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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P00740: Variant p.Arg226Gly

Coagulation factor IX
Gene: F9
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Variant information Variant position: help 226 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help 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: help From Arginine (R) to Glycine (G) at position 226 (R226G, p.Arg226Gly). 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: help Change from large size and basic (R) to glycine (G) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -2 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: help In HEMB; severe; Madrid. Any additional useful information about the variant.


Sequence information Variant position: help 226 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 461 The length of the canonical sequence.
Location on the sequence: help EAETILDNITQSTQSFNDFT R VVGGEDAKPGQFPWQVVLNG 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         EAETILDNITQSTQS------FNDFTRVVGGEDAKPGQFPWQV-VLNG

                              EVEKILDNV---TQP------LNDFTRVVGGKDAKPGQFPW

Chimpanzee                    EAETILDNITQSTQS------FNDFTRVVGGEDAKPGQFPW

Mouse                         TDGAILNNVTESSES------LNDFTRVVGGENAKPGQIPW

Rat                           TNSTILDNLTENSEP------INDFTRVVGGENAKPGQIPW

Bovine                        EAEIIWDNVTQSNQS------FDEFSRVVGGEDAERGQFPW

Cat                           EAEKNVDNV---TQP------LNDLTRIVGGKTAKPGQFPW

Chicken                       DITEPPPPPTTSAAPAKIVPITKNDTRVVGGYDSVKGQLPW
Sequence annotation in neighborhood: help 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
Propeptide 192 – 226 Activation peptide
Site 226 – 227 Cleavage; by factor XIa
Glycosylation 213 – 213 N-linked (GlcNAc...) asparagine
Glycosylation 215 – 215 O-linked (GalNAc...) threonine
Glycosylation 225 – 225 O-linked (GalNAc...) threonine
Disulfide bond 178 – 335 Interchain (between light and heavy chains)



Literature citations
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)
Cited for: VARIANTS HEMB HIS-191; GLY-226; THR-279; GLN-379; GLU-419 AND GLN-449; 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.