UniProtKB/Swiss-Prot P02679: Variant p.Arg301Cys

Fibrinogen gamma chain
Gene: FGG
Chromosomal location: 4q28
Variant information

Variant position:  301
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Polymorphism
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants implicated in disease according to literature reports.
  • Polymorphism: Variants not reported to be implicated in disease.
  • Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:  From Arginine (R) to Cysteine (C) at position 301 (R301C, p.Arg301Cys).
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 (C)
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 Tochigi/Osaka-2/Milano-5/Villajoyosa.
Any additional useful information about the variant.

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

Sequence information

Variant position:  301
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  453
The length of the canonical sequence.

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.






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.

Chain 27 – 453 Fibrinogen gamma chain
Domain 170 – 416 Fibrinogen C-terminal
Beta strand 301 – 303

Literature citations

Abnormal polymerization and normal binding of plasminogen and t-PA in three new dysfibrinogenaemias: Barcelona III and IV (gamma Arg 275-->His) and Villajoyosa (gamma Arg 275-->Cys).
Borrell M.; Gari M.; Coll I.; Vallve C.; Tirado I.; Soria J.M.; Sala N.; Munoz C.; Oliver A.; Garcia A.;
Blood Coagul. Fibrinolysis 6:198-206(1995)

Gene analyses of abnormal fibrinogens with a mutation in the gamma chain.
Mimuro J.; Muramatsu S.; Maekawa H.; Sakata Y.; Kaneko M.; Yoshitake S.; Okuma M.; Ito Y.; Takeda Y.; Matsuda M.;
Int. J. Hematol. 56:129-134(1992)
Cited for: VARIANTS OSAKA-2 CYS-301; KYOTO-1 LYS-334; ASAHI THR-336 AND KYOTO-3 TYR-356;

Fibrinogen Milano V: a congenital dysfibrinogenaemia with a gamma 275 Arg-->Cys substitution.
Steinmann C.; Boegli C.; Jungo M.; Laemmle B.; Heinemann G.; Wermuth B.; Redaelli R.; Baudo F.; Furlan M.;
Blood Coagul. Fibrinolysis 5:463-471(1994)
Cited for: VARIANT MILANO-5 CYS-301;

Substitution of gamma Arg-275 by Cys in an abnormal fibrinogen, 'fibrinogen Osaka II'. Evidence for a unique solitary cystine structure at the mutation site.
Terukina S.; Matsuda M.; Hirata H.; Takeda Y.; Miyata T.; Takao T.; Shimonishi Y.;
J. Biol. Chem. 263:13579-13587(1988)
Cited for: VARIANT OSAKA-2 CYS-301;

An apparently higher molecular weight gamma-chain variant in a new congenital abnormal fibrinogen Tochigi characterized by the replacement of gamma arginine-275 by cysteine.
Yoshida N.; Ota K.; Moroi M.; Matsuda M.;
Blood 71:480-487(1988)

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.