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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O43708: Variant p.Lys32Glu

Maleylacetoacetate isomerase
Gene: GSTZ1
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Variant information Variant position: help 32 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 Lysine (K) to Glutamate (E) at position 32 (K32E, p.Lys32Glu). 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 large size and basic (K) to medium size and acidic (E) 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 allele GSTZ1*C. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 32 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 216 The length of the canonical sequence.
Location on the sequence: help FRSSCSWRVRIALALKGIDY K TVPINLIKDRGQQFSKDFQA 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                         FRSSCSWRVRIALALKGIDYKTVPINLIKDRGQQFSKDFQA

Mouse                         FRSSCSWRVRIALALKGIDYEIVPINLIKDGGQQFTEEFQT

Rat                           FRSSCSWRVRIALALKGIDYEIVPINLIKDGGQQFSEEFQT

Caenorhabditis elegans        WRSSCSWRVRIALALKNVDYEYKTVDLLSEEAKSKLKE---

Slime mold                    WRSSCSWRVRVALAYKKIKYEYKAIHLLKDGGQQKSDEYSK

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 1 – 216 Maleylacetoacetate isomerase
Domain 4 – 87 GST N-terminal
Binding site 45 – 45
Modified residue 32 – 32 N6-acetyllysine
Alternative sequence 1 – 55 Missing. In isoform 2.
Beta strand 32 – 35



Literature citations
Characterization and chromosome location of the gene GSTZ1 encoding the human zeta class glutathione transferase and maleylacetoacetate isomerase.
Blackburn A.C.; Woollatt E.; Sutherland G.R.; Board P.G.;
Cytogenet. Cell Genet. 83:109-114(1998)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1); VARIANTS GLU-32; GLY-42 AND THR-82; Submission
NIEHS SNPs program;
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1); VARIANTS GLU-32; GLY-42; THR-82 AND HIS-133; The DNA sequence and analysis of human chromosome 14.
Heilig R.; Eckenberg R.; Petit J.-L.; Fonknechten N.; Da Silva C.; Cattolico L.; Levy M.; Barbe V.; De Berardinis V.; Ureta-Vidal A.; Pelletier E.; Vico V.; Anthouard V.; Rowen L.; Madan A.; Qin S.; Sun H.; Du H.; Pepin K.; Artiguenave F.; Robert C.; Cruaud C.; Bruels T.; Jaillon O.; Friedlander L.; Samson G.; Brottier P.; Cure S.; Segurens B.; Aniere F.; Samain S.; Crespeau H.; Abbasi N.; Aiach N.; Boscus D.; Dickhoff R.; Dors M.; Dubois I.; Friedman C.; Gouyvenoux M.; James R.; Madan A.; Mairey-Estrada B.; Mangenot S.; Martins N.; Menard M.; Oztas S.; Ratcliffe A.; Shaffer T.; Trask B.; Vacherie B.; Bellemere C.; Belser C.; Besnard-Gonnet M.; Bartol-Mavel D.; Boutard M.; Briez-Silla S.; Combette S.; Dufosse-Laurent V.; Ferron C.; Lechaplais C.; Louesse C.; Muselet D.; Magdelenat G.; Pateau E.; Petit E.; Sirvain-Trukniewicz P.; Trybou A.; Vega-Czarny N.; Bataille E.; Bluet E.; Bordelais I.; Dubois M.; Dumont C.; Guerin T.; Haffray S.; Hammadi R.; Muanga J.; Pellouin V.; Robert D.; Wunderle E.; Gauguet G.; Roy A.; Sainte-Marthe L.; Verdier J.; Verdier-Discala C.; Hillier L.W.; Fulton L.; McPherson J.; Matsuda F.; Wilson R.; Scarpelli C.; Gyapay G.; Wincker P.; Saurin W.; Quetier F.; Waterston R.; Hood L.; Weissenbach J.;
Nature 421:601-607(2003)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]; VARIANTS GLU-32 AND GLY-42; Submission
Mural R.J.; Istrail S.; Sutton G.G.; Florea L.; Halpern A.L.; Mobarry C.M.; Lippert R.; Walenz B.; Shatkay H.; Dew I.; Miller J.R.; Flanigan M.J.; Edwards N.J.; Bolanos R.; Fasulo D.; Halldorsson B.V.; Hannenhalli S.; Turner R.; Yooseph S.; Lu F.; Nusskern D.R.; Shue B.C.; Zheng X.H.; Zhong F.; Delcher A.L.; Huson D.H.; Kravitz S.A.; Mouchard L.; Reinert K.; Remington K.A.; Clark A.G.; Waterman M.S.; Eichler E.E.; Adams M.D.; Hunkapiller M.W.; Myers E.W.; Venter J.C.;
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]; VARIANTS GLU-32 AND GLY-42; 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] (ISOFORM 1); VARIANTS GLU-32 AND GLY-42; Discovery of a functional polymorphism in human glutathione transferase zeta by expressed sequence tag database analysis.
Blackburn A.C.; Tzeng H.F.; Anders M.W.; Board P.G.;
Pharmacogenetics 10:49-57(2000)
Cited for: VARIANTS GLU-32 AND GLY-42; FUNCTION; CATALYTIC ACTIVITY;
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.