Details for: F9

Gene ID: 2158

Symbol: F9

Ensembl ID: ENSG00000101981

Description: coagulation factor IX

Associated with

Cells (max top 100)

(Cell Significance Index and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

  • Cell Name: plasmablast (CL0000980)
    Fold Change: 8.3453
    Cell Significance Index: 77.4500
  • Cell Name: liver dendritic cell (CL2000055)
    Fold Change: 7.9437
    Cell Significance Index: 20.9600
  • Cell Name: hepatoblast (CL0005026)
    Fold Change: 5.9812
    Cell Significance Index: 100.6000
  • Cell Name: centrilobular region hepatocyte (CL0019029)
    Fold Change: 2.9831
    Cell Significance Index: 50.2500
  • Cell Name: CD14-low, CD16-positive monocyte (CL0002396)
    Fold Change: 1.7290
    Cell Significance Index: 41.8800
  • Cell Name: cytotoxic T cell (CL0000910)
    Fold Change: 0.4957
    Cell Significance Index: 7.2300
  • Cell Name: periportal region hepatocyte (CL0019026)
    Fold Change: 0.3570
    Cell Significance Index: 5.2700
  • Cell Name: inflammatory macrophage (CL0000863)
    Fold Change: 0.3540
    Cell Significance Index: 2.7200
  • Cell Name: midzonal region hepatocyte (CL0019028)
    Fold Change: 0.3204
    Cell Significance Index: 1.8500
  • Cell Name: hepatic pit cell (CL2000054)
    Fold Change: 0.2520
    Cell Significance Index: 0.6800
  • Cell Name: endothelial cell of periportal hepatic sinusoid (CL0019021)
    Fold Change: 0.2213
    Cell Significance Index: 0.7700
  • Cell Name: neoplastic cell (CL0001063)
    Fold Change: 0.1980
    Cell Significance Index: 39.2900
  • Cell Name: cholangiocyte (CL1000488)
    Fold Change: 0.1601
    Cell Significance Index: 1.5800
  • Cell Name: intrahepatic cholangiocyte (CL0002538)
    Fold Change: 0.1460
    Cell Significance Index: 0.5500
  • Cell Name: Kupffer cell (CL0000091)
    Fold Change: 0.1415
    Cell Significance Index: 1.3000
  • Cell Name: endothelial cell of pericentral hepatic sinusoid (CL0019022)
    Fold Change: 0.1305
    Cell Significance Index: 1.0300
  • Cell Name: cortical cell of adrenal gland (CL0002097)
    Fold Change: 0.0862
    Cell Significance Index: 2.3100
  • Cell Name: endothelial cell of hepatic sinusoid (CL1000398)
    Fold Change: 0.0747
    Cell Significance Index: 0.7100
  • Cell Name: obsolete epithelial cell of alveolus of lung (CL0010003)
    Fold Change: 0.0566
    Cell Significance Index: 1.4100
  • Cell Name: vascular associated smooth muscle cell (CL0000359)
    Fold Change: 0.0433
    Cell Significance Index: 0.4600
  • Cell Name: mesangial cell (CL0000650)
    Fold Change: 0.0387
    Cell Significance Index: 0.4900
  • Cell Name: thymocyte (CL0000893)
    Fold Change: 0.0380
    Cell Significance Index: 0.4800
  • Cell Name: endocrine cell (CL0000163)
    Fold Change: 0.0339
    Cell Significance Index: 0.4100
  • Cell Name: acinar cell (CL0000622)
    Fold Change: 0.0310
    Cell Significance Index: 0.3900
  • Cell Name: hepatic stellate cell (CL0000632)
    Fold Change: 0.0301
    Cell Significance Index: 0.3100
  • Cell Name: central memory CD4-positive, alpha-beta T cell (CL0000904)
    Fold Change: 0.0229
    Cell Significance Index: 0.2000
  • Cell Name: syncytiotrophoblast cell (CL0000525)
    Fold Change: 0.0221
    Cell Significance Index: 0.2100
  • Cell Name: intestinal epithelial cell (CL0002563)
    Fold Change: 0.0097
    Cell Significance Index: 0.1000
  • Cell Name: cell of skeletal muscle (CL0000188)
    Fold Change: 0.0094
    Cell Significance Index: 0.1200
  • Cell Name: medial ganglionic eminence derived interneuron (CL4023063)
    Fold Change: 0.0077
    Cell Significance Index: 0.1100
  • Cell Name: naive B cell (CL0000788)
    Fold Change: 0.0057
    Cell Significance Index: 0.0600
  • Cell Name: kidney epithelial cell (CL0002518)
    Fold Change: 0.0020
    Cell Significance Index: 0.0600
  • Cell Name: erythroblast (CL0000765)
    Fold Change: 0.0017
