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UniProtKB/Swiss-Prot P09211: Variant p.Ala114Val

Glutathione S-transferase P
Gene: GSTP1
Chromosomal location: 11q13
Variant information

Variant position:  114
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Polymorphism
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants implicated in disease according to literature reports.
  • Polymorphism: Variants not reported to be implicated in disease.
  • Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:  From Alanine (A) to Valine (V) at position 114 (A114V, p.Ala114Val).
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:  Change from small size and hydrophobic (A) to medium size and hydrophobic (V)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  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:  In allele GSTP1*C.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  114
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  210
The length of the canonical sequence.

Location on the sequence:   NDGVEDLRCKYISLIYTNYE  A GKDDYVKALPGQLKPFETLL
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: 
The multiple alignment of the region surrounding the variant against various orthologous sequences.

Human                         NDGVEDLRCKYISLIYTNYEAGKDDYVKA-LPGQLKPFETLL

Rhesus macaque                NDGVEDLRCKYLSLIYTNYEAGKDDYVKA-LPGQLKPFETL

Mouse                         NDGVEDLRGKYVTLIYTNYENGKNDYVKA-LPGHLKPFETL

Rat                           NDGVEDLRCKYGTLIYTNYENGKDDYVKA-LPGHLKPFETL

Pig                           NDGVEDLRCKYATLIYTNYEAGKEKYVKE-LPEHLKPFETL

Bovine                        NDGVEDLRCKYVSLIYTNYEAGKEDYVKA-LPQHLKPFETL

Goat                          NDGVEDLRCKYVSLIYTNYQAGKEDYVKA-LPQHLKPFETL

Xenopus laevis                NDGVEDLRQKYGRLIFFEYETGKDKYLKE-LPSQLDFFERI

Caenorhabditis elegans        YEGLRDLHTKYTTMIYRNYEDGKAPYIKDVLPGELARLEKL

Sequence annotation in neighborhood:  
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 – 210 Glutathione S-transferase P
Domain 83 – 204 GST C-terminal
Modified residue 103 – 103 N6-succinyllysine
Modified residue 116 – 116 N6-succinyllysine
Modified residue 128 – 128 N6-acetyllysine
Mutagenesis 99 – 99 D -> A. Reduces affinity for glutathione. Slightly reduced catalytic activity.
Helix 112 – 135


Literature citations

Molecular cloning, characterization, and expression in Escherichia coli of full-length cDNAs of three human glutathione S-transferase Pi gene variants. Evidence for differential catalytic activity of the encoded proteins.
Ali-Osman F.; Akande O.; Antoun G.; Mao J.X.; Buolamwini J.;
J. Biol. Chem. 272:10004-10012(1997)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; VARIANTS VAL-105 AND VAL-114;

Submission
NIEHS SNPs program;
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANTS VAL-105 AND VAL-114;

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.