Source: UNIPROT ×
Variant Gene Score vda Association Type Original DB Sentence supporting the association PMID PMID Year
dbSNP: rs137852231
rs137852231
F9
0.800 GeneticVariation UNIPROT

dbSNP: rs137852273
rs137852273
F9
0.800 GeneticVariation UNIPROT

dbSNP: rs137852274
rs137852274
F9
0.800 GeneticVariation UNIPROT

dbSNP: rs387906481
rs387906481
F9
0.800 GeneticVariation UNIPROT

dbSNP: rs767828752
rs767828752
F9
0.700 GeneticVariation UNIPROT

dbSNP: rs137852249
rs137852249
F9
0.800 GeneticVariation UNIPROT Hemophilia B caused by five different nondeletion mutations in the protease domain of factor IX. 1346975

1992

dbSNP: rs137852276
rs137852276
F9
0.800 GeneticVariation UNIPROT Hemophilia B caused by five different nondeletion mutations in the protease domain of factor IX. 1346975

1992

dbSNP: rs137852277
rs137852277
F9
0.800 GeneticVariation UNIPROT Hemophilia B caused by five different nondeletion mutations in the protease domain of factor IX. 1346975

1992

dbSNP: rs137852278
rs137852278
F9
0.800 GeneticVariation UNIPROT Hemophilia B caused by five different nondeletion mutations in the protease domain of factor IX. 1346975

1992

dbSNP: rs137852279
rs137852279
F9
0.800 GeneticVariation UNIPROT Hemophilia B caused by five different nondeletion mutations in the protease domain of factor IX. 1346975

1992

dbSNP: rs267606792
rs267606792
F9
0.800 GeneticVariation UNIPROT Characterization of the original Christmas disease mutation (cysteine 206----serine): from clinical recognition to molecular pathogenesis. 1615485

1992

dbSNP: rs137852268
rs137852268
F9
0.800 GeneticVariation UNIPROT Isoleucine397 is changed to threonine in two females with hemophilia B. 1902289

1991

dbSNP: rs137852275
rs137852275
F9
0.800 GeneticVariation UNIPROT Factor IX Amagasaki: a new mutation in the catalytic domain resulting in the loss of both coagulant and esterase activities. 1958666

1992

dbSNP: rs137852240
rs137852240
F9
0.800 GeneticVariation UNIPROT Mutations in hemophilia Bm occur at the Arg180-Val activation site or in the catalytic domain of factor IX. 2162822

1990

dbSNP: rs137852265
rs137852265
F9
0.800 GeneticVariation UNIPROT Mutations in hemophilia Bm occur at the Arg180-Val activation site or in the catalytic domain of factor IX. 2162822

1990

dbSNP: rs137852241
rs137852241
F9
0.700 GeneticVariation UNIPROT Mutations in hemophilia Bm occur at the Arg180-Val activation site or in the catalytic domain of factor IX. 2162822

1990

dbSNP: rs137852242
rs137852242
F9
0.700 GeneticVariation UNIPROT Mutations in hemophilia Bm occur at the Arg180-Val activation site or in the catalytic domain of factor IX. 2162822

1990

dbSNP: rs137852226
rs137852226
F9
0.800 GeneticVariation UNIPROT Factor IX Chongqing: a new mutation in the calcium-binding domain of factor IX resulting in severe hemophilia B. 2339358

1990

dbSNP: rs137852243
rs137852243
F9
0.800 GeneticVariation UNIPROT A mutation adjacent to the beta cleavage site of factor IX (valine 182 to leucine) results in mild haemophilia Bm. 2372509

1990

dbSNP: rs137852233
rs137852233
F9
0.800 GeneticVariation UNIPROT Three point mutations in the factor IX genes of five hemophilia B patients. Identification strategy using localization by altered epitopes in their hemophilic proteins. 2472424

1989

dbSNP: rs137852249
rs137852249
F9
0.800 GeneticVariation UNIPROT Three point mutations in the factor IX genes of five hemophilia B patients. Identification strategy using localization by altered epitopes in their hemophilic proteins. 2472424

1989

dbSNP: rs137852225
rs137852225
F9
0.700 GeneticVariation UNIPROT Three point mutations in the factor IX genes of five hemophilia B patients. Identification strategy using localization by altered epitopes in their hemophilic proteins. 2472424

1989

dbSNP: rs137852240
rs137852240
F9
0.800 GeneticVariation UNIPROT Blood clotting factor IX BM Nagoya. Substitution of arginine 180 by tryptophan and its activation by alpha-chymotrypsin and rat mast cell chymase. 2592373

1990

dbSNP: rs137852241
rs137852241
F9
0.700 GeneticVariation UNIPROT Functional consequences of an arginine180 to glutamine mutation in factor IX Hilo. 2713493

1989

dbSNP: rs137852267
rs137852267
F9
0.800 GeneticVariation UNIPROT Mutations in the catalytic domain of human coagulation factor IX: rapid characterization by direct genomic sequencing of DNA fragments displaying an altered melting behavior. 2714791

1989