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UniProtKB/Swiss-Prot P00740: Variant p.Arg294Gln

Coagulation factor IX
Gene: F9
Variant information

Variant position:  294
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  LP/P [Disclaimer]
The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance

Residue change:  From Arginine (R) to Glutamine (Q) at position 294 (R294Q, p.Arg294Gln).
Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.

Physico-chemical properties:  Change from large size and basic (R) to medium size and polar (Q)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  1
The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page

Variant description:  In HEMB; mild to moderate; Dreihacken, Penafiel and Seattle-4.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  294
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  461
The length of the canonical sequence.

Location on the sequence:   KITVVAGEHNIEETEHTEQK  R NVIRIIPHHNYNAAINKYNH
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.

Residue conservation: 
The multiple alignment of the region surrounding the variant against various orthologous sequences.

Human                         KITVVAGEHNIEETEHTEQKRNVIRIIPHHNYNAAINKYNH

                              KITIVAGEHNTEKREHTEQKRNVIRTILHHSYNATINKYNH

Chimpanzee                    KITVVAGEHNIEETEHTEQKRNVIRIIPHHNYNAAINKYNH

Mouse                         KIEVVAGEYNIDKKEDTEQRRNVIRTIPHHQYNATINKYSH

Rat                           KIEVVAGEHNIDEKEDTEQRRNVIRTIPHHQYNATINKYSH

Bovine                        KITVVAGEHNTEKPEPTEQKRNVIRAIPYHSYNASINKYSH

Cat                           EITVVAGEHNTEETEHTEQKRNVIRTILHHSYNASVNKYSH

Chicken                       NVTAVAGEYNTKEDDHTEQRRQVVKILPYPTYNRTRNKHHN

Sequence annotation in neighborhood:  
The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
  • Type: the type of sequence feature.
  • Positions: endpoints of the sequence feature.
  • Description: contains additional information about the feature.

TypePositionsDescription
Chain 47 – 461 Coagulation factor IX
Chain 227 – 461 Coagulation factor IXa heavy chain
Domain 227 – 459 Peptidase S1
Metal binding 281 – 281 Calcium 8
Metal binding 283 – 283 Calcium 8; via carbonyl oxygen
Metal binding 286 – 286 Calcium 8; via carbonyl oxygen
Metal binding 288 – 288 Calcium 8
Metal binding 291 – 291 Calcium 8
Disulfide bond 178 – 335 Interchain (between light and heavy chains)
Mutagenesis 305 – 305 Y -> F. Strongly increases enzyme activity with a synthetic peptide substrate; when associated with T-311; A-365 and T-391.
Mutagenesis 311 – 311 K -> T. Strongly increases enzyme activity with a synthetic peptide substrate; when associated with F-305; A-365 and T-391.
Mutagenesis 312 – 312 Y -> A. Strongly decreases enzyme activity with a synthetic peptide substrate.
Beta strand 292 – 301


Literature citations

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)
Cited for: VARIANTS HEMB LYS-73; SER-106 AND GLN-294;

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)
Cited for: VARIANTS HEMB VAL-291; GLN-294; HIS-410; GLY-411 AND ILE-411;

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)
Cited for: VARIANTS HEMB ARG-253; GLN-294; GLN-379; PRO-426 AND ILE-TYR-THR-445 INS;

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)
Cited for: VARIANTS HEMB GLN-294 AND ARG-413;

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)
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;

Disclaimer: Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.