Ref.58 Ref.72

VAR_006571

Natural variant

226

1

R → Q in HEMB; severe; Hilo and Novara. Ref.43 Ref.52 Ref.72

VAR_006572

Natural variant

226

1

R → W in HEMB; severe; Nagoya-1, Dernbach, Deventer, Idaho, etc.. Ref.14 Ref.52 Ref.72

VAR_006570

Natural variant

227

1

V → D in HEMB; mild.

VAR_006573

Natural variant

227

1

V → F in HEMB; Milano. Ref.52

VAR_017310

Natural variant

228

1

V → F in HEMB; severe; Kashihara. Ref.47

VAR_017311

Natural variant

228

1

V → L in HEMB; mild; Cardiff-2. Ref.51

VAR_006574

Natural variant

241

1

Q → H in HEMB.

VAR_006575

Natural variant

241

1

Q → K in HEMB. Ref.72

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.56

VAR_017312

Natural variant

252

1

C → Y in HEMB. Ref.72

VAR_017353

Natural variant

253

1

G → E in HEMB; severe.

VAR_006576

Natural variant

253

1

G → R in HEMB; severe; Luanda. Ref.57

VAR_006577

Natural variant

265

1

A → T in HEMB; mild.

VAR_006578

Natural variant

268

1

C → W in HEMB; moderate. Ref.45

VAR_017313

Natural variant

279

1

A → T in HEMB; mild. Ref.45 Ref.58

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.55

VAR_017314

Natural variant

294

1

R → G in HEMB; severe.

VAR_006582

Natural variant

294

1

R → Q in HEMB; mild to moderate; Dreihacken, Penafiel and Seattle-4. Ref.49 Ref.55 Ref.57 Ref.60 Ref.72

VAR_006583

Natural variant

302

1

H → R in HEMB. Ref.73

VAR_006584

Natural variant

306

1

N → S in HEMB; mild. Ref.45

VAR_017315

Natural variant

316

1

I → F in HEMB. Ref.72

VAR_006585

Natural variant

318

1

L → R in HEMB. Ref.72

VAR_017354

Natural variant

321

1

L → Q in HEMB; severe.

VAR_006586

Natural variant

333

1

P → H in HEMB; severe.

VAR_006587

Natural variant

333

1

P → T in HEMB. Ref.71

VAR_017355

Natural variant

342

1

T → K in HEMB; mild.

VAR_006588

Natural variant

342

1

T → M in HEMB; moderate. Ref.45 Ref.63 Ref.73

VAR_006589

Natural variant

344

1

I → L in HEMB. Ref.73

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.53

VAR_006592

Natural variant

357

1

G → R in HEMB. Ref.45

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.72

VAR_006596

Natural variant

379

1

R → Q in HEMB; severe; Iceland-1, London and Sesimbra. Ref.57 Ref.58 Ref.66

VAR_006597

Natural variant

382

1

C → Y in HEMB.

VAR_006598

Natural variant

383

1

L → F in HEMB. Ref.72

VAR_017358

Natural variant

383

1

L → I in HEMB. Ref.72

VAR_017357

Natural variant

384

1

R → L in THPH8; factor IX Padua; higher specific activity than wild-type. Ref.74

VAR_062999

Natural variant

387

1

K → E in HEMB; mild. Ref.66

VAR_006599

Natural variant

390

1

I → F in HEMB; severe.

VAR_006600

Natural variant

394

1

M → K in HEMB.

VAR_006601

Natural variant

395

1

F → I in HEMB. Ref.72

VAR_017359

Natural variant

395

1

F → L in HEMB. Ref.73

VAR_017360

Natural variant

396

1

C → F in HEMB. Ref.72

VAR_017361

Natural variant

396

1

C → S in HEMB; severe.

VAR_006602

Natural variant

397

1

A → P in HEMB; mild; Hong Kong-11. Ref.64

VAR_017317

Natural variant

404

1

R → T in HEMB.

VAR_006603

Natural variant

407

1

C → R in HEMB. Ref.72

VAR_017362

Natural variant

407

1

C → S in HEMB; severe.

