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UniProtKB/Swiss-Prot P04062: Variant p.Lys237Glu

Lysosomal acid glucosylceramidase
Gene: GBA
Variant information

Variant position:  237
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 Lysine (K) to Glutamate (E) at position 237 (K237E, p.Lys237Glu).
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 large size and basic (K) to medium size and acidic (E)
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 GD; severe; loss of glucosylceramidase activity; increases susceptibility to proteolytic degradation.
Any additional useful information about the variant.

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



Sequence information

Variant position:  237
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:   PWTSPTWLKTNGAVNGKGSL  K GQPGDIYHQTWARYFVKFLD
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                         PWTSPTWLKTNGAVNGKGSLKGQPGDIYHQTWARYFVKFLD

Chimpanzee                    PWTSPTWLKTNGAVNGKGSLKGQPGDIYHQTWARYFVKFLD

Mouse                         PWTSPTWLKTNGRVNGKGSLKGQPGDIFHQTWANYFVKFLD

Pig                           PWTSPTWLKTNGAVNGKGTLKGHPGDRYHQTWAKYFVKFLD

Bovine                        PWTSPTWLKTNGAVNGKGTLKGQAGDLYHKTWARYFVKFLD

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 40 – 536 Lysosomal acid glucosylceramidase
Beta strand 236 – 238


Literature citations

Analyses of variant acid beta-glucosidases: effects of Gaucher disease mutations.
Liou B.; Kazimierczuk A.; Zhang M.; Scott C.R.; Hegde R.S.; Grabowski G.A.;
J. Biol. Chem. 281:4242-4253(2006)
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 40-536; CATALYTIC ACTIVITY; PATHWAY; CHARACTERIZATION OF VARIANTS GD SER-55; GLN-87; ASN-118; LEU-161; VAL-162; VAL-166; ASN-200; PHE-213; PHE-224; GLU-232; GLU-237; LEU-298; ILE-303; CYS-343; ILE-362; LYS-365; GLY-381; LYS-388; TRP-392; CYS-402; SER-409; VAL-410; HIS-419; LYS-421; ARG-429; LEU-433; SER-436; ASN-438; HIS-448; VAL-455; PRO-483; PRO-500; CYS-502 AND PRO-502; CHARACTERIZATION OF VARIANT GD2 GLN-159; MUTAGENESIS OF CYS-43; CYS-57 AND CYS-62;

The identification of eight novel glucocerebrosidase (GBA) mutations in patients with Gaucher disease.
Orvisky E.; Park J.K.; Parker A.; Walker J.M.; Martin B.M.; Stubblefield B.K.; Uyama E.; Tayebi N.; Sidransky E.;
Hum. Mutat. 19:458-459(2002)
Cited for: VARIANTS GD GLU-175; PRO-201; GLU-237 AND PHE-441; VARIANT GDPL LEU-290;

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.