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P00740 (FA9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 202. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Coagulation factor IX

EC=3.4.21.22
Alternative name(s):
Christmas factor
Plasma thromboplastin component
Short name=PTC
Gene names
Name:F9
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length461 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.13 Ref.15 Ref.36 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.62 Ref.64 Ref.65 Ref.66 Ref.67 Ref.68 Ref.69 Ref.72 Ref.73 Ref.74

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.75

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 processBlood coagulation
Hemostasis
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Hemophilia
Thrombophilia
   DomainEGF-like domain
Repeat
Signal
   LigandCalcium
   Molecular functionHydrolase
Protease
Serine protease
   PTMCleavage on pair of basic residues
Disulfide bond
Gamma-carboxyglutamic acid
Glycoprotein
Hydroxylation
Phosphoprotein
Sulfation
Zymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Pharmaceutical
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Traceable author statement. Source: Reactome

blood coagulation, extrinsic pathway

Traceable author statement. Source: Reactome

blood coagulation, intrinsic pathway

Traceable author statement. Source: Reactome

cellular protein metabolic process

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_componentGolgi 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_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

serine-type endopeptidase activity

Traceable author statement Ref.50. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P00740-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P00740-2)

The sequence of this isoform differs from the canonical sequence as follows:
     93-130: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Propeptide29 – 4618
PRO_0000027755
Chain47 – 461415Coagulation factor IX
PRO_0000027756
Chain47 – 191145Coagulation factor IXa light chain
PRO_0000027757
Propeptide192 – 22635Activation peptide
PRO_0000027758
Chain227 – 461235Coagulation factor IXa heavy chain
PRO_0000027759

Regions

Domain47 – 9246Gla
Domain93 – 12937EGF-like 1; calcium-binding Potential
Domain130 – 17142EGF-like 2
Domain227 – 459233Peptidase S1

Sites

Active site2671Charge relay system Ref.19
Active site3151Charge relay system Ref.19
Active site4111Charge relay system Ref.19
Site191 – 1922Cleavage; by factor XIa
Site226 – 2272Cleavage; by factor XIa

Amino acid modifications

Modified residue5314-carboxyglutamate
Modified residue5414-carboxyglutamate
Modified residue6114-carboxyglutamate
Modified residue6314-carboxyglutamate
Modified residue6614-carboxyglutamate
Modified residue6714-carboxyglutamate
Modified residue7214-carboxyglutamate
Modified residue7314-carboxyglutamate
Modified residue7614-carboxyglutamate
Modified residue7914-carboxyglutamate
Modified residue8214-carboxyglutamate
Modified residue8614-carboxyglutamate
Modified residue1101(3R)-3-hydroxyaspartate
Modified residue1141Phosphoserine Ref.26
Modified residue2011Sulfotyrosine
Modified residue2041Phosphoserine
Glycosylation991O-linked (Glc...)
CAR_000009
Glycosylation1071O-linked (Fuc...)
CAR_000010
Glycosylation2031N-linked (GlcNAc...)
Glycosylation2051O-linked (GalNAc...) Ref.25
Glycosylation2131N-linked (GlcNAc...)
Glycosylation2151O-linked (GalNAc...) Ref.25
Disulfide bond64 ↔ 69
Disulfide bond97 ↔ 108
Disulfide bond102 ↔ 117
Disulfide bond119 ↔ 128
Disulfide bond134 ↔ 145
Disulfide bond141 ↔ 155
Disulfide bond157 ↔ 170
Disulfide bond178 ↔ 335
Disulfide bond252 ↔ 268
Disulfide bond382 ↔ 396
Disulfide bond407 ↔ 435

