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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P60174: Variant p.Glu105Asp

Triosephosphate isomerase
Gene: TPI1
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Variant information Variant position: help 105 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 Glutamate (E) to Aspartate (D) at position 105 (E105D, p.Glu105Asp). 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 acidic. 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 TPID; no effect on triose-phosphate isomerase activity; changed protein homodimerization activity; the homodimer stability is temperature-dependent and affects the triose-phosphate isomerase activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 105 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 KDCGATWVVLGHSERRHVFG E SDELIGQKVAHALAEGLGVI 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                         KDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVI

Gorilla                       KDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVI

                              KDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVI

Rhesus macaque                KDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVI

Chimpanzee                    KDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVI

Mouse                         KDLGATWVVLGHSERRHVFGESDELIGQKVSHALAEGLGVI

Rat                           KDLGATWVVLGHSERRHIFGESDELIGQKVNHALSEGLGVI

Pig                           KDLGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVI

Bovine                        KDLGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVI

Rabbit                        KDCGATWVVLGHSERRHVFGESDELIGQKVAHALSEGLGVI

Chicken                       KDIGAAWVILGHSERRHVFGESDELIGQKVAHALAEGLGVI

Xenopus laevis                KDCGATWVILGHSERRHVFGECDELIGQKVAHALSEGIGVI

Xenopus tropicalis            KDCGATWVILGHSERRHVFGESDELIGQKVAHALSENVGVI

Caenorhabditis elegans        KDLGLEWVILGHSERRHVFGESDALIAEKTVHALEAGIKVV

Drosophila                    KDIGADWVILGHSERRAIFGESDALIAEKAEHALAEGLKVI

Slime mold                    VDLGIPYVIIGHSERRNVFSESSELITKKTKYAISLGLTVI

Baker's yeast                 KDVGAKWVILGHSERRSYFHEDDKFIADKTKFALGQGVGVI

Fission yeast                 IDAGITYTLTGHSERRTIFKESDEFVADKTKFALEQGLTVV

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
Active site 96 – 96 Electrophile
Modified residue 106 – 106 Phosphoserine



Literature citations
Structural basis of human triosephosphate isomerase deficiency: mutation E104D is related to alterations of a conserved water network at the dimer interface.
Rodriguez-Almazan C.; Arreola R.; Rodriguez-Larrea D.; Aguirre-Lopez B.; de Gomez-Puyou M.T.; Perez-Montfort R.; Costas M.; Gomez-Puyou A.; Torres-Larios A.;
J. Biol. Chem. 283:23254-23263(2008)
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 39-289 OF MUTANT ASP-105; FUNCTION; SUBUNIT; CHARACTERIZATION OF VARIANT ASP-105; CATALYTIC ACTIVITY; BIOPHYSICOCHEMICAL PROPERTIES; PATHWAY; Human triose-phosphate isomerase deficiency: a single amino acid substitution results in a thermolabile enzyme.
Daar I.O.; Artymiuk P.J.; Phillips D.C.; Maquat L.E.;
Proc. Natl. Acad. Sci. U.S.A. 83:7903-7907(1986)
Cited for: VARIANT TPID ASP-105; 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; Molecular analysis of a series of alleles in humans with reduced activity at the triosephosphate isomerase locus.
Watanabe M.; Zingg B.C.; Mohrenweiser H.W.;
Am. J. Hum. Genet. 58:308-316(1996)
Cited for: VARIANTS TPID ALA-73; ASP-105 AND MET-155; Evidence for founder effect of the Glu104Asp substitution and identification of new mutations in triosephosphate isomerase deficiency.
Arya R.; Lalloz M.R.A.; Bellingham A.J.; Layton D.M.;
Hum. Mutat. 10:290-294(1997)
Cited for: VARIANTS TPID TYR-42; ASP-105 AND VAL-171;
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.