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:
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 TKWSDIWNATKYANSCCQNI DQSFPGFHGSEMWNPNTDLSE
Mouse NKWPDIHNATQYANSCYQNI DQAFPGFQGSEMWNPNTNLSE
Bovine TKWPDIWNATKYANSCYQNT DQSFPGFLGSEMWNPNTDLSE
Rabbit TKWSDIWNATKYANSCCQNI DQSFPGFHGSEMWNPNTDLSE
Cat TKWSDIWNATKYANSCYQNA DQSFPGFPGSEMWNPNTDLSE
Horse TKWSNIWNATKYANSCYQNT DQSFPGFLGSEMWNPNTELSE
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
110 – 110 Tacrine
85 – 85 N-linked (GlcNAc...) (complex) asparagine
93 – 120
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.;
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.;
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;
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.