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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q13510: Variant p.Asn320Asp

Acid ceramidase
Gene: ASAH1
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Variant information Variant position: help 320 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 Asparagine (N) to Aspartate (D) at position 320 (N320D, p.Asn320Asp). 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 polar (N) to medium size and acidic (D) 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 FRBRL. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 320 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 ESLDVYELDAKQGRWYVVQT N YDRWKHPFFLDDRRTPAKMC 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                         ESLDVYELDAKQGRWYVVQTNYDRWKHPFFLDDRRTPAKMC

Chimpanzee                    ESLDVYELDAKQGRWYVVQTNYDRWKHPFFLDDRRTPAKMC

Mouse                         ESLDVYELDPKHGRWYVVQTNYDRWKNTLFIDDRRTPAKKC

Rat                           ESLDVYELDPKHGRWYVVQTNYDRWKNTLFLDDRRTPAKKC

Bovine                        QSLDIYELDPKHGRWYVVQTNYDRWKNPFFLDDRRTPAKMC

Caenorhabditis elegans        KTALLTEMATSPHGWYLLETNYDQGTEDLYLDDRDTPGFRC
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 143 – 395 Acid ceramidase subunit beta
Site 320 – 320 Important for catalytic activity
Site 333 – 333 Important for catalytic activity
Disulfide bond 31 – 340 Interchain (between alpha and beta subunits)
Mutagenesis 320 – 320 N -> A. Strongly decreased autocatalytic processing. Mildly decreased ceramidase activity.
Mutagenesis 333 – 333 R -> Q. Mildly decreased autocatalytic processing. Loss of ceramidase activity.



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; Molecular analysis of acid ceramidase deficiency in patients with Farber disease.
Bar J.; Linke T.; Ferlinz K.; Neumann U.; Schuchman E.H.; Sandhoff K.;
Hum. Mutat. 17:199-209(2001)
Cited for: VARIANTS FRBRL CYS-36 AND ASP-320;
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.