Variant position: 161 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 EGLAQHKPVLLFLTHGESST GVLQPLDGFGELCHRYKCLLL
Mouse EGLAQHKPVLLFLVHGESST GVVQPLDGFGELCHRYQCLLL
Rat EGLAQHKPVLLFLTHGESST GVLQPLDGFGELCHRYQCLLL
Rabbit ECLAQHKPVLLFLTHGESST GVLQPLDGFGELCHRYKCLLL
Cat EALAQHKPVLLFLTQGESSS GVLQPLDGYGELCHRYNCLLL
Slime mold SALVQHKPSLLTLVFGETST GVKQQMEGVGELCKKYNCLLM
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 Serine--pyruvate aminotransferase
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;
Gly161 mutations associated with primary hyperoxaluria type I induce the cytosolic aggregation and the intracellular degradation of the apo-form of alanine:glyoxylate aminotransferase.
Oppici E.; Roncador A.; Montioli R.; Bianconi S.; Cellini B.;
Biochim. Biophys. Acta 1832:2277-2288(2013)
Cited for: CHARACTERIZATION OF VARIANTS HP1 ARG-161; CYS-161 AND SER-161; SUBCELLULAR LOCATION;
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.