Variant position: 296 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 SAGLLSGYPFQCLGFTPEHQ RDFIARDLGPTLANSTHHNVR
Chimpanzee SAGLLSGYPFQCLGFTPEHQ RDFIARDLGPTLANSTHHNVR
Mouse TAGLFTGYPFQCLGFTPEHQ RDFISRDLGPALANSSH-DVK
Pig SAGLFTGYPFQCLGFTPEHQ RDFIARDPGPTLANSTHRNVR
Bovine TAGLLTGYPFQCLGFTPEHQ RDFIARDLGPILANSTHRDVR
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
309 – 309 N-linked (GlcNAc...) asparagine
292 – 301
Glucocerebrosidase mutations in Gaucher disease.
Beutler E.; Demina A.; Gelbart T.;
Mol. Med. 1:82-92(1994)
Cited for: VARIANTS GD ASP-215; THR-221; ARG-241; GLN-296; CYS-324; GLY-417 AND ASN-419;
Analysis and classification of 304 mutant alleles in patients with type 1 and type 3 Gaucher disease.
Koprivica V.; Stone D.L.; Park J.K.; Callahan M.; Frisch A.; Cohen I.J.; Tayebi N.; Sidransky E.;
Am. J. Hum. Genet. 66:1777-1786(2000)
Cited for: VARIANTS GD TRP-87; ASN-118; THR-129; ASP-156; GLN-159; TRP-159; LEU-170; ILE-173; CYS-209; PRO-209; SER-227; THR-229; PRO-235; ARG-241; ILE-252; GLN-296; CYS-324; THR-380; MET-408; SER-409; SER-416; LEU-433; TYR-438; HIS-448; PRO-483 AND CYS-502; VARIANT LYS-365; VARIANT GD2 GLN-159;
Glucocerebrosidase mutations in clinical and pathologically proven Parkinson's disease.
Neumann J.; Bras J.; Deas E.; O'Sullivan S.S.; Parkkinen L.; Lachmann R.H.; Li A.; Holton J.; Guerreiro R.; Paudel R.; Segarane B.; Singleton A.; Lees A.; Hardy J.; Houlden H.; Revesz T.; Wood N.W.;
Cited for: INVOLVEMENT IN PARKINSON DISEASE; VARIANTS GLU-46; CYS-170; GLU-232; GLN-296; SER-409; ALA-419; HIS-448; ASN-482; PRO-483; PRO-495; LEU-497 AND CYS-502;
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