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UniProtKB/Swiss-Prot P06276: Variant p.Asp98Gly

Cholinesterase
Gene: BCHE
Variant information

Variant position:  98
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  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:  From Aspartate (D) to Glycine (G) at position 98 (D98G, p.Asp98Gly).
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:  Change from medium size and acidic (D) to glycine (G)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -1
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:  In BCHED; atypical form; reduced enzyme activity with butyrylthiocholine as substrate; inactive with butyrylthiocholine as substrate in the presence of V-62; 2-fold lower affinity for butyrylthiocholine; 10-fold lower affinity for butyrylthiocholine in the presence of V-62 or at homozygosity.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  98
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:   TKWSDIWNATKYANSCCQNI  D QSFPGFHGSEMWNPNTDLSE
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                         TKWSDIWNATKYANSCCQNIDQSFPGFHGSEMWNPNTDLSE

Mouse                         NKWPDIHNATQYANSCYQNIDQAFPGFQGSEMWNPNTNLSE

Bovine                        TKWPDIWNATKYANSCYQNTDQSFPGFLGSEMWNPNTDLSE

Rabbit                        TKWSDIWNATKYANSCCQNIDQSFPGFHGSEMWNPNTDLSE

Cat                           TKWSDIWNATKYANSCYQNADQSFPGFPGSEMWNPNTDLSE

Horse                         TKWSNIWNATKYANSCYQNTDQSFPGFLGSEMWNPNTELSE

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.

TypePositionsDescription
Chain 29 – 602 Cholinesterase
Binding site 110 – 110 Tacrine
Glycosylation 85 – 85 N-linked (GlcNAc...) (complex) asparagine
Disulfide bond 93 – 120


Literature citations

Identification of the structural mutation responsible for the dibucaine-resistant (atypical) variant form of human serum cholinesterase.
McGuire M.C.; Nogueira C.P.; Bartels C.F.; Lightstone H.; Hajra A.; van der Spek A.F.L.; Lockridge O.; la Du B.N.;
Proc. Natl. Acad. Sci. U.S.A. 86:953-957(1989)
Cited for: VARIANT BCHED GLY-98;

Structural basis of the butyrylcholinesterase H-variant segregating in two Danish families.
Jensen F.S.; Bartels C.F.; La Du B.N.;
Pharmacogenetics 2:234-240(1992)
Cited for: VARIANTS BCHED GLY-98 AND MET-170;

Characterization of an unstable variant (BChE115D) of human butyrylcholinesterase.
Primo-Parmo S.L.; Lightstone H.; La Du B.N.;
Pharmacogenetics 7:27-34(1997)
Cited for: VARIANTS BCHED GLY-98 AND ASP-143;

Naturally occurring mutation, Asp70His, in human butyrylcholinesterase.
Boeck A.T.; Fry D.L.; Sastre A.; Lockridge O.;
Ann. Clin. Biochem. 39:154-156(2002)
Cited for: VARIANTS BCHED GLY-98; HIS-98; MET-271 AND THR-567;

Four new mutations in the BCHE gene of human butyrylcholinesterase in a Brazilian blood donor sample.
Souza R.L.; Mikami L.R.; Maegawa R.O.; Chautard-Freire-Maia E.A.;
Mol. Genet. Metab. 84:349-353(2005)
Cited for: VARIANT MET-127; VARIANTS BCHED GLY-98; ARG-103 AND ASP-118;

Characterization of a novel butyrylcholinesterase point mutation (p.Ala34Val), 'silent' with mivacurium.
Delacour H.; Lushchekina S.; Mabboux I.; Ceppa F.; Masson P.; Schopfer L.M.; Lockridge O.;
Biochem. Pharmacol. 92:476-483(2014)
Cited for: VARIANTS BCHED VAL-62 AND GLY-98; CHARACTERIZATION OF VARIANTS BCHED VAL-62 AND GLY-98;

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.