Details for: F9

Gene ID: 2158

Symbol: F9

Ensembl ID: ENSG00000101981

Description: coagulation factor IX

Associated with

Cells (max top 100)

(Marker Score score is uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

  • Cell Name: T cell (CL0000084)
    Fold Change: 2.33
    Marker Score: 4016
  • Cell Name: plasma cell (CL0000786)
    Fold Change: 1.96
    Marker Score: 2194
  • Cell Name: periportal region hepatocyte (CL0019026)
    Fold Change: 1.84
    Marker Score: 9867
  • Cell Name: hepatocyte (CL0000182)
    Fold Change: 1.7
    Marker Score: 1157.5
  • Cell Name: midzonal region hepatocyte (CL0019028)
    Fold Change: 1.68
    Marker Score: 7240
  • Cell Name: centrilobular region hepatocyte (CL0019029)
    Fold Change: 1.49
    Marker Score: 9562
  • Cell Name: hepatic stellate cell (CL0000632)
    Fold Change: 1.26
    Marker Score: 476
  • Cell Name: B cell (CL0000236)
    Fold Change: 1.16
    Marker Score: 1105
  • Cell Name: goblet cell (CL0000160)
    Fold Change: 1.16
    Marker Score: 7692
  • Cell Name: endothelial cell of pericentral hepatic sinusoid (CL0019022)
    Fold Change: 1.04
    Marker Score: 1115
  • Cell Name: absorptive cell (CL0000212)
    Fold Change: 0.98
    Marker Score: 30405
  • Cell Name: cholangiocyte (CL1000488)
    Fold Change: 0.97
    Marker Score: 364
  • Cell Name: intestinal crypt stem cell of colon (CL0009043)
    Fold Change: 0.95
    Marker Score: 2413
  • Cell Name: transit amplifying cell (CL0009010)
    Fold Change: 0.94
    Marker Score: 5350
  • Cell Name: abnormal cell (CL0001061)
    Fold Change: 0.92
    Marker Score: 2741
  • Cell Name: neoplastic cell (CL0001063)
    Fold Change: 0.87
    Marker Score: 5285
  • Cell Name: mast cell (CL0000097)
    Fold Change: 0.85
    Marker Score: 494
  • Cell Name: intestinal epithelial cell (CL0002563)
    Fold Change: 0.78
    Marker Score: 1268
  • Cell Name: brush cell (CL0002204)
    Fold Change: 0.78
    Marker Score: 712
  • Cell Name: myeloid cell (CL0000763)
    Fold Change: 0.7
    Marker Score: 1118
  • Cell Name: inflammatory macrophage (CL0000863)
    Fold Change: 0.69
    Marker Score: 214
  • Cell Name: pericyte (CL0000669)
    Fold Change: 0.67
    Marker Score: 391
  • Cell Name: intestinal enteroendocrine cell (CL1001516)
    Fold Change: 0.66
    Marker Score: 526
  • Cell Name: immature innate lymphoid cell (CL0001082)
    Fold Change: 0.6
    Marker Score: 1228
  • Cell Name: fibroblast (CL0000057)
    Fold Change: 0.57
    Marker Score: 552
  • Cell Name: kidney proximal convoluted tubule epithelial cell (CL1000838)
    Fold Change: 0.56
    Marker Score: 1158.5
  • Cell Name: cardiac endothelial cell (CL0010008)
    Fold Change: 0.55
    Marker Score: 1049
  • Cell Name: endothelial cell of periportal hepatic sinusoid (CL0019021)
    Fold Change: 0.43
    Marker Score: 117
  • Cell Name: endothelial cell (CL0000115)
    Fold Change: 0.4
    Marker Score: 361
  • Cell Name: Kupffer cell (CL0000091)
    Fold Change: 0.37
    Marker Score: 373
  • Cell Name: hepatoblast (CL0005026)
    Fold Change: 0.35
    Marker Score: 1155
  • Cell Name: lymphoid lineage restricted progenitor cell (CL0000838)
    Fold Change: 0.32
    Marker Score: 195