Natural variations

Alternative sequence93 – 13038Missing in isoform 2.
VSP_047689
Natural variant71I → F. Ref.46
Corresponds to variant rs150190385 [ dbSNP | Ensembl ].
VAR_006520
Natural variant171I → N in HEMB; severe; UK 22.
VAR_006521
Natural variant281C → R in HEMB; moderate; HB130.
VAR_006522
Natural variant281C → Y in HEMB. Ref.73
VAR_017343
Natural variant301V → I in HEMB.
VAR_006523
Natural variant371A → T in warfarin sensitivity; reduced affinity of the glutamate carboxylase for the factor IX precursor. Ref.63
VAR_017307
Natural variant431R → L in HEMB; severe; Bendorf, Beuten, Gleiwitz, etc.. Ref.73
VAR_006525
Natural variant431R → Q in HEMB; severe; San Dimas, Oxford-3, Strasbourg-2, etc.. Ref.13 Ref.40 Ref.49 Ref.67 Ref.73
VAR_006524
Natural variant431R → W in HEMB; severe; Boxtel, Heiden, Lienen, etc.. Ref.67 Ref.74
VAR_006526
Natural variant451K → N in HEMB; severe; Seattle E.
VAR_006527
Natural variant461R → S in HEMB; severe; Cambridge.
VAR_006528
Natural variant461R → T in HEMB; severe. Ref.67
VAR_006529
Natural variant481N → I in HEMB; severe; Calgary-16.
VAR_006530
Natural variant491S → P in HEMB.
VAR_006531
Natural variant521L → S in HEMB; severe; Gla mutant. Ref.73
VAR_017344
Natural variant531E → A in HEMB; severe; Oxford-B2; Gla mutant.
VAR_006532
Natural variant541E → G in HEMB; severe; HB151; Gla mutant.
VAR_006533
Natural variant551F → C in HEMB.
VAR_006534
Natural variant581G → A in HEMB; severe; Hong Kong-1.
VAR_006535
Natural variant581G → R in HEMB; severe; Los Angeles-4.
VAR_006536
Natural variant62 – 632Missing in HEMB; severe.
VAR_006537
Natural variant661E → V in HEMB; moderate.
VAR_006538
Natural variant671E → K in HEMB; severe; Nagoya-4; Gla mutant.
VAR_006539
Natural variant711F → S in HEMB; severe.
VAR_006540
Natural variant731E → K in HEMB; severe; Seattle-3; Gla mutant. Ref.50
VAR_006541
Natural variant731E → V in HEMB; severe; Chongqing; Gla mutant. Ref.51
VAR_006542
Natural variant751R → Q in HEMB; mild. Ref.46
VAR_017308
Natural variant791E → D in HEMB. Ref.46
VAR_017309
Natural variant841T → R in HEMB. Ref.74
VAR_017345
Natural variant911Y → C in HEMB; moderate.
VAR_006543
Natural variant931D → G in HEMB; moderate; Alabama. Ref.41
VAR_006544
Natural variant961Q → P in HEMB; severe; New London.
VAR_006545
Natural variant971C → S in HEMB.
VAR_006546
Natural variant1011P → R in HEMB.
VAR_006547
Natural variant1021C → R in HEMB; severe; Basel.
VAR_006548
Natural variant1061G → D in HEMB. Ref.73
VAR_017346
Natural variant1061G → S in HEMB; mild; Durham. Ref.50 Ref.67
VAR_006549
Natural variant1081C → S in HEMB.
VAR_006550
Natural variant1101D → N in HEMB; severe; Oxford-D1.
VAR_006551
Natural variant1121I → S in HEMB.
VAR_006552
Natural variant1131N → K in HEMB; mild. Ref.64
VAR_006553
Natural variant1151Y → C in HEMB; severe. Ref.67
VAR_006554
Natural variant1191C → F in HEMB; severe.
VAR_006555
Natural variant1191C → R in HEMB; Iran. Ref.66
VAR_006556
Natural variant1241E → K in HEMB. Ref.73
VAR_017347
Natural variant1251G → E in HEMB.
VAR_006557
