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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P00742: Variant p.Gly406Ser

Coagulation factor X
Gene: F10
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Variant information Variant position: help 406 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 Glycine (G) to Serine (S) at position 406 (G406S, p.Gly406Ser). 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 glycine (G) to small size and polar (S) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 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 FA10D; almost complete loss of activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 406 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 488 The length of the canonical sequence.
Location on the sequence: help DRNSCKLSSSFIITQNMFCA G YDTKQEDACQGDSGGPHVTR 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                         DRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDSGGPHVTR

Mouse                         DRNTCKLSTSFSITQNMFCAGYEAKLEDACQGDSGGPHVTR

Rat                           DRNTCRLSTSFSITQNMFCAGYDAKQEDACQGDSGGPHVTR

Bovine                        DRSTCKLSSSFTITPNMFCAGYDTQPEDACQGDSGGPHVTR

Rabbit                        DRNSCKRSSSFTITQNMFCAGYDARPEDACQGDSGGPHVTR

Chicken                       DRSTCKQSTNFAITENMFCAGYETEQKDACQGDSGGPHVTR

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 41 – 488 Coagulation factor X
Chain 183 – 488 Factor X heavy chain
Chain 235 – 488 Activated factor Xa heavy chain
Domain 235 – 467 Peptidase S1
Active site 419 – 419 Charge relay system
Beta strand 402 – 406



Literature citations
Genetic analysis of hereditary factor X deficiency in a French patient of Sri Lankan ancestry: in vitro expression study identified Gly366Ser substitution as the molecular basis of the dysfunctional factor X.
Isshiki I.; Favier R.; Moriki T.; Uchida T.; Ishihara H.; Van Dreden P.; Murata M.; Ikeda Y.;
Blood Coagul. Fibrinolysis 16:9-16(2005)
Cited for: VARIANT FA10D SER-406; CHARACTERIZATION OF VARIANT FA10D SER-406; Molecular dynamics characterization of five pathogenic Factor X mutants associated with decreased catalytic activity.
Abdel-Azeim S.; Oliva R.; Chermak E.; De Cristofaro R.; Cavallo L.;
Biochemistry 53:6992-7001(2014)
Cited for: VARIANTS FA10D ASN-322; MET-358; ALA-382; SER-406 AND ASP-421; CHARACTERIZATION OF VARIANTS FA10D ASN-322; MET-358; ALA-382; SER-406 AND ASP-421;
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.