    Cell Significance Index: 0.0200
  • Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
    Fold Change: 0.0011
    Cell Significance Index: 0.3800
  • Cell Name: pancreatic acinar cell (CL0002064)
    Fold Change: 0.0006
    Cell Significance Index: 0.1000
  • Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
    Fold Change: 0.0005
    Cell Significance Index: 0.1000
  • Cell Name: acinar cell of salivary gland (CL0002623)
    Fold Change: 0.0005
    Cell Significance Index: 0.0300
  • Cell Name: pigmented epithelial cell (CL0000529)
    Fold Change: 0.0000
    Cell Significance Index: 0.0000
  • Cell Name: anterior lens cell (CL0002223)
    Fold Change: -0.0001
    Cell Significance Index: -0.1400
  • Cell Name: lens epithelial cell (CL0002224)
    Fold Change: -0.0001
    Cell Significance Index: -0.1400
  • Cell Name: secondary lens fiber (CL0002225)
    Fold Change: -0.0001
    Cell Significance Index: -0.1400
  • Cell Name: pancreatic A cell (CL0000171)
    Fold Change: -0.0005
    Cell Significance Index: -0.3600
  • Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
    Fold Change: -0.0013
    Cell Significance Index: -0.8400
  • Cell Name: ciliary muscle cell (CL1000443)
    Fold Change: -0.0013
    Cell Significance Index: -0.5700
  • Cell Name: pancreatic ductal cell (CL0002079)
    Fold Change: -0.0026
    Cell Significance Index: -0.3000
  • Cell Name: ON-bipolar cell (CL0000749)
    Fold Change: -0.0027
    Cell Significance Index: -0.0300
  • Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
    Fold Change: -0.0036
    Cell Significance Index: -0.3800
  • Cell Name: hepatocyte (CL0000182)
    Fold Change: -0.0043
    Cell Significance Index: -0.0600
  • Cell Name: lens fiber cell (CL0011004)
    Fold Change: -0.0044
    Cell Significance Index: -0.1400
  • Cell Name: hippocampal granule cell (CL0001033)
    Fold Change: -0.0045
    Cell Significance Index: -0.3000
  • Cell Name: enterocyte of epithelium of small intestine (CL1000334)
    Fold Change: -0.0049
    Cell Significance Index: -0.1400
  • Cell Name: pigmented ciliary epithelial cell (CL0002303)
    Fold Change: -0.0056
    Cell Significance Index: -0.8100
  • Cell Name: alpha-beta T cell (CL0000789)
    Fold Change: -0.0070
    Cell Significance Index: -0.0600
  • Cell Name: gamma-delta T cell (CL0000798)
    Fold Change: -0.0070
    Cell Significance Index: -0.0700
  • Cell Name: retinal progenitor cell (CL0002672)
    Fold Change: -0.0071
    Cell Significance Index: -0.4000
  • Cell Name: indirect pathway medium spiny neuron (CL4023029)
    Fold Change: -0.0075
    Cell Significance Index: -0.3300
  • Cell Name: direct pathway medium spiny neuron (CL4023026)
    Fold Change: -0.0085
    Cell Significance Index: -0.3200
  • Cell Name: forebrain neuroblast (CL1000042)
    Fold Change: -0.0086
    Cell Significance Index: -0.5300
  • Cell Name: mature NK T cell (CL0000814)
    Fold Change: -0.0089
    Cell Significance Index: -0.1000
  • Cell Name: L6b glutamatergic cortical neuron (CL4023038)
    Fold Change: -0.0089
    Cell Significance Index: -0.2900
  • Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
    Fold Change: -0.0090
    Cell Significance Index: -0.2500
  • Cell Name: corticothalamic-projecting glutamatergic cortical neuron (CL4023013)
    Fold Change: -0.0096
    Cell Significance Index: -0.3100
  • Cell Name: CD14-positive monocyte (CL0001054)
    Fold Change: -0.0100
    Cell Significance Index: -0.2000
  • Cell Name: L2/3 intratelencephalic projecting glutamatergic neuron (CL4030059)
    Fold Change: -0.0105
    Cell Significance Index: -0.1400
  • Cell Name: L5 extratelencephalic projecting glutamatergic cortical neuron (CL4023041)
    Fold Change: -0.0108
    Cell Significance Index: -0.3800
  • Cell Name: mucosal invariant T cell (CL0000940)
    Fold Change: -0.0113
    Cell Significance Index: -0.1300
  • Cell Name: skeletal muscle fiber (CL0008002)
