Sequence information
Variant position: 138 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 395 The length of the canonical sequence.
Location on the sequence:
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: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human GIAAVTDIPLGEIISFNIFYE LFTICTSIVAEDKKGHLIHG
Chimpanzee GIAAVTDIPLGEIISFNIFYE LFTICTSIVAEDKKGHLIHG
Mouse GIADVTGIPLGEIISFNIFYE LFTMCTSIITEDEKGHLLHG
Rat GIADVTGIPLGEIISFNIFYE LFTMCTSIITEDGKGHLLHG
Bovine GIAAVTEIPLGEIILFNIFYE FFTICTSIITEDKEGHLLHG
Caenorhabditis elegans SIANATGIPLGQITMYNIFYE IFTVCTSVIAQDKDGHVFHA
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.
Type Positions Description
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.