Natural variant1251G → R in HEMB. Ref.74
VAR_017348
Natural variant1251G → V in HEMB. Ref.74
VAR_006558
Natural variant129 – 1302Missing in HEMB.
VAR_006559
Natural variant1341C → Y in HEMB. Ref.73
VAR_017349
Natural variant1361I → T in HEMB; mild.
VAR_006560
Natural variant1391G → D in HEMB; severe.
VAR_006561
Natural variant1391G → S in HEMB.
VAR_006562
Natural variant1551C → F in HEMB; severe. Ref.67
VAR_006563
Natural variant1601G → E in HEMB; mild.
VAR_006564
Natural variant1671Q → H in HEMB; mild.
VAR_006565
Natural variant1691S → C in HEMB. Ref.72
VAR_017350
Natural variant1701C → F in HEMB. Ref.74
VAR_017351
Natural variant1781C → R in HEMB.
VAR_006566
Natural variant1781C → W in HEMB; severe.
VAR_006567
Natural variant1911R → C in HEMB; moderate; Albuquerque, Cardiff-1, etc.. Ref.47
VAR_006569
Natural variant1911R → H in HEMB; moderate; Chapel-Hill, Chicago-2, etc.. Ref.39 Ref.59
VAR_006568
Natural variant1941T → A. Ref.3 Ref.4 Ref.5 Ref.70
Corresponds to variant rs6048 [ dbSNP | Ensembl ].
VAR_011773
Natural variant2261R → G in HEMB; severe; Madrid. Ref.59 Ref.73
VAR_006571
Natural variant2261R → Q in HEMB; severe; Hilo and Novara. Ref.44 Ref.53 Ref.73
VAR_006572
Natural variant2261R → W in HEMB; severe; Nagoya-1, Dernbach, Deventer, Idaho, etc.. Ref.15 Ref.53 Ref.73
VAR_006570
Natural variant2271V → D in HEMB; mild.
VAR_006573
Natural variant2271V → F in HEMB; Milano. Ref.53
VAR_017310
Natural variant2281V → F in HEMB; severe; Kashihara. Ref.48
VAR_017311
Natural variant2281V → L in HEMB; mild; Cardiff-2. Ref.52
VAR_006574
Natural variant2411Q → H in HEMB.
VAR_006575
Natural variant2411Q → K in HEMB. Ref.73
VAR_017352
Natural variant2521C → S in HEMB; severe. Ref.57
VAR_017312
Natural variant2521C → Y in HEMB. Ref.73
VAR_017353
Natural variant2531G → E in HEMB; severe.
VAR_006576
Natural variant2531G → R in HEMB; severe; Luanda. Ref.58
VAR_006577
Natural variant2651A → T in HEMB; mild.
VAR_006578
Natural variant2681C → W in HEMB; moderate. Ref.46
VAR_017313
Natural variant2791A → T in HEMB; mild. Ref.46 Ref.59
VAR_006579
Natural variant2831N → D in HEMB; severe.
VAR_006580
Natural variant2861Missing in HEMB; severe.
VAR_006581
Natural variant2911E → V in HEMB; Monschau. Ref.56
VAR_017314
Natural variant2941R → G in HEMB; severe.
VAR_006582
Natural variant2941R → Q in HEMB; mild to moderate; Dreihacken, Penafiel and Seattle-4. Ref.50 Ref.56 Ref.58 Ref.61 Ref.73
VAR_006583
Natural variant3021H → R in HEMB. Ref.74
VAR_006584
Natural variant3061N → S in HEMB; mild. Ref.46
VAR_017315
Natural variant3161I → F in HEMB. Ref.73
VAR_006585
Natural variant3181L → R in HEMB. Ref.73
VAR_017354
Natural variant3211L → Q in HEMB; severe.
VAR_006586
Natural variant3331P → H in HEMB; severe.
VAR_006587
Natural variant3331P → T in HEMB. Ref.72
VAR_017355
Natural variant3421T → K in HEMB; mild.
VAR_006588
Natural variant3421T → M in HEMB; moderate. Ref.46 Ref.64 Ref.74
VAR_006589
Natural variant3441I → L in HEMB. Ref.74
VAR_017356
Natural variant3511G → D in HEMB.
VAR_006590
Natural variant3561W → C in HEMB; severe.