VAR_006604

Natural variant

410

1

D → H in HEMB; Mechtal. Ref.55

VAR_017318

Natural variant

411

1

S → G in HEMB; Varel. Ref.55

VAR_017320

Natural variant

411

1

S → I in HEMB; Schmallenberg. Ref.55

VAR_017319

Natural variant

412

1

G → E in HEMB. Ref.72

VAR_017363

Natural variant

413

1

G → R in HEMB; moderate to severe. Ref.60 Ref.63

VAR_006605

Natural variant

414

1

P → T in HEMB; Bergamo. Ref.52 Ref.73

VAR_017321

Natural variant

419

1

V → E in HEMB; moderately severe. Ref.58 Ref.59

VAR_006606

Natural variant

424

1

F → V in HEMB. Ref.63

VAR_006607

Natural variant

426

1

T → P in HEMB; severe; Barcelos. Ref.57

VAR_006608

Natural variant

430

1

S → T in HEMB.

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.

VAR_006612

Natural variant

432

1

G → V in HEMB; severe. Ref.66

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.73

VAR_017364

Natural variant

436

1

A → V in HEMB; moderately severe; Niigata. Ref.42

VAR_006616

Natural variant

442

1

G → E in HEMB. Ref.73

VAR_017365

Natural variant

442

1

G → R in HEMB; severe; Angers. Ref.44

VAR_017322

Natural variant

443

1

I → T in HEMB; moderately severe; Long Beach, Los Angeles and Vancouver. Ref.41 Ref.54

VAR_017323

Natural variant

445

1

T → TIYT in HEMB; severe; Lousada.

VAR_006617

Natural variant

449

1

R → Q in HEMB; mild. Ref.58

VAR_006618

Natural variant

449

1

R → W in HEMB; mild. Ref.73

VAR_006619

Natural variant

450

1

Y → C in HEMB; severe. Ref.66

VAR_006620

Natural variant

453

1

W → R in HEMB. Ref.45

VAR_017324

Natural variant

454

1

I → T in HEMB; Italy. Ref.65

VAR_006621

Natural variant

461

1

T → P. Ref.6
Corresponds to variant rs4149751 [ dbSNP | Ensembl ].

VAR_014308

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

461

Helix Strand Turn

Details...

Beta strand

50 – 52

3

Helix

60 – 64

5

Beta strand

65 – 67

3

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

Turn

125 – 128

4

Sequences

	Sequence		Length	Mass (Da)
	P00740 [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

