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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9Y223: Variant p.Gly576Glu

Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
Gene: GNE
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Variant information Variant position: help 576 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 Glycine (G) to Glutamate (E) at position 576 (G576E, p.Gly576Glu). 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 glycine (G) to medium size and acidic (E) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -2 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 NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 576 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 722 The length of the canonical sequence.
Location on the sequence: help LIHGSSFCAAELGHLVVSLD G PDCSCGSHGCIEAYASGMAL 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                         LIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMAL

Mouse                         LIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMAL

Rat                           LIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMAL
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 – 722 Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
Region 406 – 722 N-acetylmannosamine kinase
Binding site 566 – 566
Binding site 569 – 569
Binding site 569 – 569
Binding site 569 – 569
Binding site 579 – 579
Binding site 581 – 581
Binding site 586 – 586
Binding site 588 – 588
Binding site 588 – 588



Literature citations
The UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase gene is mutated in recessive hereditary inclusion body myopathy.
Eisenberg I.; Avidan N.; Potikha T.; Hochner H.; Chen M.; Olender T.; Barash M.; Shemesh M.; Sadeh M.; Grabov-Nardini G.; Shmilevich I.; Friedmann A.; Karpati G.; Bradley W.G.; Baumbach L.; Lancet D.; Asher E.B.; Beckmann J.S.; Argov Z.; Mitrani-Rosenbaum S.;
Nat. Genet. 29:83-87(2001)
Cited for: VARIANTS NM ASN-225; GLN-246; GLU-576; THR-631; MET-696 AND THR-712; Four novel mutations associated with autosomal recessive inclusion body myopathy (MIM: 600737).
Darvish D.; Vahedifar P.; Huo Y.;
Mol. Genet. Metab. 77:252-256(2002)
Cited for: VARIANTS NM ASN-225; GLN-246; TRP-246; VAL-460; VAL-524; LEU-572; GLU-576; THR-631; HIS-675; MET-696 AND THR-712; Mutations spectrum of GNE in hereditary inclusion body myopathy sparing the quadriceps.
Eisenberg I.; Grabov-Nardini G.; Hochner H.; Korner M.; Sadeh M.; Bertorini T.; Bushby K.; Castellan C.; Felice K.; Mendell J.; Merlini L.; Shilling C.; Wirguin I.; Argov Z.; Mitrani-Rosenbaum S.;
Hum. Mutat. 21:99-99(2003)
Cited for: VARIANTS NM LEU-36; PHE-200; ASN-225; GLN-246; VAL-303; TYR-378; VAL-460; CYS-528; THR-557; LEU-572; GLU-576; THR-587; THR-631; VAL-631; MET-696 AND THR-712; Influence of UDP-GlcNAc 2-epimerase/ManNAc kinase mutant proteins on hereditary inclusion body myopathy.
Penner J.; Mantey L.R.; Elgavish S.; Ghaderi D.; Cirak S.; Berger M.; Krause S.; Lucka L.; Voit T.; Mitrani-Rosenbaum S.; Hinderlich S.;
Biochemistry 45:2968-2977(2006)
Cited for: CHARACTERIZATION OF VARIANTS NM TYR-378; SER-519; CYS-528; GLU-576 AND THR-587; FUNCTION; CATALYTIC ACTIVITY; PATHWAY;
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.