  • Cell Name: natural killer cell (CL0000623)
    Fold Change: 0.31
    Marker Score: 402
  • Cell Name: cardiac muscle myoblast (CL0000513)
    Fold Change: 0.31
    Marker Score: 4842
  • Cell Name: kidney distal convoluted tubule epithelial cell (CL1000849)
    Fold Change: 0.29
    Marker Score: 307
  • Cell Name: blood vessel endothelial cell (CL0000071)
    Fold Change: 0.27
    Marker Score: 272
  • Cell Name: stromal cell (CL0000499)
    Fold Change: 0.22
    Marker Score: 253
  • Cell Name: renal alpha-intercalated cell (CL0005011)
    Fold Change: 0.21
    Marker Score: 112
  • Cell Name: endothelial cell of hepatic sinusoid (CL1000398)
    Fold Change: 0.2
    Marker Score: 43
  • Cell Name: epithelial cell of alveolus of lung (CL0010003)
    Fold Change: 0.17
    Marker Score: 77
  • Cell Name: smooth muscle cell (CL0000192)
    Fold Change: 0.16
    Marker Score: 102
  • Cell Name: smooth muscle myoblast (CL0000514)
    Fold Change: 0.15
    Marker Score: 71
  • Cell Name: alpha-beta T cell (CL0000789)
    Fold Change: 0.14
    Marker Score: 105
  • Cell Name: kidney loop of Henle thin ascending limb epithelial cell (CL1001107)
    Fold Change: 0.13
    Marker Score: 136
  • Cell Name: kidney proximal straight tubule epithelial cell (CL1000839)
    Fold Change: 0.13
    Marker Score: 305
  • Cell Name: mature NK T cell (CL0000814)
    Fold Change: 0.13
    Marker Score: 59
  • Cell Name: neuronal receptor cell (CL0000006)
    Fold Change: 0.13
    Marker Score: 56
  • Cell Name: mononuclear cell (CL0000842)
    Fold Change: 0.12
    Marker Score: 39
  • Cell Name: renal principal cell (CL0005009)
    Fold Change: 0.12
    Marker Score: 93
  • Cell Name: skin fibroblast (CL0002620)
    Fold Change: 0.12
    Marker Score: 30
  • Cell Name: fibroblast of cardiac tissue (CL0002548)
    Fold Change: 0.11
    Marker Score: 652
  • Cell Name: kidney loop of Henle thick ascending limb epithelial cell (CL1001106)
    Fold Change: 0.11
    Marker Score: 284
  • Cell Name: renal beta-intercalated cell (CL0002201)
    Fold Change: 0.1
    Marker Score: 31
  • Cell Name: pigmented ciliary epithelial cell (CL0002303)
    Fold Change: 0.09
    Marker Score: 32
  • Cell Name: secretory cell (CL0000151)
    Fold Change: 0.09
    Marker Score: 171
  • Cell Name: Schwann cell (CL0002573)
    Fold Change: 0.09
    Marker Score: 31
  • Cell Name: mature microglial cell (CL0002629)
    Fold Change: 0.09
    Marker Score: 32
  • Cell Name: Bergmann glial cell (CL0000644)
    Fold Change: 0.08
    Marker Score: 32
  • Cell Name: connective tissue cell (CL0002320)
    Fold Change: 0.08
    Marker Score: 20
  • Cell Name: podocyte (CL0000653)
    Fold Change: 0.07
    Marker Score: 27
  • Cell Name: ciliated epithelial cell (CL0000067)
    Fold Change: 0.07
    Marker Score: 32
  • Cell Name: memory T cell (CL0000813)
    Fold Change: 0.07
    Marker Score: 30
  • Cell Name: parietal epithelial cell (CL1000452)
    Fold Change: 0.07
    Marker Score: 25
  • Cell Name: gamma-delta T cell (CL0000798)
    Fold Change: 0.07
    Marker Score: 46
  • Cell Name: macrophage (CL0000235)
    Fold Change: 0.07
    Marker Score: 76
  • Cell Name: central nervous system macrophage (CL0000878)
