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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P78417: Variant p.Ala140Asp

Glutathione S-transferase omega-1
Gene: GSTO1
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Variant information Variant position: help 140 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LB/B 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 Alanine (A) to Aspartate (D) at position 140 (A140D, p.Ala140Asp). 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 small size and hydrophobic (A) to medium size and acidic (D) 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 allele GSTO1*C; no effect on protein stability. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 140 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 241 The length of the canonical sequence.
Location on the sequence: help FSKVPSLVGSFIRSQNKEDY A GLKEEFRKEFTKLEEVLTNK 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                         FSKVP---SLVGSFIRSQNKEDYAGLKEEFRKEFTKLEEVLTNK

Mouse                         FSKVP---PLIASFVRSKRKEDSPNLREALENEFKKLEEGM

Rat                           FSKVP---SLVTSFIRAKRKEDHPGIKEELKKEFSKLEEAM

Pig                           SSKVP---PLLIRFIRRENEADCSGLKEELRKEFSKLEEVL

Caenorhabditis elegans        LTAVAHAVPLLFAVMRDRTLKD-----EKQRKVFEVLKQAE

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 2 – 241 Glutathione S-transferase omega-1
Domain 106 – 230 GST C-terminal
Modified residue 129 – 129 Phosphoserine
Modified residue 143 – 143 N6-acetyllysine
Modified residue 148 – 148 N6-acetyllysine
Modified residue 152 – 152 N6-acetyllysine
Alternative sequence 123 – 155 Missing. In isoform 2.
Helix 136 – 160



Literature citations
Genetic variation in genes associated with arsenic metabolism: glutathione S-transferase omega 1-1 and purine nucleoside phosphorylase polymorphisms in European and indigenous Americans.
Yu L.; Kalla K.; Guthrie E.; Vidrine A.; Klimecki W.T.;
Environ. Health Perspect. 111:1421-1427(2003)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANTS ASP-140; GLU-155 DEL; LYS-208 AND VAL-236; Novel folding and stability defects cause a deficiency of human glutathione transferase omega 1.
Zhou H.; Brock J.; Casarotto M.G.; Oakley A.J.; Board P.G.;
J. Biol. Chem. 286:4271-4279(2011)
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF VARIANT GLU-155 DEL IN COMPLEX WITH GLUTATHIONE; FUNCTION; CATALYTIC ACTIVITY; SUBUNIT; CHARACTERIZATION OF VARIANTS ASP-140 AND GLU-155 DEL; Characterization of the human Omega class glutathione transferase genes and associated polymorphisms.
Whitbread A.K.; Tetlow N.; Eyre H.J.; Sutherland G.R.; Board P.G.;
Pharmacogenetics 13:131-144(2003)
Cited for: VARIANTS ASP-140 AND GLU-155 DEL;
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.