	« Hide 'large scale' referencesShow 'large scale' references »
[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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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]	"Homo sapiens coagulation factor IX (F9), mRNA." Nguyen D.T., Nguyen P.V., Nong H.V. Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[8]	"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]. Tissue: Liver.
[9]	"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].
[10]	Mural R.J., Istrail S., Sutton G.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].
[11]	"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].
[12]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 30-84, VARIANT HEMB GLN-43.
[13]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 36-326. Tissue: Liver.
[14]	"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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 47-461, VARIANT HEMB TRP-226.
[15]	"Genomic amplification with transcript sequencing." Stoflet E.S., Koeberl D.D., Sarkar G., Sommer S.S. Science 239:491-494(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 290-359.
[16]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 444-461.
[17]	"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] [Europe PMC] [Abstract] Cited for: HYDROXYLATION AT ASP-110.
[18]	"Activation of human factor IX (Christmas factor)." di Scipio R.G., Kurachi K., Davie E.W. J. Clin. Invest. 61:1528-1538(1978) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEOLYTIC PROCESSING, ACTIVE SITE.
[19]	"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] [Europe PMC] [Abstract] Cited for: CALCIUM-BINDING.
[20]	Erratum Morita T., Isaacs B.S., Esmon C.T., Johnson A.E. J. Biol. Chem. 260:2583-2583(1985)
[21]	"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] [Europe PMC] [Abstract] Cited for: STRUCTURE OF CARBOHYDRATE ON SER-99.
[22]	"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] [Europe PMC] [Abstract] Cited for: STRUCTURE OF CARBOHYDRATE ON SER-99.
[23]	"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] [Europe PMC] [Abstract] Cited for: STRUCTURE OF CARBOHYDRATE ON SER-107.
[24]	"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] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT THR-205 AND THR-215.
[25]	"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.
[26]	"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] [Europe PMC] [Abstract] Cited for: POST-TRANSLATIONAL MODIFICATIONS.
[27]	"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] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 47-93.
[28]	"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] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 47-93.
[29]	"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] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 47-93.
[30]	"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] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 47-93.
[31]	"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] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 91-133.
[32]	"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] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 92-130.
[33]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 92-130.
[34]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 133-461.
[35]	"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] [Europe PMC] [Abstract] Cited for: MOLECULAR PATHOLOGY OF HEMB B.
[36]	"Assessing the underlying pattern of human germline mutations: lessons from the factor IX gene." Sommer S.S. FASEB J. 6:2767-2774(1992) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON HEMB VARIANTS.
[37]	"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] [Europe PMC] [Abstract] Cited for: REVIEW ON HEMB VARIANTS.
[38]	"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] [Europe PMC] [Abstract] Cited for: VARIANT HEMB HIS-191.
[39]	"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] [Europe PMC] [Abstract] Cited for: VARIANT HEMB GLN-43.
[40]	"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] [Europe PMC] [Abstract] Cited for: VARIANT HEMB GLY-93.
[41]	"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] [Europe PMC] [Abstract] Cited for: VARIANT HEMB THR-443.
[42]	"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] [Europe PMC] [Abstract] Cited for: VARIANT HEMB VAL-436.
[43]	"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] [Europe PMC] [Abstract] Cited for: VARIANT HEMB GLN-226.
[44]	"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] [Europe PMC] [Abstract] Cited for: VARIANT HEMB ARG-442.
[45]	"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] [Europe PMC] [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.
[46]	"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] [Europe PMC] [Abstract] Cited for: VARIANT HEMB CYS-191.
[47]	"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] [Europe PMC] [Abstract] Cited for: VARIANT HEMB PHE-228.
[48]	"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] [Europe PMC] [Abstract] Cited for: VARIANT HEMB GLN-43.
[49]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS HEMB LYS-73; SER-106 AND GLN-294.
[50]	"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] [Europe PMC] [Abstract] Cited for: VARIANT HEMB VAL-73.
[51]	"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] [Europe PMC] [Abstract] Cited for: VARIANT HEMB LEU-228.
[52]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS HEMB GLN-226; TRP-226; PHE-227 AND THR-414.
[53]	"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] [Europe PMC] [Abstract] Cited for: VARIANT HEMB GLU-357.
[54]	"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] [Europe PMC] [Abstract] Cited for: VARIANT HEMB THR-443.
[55]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS HEMB VAL-291; GLN-294; HIS-410; GLY-411 AND ILE-411.
[56]	"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] [Europe PMC] [Abstract] Cited for: VARIANT HEMB SER-252.
[57]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS HEMB ARG-253; GLN-294; GLN-379; PRO-426 AND ILE-TYR-THR-445 INS.
[58]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS HEMB HIS-191; GLY-226; THR-279; GLN-379; GLU-419 AND GLN-449.
[59]	"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] [Europe PMC] [Abstract] Cited for: VARIANT HEMB GLU-419.
[60]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS HEMB GLN-294 AND ARG-413.
[61]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS HEMB.
[62]	"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] [Europe PMC] [Abstract] Cited for: VARIANT WARFARIN SENSITIVITY THR-37.
[63]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS HEMB LYS-113; MET-342; ARG-413 AND VAL-424.
[64]	"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] [Europe PMC] [Abstract] Cited for: VARIANT HEMB PRO-397.
[65]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS HEMB ARG-119 AND THR-454.
[66]	"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] [Europe PMC] [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.
[67]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS HEMB.
[68]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS HEMB.
[69]	"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] [Europe PMC] [Abstract] Cited for: VARIANT ALA-194.
[70]	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)
[71]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS HEMB CYS-169 AND THR-333.
[72]	"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] [Europe PMC] [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.
[73]	"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] [Europe PMC] [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.
[74]	"X-linked thrombophilia with a mutant factor IX (factor IX Padua)." Simioni P., Tormene D., Tognin G., Gavasso S., Bulato C., Iacobelli N.P., Finn J.D., Spiezia L., Radu C., Arruda V.R. N. Engl. J. Med. 361:1671-1675(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT THPH8 LEU-384, CHARACTERIZATION OF VARIANT THPH8 LEU-384.
+	Additional computationally mapped references.

Web resources

Wikipedia

Factor IX entry

Factor IX Mutation Database

GeneReviews

SeattleSNPs

BeneFix

Clinical information on BeneFix

Protein Spotlight

The Christmas Factor - Issue 41 of December 2003

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.
FR846239 mRNA. Translation: CCA61111.1.
AK292749 mRNA. Translation: BAF85438.1.
CH471150 Genomic DNA. Translation: EAW88433.1.
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. NM_000133.3.

UniGene

Hs.522798.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]
2WPH	X-ray	1.50	E	133-191	[»]
			S	227-461	[»]
2WPI	X-ray	1.99	E	133-191	[»]
			S	227-461	[»]
2WPJ	X-ray	1.60	E	133-191	[»]
			S	227-461	[»]
2WPK	X-ray	2.21	E	133-191	[»]
			S	227-461	[»]
2WPL	X-ray	1.82	E	133-191	[»]
			S	227-461	[»]
2WPM	X-ray	2.00	E	133-191	[»]
			S	227-461	[»]
3KCG	X-ray	1.70	H	227-461	[»]
			L	131-188	[»]
3LC3	X-ray	1.90	A/C	227-461	[»]
			B/D	133-188	[»]
3LC5	X-ray	2.62	A	227-461	[»]
			B	133-188	[»]

ProteinModelPortal

P00740.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-58520N.

STRING

9606.ENSP00000218099.

Protein family/group databases

Allergome

9616. Hom s Factor IX.

MEROPS

S01.214.

PTM databases

GlycoSuiteDB

P00740.

PhosphoSite

P00740.

Polymorphism databases

DMDM

67476446.

Proteomic databases

PaxDb

P00740.

PeptideAtlas

P00740.

PRIDE

P00740.

Protocols and materials databases

DNASU

2158.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000218099; ENSP00000218099; ENSG00000101981.

GeneID

2158.

KEGG

hsa:2158.

UCSC

uc004fas.1. human.

Organism-specific databases

CTD

2158.

GeneCards

GC0XP138612.

HGNC

HGNC:3551. F9.

HPA

HPA000254.

MIM

300746. gene.
300807. phenotype.
306900. phenotype.

neXtProt

NX_P00740.

Orphanet

169799. Mild hemophilia B.
169796. Moderately severe hemophilia B.
169793. Severe hemophilia B.
177929. Symptomatic form of hemophilia B in female carriers.

PharmGKB

PA27954.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5640.

HOGENOM

HOG000251821.

HOVERGEN

HBG013304.

InParanoid

P00740.

KO

K01321.

OMA

SAECTVF.

OrthoDB

EOG4THVTF.

PhylomeDB

P00740.

Enzyme and pathway databases

Reactome

REACT_17015. Metabolism of proteins.
REACT_604. Hemostasis.

SABIO-RK

P00740.

Gene expression databases

ArrayExpress

P00740.

Bgee

P00740.

CleanEx

HS_F9.

Genevestigator

P00740.

GermOnline

ENSG00000101981. Homo sapiens.

Family and domain databases

Gene3D

4.10.740.10. 1 hit.

InterPro

IPR017857. Coagulation_fac_subgr_Gla_dom.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]

Pfam

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

PIRSF

PIRSF001143. Factor_X. 1 hit.

PRINTS

PR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.

SMART

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

SUPFAM

SSF50494. Pept_Ser_Cys. 1 hit.
SSF57630. VitK_dep_GLA. 1 hit.

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

BindingDB

P00740.

ChEMBL

CHEMBL2016.

DrugBank

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

EvolutionaryTrace

P00740.

GenomeRNAi

2158.

NextBio

8719.

PMAP-CutDB

P00740.

SOURCE

Search...

Entry information

Entry name

FA9_HUMAN

Accession

Primary (citable) accession number: P00740
Secondary accession number(s): A8K9N4, F2RM36, Q5JYJ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	June 7, 2005
Last modified:	May 1, 2013
This is version 192 of the entry and version 2 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.