    Fold Change: 0.06
    Marker Score: 32
  • Cell Name: erythroid lineage cell (CL0000764)
    Fold Change: 0.06
    Marker Score: 31
  • Cell Name: endocrine cell (CL0000163)
    Fold Change: 0.06
    Marker Score: 32
  • Cell Name: vascular associated smooth muscle cell (CL0000359)
    Fold Change: 0.06
    Marker Score: 28
  • Cell Name: lymphocyte (CL0000542)
    Fold Change: 0.06
    Marker Score: 30
  • Cell Name: melanocyte (CL0000148)
    Fold Change: 0.06
    Marker Score: 24
  • Cell Name: CD8-positive, alpha-beta memory T cell (CL0000909)
    Fold Change: 0.06
    Marker Score: 50
  • Cell Name: innate lymphoid cell (CL0001065)
    Fold Change: 0.06
    Marker Score: 21
  • Cell Name: leukocyte (CL0000738)
    Fold Change: 0.06
    Marker Score: 32.5
  • Cell Name: erythrocyte (CL0000232)
    Fold Change: 0.06
    Marker Score: 31
  • Cell Name: luminal cell of prostate epithelium (CL0002340)
    Fold Change: 0.05
    Marker Score: 32
  • Cell Name: endothelial cell of lymphatic vessel (CL0002138)
    Fold Change: 0.05
    Marker Score: 33
  • Cell Name: neutrophil (CL0000775)
    Fold Change: 0.05
    Marker Score: 32
  • Cell Name: kidney capillary endothelial cell (CL1000892)
    Fold Change: 0.05
    Marker Score: 16
  • Cell Name: squamous epithelial cell (CL0000076)
    Fold Change: 0.05
    Marker Score: 33.5
  • Cell Name: mature astrocyte (CL0002627)
    Fold Change: 0.05
    Marker Score: 32
  • Cell Name: epithelial cell of proximal tubule (CL0002306)
    Fold Change: 0.05
    Marker Score: 172
  • Cell Name: skeletal muscle fibroblast (CL0011027)
    Fold Change: 0.05
    Marker Score: 31
  • Cell Name: acinar cell (CL0000622)
    Fold Change: 0.05
    Marker Score: 32
  • Cell Name: erythroblast (CL0000765)
    Fold Change: 0.04
    Marker Score: 27
  • Cell Name: epithelial cell (CL0000066)
    Fold Change: 0.04
    Marker Score: 58
  • Cell Name: oligodendrocyte (CL0000128)
    Fold Change: 0.03
    Marker Score: 80
  • Cell Name: retina horizontal cell (CL0000745)
    Fold Change: 0.03
    Marker Score: 32
  • Cell Name: enterocyte of epithelium of large intestine (CL0002071)
    Fold Change: 0.03
    Marker Score: 32
  • Cell Name: progenitor cell (CL0011026)
    Fold Change: 0.03
    Marker Score: 201
  • Cell Name: astrocyte (CL0000127)
    Fold Change: 0.03
    Marker Score: 26
  • Cell Name: erythroid progenitor cell (CL0000038)
    Fold Change: 0.03
    Marker Score: 31
  • Cell Name: kidney connecting tubule epithelial cell (CL1000768)
    Fold Change: 0.03
    Marker Score: 41
  • Cell Name: corneal epithelial cell (CL0000575)
    Fold Change: 0.03
    Marker Score: 32
  • Cell Name: kidney loop of Henle thin descending limb epithelial cell (CL1001111)
    Fold Change: 0.03
    Marker Score: 31
  • Cell Name: basal epithelial cell of prostatic duct (CL0002236)
    Fold Change: 0.03
    Marker Score: 24
  • Cell Name: mature B cell (CL0000785)
    Fold Change: 0.03
    Marker Score: 19
  • Cell Name: mucosal invariant T cell (CL0000940)
    Fold Change: 0.03
    Marker Score: 23
  • Cell Name: retinal ganglion cell (CL0000740)
    Fold Change: 0.03
    Marker Score: 32
  • Cell Name: neuron (CL0000540)
    Fold Change: 0.03
    Marker Score: 103

