UniProtKB/Swiss-Prot P00740 : Variant p.Arg226Trp
Coagulation factor IX
Gene: F9
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Variant information
Variant position:
226
The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:
LP/P [Disclaimer : Variants classification is intended for research purposes only, not for clinical and diagnostic use . The label disease variant is assigned according to literature reports on probable disease-association that can be based on theoretical reasons. This label must not be considered as a definitive proof for the pathogenic role of a variant. ]
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 Tryptophan (W) at position 226 (R226W, p.Arg226Trp).
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 large size and aromatic (W)
The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:
-3
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; severe; Nagoya-1, Dernbach, Deventer, Idaho.
Any additional useful information about the variant.
Other resources:
Links to websites of interest for the variant.
Sequence information
Variant position:
226
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:
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:
The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human EAETILDNITQSTQS------FNDFTR VVGGEDAKPGQFPWQV-VLNG
EVEKILDNV---TQP------LNDFTR VVGGKDAKPGQFPW
Chimpanzee EAETILDNITQSTQS------FNDFTR VVGGEDAKPGQFPW
Mouse TDGAILNNVTESSES------LNDFTR VVGGENAKPGQIPW
Rat TNSTILDNLTENSEP------INDFTR VVGGENAKPGQIPW
Bovine EAEIIWDNVTQSNQS------FDEFSR VVGGEDAERGQFPW
Cat EAEKNVDNV---TQP------LNDLTR IVGGKTAKPGQFPW
Chicken DITEPPPPPTTSAAPAKIVPITKNDTR VVGGYDSVKGQLPW
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.
Type Positions Description
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
Blood clotting factor IX BM Nagoya. Substitution of arginine 180 by tryptophan and its activation by alpha-chymotrypsin and rat mast cell chymase.
Suehiro K.; Kawabata S.; Miyata T.; Takeya H.; Takamatsu J.; Ogata K.; Kamiya T.; Saito H.; Niho Y.; Iwanaga S.;
J. Biol. Chem. 264:21257-21265(1989)
Cited for: PROTEIN SEQUENCE OF 47-461; VARIANT HEMB TRP-226; FUNCTION; CATALYTIC ACTIVITY; PROTEOLYTIC CLEAVAGE; SUBCELLULAR LOCATION; SUBUNIT; TISSUE SPECIFICITY;
Mutations in hemophilia Bm occur at the Arg180-Val activation site or in the catalytic domain of factor IX.
Bertina R.M.; van der Linden I.K.; Mannucci P.M.; Reinalda-Poot H.H.; Cupers R.; Poort S.R.; Reitsma P.H.;
J. Biol. Chem. 265:10876-10883(1990)
Cited for: VARIANTS HEMB GLN-226; TRP-226; PHE-227 AND THR-414;
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.