    Fold Change: -0.0114
    Cell Significance Index: -0.2900
  • Cell Name: hippocampal pyramidal neuron (CL1001571)
    Fold Change: -0.0119
    Cell Significance Index: -0.3400
  • Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
    Fold Change: -0.0127
    Cell Significance Index: -0.6000
  • Cell Name: near-projecting glutamatergic cortical neuron (CL4023012)
    Fold Change: -0.0128
    Cell Significance Index: -0.3200
  • Cell Name: luminal epithelial cell of mammary gland (CL0002326)
    Fold Change: -0.0140
    Cell Significance Index: -0.1800
  • Cell Name: type I muscle cell (CL0002211)
    Fold Change: -0.0148
    Cell Significance Index: -0.3600
  • Cell Name: lymphocyte (CL0000542)
    Fold Change: -0.0154
    Cell Significance Index: -0.2100
  • Cell Name: pvalb GABAergic cortical interneuron (CL4023018)
    Fold Change: -0.0155
    Cell Significance Index: -0.3300
  • Cell Name: lamp5 GABAergic cortical interneuron (CL4023011)
    Fold Change: -0.0157
    Cell Significance Index: -0.3400
  • Cell Name: caudal ganglionic eminence derived cortical interneuron (CL4023064)
    Fold Change: -0.0160
    Cell Significance Index: -0.3200
  • Cell Name: neuron associated cell (CL0000095)
    Fold Change: -0.0160
    Cell Significance Index: -0.6600
  • Cell Name: renal interstitial pericyte (CL1001318)
    Fold Change: -0.0162
    Cell Significance Index: -0.1700
  • Cell Name: innate lymphoid cell (CL0001065)
    Fold Change: -0.0163
    Cell Significance Index: -0.2100
  • Cell Name: chandelier pvalb GABAergic cortical interneuron (CL4023036)
    Fold Change: -0.0168
    Cell Significance Index: -0.3500
  • Cell Name: VIP GABAergic cortical interneuron (CL4023016)
    Fold Change: -0.0169
    Cell Significance Index: -0.3400
  • Cell Name: cardiac muscle cell (CL0000746)
    Fold Change: -0.0169
    Cell Significance Index: -0.2500
  • Cell Name: photoreceptor cell (CL0000210)
    Fold Change: -0.0171
    Cell Significance Index: -0.2400
  • Cell Name: sst GABAergic cortical interneuron (CL4023017)
    Fold Change: -0.0172
    Cell Significance Index: -0.3400
  • Cell Name: Hofbauer cell (CL3000001)
    Fold Change: -0.0172
    Cell Significance Index: -0.1400
  • Cell Name: erythrocyte (CL0000232)
    Fold Change: -0.0173
    Cell Significance Index: -0.4400
  • Cell Name: megakaryocyte (CL0000556)
    Fold Change: -0.0173
    Cell Significance Index: -0.2800
  • Cell Name: Purkinje cell (CL0000121)
    Fold Change: -0.0174
    Cell Significance Index: -0.3800
  • Cell Name: lung endothelial cell (CL1001567)
    Fold Change: -0.0175
    Cell Significance Index: -0.9100
  • Cell Name: corneal epithelial cell (CL0000575)
    Fold Change: -0.0183
    Cell Significance Index: -0.2600
  • Cell Name: blood vessel endothelial cell (CL0000071)
    Fold Change: -0.0184
    Cell Significance Index: -0.2000
  • Cell Name: regular atrial cardiac myocyte (CL0002129)
    Fold Change: -0.0185
    Cell Significance Index: -0.2500
  • Cell Name: epithelial cell (CL0000066)
    Fold Change: -0.0190
    Cell Significance Index: -0.2000
  • Cell Name: sncg GABAergic cortical interneuron (CL4023015)
    Fold Change: -0.0193
    Cell Significance Index: -0.3800
  • Cell Name: astrocyte of the cerebral cortex (CL0002605)
    Fold Change: -0.0197
    Cell Significance Index: -0.3400
  • Cell Name: placental villous trophoblast (CL2000060)
    Fold Change: -0.0210
    Cell Significance Index: -0.5600
  • Cell Name: regular ventricular cardiac myocyte (CL0002131)
    Fold Change: -0.0211
    Cell Significance Index: -0.2700
  • Cell Name: cortical interneuron (CL0008031)
    Fold Change: -0.0221
    Cell Significance Index: -0.5300
  • Cell Name: type II muscle cell (CL0002212)
    Fold Change: -0.0229
    Cell Significance Index: -0.3700
  • Cell Name: fibroblast of cardiac tissue (CL0002548)
    Fold Change: -0.0230
    Cell Significance Index: -0.3300

