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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q13510: Variant p.Glu138Val

Acid ceramidase
Gene: ASAH1
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Variant information Variant position: help 138 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 Valine (V) at position 138 (E138V, p.Glu138Val). 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 medium size and hydrophobic (V) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -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
Variant description: help In FRBRL; loss of ceramidase activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 138 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 395 The length of the canonical sequence.
Location on the sequence: help GIAAVTDIPLGEIISFNIFY E LFTICTSIVAEDKKGHLIHG 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         GIAAVTDIPLGEIISFNIFYELFTICTSIVAEDKKGHLIHG

Chimpanzee                    GIAAVTDIPLGEIISFNIFYELFTICTSIVAEDKKGHLIHG

Mouse                         GIADVTGIPLGEIISFNIFYELFTMCTSIITEDEKGHLLHG

Rat                           GIADVTGIPLGEIISFNIFYELFTMCTSIITEDGKGHLLHG

Bovine                        GIAAVTEIPLGEIILFNIFYEFFTICTSIITEDKEGHLLHG

Caenorhabditis elegans        SIANATGIPLGQITMYNIFYEIFTVCTSVIAQDKDGHVFHA
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 22 – 142 Acid ceramidase subunit alpha
Active site 143 – 143 Nucleophile
Disulfide bond 31 – 340 Interchain (between alpha and beta subunits)
Mutagenesis 141 – 141 T -> A. Decreased rate of autocatalytic processing.
Mutagenesis 143 – 143 C -> A. Loss of autocatalytic processing. Loss of ceramidase activity.
Helix 136 – 139



Literature citations
Human acid ceramidase gene: novel mutations in Farber disease.
Zhang Z.; Mandal A.K.; Mital A.; Popescu N.; Zimonjic D.; Moser A.; Moser H.; Mukherjee A.B.;
Mol. Genet. Metab. 70:301-309(2000)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANTS FRBRL HIS-22; ASP-23; VAL-138; LYS-222 AND ASP-320; VARIANTS MET-72; VAL-93 AND ALA-246; The human acid ceramidase gene (ASAH): structure, chromosomal location, mutation analysis, and expression.
Li C.M.; Park J.H.; He X.; Levy B.; Chen F.; Arai K.; Adler D.A.; Disteche C.M.; Koch J.; Sandhoff K.; Schuchman E.H.;
Genomics 62:223-231(1999)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; FUNCTION; CATALYTIC ACTIVITY; PATHWAY; VARIANTS FRBRL VAL-138; GLY-254 AND ARG-362; CHARACTERIZATION OF VARIANTS FRBRL VAL-138; GLY-254 AND ARG-362; TISSUE SPECIFICITY;
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.