Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P45381: Variant p.Glu285Ala

Aspartoacylase
Gene: ASPA
Feedback?
Variant information Variant position: help 285 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 Glutamate (E) to Alanine (A) at position 285 (E285A, p.Glu285Ala). 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 (E) to small size and hydrophobic (A) 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 CAND; predominant mutation in Ashkenazi Jewish population; 99% loss of activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 285 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 313 The length of the canonical sequence.
Location on the sequence: help LDGKTIPLGGDCTVYPVFVN E AAYYEKKEAFAKTTKLTLNA 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 – 313 Aspartoacylase
Binding site 288 – 288
Mutagenesis 285 – 285 E -> D. 5-fold decrease in activity.
Mutagenesis 288 – 288 Y -> F. Reduces activity by 99%.



Literature citations
Cloning of the human aspartoacylase cDNA and a common missense mutation in Canavan disease.
Kaul R.; Gao G.P.; Balamurugan K.; Matalon R.;
Nat. Genet. 5:118-123(1993)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; FUNCTION; CATALYTIC ACTIVITY; TISSUE SPECIFICITY; VARIANT CAND ALA-285; Purification and preliminary characterization of brain aspartoacylase.
Moore R.A.; Le Coq J.; Faehnle C.R.; Viola R.E.;
Arch. Biochem. Biophys. 413:1-8(2003)
Cited for: CATALYTIC ACTIVITY; CHARACTERIZATION; CHARACTERIZATION OF VARIANT CAND ALA-285; MUTAGENESIS OF GLU-285; Canavan disease: mutations among Jewish and non-Jewish patients.
Kaul R.; Gao G.P.; Aloya M.; Balamurugan K.; Petrosky A.; Michals K.; Matalon R.;
Am. J. Hum. Genet. 55:34-41(1994)
Cited for: VARIANTS CAND ALA-285 AND GLU-305; Identification and expression of eight novel mutations among non-Jewish patients with Canavan disease.
Kaul R.; Gao G.P.; Matalon R.; Aloya M.; Su Q.; Jin M.; Johnson A.B.; Schutgens R.B.H.; Clarke J.T.R.;
Am. J. Hum. Genet. 59:95-102(1996)
Cited for: VARIANTS CAND THR-16; ARG-27; GLU-114; GLU-123; TYR-152; CYS-168; ALA-285 AND GLU-305; VARIANT GLY-310; CHARACTERIZATION OF VARIANTS CAND THR-16; ARG-27; GLU-114; GLU-123; TYR-152 AND CYS-168; Clinically distinct phenotypes of Canavan disease correlate with residual aspartoacylase enzyme activity.
Mendes M.I.; Smith D.E.; Pop A.; Lennertz P.; Fernandez Ojeda M.R.; Kanhai W.A.; van Dooren S.J.; Anikster Y.; Baric I.; Boelen C.; Campistol J.; de Boer L.; Kariminejad A.; Kayserili H.; Roubertie A.; Verbruggen K.T.; Vianey-Saban C.; Williams M.; Salomons G.S.;
Hum. Mutat. 38:524-531(2017)
Cited for: VARIANTS CAND LYS-24; PRO-30; VAL-57; THR-63; ARG-69; VAL-101; LYS-129; THR-170; VAL-180; HIS-204; ARG-248 AND ASP-286; CHARACTERIZATION OF VARIANTS CAND LYS-24; PRO-30; VAL-57; THR-63; ARG-69; VAL-101; LYS-129; THR-170; VAL-180; HIS-204; ARG-248; ALA-285 AND ASP-286; CATALYTIC ACTIVITY; BIOPHYSICOCHEMICAL PROPERTIES;
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.