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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P21549: Variant p.Pro11Leu

Alanine--glyoxylate aminotransferase
Gene: AGXT
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Variant information Variant position: help 11 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 Proline (P) to Leucine (L) at position 11 (P11L, p.Pro11Leu). 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 Similar physico-chemical property. Both residues are medium size and hydrophobic. The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -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

Polymorphism: help Variant p.Pro11Leu acts synergistically with other variants in AGXT producing specific enzymatic phenotypes in HP1 patients. The combined presence of variants p.Pro11Leu and p.Ile340Met defines the minor AGXT allele, whereas their absence defines the major allele. The minor allele has frequencies of 20% in normal European and North American populations, and 50% in HP1 patients. Additional information on the polymorphism described.
Variant description: help In allele minor; associated in cis with M-340; decreased specific alanine--glyoxylate aminotransferase activity in vitro when associated with M-340; loss of alanine--glyoxylate aminotransferase activity in vitro when associated with I-152 and M-340; loss of alanine--glyoxylate aminotransferase activity in vitro when associated with R-170 and M-340; loss of alanine--glyoxylate aminotransferase activity in vitro when associated with T-244 and M-340; causes mitochondrial mistargeting when associated with R-170 and M-340. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 11 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 392 The length of the canonical sequence.
Location on the sequence: help MASHKLLVTP P KALLKPLSIPNQLLLGPGPS 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.
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 – 392 Alanine--glyoxylate aminotransferase
Modified residue 9 – 9 Phosphothreonine



Literature citations
Identification of mutations associated with peroxisome-to-mitochondrion mistargeting of alanine/glyoxylate aminotransferase in primary hyperoxaluria type 1.
Purdue P.E.; Takada Y.; Danpure C.J.;
J. Cell Biol. 111:2341-2351(1990)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; VARIANTS LEU-11 AND MET-340; VARIANT HP1 ARG-170; SUBCELLULAR LOCATION; Functional synergism between the most common polymorphism in human alanine:glyoxylate aminotransferase and four of the most common disease-causing mutations.
Lumb M.J.; Danpure C.J.;
J. Biol. Chem. 275:36415-36422(2000)
Cited for: CHARACTERIZATION OF VARIANTS HP1 ARG-41; GLU-82; ILE-152; ARG-170 AND THR-244; CHARACTERIZATION OF VARIANT LEU-11; MUTAGENESIS OF LYS-209; FUNCTION; CATALYTIC ACTIVITY; SUBCELLULAR LOCATION; COFACTOR; SUBUNIT; BIOPHYSICOCHEMICAL PROPERTIES; ACTIVITY REGULATION;
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.