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Other Information

**Key characteristics**: - F9 is a glycoprotein that is synthesized as a pro-protein and then undergoes proteolytic cleavage to form the mature form. - It is a cofactor for factor VIII, which is essential for the formation of fibrin, a protein that is crucial for blood clot formation. - Mutations in the F9 gene can lead to the production of a defective protein that is unable to activate factor VIII, resulting in hemophilia b. **Pathways and functions**: - F9 is involved in the intrinsic pathway of blood clot formation, which is initiated by the activation of factor VIII. - It acts downstream of factor VIII, facilitating the conversion of prothrombin into thrombin. - Thrombin is essential for the subsequent steps of blood clot formation, including the conversion of fibrinogen into fibrin. **Clinical significance**: - Hemophilia b is an X-linked recessive bleeding disorder caused by mutations in the F9 gene. - People with hemophilia b are unable to form normal fibrin, which can lead to prolonged bleeding and life-threatening bleeding episodes. - Hemophilia b is a severe condition that requires regular medical attention and management to prevent bleeding complications. **Conclusion**: F9 is a critical factor for blood clot formation in the intrinsic pathway. Mutations in the F9 gene can have significant clinical implications, leading to hemophilia b, a severe bleeding disorder that can be life-threatening. Understanding the molecular mechanisms of F9 and its role in blood clot formation is crucial for developing therapeutic strategies to prevent and treat this disorder.

Genular Protein ID: 4271199342

Symbol: FA9_HUMAN

Name: Christmas factor

UniProtKB Accession Codes:

P00740 A8K9N4 F2RM36 Q5FBE1 Q5JYJ8

Database IDs:

ABCD 1 AGR 1 Allergome 1 AlphaFoldDB 1 Antibodypedia 1 BRENDA 1 Bgee 1 BindingDB 1 BioCyc 1 BioGRID 1 BioGRID-ORCS 1 BioMuta 1 CCDS 2 CDD 2 CPTAC 1 CTD 1 ChEBI 35 ChEMBL 1 ComplexPortal 1 DIP 1 DNASU 1 DisGeNET 1 DrugBank 11 EC 1 ELM 1 EMBL 21 Ensembl 2 EvolutionaryTrace 1 GO 14 Gene3D 3 GeneCards 1 GeneReviews 1 GeneTree 1 GeneWiki 1 Genevisible 1 GenomeRNAi 1 GlyConnect 1 GlyCosmos 1 GlyGen 1 GuidetoPHARMACOLOGY 1 HGNC 1 HOGENOM 1 HPA 1 InParanoid 1 IntAct 1 InterPro 14 KEGG 1 MANE-Select 1 MEROPS 1 MIM 7 MINT 1 MalaCards 1 MassIVE 1 NCBI Taxonomy 1 OMA 1 OpenTargets 1 Orphanet 4 OrthoDB 1 PANTHER 2 PDB 68 PDBsum 45 PIR 1 PIRSF 1 PRINTS 3 PRO 1 PROSITE 10 PROSITE-ProRule 3 PathwayCommons 1 PaxDb 1 PeptideAtlas 1 Pfam 4 PharmGKB 1 Pharos 1 PhosphoSitePlus 1 PhylomeDB 1 Proteomes 1 ProteomicsDB 1 RNAct 1 Reactome 12 RefSeq 2 SABIO-RK 1 SIGNOR 1 SMART 4 SMR 1 STRING 1 SUPFAM 3 SignaLink 1 TreeFam 1 UCSC 1 UniProtKB 2 VEuPathDB 1 eggNOG 1 iPTMnet 1 jPOST 1 neXtProt 1

Citations:

PubMed ID: 6959130

Title: Isolation and characterization of a cDNA coding for human factor IX.

PubMed ID: 6959130

DOI: 10.1073/pnas.79.21.6461

PubMed ID: 6687940

Title: 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.

PubMed ID: 6687940

DOI: 10.1093/nar/11.8.2325

PubMed ID: 6329734

Title: The gene structure of human anti-haemophilic factor IX.

PubMed ID: 6329734

DOI: 10.1002/j.1460-2075.1984.tb01926.x

PubMed ID: 2994716

Title: Nucleotide sequence of the gene for human factor IX (antihemophilic factor B).

PubMed ID: 2994716

DOI: 10.1021/bi00335a049

PubMed ID: 3857619

Title: Evidence for a prevalent dimorphism in the activation peptide of human coagulation factor IX.

PubMed ID: 3857619

DOI: 10.1073/pnas.82.9.2847

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 15772651

Title: The DNA sequence of the human X chromosome.

