UniProtKB/Swiss-Prot P09211: Variant p.Ile105Val

Glutathione S-transferase P
Gene: GSTP1
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Variant information Variant position:

105 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

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:

From Isoleucine (I) to Valine (V) at position 105 (I105V, p.Ile105Val). 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:

Similar physico-chemical property. Both residues are medium size and hydrophobic. The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

3 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*B and allele GSTP1*C. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs1695 [ dbSNP | Ensembl ]

Sequence information Variant position:

105 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:

QEAALVDMVNDGVEDLRCKY I SLIYTNYEAGKDDYVKALPG 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                         QEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYVKA-LPG

Rhesus macaque                REAALVDMVNDGVEDLRCKYLSLIYTNYEAGKDDYVKA-LP

Mouse                         REAAQMDMVNDGVEDLRGKYVTLIYTNYENGKNDYVKA-LP

Rat                           KEAALVDMVNDGVEDLRCKYGTLIYTNYENGKDDYVKA-LP

Pig                           KEAALVDMVNDGVEDLRCKYATLIYTNYEAGKEKYVKE-LP

Bovine                        QEAALVDMVNDGVEDLRCKYVSLIYTNYEAGKEDYVKA-LP

Goat                          REAALVDMVNDGVEDLRCKYVSLIYTNYQAGKEDYVKA-LP

Xenopus laevis                EERGHIDMVNDGVEDLRQKYGRLIFFEYETGKDKYLKE-LP

Caenorhabditis elegans        TETTFIDMFYEGLRDLHTKYTTMIYRNYEDGKAPYIKDVLP

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.

Type	Positions	Description
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
Mutagenesis	99 – 99	D -> A. Reduces affinity for glutathione. Slightly reduced catalytic activity.
Helix	84 – 110

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; The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
The MGC Project Team;
Genome Res. 14:2121-2127(2004)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]; VARIANT VAL-105;

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.