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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q16595: Variant p.Gly130Val

Frataxin, mitochondrial
Gene: FXN
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Variant information Variant position: help 130 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 Valine (V) at position 130 (G130V, p.Gly130Val). 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 medium size and hydrophobic (V) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -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: help In FRDA; does not affect interaction with the core iron-sulfur cluster assembly complex; does not affect mitochondrial localization; does not affect proteolytic processing.. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 130 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 210 The length of the canonical sequence.
Location on the sequence: help FEDLADKPYTFEDYDVSFGS G VLTVKLGGDLGTYVINKQTP 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                         FEDLADKPYTFEDYDVSFGSGVLTVKLGGDLGTYVINKQTP

Mouse                         FEDLADKPYTLEDYDVSFGDGVLTIKLGGDLGTYVINKQTP

Rat                           FEDLADKPYTLKDYDVSFGDGVLTIKLGGDLGTYVINKQTP

Bovine                        FEDLADKPYTFEDYDVSFGSGVLTVKLGGDLGTYVINKQTP

Caenorhabditis elegans        FDQIADSFPVSEQFDVSHAMGVLTVNVSKSVGTYVINKQSP

Drosophila                    FEELTENASELQGTDVAYSDGVLTVNLGGQHGTYVINRQTP

Slime mold                    LEILSE-ANTCEGFEVEGNDGVLTIIVGNK-GTYVINKQTP

Baker's yeast                 LEELSEAHPDCIP-DVELSHGVMTLEIPAF-GTYVINKQPP

Fission yeast                 FEDLLEEVGK-KDYDIQYANGVITLMLGEK-GTYVINKQPP
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 42 – 210 Frataxin intermediate form
Chain 56 – 210 Frataxin(56-210)
Chain 78 – 210 Frataxin(78-210)
Chain 81 – 210 Extramitochondrial frataxin
Chain 81 – 210 Frataxin mature form
Mutagenesis 111 – 111 E -> K. Significantly reduces interaction with the core iron-sulfur cluster assembly complex. Does not affect mitochondrial localization. Does not affect proteolytic processing.
Mutagenesis 115 – 115 D -> K. Does not affect interaction with the core iron-sulfur cluster assembly complex. Does not affect mitochondrial localization. Does not affect proteolytic processing.
Mutagenesis 124 – 124 D -> K. Drasticly reduces interaction with the core iron-sulfur cluster assembly complex. Does not affect mitochondrial localization. Does not affect proteolytic processing.
Mutagenesis 146 – 146 N -> A. Does not affect interaction with the core iron-sulfur cluster assembly complex. Does not affect mitochondrial localization. Does not affect proteolytic processing.



Literature citations
Mammalian frataxin: an essential function for cellular viability through an interaction with a preformed ISCU/NFS1/ISD11 iron-sulfur assembly complex.
Schmucker S.; Martelli A.; Colin F.; Page A.; Wattenhofer-Donze M.; Reutenauer L.; Puccio H.;
PLoS ONE 6:e16199-e16199(2011)
Cited for: COMPONENT OF CORE (FE-S) CLUSTER ASSEMBLY COMPLEX; MUTAGENESIS OF GLU-96; ASP-104; GLU-108; GLU-111; ASP-115; ASP-124; ASN-146 AND TRP-173; SUBCELLULAR LOCATION; PROTEOLYTIC PROCESSING; CHARACTERIZATION OF VARIANTS FRDA TYR-122; VAL-130 AND PHE-154; Atypical Friedreich ataxia caused by compound heterozygosity for a novel missense mutation and the GAA triplet-repeat expansion.
Bidichandani S.I.; Ashizawa T.; Patel P.I.;
Am. J. Hum. Genet. 60:1251-1256(1997)
Cited for: VARIANTS FRDA VAL-130 AND PHE-154; The correlation of clinical phenotype in Friedreich ataxia with the site of point mutations in the FRDA gene.
Forrest S.M.; Knight M.; Delatycki M.B.; Paris D.; Williamson R.; King J.; Yeung L.; Nassif N.; Nicholson G.A.;
Neurogenetics 1:253-257(1998)
Cited for: VARIANTS FRDA VAL-130; CYS-165 AND PHE-182; Friedreich's ataxia: point mutations and clinical presentation of compound heterozygotes.
Cossee M.; Duerr A.; Schmitt M.; Dahl N.; Trouillas P.; Allinson P.; Kostrzewa M.; Nivelon-Chevallier A.; Gustavson K.-H.; Kohlschuetter A.; Mueller U.; Mandel J.-L.; Brice A.; Koenig M.; Cavalcanti F.; Tammaro A.; de Michele G.; Filla A.; Cocozza S.; Labuda M.; Montermini L.; Poirier J.; Pandolfo M.;
Ann. Neurol. 45:200-206(1999)
Cited for: VARIANTS FRDA TYR-122 AND VAL-130;
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.