PubMed ID: 15772651

DOI: 10.1038/nature03440

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 8295821

Title: The Arg-4 mutant factor IX Strasbourg 2 shows a delayed activation by factor XIa.

PubMed ID: 8295821

PubMed ID: 6089357

Title: Isolation and characterization of human factor IX cDNA: identification of Taq I polymorphism and regional assignment.

PubMed ID: 6089357

DOI: 10.1007/bf01534851

PubMed ID: 2592373

Title: Blood clotting factor IX BM Nagoya. Substitution of arginine 180 by tryptophan and its activation by alpha-chymotrypsin and rat mast cell chymase.

PubMed ID: 2592373

DOI: 10.1016/s0021-9258(19)30074-2

PubMed ID: 9169594

Title: Modification of the N-terminus of human factor IX by defective propeptide cleavage or acetylation results in a destabilized calcium-induced conformation: effects on phospholipid binding and activation by factor XIa.

PubMed ID: 9169594

DOI: 10.1042/bj3230629

PubMed ID: 3340835

Title: Genomic amplification with transcript sequencing.

PubMed ID: 3340835

DOI: 10.1126/science.3340835

PubMed ID: 8236150

Title: A deletion located in the 3' non translated part of the factor IX gene responsible for mild haemophilia B.

PubMed ID: 8236150

PubMed ID: 6688526

Title: The occurrence of beta-hydroxyaspartic acid in the vitamin K-dependent blood coagulation zymogens.

PubMed ID: 6688526

DOI: 10.1016/0006-291x(83)90961-0

PubMed ID: 659613

Title: Activation of human factor IX (Christmas factor).

PubMed ID: 659613

DOI: 10.1172/jci109073

PubMed ID: 6425296

Title: Derivatives of blood coagulation factor IX contain a high affinity Ca2+-binding site that lacks gamma-carboxyglutamic acid.

PubMed ID: 6425296

DOI: 10.1016/s0021-9258(18)91070-7

PubMed ID: 2511201

Title: 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.

PubMed ID: 2511201

DOI: 10.1016/s0021-9258(19)47065-8

PubMed ID: 2129367

Title: 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.

PubMed ID: 2129367

DOI: 10.1007/978-1-4615-3806-6_12

PubMed ID: 1730085

Title: Role of gamma-carboxyglutamic acid residues in the binding of factor IXa to platelets and in factor-X activation.

PubMed ID: 1730085

PubMed ID: 1517205

Title: Human factor IX has a tetrasaccharide O-glycosidically linked to serine 61 through the fucose residue.

PubMed ID: 1517205

DOI: 10.1016/s0021-9258(19)37073-5

PubMed ID: 8172892

Title: Activation peptide of human factor IX has oligosaccharides O-glycosidically linked to threonine residues at 159 and 169.

PubMed ID: 8172892

DOI: 10.1021/bi00183a021

PubMed ID: 11133752

Title: Posttranslational modifications of recombinant myotube-synthesized human factor IX.

PubMed ID: 11133752

DOI: 10.1182/blood.v97.1.130

PubMed ID: 12444082

Title: Physiological fIXa activation involves a cooperative conformational rearrangement of the 99-loop.

PubMed ID: 12444082

DOI: 10.1074/jbc.m210722200

PubMed ID: 25456591

Title: Identification of protein O-glycosylation site and corresponding glycans using liquid chromatography-tandem mass spectrometry via mapping accurate mass and retention time shift.

PubMed ID: 25456591

DOI: 10.1016/j.chroma.2014.10.046

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 7713897

Title: Structure of the metal-free gamma-carboxyglutamic acid-rich membrane binding region of factor IX by two-dimensional NMR spectroscopy.

PubMed ID: 7713897

DOI: 10.1074/jbc.270.14.7980

PubMed ID: 7547952

Title: Structure of the calcium ion-bound gamma-carboxyglutamic acid-rich domain of factor IX.

PubMed ID: 7547952

DOI: 10.1021/bi00038a005

PubMed ID: 8663165

Title: Identification of the phospholipid binding site in the vitamin K-dependent blood coagulation protein factor IX.

