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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P53007: Variant p.Arg247Gln

Tricarboxylate transport protein, mitochondrial
Gene: SLC25A1
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Variant information Variant position: help 247 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 Arginine (R) to Glutamine (Q) at position 247 (R247Q, p.Arg247Gln). 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 large size and basic (R) to medium size and polar (Q) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 1 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 CMS23; reduced rates of citrate transport. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 247 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 311 The length of the canonical sequence.
Location on the sequence: help GAIAGAASVFGNTPLDVIKT R MQGLEAHKYRNTWDCGLQIL 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                         GAIAGAASVFGNTPLDVIKTRMQGLEAHKYRNTWDCGLQIL

Mouse                         GATAGAASVFGNTPLDVIKTRMQGLEAHKYRNTLDCGLKIL

Rat                           GAVAGAASVFGNTPLDVIKTRMQGLEAHKYRNTLDCGVQIL

Bovine                        GAIAGAASVFGNTPLDVIKTRMQGLEAHKYRNTLDCGLQIL

Caenorhabditis elegans        GAVAGAASVYGNTPIDVVKTRMQGLEAKKYKNTLDCAMQIW

Baker's yeast                 GAFSGIVTVYSTMPLDTVKTRMQSLDSTKYSSTMNCFATIF
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 14 – 311 Tricarboxylate transport protein, mitochondrial
Repeat 218 – 303 Solcar 3



Literature citations
Mutations in the mitochondrial citrate carrier SLC25A1 are associated with impaired neuromuscular transmission.
Chaouch A.; Porcelli V.; Cox D.; Edvardson S.; Scarcia P.; De Grassi A.; Pierri C.L.; Cossins J.; Laval S.H.; Griffin H.; Mueller J.S.; Evangelista T.; Toepf A.; Abicht A.; Huebner A.; von der Hagen M.; Bushby K.; Straub V.; Horvath R.; Elpeleg O.; Palace J.; Senderek J.; Beeson D.; Palmieri L.; Lochmueller H.;
J. Neuromuscul. Dis. 1:75-90(2014)
Cited for: FUNCTION; INVOLVEMENT IN CMS23; VARIANT CMS23 GLN-247; Pathogenic mutations of the human mitochondrial citrate carrier SLC25A1 lead to impaired citrate export required for lipid, dolichol, ubiquinone and sterol synthesis.
Majd H.; King M.S.; Smith A.C.; Kunji E.R.S.;
Biochim. Biophys. Acta 1859:1-7(2018)
Cited for: FUNCTION; TRANSPORTER ACTIVITY; BIOPHYSICOCHEMICAL PROPERTIES; CHARACTERIZATION OF VARIANTS D2L2AD LEU-45; ASP-130; GLN-144; TRP-193; HIS-198; THR-202; CYS-282; GLY-282; HIS-282 AND CYS-297; CHARACTERIZATION OF VARIANT CMS23 GLN-247;
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.