Variant position: 218 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 392 The length of the canonical sequence.
Location on the sequence:
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 QGIDILYSGSQKALNAPPGT SLISFSDKAKKKMYSRKTKPF
Mouse QGIDIMYSSSQKVLNAPPGI SLISFNDKAKYKVYSRKTKPV
Rat QGIDILYSGSQKVLNAPPGI SLISFNDKAKSKVYSRKTKPV
Rabbit QGIDVLYSGSQKALNAPPGT SLISFSDKAKSKIYARKTKPF
Cat QGIDVLYSGSQKVLNSPPGT SLISFSDKAKNKIYTRKTKPV
Slime mold WKIDACYTGTQKCLSGPPGI SPLTFSNAACHKIATRKTPVA
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
1 – 392 Alanine--glyoxylate aminotransferase
209 – 209 N6-(pyridoxal phosphate)lysine
225 – 225 N6-acetyllysine; alternate
225 – 225 N6-succinyllysine; alternate
234 – 234 N6-acetyllysine
209 – 209 K -> R. Affects pyridoxal phosphate binding; loss of alanine--glyoxylate aminotransferase activity.
218 – 222
The major allele of the alanine:glyoxylate aminotransferase gene: nine novel mutations and polymorphisms associated with primary hyperoxaluria type 1.
Coulter-Mackie M.B.; Lian Q.; Applegarth D.; Toone J.;
Mol. Genet. Metab. 86:172-178(2005)
Cited for: VARIANTS HP1 ARG-161 AND LEU-218; VARIANTS THR-279 AND VAL-280;
Consequences of missense mutations for dimerization and turnover of alanine:glyoxylate aminotransferase: study of a spectrum of mutations.
Coulter-Mackie M.B.; Lian Q.;
Mol. Genet. Metab. 89:349-359(2006)
Cited for: CHARACTERIZATION OF VARIANTS HP1 ARG-41; VAL-41; GLU-82; ARG-108; ASP-112; ARG-156; ARG-161; ARG-170; TYR-173; ASN-183; PHE-187; PRO-205 AND LEU-218; MUTAGENESIS OF LYS-209; SUBUNIT;
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.