PubMed ID: 8663165

DOI: 10.1074/jbc.271.27.16227

PubMed ID: 9047312

Title: 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.

PubMed ID: 9047312

DOI: 10.1021/bi962250r

PubMed ID: 1854745

Title: 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.

PubMed ID: 1854745

DOI: 10.1021/bi00244a006

PubMed ID: 1304885

Title: The three-dimensional structure of the first EGF-like module of human factor IX: comparison with EGF and TGF-alpha.

PubMed ID: 1304885

DOI: 10.1002/pro.5560010109

PubMed ID: 7606779

Title: The structure of a Ca(2+)-binding epidermal growth factor-like domain: its role in protein-protein interactions.

PubMed ID: 7606779

DOI: 10.1016/0092-8674(95)90059-4

PubMed ID: 10467148

Title: Coagulation factor IXa: the relaxed conformation of Tyr99 blocks substrate binding.

PubMed ID: 10467148

DOI: 10.1016/s0969-2126(99)80125-7

PubMed ID: 14722079

Title: Crystal structure of the calcium-stabilized human factor IX Gla domain bound to a conformation-specific anti-factor IX antibody.

PubMed ID: 14722079

DOI: 10.1074/jbc.m314011200

PubMed ID: 20004170

Title: Structural basis of the cofactor- and substrate-assisted activation of human coagulation factor IXa.

PubMed ID: 20004170

DOI: 10.1016/j.str.2009.10.011

PubMed ID: 20121198

Title: Studies of benzothiophene template as potent factor IXa (FIXa) inhibitors in thrombosis.

PubMed ID: 20121198

DOI: 10.1021/jm901475e

PubMed ID: 20121197

Title: Structure based drug design: development of potent and selective factor IXa (FIXa) inhibitors.

PubMed ID: 20121197

DOI: 10.1021/jm901476x

PubMed ID: 20080729

Title: Molecular basis of factor IXa recognition by heparin-activated antithrombin revealed by a 1.7-A structure of the ternary complex.

PubMed ID: 20080729

DOI: 10.1073/pnas.0910144107

PubMed ID: 2743975

Title: Molecular pathology of haemophilia B.

PubMed ID: 2743975

DOI: 10.1002/j.1460-2075.1989.tb03474.x

PubMed ID: 1634040

Title: Assessing the underlying pattern of human germline mutations: lessons from the factor IX gene.

PubMed ID: 1634040

DOI: 10.1096/fasebj.6.10.1634040

PubMed ID: 8392713

Title: Haemophilia B: database of point mutations and short additions and deletions -- fourth edition, 1993.

PubMed ID: 8392713

DOI: 10.1093/nar/21.13.3075

PubMed ID: 6603618

Title: Identification of the molecular defect in factor IX Chapel Hill: substitution of histidine for arginine at position 145.

PubMed ID: 6603618

DOI: 10.1073/pnas.80.14.4200

PubMed ID: 3009023

Title: Defective propeptide processing of blood clotting factor IX caused by mutation of arginine to glutamine at position -4.

PubMed ID: 3009023

DOI: 10.1016/0092-8674(86)90319-3

PubMed ID: 3790720

Title: Factor IXAlabama: a point mutation in a clotting protein results in hemophilia B.

PubMed ID: 3790720

PubMed ID: 3401602

Title: Genetic defect responsible for the dysfunctional protein: factor IX (Long Beach).

PubMed ID: 3401602

PubMed ID: 3243764

Title: Blood clotting factor IX Niigata: substitution of alanine-390 by valine in the catalytic domain.

PubMed ID: 3243764

DOI: 10.1093/oxfordjournals.jbchem.a122575

PubMed ID: 2713493

Title: Functional consequences of an arginine180 to glutamine mutation in factor IX Hilo.

PubMed ID: 2713493

PubMed ID: 2714791

Title: Mutations in the catalytic domain of human coagulation factor IX: rapid characterization by direct genomic sequencing of DNA fragments displaying an altered melting behavior.

PubMed ID: 2714791

DOI: 10.1016/0888-7543(89)90330-3

PubMed ID: 2773937

Title: Functionally important regions of the factor IX gene have a low rate of polymorphism and a high rate of mutation in the dinucleotide CpG.

