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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P23526: Variant p.Asp86Gly

Gene: AHCY
Variant information Variant position: help 86 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help 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: help From Aspartate (D) to Glycine (G) at position 86 (D86G, p.Asp86Gly). 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 Change from medium size and acidic (D) to glycine (G) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -1 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: help In HMAHCHD; results in high molecular weight protein aggregates; severely decreased function in homocysteine synthesis; affects nuclear-cytoplasmic protein distribution resulting in slightly decreased protein amount in the nucleus. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.

Sequence information Variant position: help 86 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 432 The length of the canonical sequence.
Location on the sequence: help TLVTLGAEVQWSSCNIFSTQ D HAAAAIAKAGIPVYAWKGET 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.
Chain 2 – 432 Adenosylhomocysteinase
Mutagenesis 1 – 127 Missing. Affects nuclear-cytoplasmic protein distribution resulting in increased protein amount in the nucleus.
Mutagenesis 84 – 84 T -> A. Severely decreased adenosylhomocysteinase activity.
Mutagenesis 84 – 84 T -> S. Decreased adenosylhomocysteinase activity; when associated with V-89.
Mutagenesis 84 – 84 T -> S. No effect on adenosylhomocysteinase activity.
Mutagenesis 89 – 89 A -> V. Decreased adenosylhomocysteinase activity; when associated with S-84.
Helix 86 – 94

Literature citations
S-adenosylhomocysteine hydrolase (AHCY) deficiency: two novel mutations with lethal outcome.
Vugrek O.; Beluzic R.; Nakic N.; Mudd S.H.;
Hum. Mutat. 30:E555-E565(2009)
Cited for: VARIANTS HMAHCHD CYS-49 AND GLY-86; SUBUNIT; CHARACTERIZATION OF VARIANTS HMAHCHD CYS-49 AND GLY-86; S-adenosylhomocysteine hydrolase deficiency: two siblings with fetal hydrops and fatal outcomes.
Grubbs R.; Vugrek O.; Deisch J.; Wagner C.; Stabler S.; Allen R.; Baric I.; Rados M.; Mudd S.H.;
J. Inherit. Metab. Dis. 33:705-713(2010)
Cited for: VARIANTS HMAHCHD CYS-49 AND GLY-86; Mutations in S-adenosylhomocysteine hydrolase (AHCY) affect its nucleocytoplasmic distribution and capability to interact with S-adenosylhomocysteine hydrolase-like 1 protein.
Grbesa I.; Kalo A.; Beluzic R.; Kovacevic L.; Lepur A.; Rokic F.; Hochberg H.; Kanter I.; Simunovic V.; Munoz-Torres P.M.; Shav-Tal Y.; Vugrek O.;
Eur. J. Cell Biol. 96:579-590(2017)
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.