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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9Y619: Variant p.Gly27Arg

Mitochondrial ornithine transporter 1
Gene: SLC25A15
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Variant information Variant position: help 27 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 Arginine (R) at position 27 (G27R, p.Gly27Arg). 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 large size and basic (R) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -2 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 HHHS; incapable of catalyzing homo-exchanges of ornithine, arginine, lysine and citrulline. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 27 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 301 The length of the canonical sequence.
Location on the sequence: help IQAAIDLTAGAAGGTACVLT G QPFDTMKVKMQTFPDLYRGL 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                         IQAAIDLTAGAAGGTACVLTGQPFDTMKVKMQTFPDLYRGL

Mouse                         IQAAIDLTAGAAGGTACVLTGQPFDTMKVKMQTFPDLYRGL

Rat                           IQAAIDLTAGAAGGTACVLTGQPFDTMKVKMQTFPDLYRGL
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 1 – 301 Mitochondrial ornithine transporter 1
Repeat 7 – 91 Solcar 1



Literature citations
The mitochondrial ornithine transporter. Bacterial expression, reconstitution, functional characterization, and tissue distribution of two human isoforms.
Fiermonte G.; Dolce V.; David L.; Santorelli F.M.; Dionisi-Vici C.; Palmieri F.; Walker J.E.;
J. Biol. Chem. 278:32778-32783(2003)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; FUNCTION; TRANSPORTER ACTIVITY; TISSUE SPECIFICITY; BIOPHYSICOCHEMICAL PROPERTIES; CHARACTERIZATION OF VARIANTS HHHS ARG-27; PHE-188 DEL; ASP-190 AND GLN-275; MUTAGENESIS OF 179-ARG--TYR-301; ACTIVITY REGULATION; Seven novel mutations in the ORNT1 gene (SLC25A15) in patients with hyperornithinemia, hyperammonemia, and homocitrullinuria syndrome.
Salvi S.; Dionisi-Vici C.; Bertini E.; Verardo M.; Santorelli F.M.;
Hum. Mutat. 18:460-460(2001)
Cited for: VARIANTS HHHS ARG-27; PHE-188 DEL; ASP-190 AND GLN-275; Clinical and molecular findings in hyperornithinemia-hyperammonemia-homocitrullinuria syndrome.
Salvi S.; Santorelli F.M.; Bertini E.; Boldrini R.; Meli C.; Donati A.; Burlina A.B.; Rizzo C.; Di Capua M.; Fariello G.; Dionisi-Vici C.;
Neurology 57:911-914(2001)
Cited for: VARIANTS HHHS ARG-27; PHE-188 DEL; ASP-190 AND GLN-275; Identification of novel mutations in the SLC25A15 gene in hyperornithinemia-hyperammonemia-homocitrullinuria (HHH) syndrome: a clinical, molecular, and functional study.
Tessa A.; Fiermonte G.; Dionisi-Vici C.; Paradies E.; Baumgartner M.R.; Chien Y.-H.; Loguercio C.; de Baulny H.O.; Nassogne M.-C.; Schiff M.; Deodato F.; Parenti G.; Rutledge S.L.; Vilaseca M.A.; Melone M.A.B.; Scarano G.; Aldamiz-Echevarria L.; Besley G.; Walter J.; Martinez-Hernandez E.; Hernandez J.M.; Pierri C.L.; Palmieri F.; Santorelli F.M.;
Hum. Mutat. 30:741-748(2009)
Cited for: VARIANTS HHHS ARG-27; ARG-37; LEU-70; GLN-71; LEU-188; SER-216; ILE-272 AND PHE-283; CHARACTERIZATION OF VARIANTS HHHS ARG-37; GLN-71; CYS-113; ILE-272; LYS-273 AND PHE-283; FUNCTION;
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.