PubMed ID: 2773937

PubMed ID: 2775660

Title: Factor IX Cardiff: a variant factor IX protein that shows abnormal activation is caused by an arginine to cysteine substitution at position 145.

PubMed ID: 2775660

DOI: 10.1111/j.1365-2141.1989.tb04323.x

PubMed ID: 2753873

Title: Blood clotting factor IX Kashihara: amino acid substitution of valine-182 by phenylalanine.

PubMed ID: 2753873

DOI: 10.1093/oxfordjournals.jbchem.a122740

PubMed ID: 2738071

Title: Factor IX San Dimas. Substitution of glutamine for Arg-4 in the propeptide leads to incomplete gamma-carboxylation and altered phospholipid binding properties.

PubMed ID: 2738071

DOI: 10.1016/s0021-9258(18)60478-8

PubMed ID: 2472424

Title: Three point mutations in the factor IX genes of five hemophilia B patients. Identification strategy using localization by altered epitopes in their hemophilic proteins.

PubMed ID: 2472424

DOI: 10.1172/jci114130

PubMed ID: 2339358

Title: Factor IX Chongqing: a new mutation in the calcium-binding domain of factor IX resulting in severe hemophilia B.

PubMed ID: 2339358

PubMed ID: 2372509

Title: A mutation adjacent to the beta cleavage site of factor IX (valine 182 to leucine) results in mild haemophilia Bm.

PubMed ID: 2372509

DOI: 10.1111/j.1365-2141.1990.tb02652.x

PubMed ID: 2162822

Title: Mutations in hemophilia Bm occur at the Arg180-Val activation site or in the catalytic domain of factor IX.

PubMed ID: 2162822

DOI: 10.1016/s0021-9258(19)38528-x

PubMed ID: 1958666

Title: Factor IX Amagasaki: a new mutation in the catalytic domain resulting in the loss of both coagulant and esterase activities.

PubMed ID: 1958666

DOI: 10.1021/bi00111a014

PubMed ID: 1902289

Title: Isoleucine-397 is changed to threonine in two females with hemophilia B.

PubMed ID: 1902289

DOI: 10.1093/nar/19.5.1165

PubMed ID: 1346975

Title: Hemophilia B caused by five different nondeletion mutations in the protease domain of factor IX.

PubMed ID: 1346975

PubMed ID: 1615485

Title: Characterization of the original Christmas disease mutation (cysteine 206-->serine): from clinical recognition to molecular pathogenesis.

PubMed ID: 1615485

PubMed ID: 8257988

Title: Single-strand conformation polymorphism (SSCP) analysis of the molecular pathology of hemophilia B.

PubMed ID: 8257988

DOI: 10.1002/humu.1380020506

PubMed ID: 8076946

Title: Factor IX gene mutations causing haemophilia B: comparison of SSC screening versus systematic DNA sequencing and diagnostic applications.

PubMed ID: 8076946

DOI: 10.1007/bf00208285

PubMed ID: 8199596

Title: 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.

PubMed ID: 8199596

DOI: 10.1002/humu.1380030211

PubMed ID: 7981722

Title: Identification of mutations in four hemophilia B patients of Turkish origin, including a novel deletion of base 6411.

PubMed ID: 7981722

DOI: 10.1002/humu.1380040214

PubMed ID: 8680410

Title: Twenty-five novel mutations of the factor IX gene in haemophilia B.

PubMed ID: 8680410

DOI: 10.1002/humu.1380060410

PubMed ID: 8833911

Title: A mutation in the propeptide of factor IX leads to warfarin sensitivity by a novel mechanism.

PubMed ID: 8833911

DOI: 10.1172/jci118956

PubMed ID: 9233593

Title: Missense mutations at ALA-10 in the factor IX propeptide: an insignificant variant in normal life but a decisive cause of bleeding during oral anticoagulant therapy.

PubMed ID: 9233593

DOI: 10.1046/j.1365-2141.1997.2213036.x

PubMed ID: 9222764

Title: Mutations associated with hemophilia B in Turkish patients.

PubMed ID: 9222764

DOI: 10.1002/(sici)1098-1004(1997)10:1<76::aid-humu11>3.0.co;2-x

PubMed ID: 9590153

Title: Hemophilia B in a female carrier due to skewed inactivation of the normal X-chromosome.

