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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q14376: Variant p.Arg51Trp

UDP-glucose 4-epimerase
Gene: GALE
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Variant information Variant position: help 51 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 Arginine (R) to Tryptophan (W) at position 51 (R51W, p.Arg51Trp). 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 Change from large size and basic (R) to large size and aromatic (W) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -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
Variant description: help In THC13; likely pathogenic; decreased UDP-galactose epimerization activity; decreased UDP-N-acetylglucosamine epimerase activity; reduced NAD+ binding; decreased thermal stability. Any additional useful information about the variant.


Sequence information Variant position: help 51 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 348 The length of the canonical sequence.
Location on the sequence: help VIDNFHNAFRGGGSLPESLR R VQELTGRSVEFEEMDILDQG 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                         VIDNFHNAFRGGGSLPES--LRRVQELTGRSVEFEEMDILDQG

Mouse                         VIDNFHNAIRGEDSMPES--LRRVQELTGRSVEFEEMDILD

Rat                           VIDNFHNSIRGEDSMPES--LRRVQELTGRSVEFEEMDILD

Bovine                        VIDNFHNAIRGGGSMPES--LRRVQDLTGRSVEFEEMDILD

Caenorhabditis elegans        CIDNFANAISVTDEHGNAISLKRVAQLTGKDVPFQNVDVCD

Drosophila                    CVDNLCNAYSSGAKLPEA--LSRVQEITGKKVNFYRVDITD

Slime mold                    IVDNLSN------SSLEA--IKRVESITGKEIEFHHVDIMN
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 1 – 348 UDP-glucose 4-epimerase
Alternative sequence 1 – 79 MAEKVLVTGGAGYIGSHTVLELLEAGYLPVVIDNFHNAFRGGGSLPESLRRVQELTGRSVEFEEMDILDQGALQRLFKK -> MSPLQ. In isoform 2.
Helix 47 – 56



Literature citations
Inherited thrombocytopenia associated with mutation of UDP-galactose-4-epimerase (GALE).
Seo A.; Gulsuner S.; Pierce S.; Ben-Harosh M.; Shalev H.; Walsh T.; Krasnov T.; Dgany O.; Doulatov S.; Tamary H.; Shimamura A.; King M.C.;
Hum. Mol. Genet. 28:133-142(2019)
Cited for: VARIANT THC13 TRP-51; CHARACTERIZATION OF VARIANT THC13 TRP-51; INVOLVEMENT IN THC13;
A case of UDP-galactose 4'-epimerase deficiency associated with dyshematopoiesis and atrioventricular valve malformations: An exceptional clinical phenotype explained by altered N-glycosylation with relative preservation of the Leloir pathway.
Febres-Aldana C.A.; Pelaez L.; Wright M.S.; Maher O.M.; Febres-Aldana A.J.; Sasaki J.; Jayakar P.; Jayakar A.; Diaz-Barbosa M.; Janvier M.; Totapally B.; Salyakina D.; Galvez-Silva J.R.;
Mol. Syndromol. 11:320-329(2020)
Cited for: VARIANTS THC13 TRP-51 AND ASP-237; INVOLVEMENT IN THC13;
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.