Variant position: 55 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 536 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 SWASGARPCIPKSFGYSSVV CVCNATYCDSFDPPTFPALGT
Chimpanzee SWASGARPCIPKSFGYSSVV CVCNATYCDSFDPPTFPALGT
Mouse SWAYGAQPCIPKSFGYSSVV CVCNASYCDSLDPVTLPALGT
Pig SWASGARPCSPKSFGYSSVV CVCNATYCDSLDPLTLPDPGT
Bovine SWVSGARPCSPKSFGYSSVV CVCNGTYCDSLDPLTLPDPGT
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
40 – 536 Lysosomal acid glucosylceramidase
58 – 58 N-linked (GlcNAc...) asparagine
43 – 55
1 – 161 Missing. In isoform 3.
1 – 87 Missing. In isoform 4.
43 – 43 C -> S. Loss of glucosylceramidase activity.
57 – 57 C -> S. Loss of glucosylceramidase activity.
62 – 62 C -> S. Loss of glucosylceramidase activity.
54 – 57
Analyses of variant acid beta-glucosidases: effects of Gaucher disease mutations.
Liou B.; Kazimierczuk A.; Zhang M.; Scott C.R.; Hegde R.S.; Grabowski G.A.;
J. Biol. Chem. 281:4242-4253(2006)
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 40-536; CATALYTIC ACTIVITY; PATHWAY; CHARACTERIZATION OF VARIANTS GD SER-55; GLN-87; ASN-118; LEU-161; VAL-162; VAL-166; ASN-200; PHE-213; PHE-224; GLU-232; GLU-237; LEU-298; ILE-303; CYS-343; ILE-362; LYS-365; GLY-381; LYS-388; TRP-392; CYS-402; SER-409; VAL-410; HIS-419; LYS-421; ARG-429; LEU-433; SER-436; ASN-438; HIS-448; VAL-455; PRO-483; PRO-500; CYS-502 AND PRO-502; CHARACTERIZATION OF VARIANT GD2 GLN-159; MUTAGENESIS OF CYS-43; CYS-57 AND CYS-62;
Variant Gaucher disease characterized by dysmorphic features, absence of cardiovascular involvement, laryngospasm, and compound heterozygosity for a novel mutation (D409H/C16S).
Bodamer O.A.F.; Church H.J.; Cooper A.; Wraith J.E.; Scott C.R.; Scaglia F.;
Am. J. Med. Genet. 109:328-331(2002)
Cited for: VARIANTS GD SER-55 AND HIS-448;
Homozygous loss of a cysteine residue in the glucocerebrosidase gene results in Gaucher's disease with a hydropic phenotype.
Church H.J.; Cooper A.; Stewart F.; Thornton C.M.; Wraith J.E.;
Eur. J. Hum. Genet. 12:975-978(2004)
Cited for: VARIANT GD SER-55;
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