PubMed ID: 9590153

DOI: 10.1002/(sici)1096-8652(199805)58:1<72::aid-ajh13>3.0.co;2-7

PubMed ID: 9452115

Title: Five novel factor IX mutations in unrelated hemophilia B patients.

PubMed ID: 9452115

DOI: 10.1002/humu.1380110194

PubMed ID: 9600455

Title: Germline mutations in Peruvian patients with hemophilia B: pattern of mutation in Amerindians is similar to the putative endogenous germline pattern.

PubMed ID: 9600455

DOI: 10.1002/(sici)1098-1004(1998)11:5<372::aid-humu4>3.0.co;2-m

PubMed ID: 10698280

Title: Molecular analysis of hemophilia B in Poland: 12 novel mutations of the factor IX gene.

PubMed ID: 10698280

PubMed ID: 10094553

Title: Identification of twenty-one new mutations in the factor IX gene by SSCP analysis.

PubMed ID: 10094553

DOI: 10.1002/(sici)1098-1004(1999)13:2<160::aid-humu9>3.0.co;2-c

PubMed ID: 10391209

Title: Characterization of single-nucleotide polymorphisms in coding regions of human genes.

PubMed ID: 10391209

DOI: 10.1038/10290

PubMed ID: 11122099

Title: Factor IX gene sequencing by a simple and sensitive 15-hour procedure for haemophilia B diagnosis: identification of two novel mutations.

PubMed ID: 11122099

DOI: 10.1046/j.1365-2141.2000.02389.x

PubMed ID: 12588353

Title: Molecular pathology of haemophilia B in Turkish patients: identification of a large deletion and 33 independent point mutations.

PubMed ID: 12588353

DOI: 10.1046/j.1365-2141.2003.04141.x

PubMed ID: 12604421

Title: Molecular analyses in hemophilia B families: identification of six new mutations in the factor IX gene.

PubMed ID: 12604421

PubMed ID: 19846852

Title: X-linked thrombophilia with a mutant factor IX (factor IX Padua).

PubMed ID: 19846852

DOI: 10.1056/nejmoa0904377

PubMed ID: 25470321

Title: Genetic determinants of immunogenicity to factor IX during the treatment of haemophilia B.

PubMed ID: 25470321

DOI: 10.1111/hae.12553

PubMed ID: 25251685

Title: Comprehensive analysis of phenotypes and genetics in 21 Chinese families with haemophilia B: characterization of five novel mutations.

PubMed ID: 25251685

DOI: 10.1111/hae.12534

PubMed ID: 29450643

Title: Variants in FIX propeptide associated with vitamin K antagonist hypersensitivity: functional analysis and additional data confirming the common founder mutations.

PubMed ID: 29450643

DOI: 10.1007/s00277-018-3264-2

Sequence Information:

  • Length: 461
  • Mass: 51778
  • Checksum: C4720C1234477EF5
  • Sequence:
    • MQRVNMIMAE SPGLITICLL GYLLSAECTV FLDHENANKI LNRPKRYNSG KLEEFVQGNL 
ERECMEEKCS FEEAREVFEN TERTTEFWKQ YVDGDQCESN PCLNGGSCKD DINSYECWCP 
FGFEGKNCEL DVTCNIKNGR CEQFCKNSAD NKVVCSCTEG YRLAENQKSC EPAVPFPCGR 
VSVSQTSKLT RAETVFPDVD YVNSTEAETI LDNITQSTQS FNDFTRVVGG EDAKPGQFPW 
QVVLNGKVDA FCGGSIVNEK WIVTAAHCVE TGVKITVVAG EHNIEETEHT EQKRNVIRII 
PHHNYNAAIN KYNHDIALLE LDEPLVLNSY VTPICIADKE YTNIFLKFGS GYVSGWGRVF 
HKGRSALVLQ YLRVPLVDRA TCLRSTKFTI YNNMFCAGFH EGGRDSCQGD SGGPHVTEVE 
GTSFLTGIIS WGEECAMKGK YGIYTKVSRY VNWIKEKTKL T

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. For the full schema, download it here.