Variant position: 358 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 602 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 GQFKKTQILVGVNKDEGTAF LVYGAPGFSKDNNSIITRKEF
Mouse GKVKKAQILVGVNKDEGTAF LVYGAPGFSKDNDSLITRKEF
Bovine GQFKKTQILVGVNKDEGTAF LVYGAPGFSKDNNSIITRKEF
Rabbit GQLKKTQILVGVNKDEGTAF LVYGAPGFSKDNTSIITRKEF
Cat GQFKKTQILVGVNKDEGTAF LVYGAPGFSKDNDSIITRKEF
Horse GQFKRTQILVGVNKDEGTAF LVYGAPGFSKDNNSIITRKEF
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
29 – 602 Cholinesterase
353 – 353 Charge relay system
369 – 369 N-linked (GlcNAc...) (complex) asparagine
355 – 358
Mutations of human butyrylcholinesterase gene in a family with hypocholinesterasemia.
Iida S.; Kinoshita M.; Fujii H.; Moriyama Y.; Nakamura Y.; Yura N.; Moriwaki K.;
Hum. Mutat. 6:349-351(1995)
Cited for: VARIANT BCHED ILE-358;
Human butyrylcholinesterase L330I mutation belongs to a fluoride-resistant gene, by expression in human fetal kidney cells.
Sudo K.; Maekawa M.; Akizuki S.; Magara T.; Ogasawara H.; Tanaka T.;
Biochem. Biophys. Res. Commun. 240:372-375(1997)
Cited for: VARIANT BUTYRYLCHOLINESTERASE DEFICIENCY ILE-358;
Genetic mutations of butyrylcholine esterase identified from phenotypic abnormalities in Japan.
Maekawa M.; Sudo K.; Dey D.C.; Ishikawa J.; Izumi M.; Kotani K.; Kanno T.;
Clin. Chem. 43:924-929(1997)
Cited for: VARIANTS BCHED ILE-32 DEL; MET-52; SER-128; PRO-278; ARG-295; ILE-358; ARG-393; SER-446; CYS-543 AND THR-567;
Three point mutations of human butyrylcholinesterase in a Japanese family and the alterations of three-dimensional structure.
Asanuma K.; Yagihashi A.; Uehara N.; Kida T.; Watanabe N.;
Clin. Chim. Acta 283:33-42(1999)
Cited for: VARIANTS BCHED ILE-358; ARG-393 AND CYS-543;
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