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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P60174: Variant p.Val232Met

Triosephosphate isomerase
Gene: TPI1
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Variant information Variant position: help 232 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 Valine (V) to Methionine (M) at position 232 (V232M, p.Val232Met). 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 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: 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 TPID. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 232 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 249 The length of the canonical sequence.
Location on the sequence: help SVTGATCKELASQPDVDGFL V GGASLKPEFVDIINAKQ 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                         SVTGATCKELASQPDVDGFLVGGASL-KPEFVDIINA---KQ-

Gorilla                       SVTGATCKELASQPDVDGFLVGGASL-KPEFVDIINA-

                              SVTGATCKELASQPDVDGFLVGGASL-KPEFVDIINA-

Rhesus macaque                SVTGATCKELASQPDVDGFLVGGASL-KPEFVDIINA-

Chimpanzee                    SVTGATCKELASQPDVDGFLVGGASL-KPEFVDIINA-

Mouse                         SVTGATCKELASQPDVDGFLVGGASL-KPEFVDIINA-

Rat                           SVTGATCKELASQPDVDGFLVGGASL-KPEFVDIINA-

Pig                           SVTGATCKELASQPDVDGFRVSGASL-KPEFVDIINA-

Bovine                        SVTGATCKELASQPDVDGFLVGGASL-KPEFVDIINA-

Rabbit                        SVTGATCKELASQPDVDGFLVGGASL-KPEFVDIINA-

Chicken                       SVTGGNCKELASQHDVDGFLVGGASL-KPEFVDIINA-

Xenopus laevis                SVTGGTCRELAGQPDIDGFLVGGASL-KPEFIEIINA-

Xenopus tropicalis            SVTGGTCKELGAQPDIDGFLVGGASL-KPEFIDIINA-

Caenorhabditis elegans        SVTADNAAELGKKPDIDGFLVGGASL-KPDFVKIINA-

Drosophila                    SVTAANAKELAKKPDIDGFLVGGASL-KPEFVDIINA-

Slime mold                    SVNADNCHNLSKQSDIDGFLVGGASLVASDFIAIIKSA

Baker's yeast                 SANGSNAVTFKDKADVDGFLVGGASL-KPEFVDIINS-

Fission yeast                 SVNGGNCKEFLKFHDIDGFLVGGASL-KPEFHNIVNV-

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 – 249 Triosephosphate isomerase
Modified residue 212 – 212 Phosphoserine
Modified residue 214 – 214 Phosphothreonine
Modified residue 223 – 223 Phosphoserine
Modified residue 238 – 238 N6-acetyllysine
Beta strand 229 – 233



Literature citations
Relation between genetic defect, altered protein structure, and enzyme function in triose-phosphate isomerase (TPI) deficiency.
Neubauer B.A.; Pekrun A.; Eber S.W.; Lakomek M.; Schroeter W.;
Cited for: VARIANTS TPID ASP-105 AND MET-232;
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.