Home  |  Contact

UniProtKB/Swiss-Prot Q14376: Variant p.Leu183Pro

UDP-glucose 4-epimerase
Gene: GALE
Chromosomal location: 1p35.1-p36.12
Variant information

Variant position:  183
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Disease [Disclaimer]
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants implicated in disease according to literature reports.
  • Polymorphism: Variants not reported to be implicated in disease.
  • Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:  From Leucine (L) to Proline (P) at position 183 (L183P, p.Leu183Pro).
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:  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:  -3
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

Involvement in disease:  Epimerase-deficiency galactosemia (EDG) [MIM:230350]: Clinical features include early-onset cataracts, liver damage, deafness and mental retardation. There are two clinically distinct forms of EDG. (1) A benign, or 'peripheral' form with no detectable GALE activity in red blood cells and characterized by mild symptoms. Some patients may suffer no symptoms beyond raised levels of galactose-1-phosphate in the blood. (2) A much rarer 'generalized' form with undetectable levels of GALE activity in all tissues and resulting in severe features such as restricted growth and mental development. {ECO:0000269|PubMed:11279193, ECO:0000269|PubMed:11903335, ECO:0000269|PubMed:15639193, ECO:0000269|PubMed:16301867, ECO:0000269|PubMed:16302980, ECO:0000269|PubMed:9326324, ECO:0000269|PubMed:9538513, ECO:0000269|PubMed:9973283}. Note=The disease is caused by mutations affecting the gene represented in this entry.
The name and a short description of the disease associated with the variant. For more information about the disease, the user can refer to OMIM, following the link provided after the disease acronym.

Variant description:  In EDG; peripheral; 3-fold decrease in UDP-galactose epimerization activity.
Any additional useful information about the variant.

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



Sequence information

Variant position:  183
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  348
The length of the canonical sequence.

Location on the sequence:   FIEEMIRDLCQADKTWNAVL  L RYFNPTGAHASGCIGEDPQG
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                         FIEEMIRDLCQADKTWNAVLLRYFNPTGAHASGCIGEDPQG

Mouse                         FIEEMIRDLCRADTAWNAVLLRYFNPIGAHASGRIGEDPQG

Rat                           FIEEMIQDLCRADTAWNAVLLRYFIPIGAHRSARIGEDPQG

Bovine                        FIEEMIRDLCQADKAWNAVLLRYFNPIGAHASGCIGEDPQG

Caenorhabditis elegans        MMEQILIDVGKANPEWNVVLLRYFNPVGAHKSGLIGEDPKG

Drosophila                    FTEEILKDLCKSDKRWAVVSLRYFNPVGAHISGRIGEDPNG

Slime mold                    YVEGILQDLCASDPEWNCIMLRYFNPVGAHPSGLIGEDPKD

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 1 – 348 UDP-glucose 4-epimerase
Binding site 185 – 185 NAD
Beta strand 179 – 185


Literature citations

Characterization of two mutations associated with epimerase-deficiency galactosemia, by use of a yeast expression system for human UDP-galactose-4-epimerase.
Quimby B.B.; Alano A.; Almashanu S.; Desandro A.M.; Cowan T.M.; Fridovich-Keil J.L.;
Am. J. Hum. Genet. 61:590-598(1997)
Cited for: VARIANTS EDG SER-34 AND PRO-183; VARIANT VAL-180;

A PCR-based method for detecting known mutations in the human UDP galactose-4'-epimerase gene associated with epimerase-deficiency galactosemia.
Henderson J.M.; Huguenin S.M.; Cowan T.M.; Fridovich-Keil J.L.;
Clin. Genet. 60:350-355(2001)
Cited for: VARIANTS EDG SER-34; GLU-90; MET-94; GLY-103; PRO-183; ARG-257; MET-313; GLU-319 AND HIS-335;

Functional analysis of disease-causing mutations in human UDP-galactose 4-epimerase.
Timson D.J.;
FEBS J. 272:6170-6177(2005)
Cited for: BIOPHYSICOCHEMICAL PROPERTIES; CHARACTERIZATION OF VARIANTS EDG SER-34; GLU-90; MET-94; GLY-103; PRO-183; ARG-257; MET-313; GLU-319 AND HIS-335; SUBUNIT;

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.