VAR_006591
Natural variant3571G → E in HEMB; severe; Amagasaki. Ref.54
VAR_006592
Natural variant3571G → R in HEMB. Ref.46
VAR_017316
Natural variant3621K → E in HEMB; moderate.
VAR_006593
Natural variant3631G → W in HEMB.
VAR_006594
Natural variant3661A → D in HEMB.
VAR_006595
Natural variant3791R → G in HEMB; moderate. Ref.73
VAR_006596
Natural variant3791R → Q in HEMB; severe; Iceland-1, London and Sesimbra. Ref.58 Ref.59 Ref.67
VAR_006597
Natural variant3821C → Y in HEMB.
VAR_006598
Natural variant3831L → F in HEMB. Ref.73
VAR_017358
Natural variant3831L → I in HEMB. Ref.73
VAR_017357
Natural variant3841R → L in THPH8; factor IX Padua; higher specific activity than wild-type. Ref.75
VAR_062999
Natural variant3871K → E in HEMB; mild. Ref.67
VAR_006599
Natural variant3901I → F in HEMB; severe.
VAR_006600
Natural variant3941M → K in HEMB.
VAR_006601
Natural variant3951F → I in HEMB. Ref.73
VAR_017359
Natural variant3951F → L in HEMB. Ref.74
VAR_017360
Natural variant3961C → F in HEMB. Ref.73
VAR_017361
Natural variant3961C → S in HEMB; severe.
VAR_006602
Natural variant3971A → P in HEMB; mild; Hong Kong-11. Ref.65
VAR_017317
Natural variant4041R → T in HEMB.
VAR_006603
Natural variant4071C → R in HEMB. Ref.73
VAR_017362
Natural variant4071C → S in HEMB; severe.
VAR_006604
Natural variant4101D → H in HEMB; Mechtal. Ref.56
VAR_017318
Natural variant4111S → G in HEMB; Varel. Ref.56
VAR_017320
Natural variant4111S → I in HEMB; Schmallenberg. Ref.56
VAR_017319
Natural variant4121G → E in HEMB. Ref.73
VAR_017363
Natural variant4131G → R in HEMB; moderate to severe. Ref.61 Ref.64
VAR_006605
Natural variant4141P → T in HEMB; Bergamo. Ref.53 Ref.74
VAR_017321
Natural variant4191V → E in HEMB; moderately severe. Ref.59 Ref.60
VAR_006606
Natural variant4241F → V in HEMB. Ref.64
VAR_006607
Natural variant4261T → P in HEMB; severe; Barcelos. Ref.58
VAR_006608
Natural variant4301S → T in HEMB.
VAR_006609
Natural variant4311W → G in HEMB.
VAR_006610
Natural variant4311W → R in HEMB; moderate.
VAR_006611
Natural variant4321G → S in HEMB; severe.
VAR_006612
Natural variant4321G → V in HEMB; severe. Ref.67
VAR_006613
Natural variant4331E → A in HEMB.
VAR_006614
Natural variant4331E → K in HEMB.
VAR_006615
Natural variant4351C → Y in HEMB. Ref.74
VAR_017364
Natural variant4361A → V in HEMB; moderately severe; Niigata. Ref.43
VAR_006616
Natural variant4421G → E in HEMB. Ref.74
VAR_017365
Natural variant4421G → R in HEMB; severe; Angers. Ref.45
VAR_017322
Natural variant4431I → T in HEMB; moderately severe; Long Beach, Los Angeles and Vancouver. Ref.42 Ref.55
VAR_017323
Natural variant4451T → TIYT in HEMB; severe; Lousada.
VAR_006617
Natural variant4491R → Q in HEMB; mild. Ref.59
VAR_006618
Natural variant4491R → W in HEMB; mild. Ref.74
VAR_006619
Natural variant4501Y → C in HEMB; severe. Ref.67
VAR_006620
Natural variant4531W → R in HEMB. Ref.46
VAR_017324
Natural variant4541I → T in HEMB; Italy. Ref.66
VAR_006621
Natural variant4611T → P. Ref.7
Corresponds to variant rs4149751 [ dbSNP | Ensembl ].
VAR_014308

