UniProtKB/Swiss-Prot Q03154: Variant p.Glu233Asp

Aminoacylase-1
Gene: ACY1
Chromosomal location: 3p21.1
Variant information

Variant position:  233
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Disease [Disclaimer]
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants have been found in patients and disease-association is reported in literature. However, this classification is not a definitive assessment of variant pathogenicity.
  • Polymorphism: No disease-association has been reported.
  • Unclassified: Variants have been found in patients but disease-association remains unclear.

Residue change:  From Glutamate (E) to Aspartate (D) at position 233 (E233D, p.Glu233Asp).
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:  Similar physico-chemical property. Both residues are medium size and acidic.
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  2
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

Involvement in disease:  Aminoacylase-1 deficiency (ACY1D) [MIM:609924]: An enzymatic deficiency resulting in encephalopathy, unspecific psychomotor delay, psychomotor delay with atrophy of the vermis and syringomyelia, marked muscular hypotonia or normal clinical features. Epileptic seizures are a frequent feature. All affected individuals exhibit markedly increased urinary excretion of several N-acetylated amino acids. {ECO:0000269|PubMed:16274666, ECO:0000269|PubMed:16465618, ECO:0000269|PubMed:17562838, ECO:0000269|PubMed:21414403}. Note=The disease is caused by mutations affecting the gene represented in this entry.
The name and a short description of the disease associated with the variant. For more information about the disease, the user can refer to OMIM, following the link provided after the disease acronym.

Variant description:  In ACY1D; loss of activity.
Any additional useful information about the variant.



Sequence information

Variant position:  233
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  408
The length of the canonical sequence.

Location on the sequence:   DTAAEKLHKVVNSILAFREK  E WQRLQSNPHLKEGSVTSVNL
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:  
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 2 – 408 Aminoacylase-1
Alternative sequence 220 – 284 Missing. In isoform 3.


Literature citations

Mutations in ACY1, the gene encoding aminoacylase 1, cause a novel inborn error of metabolism.
Sass J.O.; Mohr V.; Olbrich H.; Engelke U.; Horvath J.; Fliegauf M.; Loges N.T.; Schweitzer-Krantz S.; Moebus R.; Weiler P.; Kispert A.; Superti-Furga A.; Wevers R.A.; Omran H.;
Am. J. Hum. Genet. 78:401-409(2006)
Cited for: VARIANTS ACY1D ASP-233 AND CYS-353; TISSUE SPECIFICITY;

The molecular basis of aminoacylase 1 deficiency.
Sommer A.; Christensen E.; Schwenger S.; Seul R.; Haas D.; Olbrich H.; Omran H.; Sass J.O.;
Biochim. Biophys. Acta 1812:685-690(2011)
Cited for: VARIANTS ACY1D GLN-378; TRP-378 AND CYS-386; CHARACTERIZATION OF VARIANTS ACY1D TRP-197; ASP-233; CYS-353; TRP-378 AND CYS-386;

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.