UniProtKB/Swiss-Prot P00505: Variant p.Gly366Val

Aspartate aminotransferase, mitochondrial
Gene: GOT2
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Variant information Variant position:

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

US 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 Glycine (G) to Valine (V) at position 366 (G366V, p.Gly366Val). 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 glycine (G) to medium size and hydrophobic (V) 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 DEE82; uncertain significance; decreased glutamate oxaloacetate transferase activity. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs1597696047 [ dbSNP | Ensembl ]

Sequence information Variant position:

366 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:

VMADRIIGMRTQLVSNLKKE G STHNWQHITDQIGMFCFTGL 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                         VMADRIIGMRTQLVSNLKKE-GSTHNWQ---HITDQIGMFCFTGL

Mouse                         GMADRIISMRTQLVSNLKKE-GSSHNWQ---HITDQIGMFC

Rat                           GMADRIISMRTQLVSNLKKE-GSSHNWQ---HITDQIGMFC

Pig                           GMADRIISMRTQLVSNLKKE-GSSHNWQ---HIVDQIGMFC

Bovine                        GMADRIISMRTQLVSNLKKE-GSSHNWQ---HIIDQIGMFC

Rabbit                        GMADRIIGMRTQLVSNLKKE-GSTHSWQ---HITDQIGMFC

Horse                         GMADRIISMRTQLVSNLKKE-GSSHSWQ---HIADQIGMFC

Chicken                       GMADRIISMRTQLVSNLKKE-GSSHNWQ---HITDQIGMFC

Xenopus tropicalis            GMANRIISMREQLVSNLKKE-GSIHNWQ---HISDQIGMFC

Zebrafish                     GMADRIIRMREMLVSNLKKE-GSTHNWQ---HVTDQIGMFC

Slime mold                    GMADRIINMREQLVKYLKKH-GSTRDWS---HITTQIGMFC

Baker's yeast                 FMVQRLHHVRQEMFDRL----G----WPDLVNFAQQHGMFY

Fission yeast                 GMSERLKSMRKALRNILEKDLKNKHSWK---HITDQIGMFC

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	30 – 430	Aspartate aminotransferase, mitochondrial
Modified residue	363 – 363	N6-acetyllysine; alternate
Modified residue	363 – 363	N6-succinyllysine; alternate
Modified residue	364 – 364	N6-acetyllysine

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.