Secondary structure

.............................................................................. 461
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 7, 2005. Version 2.
Checksum: C4720C1234477EF5

FASTA46151,778
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 2556B3F27FB23A77
Show »

FASTA42347,618

References

« Hide '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] (ISOFORM 1).
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] (ISOFORM 1).
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] (ISOFORM 1), VARIANT ALA-194.
[6]"Alternative splicing variant of Homo sapiens coagulation factor IX lacking EGF like domain."
Sata S., Yonemitsu Y., Nakagawa K., Sueishi K.
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
Tissue: Liver.
[7]SeattleSNPs variation discovery resource
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PRO-461.
[8]"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] (ISOFORM 1).
Tissue: Liver.
[9]"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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Liver.
[10]"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. expand/collapse author list , 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].
[11]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. expand/collapse author list , 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].
[12]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[13]"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.
[14]"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 (ISOFORM 1).
Tissue: Liver.
[15]"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.
[16]"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.
[17]"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.
[18]"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.
[19]"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.
[20]"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.
[21]Erratum
Morita T., Isaacs B.S., Esmon C.T., Johnson A.E.
J. Biol. Chem. 260:2583-2583(1985)
[22]"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.
[23]"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.
[24]"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.
[25]"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.
[26]"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.
[27]"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.
[28]"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.
[29]"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.
[30]"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.
[31]"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.
[32]"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.
[33]"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.
[34]"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.
[35]"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.
[36]"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.
[37]"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.
[38]"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.
[39]"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.
[40]"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.
[41]"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.
[42]"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.
[43]"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.
[44]"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.
[45]"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.
[46]"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.
[47]"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.
[48]"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.
[49]"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.
[50]"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.
[51]"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.
[52]"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.
[53]"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.
[54]"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.
[55]"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.
[56]"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.
[57]"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.
[58]"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.
[59]"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.
[60]"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.
[61]"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.
[62]"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.
[63]"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.
[64]"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.
[65]"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.
[66]"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.
[67]"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.
[68]"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.
[69]"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.
[70]"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.
[71]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)
[72]"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.
[73]"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.
[74]"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.
[75]"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 expand/collapse EMBL AC list , 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.
AB186358 mRNA. Translation: BAD89383.1.
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.
PIRKFHU. A00922.
RefSeqNP_000124.1. NM_000133.3.
UniGeneHs.522798.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CFHNMR-A47-93[»]
1CFINMR-A47-93[»]
1EDMX-ray1.50B/C92-130[»]
1IXANMR-A92-130[»]
1MGXNMR-A47-93[»]
1NL0X-ray2.20G47-91[»]
1RFNX-ray2.80A227-461[»]
B133-188[»]
2WPHX-ray1.50E133-191[»]
S227-461[»]
2WPIX-ray1.99E133-191[»]
S227-461[»]
2WPJX-ray1.60E133-191[»]
S227-461[»]
2WPKX-ray2.21E133-191[»]
S227-461[»]
2WPLX-ray1.82E133-191[»]
S227-461[»]
2WPMX-ray2.00E133-191[»]
S227-461[»]
3KCGX-ray1.70H227-461[»]
L131-188[»]
3LC3X-ray1.90A/C227-461[»]
B/D133-188[»]
3LC5X-ray2.62A227-461[»]
B133-188[»]
ProteinModelPortalP00740.
SMRP00740. Positions 47-191, 227-461.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108456. 1 interaction.
DIPDIP-58520N.
STRING9606.ENSP00000218099.

Chemistry

BindingDBP00740.
ChEMBLCHEMBL2016.
DrugBankDB00025. Antihemophilic Factor.
DB00100. Coagulation Factor IX.
DB01109. Heparin.
DB00170. Menadione.
GuidetoPHARMACOLOGY2364.

Protein family/group databases

Allergome9616. Hom s Factor IX.
MEROPSS01.214.

PTM databases

PhosphoSiteP00740.
UniCarbKBP00740.

Proteomic databases

PaxDbP00740.
PeptideAtlasP00740.
PRIDEP00740.

Protocols and materials databases

DNASU2158.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000218099; ENSP00000218099; ENSG00000101981. [P00740-1]
ENST00000394090; ENSP00000377650; ENSG00000101981. [P00740-2]
GeneID2158.
KEGGhsa:2158.
UCSCuc004fas.1. human. [P00740-1]

Organism-specific databases

CTD2158.
GeneCardsGC0XP138612.
HGNCHGNC:3551. F9.
MIM300746. gene.
300807. phenotype.
306900. phenotype.
neXtProtNX_P00740.
Orphanet169799. Mild hemophilia B.
169796. Moderately severe hemophilia B.
169793. Severe hemophilia B.
177929. Symptomatic form of hemophilia B in female carriers.
PharmGKBPA27954.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5640.
HOGENOMHOG000251821.
HOVERGENHBG013304.
InParanoidP00740.
KOK01321.
OMASAECTVF.
OrthoDBEOG75B84T.
PhylomeDBP00740.
TreeFamTF327329.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
REACT_604. Hemostasis.
SABIO-RKP00740.

Gene expression databases

ArrayExpressP00740.
BgeeP00740.
CleanExHS_F9.
GenevestigatorP00740.

Family and domain databases

Gene3D4.10.740.10. 1 hit.
InterProIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
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]
PfamPF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFPIRSF001143. Factor_X. 1 hit.
PRINTSPR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
SMARTSM00181. EGF. 1 hit.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
SSF57630. SSF57630. 1 hit.
PROSITEPS00010. 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]
ProtoNetSearch...

Other

EvolutionaryTraceP00740.
GeneWikiFactor_IX.
GenomeRNAi2158.
NextBio8719.
PMAP-CutDBP00740.
PROP00740.
SOURCESearch...

Entry information

Entry nameFA9_HUMAN
AccessionPrimary (citable) accession number: P00740
Secondary accession number(s): A8K9N4 expand/collapse secondary AC list , F2RM36, Q5FBE1, Q5JYJ8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 7, 2005
Last modified: April 16, 2014
This is version 202 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM