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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q99519: Variant p.Leu363Pro

Sialidase-1
Gene: NEU1
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Variant information Variant position: help 363 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 Leucine (L) to Proline (P) at position 363 (L363P, p.Leu363Pro). 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 Similar physico-chemical property. Both residues are medium size and hydrophobic. The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 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 SIALIDOSIS; infantile type 2; unable to reach the lysosomes. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 363 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 415 The length of the canonical sequence.
Location on the sequence: help NLTLRWSFSNGTSWRKETVQ L WPGPSGYSSLATLEGSMDGE 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                         NLTLRWSFSNGTSWRKETVQLWPGPSGYSSLATLEGSMDGE

Mouse                         NLTLRWSFSNGTSWQKERVQVWPGPSGYSSLTALENSTDGK

Rat                           NLTLRWSFSNGTFWQKERVQLWPGPSGYSSLTALENSTDGK

Pig                           NLTLRWSFSNGTSWRKETVQIWPGPSGYSSLATLEGSVGGE

Bovine                        NLTLRWSFSNGTSWRKETVQLWPGPSGYSSLTTLEGNVDGK
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 48 – 415 Sialidase-1
Active site 370 – 370 Nucleophile
Glycosylation 343 – 343 N-linked (GlcNAc...) asparagine
Glycosylation 352 – 352 N-linked (GlcNAc...) asparagine



Literature citations
Cloning, expression and chromosomal mapping of human lysosomal sialidase and characterization of mutations in sialidosis.
Pshezhetsky A.V.; Richard C.; Michaud L.; Igdoura S.A.; Wang S.; Elsliger M.-A.; Ou J.; Leclerc D.; Gravel R.A.; Dallaire L.; Potier M.;
Nat. Genet. 15:316-320(1997)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; CATALYTIC ACTIVITY; TISSUE SPECIFICITY; VARIANTS SIALIDOSIS TYR-260 AND PRO-363; Characterization of the sialidase molecular defects in sialidosis patients suggests the structural organization of the lysosomal multienzyme complex.
Lukong K.E.; Elsliger M.-A.; Chang Y.; Richard C.; Thomas G.; Carey W.; Tylki-Szymanska A.; Czartoryska B.; Buchholz T.; Rodriguez Criado G.; Palmeri S.; Pshezhetsky A.V.;
Hum. Mol. Genet. 9:1075-1085(2000)
Cited for: CHARACTERIZATION OF VARIANTS SIALIDOSIS VAL-68; GLY-182; ARG-227; TYR-260; PHE-270; VAL-298; SER-328 AND PRO-363; Novel mutations in lysosomal neuraminidase identify functional domains and determine clinical severity in sialidosis.
Bonten E.J.; Arts W.F.; Beck M.; Covanis A.; Donati M.A.; Parini R.; Zammarchi E.; d'Azzo A.;
Hum. Mol. Genet. 9:2715-2725(2000)
Cited for: VARIANTS SIALIDOSIS MET-54; VAL-68; ARG-91; GLY-182; ALA-219; ARG-227; HIS-231; TYR-260; PRO-270; SER-294; VAL-298; SER-328; GLN-335; PRO-363; CYS-370 AND HIS-TYR-400 INS; Mutations in sialidosis impair sialidase binding to the lysosomal multienzyme complex.
Lukong K.E.; Landry K.; Elsliger M.-A.; Chang Y.; Lefrancois S.; Morales C.R.; Pshezhetsky A.V.;
J. Biol. Chem. 276:17286-17290(2001)
Cited for: VARIANTS SIALIDOSIS VAL-68; GLY-182; ARG-227; ARG-240; TYR-260; PHE-270; VAL-298; SER-328 AND PRO-363; CHARACTERIZATION OF VARIANTS SIALIDOSIS VAL-68; GLY-182; ARG-227; TYR-260; PHE-270; VAL-298; SER-328 AND PRO-363;
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.