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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q16595: Variant p.Leu182Phe

Frataxin, mitochondrial
Gene: FXN
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Variant information Variant position: help 182 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 Leucine (L) to Phenylalanine (F) at position 182 (L182F, p.Leu182Phe). 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 medium size and hydrophobic (L) to large size and aromatic (F) 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 FRDA. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 182 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 GPKRYDWTGKNWVYSHDGVS L HELLAAELTKALKTKLDLSS 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                         GPKRYDW----TGKNWVYSHDGVSLHELLAAELTKALKT-KLDLSS

Mouse                         GPKRYDW----TGKNWVYSHDGVSLHELLARELTKALNT-K

Rat                           GPKRYDW----TGKNWVYSHDGVSLHELLARELTEALNT-K

Bovine                        GPKRYDW----TGRNWVYSHDGVSLHELLATELTQALKT-K

Caenorhabditis elegans        GPKRYDL---EEEGKWTYAHDGEQLDSLLNREFRKILADDR

Drosophila                    GPKRYDFVGTVAAGRWIYKHSGQSLHELLQQEIPGILKSQS

Slime mold                    GPKRFDY--DSVEKRWVDNRDGTPLRQLLNSEINTLCKY-D

Baker's yeast                 GPNRFDL----LNGEWVSLRNGTKLTDILTEEVEKAISKSQ

Fission yeast                 GPKHYEY--SLKSKTWCSTRDEGTLLGILSSEFSKWFSR-P
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
Alternative sequence 161 – 210 SGPKRYDWTGKNWVYSHDGVSLHELLAAELTKALKTKLDLSSLAYSGKDA -> RLTWLLWLFHP. In isoform 2.
Alternative sequence 161 – 210 SGPKRYDWTGKNWVYSHDGVSLHELLAAELTKALKTKLDLSSLAYSGKDA -> RYVVDLSVMTGLGKTGCTPTTACPSMSCWPQSSLKP. In isoform 3.
Mutagenesis 173 – 173 W -> G. Loss of interaction with the core iron-sulfur cluster assembly complex. Does not affect mitochondrial localization. Does not affect proteolytic processing.
Helix 182 – 194



Literature citations
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;
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.