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UniProtKB/Swiss-Prot P00505: Variant p.Arg262Gly

Aspartate aminotransferase, mitochondrial
Gene: GOT2
Variant information

Variant position:  262
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  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:  From Arginine (R) to Glycine (G) at position 262 (R262G, p.Arg262Gly).
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 large size and basic (R) to glycine (G)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -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:  In DEE82; decreased glutamate oxaloacetate transferase activity.
Any additional useful information about the variant.



Sequence information

Variant position:  262
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  430
The length of the canonical sequence.

Location on the sequence:   FDMAYQGFASGDGDKDAWAV  R HFIEQGINVCLCQSYAKNMG
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                         FDMAYQGFASGDGDKDAWAVRH------FIEQGINVCLCQSYAKNMG

Mouse                         FDMAYQGFASGDGDKDAWAVRH------FIEQGINVCLCQS

Rat                           FDMAYQGFASGDGDKDAWAVRH------FIEQGINVCLCQS

Pig                           FDMAYQGFASGDGNKDAWAVRH------FIEQGINVCLCQS

Bovine                        FDMAYQGFASGDGNKDAWAVRH------FIEQGINVCLCQS

Rabbit                        FDMAYQGFASGDGDKDAWAVRH------FIEQGINVCLCQS

Horse                         FDMAYQGFASGDGNKDAWAVRY------FIEQGINVCLCQS

Chicken                       FDMAYQGFASGDINRDAWALRH------FIEQGIDVVLSQS

Xenopus tropicalis            FDMAYQGFASGDTNRDAWAVRH------FIQEGINVVLSQS

Zebrafish                     FDMAYQGFASGDIDRDAWAVRY------FIEQGHNILLSQS

Slime mold                    FDFAYQGFASGSPEKDAAAVRM------FVEDGHNIALCQS

Baker's yeast                 VDMAYQGLESGNLLKDAYLLRLCLNVNKYPNWSNGIFLCQS

Fission yeast                 LDMAYQGFASGDFARDAYATRL------FASSNVPMLLCQS

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 30 – 430 Aspartate aminotransferase, mitochondrial
Modified residue 279 – 279 N6-(pyridoxal phosphate)lysine; alternate
Modified residue 279 – 279 N6-acetyllysine; alternate
Helix 259 – 266


Literature citations

Bi-allelic GOT2 mutations cause a treatable malate-aspartate shuttle-related encephalopathy.
van Karnebeek C.D.M.; Ramos R.J.; Wen X.Y.; Tarailo-Graovac M.; Gleeson J.G.; Skrypnyk C.; Brand-Arzamendi K.; Karbassi F.; Issa M.Y.; van der Lee R.; Droegemoeller B.I.; Koster J.; Rousseau J.; Campeau P.M.; Wang Y.; Cao F.; Li M.; Ruiter J.; Ciapaite J.; Kluijtmans L.A.J.; Willemsen M.A.A.P.; Jans J.J.; Ross C.J.; Wintjes L.T.; Rodenburg R.J.; Huigen M.C.D.G.; Jia Z.; Waterham H.R.; Wasserman W.W.; Wanders R.J.A.; Verhoeven-Duif N.M.; Zaki M.S.; Wevers R.A.;
Am. J. Hum. Genet. 105:534-548(2019)
Cited for: FUNCTION; CATALYTIC ACTIVITY; INVOLVEMENT IN DEE82; VARIANTS DEE82 LEU-209 DEL; GLY-262; GLY-337 AND VAL-366; CHARACTERIZATION OF VARIANTS DEE82 GLY-262 AND VAL-366;

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.