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.

Other Information

**Key Characteristics:** Coagulation factor IX is a single-chain protein composed of 299 amino acids, with a molecular weight of approximately 50 kDa. It is synthesized in the liver and secreted into the bloodstream, where it binds to phospholipid surfaces to initiate the intrinsic coagulation pathway. Factor IX is also known for its high specificity and sensitivity, making it an essential component of the coagulation cascade. **Pathways and Functions:** The coagulation factor IX plays a central role in the intrinsic pathway of blood coagulation, which is activated in response to tissue damage. The factor IX-IXa complex binds to phospholipid surfaces, activating factor X, which in turn triggers a cascade of reactions leading to the formation of thrombin and fibrin clots. Factor IX also interacts with other proteins, including factor VIII, to regulate the coagulation cascade and prevent excessive thrombin generation. **Clinical Significance:** Deficiencies in coagulation factor IX lead to Hemophilia B, a severe bleeding disorder characterized by prolonged bleeding episodes, joint deformities, and increased risk of spontaneous hemorrhage. Hemophilia B is caused by mutations in the F9 gene, which encodes the factor IX protein. The disease is typically inherited in an X-linked recessive pattern, affecting males more frequently than females. In addition to its role in Hemophilia B, factor IX has also been implicated in thrombophilia, a condition characterized by an increased risk of blood clots. Elevated levels of factor IX have been associated with an increased risk of deep vein thrombosis and pulmonary embolism. **Disease Associations:** Coagulation factor IX has been linked to various diseases, including: * Hemophilia B: A severe bleeding disorder caused by deficiencies in factor IX. * Thrombophilia: An increased risk of blood clots due to elevated levels of factor IX. * Hemostasis disorders: Defects in the coagulation cascade, including the intrinsic pathway, can lead to impaired hemostasis. * Cancer: Elevated levels of factor IX have been observed in various types of cancer, including breast, lung, and colon cancer. **Cellular Expression:** Factor IX is expressed in various cells, including: * Hepatocytes: The primary site of factor IX production. * Endothelial cells: Factor IX is also produced by endothelial cells, which play a critical role in maintaining vascular integrity. * B cells: Factor IX is expressed in B cells, which are involved in the immune response. **Conclusion:** Coagulation factor IX is a crucial protein involved in the blood coagulation cascade, playing a central role in regulating the formation of fibrin clots. Deficiencies in factor IX lead to Hemophilia B, a severe bleeding disorder that affects millions worldwide. Understanding the key characteristics, pathways, functions, and clinical significance of factor IX is essential for the development of effective treatments and diagnostic tools for this debilitating disease.

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 12 DrugCentral 1 EC 1 ELM 1 EMBL 21 Ensembl 2 EvolutionaryTrace 1 GO 14 Gene3D 3 GeneCards 1 GeneReviews 1 GeneTree 1 GeneWiki 1 GenomeRNAi 1 GlyConnect 1 GlyCosmos 1 GlyGen 1 GuidetoPHARMACOLOGY 1 HGNC 1 HOGENOM 1 HPA 1 InParanoid 1 IntAct 1 InterPro 15 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 45 PDBsum 45 PIR 1 PIRSF 1 PRINTS 3 PRO 1 PROSITE 10 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 1 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: 34502392

Title: Ixodes ricinus Salivary Serpin Iripin-8 Inhibits the Intrinsic Pathway of Coagulation and Complement.

PubMed ID: 34502392

DOI: 10.3390/ijms22179480

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. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.