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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P06276: Variant p.Leu358Ile

Cholinesterase
Gene: BCHE
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Variant information Variant position: help 358 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 Isoleucine (I) at position 358 (L358I, p.Leu358Ile). 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 2 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 BCHED; BChE variant form; fluoride-resistant. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 358 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 602 The length of the canonical sequence.
Location on the sequence: help GQFKKTQILVGVNKDEGTAF L VYGAPGFSKDNNSIITRKEF 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                         GQFKKTQILVGVNKDEGTAFLVYGAPGFSKDNNSIITRKEF

Mouse                         GKVKKAQILVGVNKDEGTAFLVYGAPGFSKDNDSLITRKEF

Bovine                        GQFKKTQILVGVNKDEGTAFLVYGAPGFSKDNNSIITRKEF

Rabbit                        GQLKKTQILVGVNKDEGTAFLVYGAPGFSKDNTSIITRKEF

Cat                           GQFKKTQILVGVNKDEGTAFLVYGAPGFSKDNDSIITRKEF

Horse                         GQFKRTQILVGVNKDEGTAFLVYGAPGFSKDNNSIITRKEF

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 29 – 602 Cholinesterase
Active site 353 – 353 Charge relay system
Glycosylation 369 – 369 N-linked (GlcNAc...) (complex) asparagine
Helix 355 – 358



Literature citations
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;
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.