Variant position: 298 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 415 The length of the canonical sequence.
Location on the sequence:
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 NARNQNNYHCHCRIVLRSYD ACDTLRPRDVTFDPELVDPVV
Mouse NARNQNNYHCRCRIVLRSYD ACDTLRPRDVTFDPELVDPVV
Rat NARNQNNYHCRCRIVLRSYD ACDTLRPRDVTFDPELVDPVV
Pig NARNQNNYHCRCRIVLRSYD ACDTLRPRDVTFDPELVDPVV
Bovine NARNQNNYHCHCRIILRSYD ACDTLRPRDVTFDTELVDPVV
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.
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;
Five novel mutations in the lysosomal sialidase gene (NEU1) in type II sialidosis patients and assessment of their impact on enzyme activity and intracellular targeting using adenovirus-mediated expression.
Pattison S.; Pankarican M.; Rupar C.A.; Graham F.L.; Igdoura S.A.;
Hum. Mutat. 23:32-39(2004)
Cited for: VARIANTS SIALIDOSIS PRO-225; VAL-298 AND GLY-341; CATALYTIC ACTIVITY; SUBCELLULAR LOCATION; CHARACTERIZATION OF VARIANTS SIALIDOSIS PRO-225; VAL-298 AND GLY-341;
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