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Literature summary extracted from

  • Yardeni, T.; Jacobs, K.; Niethamer, T.K.; Ciccone, C.; Anikster, Y.; Kurochkina, N.; Gahl, W.A.; Huizing, M.
    Murine isoforms of UDP-GlcNAc 2-epimerase/ManNAc kinase: secondary structures, expression profiles, and response to ManNAc therapy (2013), Glycoconj. J., 30, 609-618.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.60 cloning of isozymes mGNE1 and mGNE2, DNA and amino acid sequence determination and analysis, quantitative real-time PCR expression analysis and sequence comparison Mus musculus
3.2.1.183 gene Gne1, sequence comparison with the human isozyme Gne1 Mus musculus
3.2.1.183 gene Gne2, sequence comparison with the human isozyme Gne2 Mus musculus

Protein Variants

EC Number Protein Variants Comment Organism
2.7.1.60 D176V oral administration of the sialic acid precursor N-acetylmannosamine rescues the muscle phenotype in the transgenic Gne p.D176V mouse and partially rescues the glomerular disease and early lethality in the knockin Gne mutant M712T mouse model Mus musculus
2.7.1.60 M712T naturally occuring mutation of isozyme mGne2. Tissues of the knock-in Gne p.M712T mouse model has similar mGne transcript expression levels among genotypes, indicating no effect of the mutation on mRNA expression, but the mutant shows increased activity in presence of N-acetylmannosamine compared to the wild-type enzyme. M712T mouse mutants die within 72 h of birth from severe glomerular disease Mus musculus
3.2.1.183 additional information tissues of the knock-in Gne p.M712T mouse model have similar mGne transcript expression levels among genotypes, indicating no effect of the mutation on mRNA expression Mus musculus

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.60 Mus musculus Q91WG8 two mouse Gne mRNA transcripts, encoding mGne1 and mGne2, gene Gne
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3.2.1.183 Mus musculus Q3UW64 isozyme mGne2
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3.2.1.183 Mus musculus Q91WG8 isozyme mGne1
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3.2.1.183 Mus musculus C57/BL6J Q3UW64 isozyme mGne2
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3.2.1.183 Mus musculus C57/BL6J Q91WG8 isozyme mGne1
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Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.183 additional information mGne1 is the ubiquitously expressed, major mouse isoform, isozyme mGne2 encoding transcript is differentially expressed, quantitative real-time PCR isozyme expression analysis Mus musculus
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3.2.1.183 additional information mGne2 encoding transcript is differentially expressed mGne2. Expression is significantly increased the first 2 days of life, possibly reflecting the high sialic acid demand during this period, quantitative real-time PCR isozyme expression analysis Mus musculus
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Subunits

EC Number Subunits Comment Organism
2.7.1.60 More the GNE enzyme consists of two enzymatic domains, sequence comparisons, secondary structures, and modeling of isozymes mGNE1 and mGNE2 Mus musculus
3.2.1.183 More isozyme Gne2, secondary structure comparison with the human isozyme Gne2, the isozymes differ most in the N-terminal extension of 31 amino acids Mus musculus
3.2.1.183 More isozyme mGne1, secondary structure comparison with the human isozyme hGne1. The four homologous amino acid changes between mGne1 and hGNE1 are all located in the ManNAc kinase activity encoding domain of Gne; N447S and L523M in an alpha-helix domain, and R481Q and I484V in a coil domain, overview Mus musculus

Synonyms

EC Number Synonyms Comment Organism
2.7.1.60 GNE
-
 Mus musculus
2.7.1.60 UDP-GlcNAc 2-epimerase/ManNAc kinase
-
 Mus musculus
3.2.1.183 GNE
-
 Mus musculus
3.2.1.183 UDP-GlcNAc 2-epimerase/ManNAc kinase
-
 Mus musculus

Expression

EC Number Organism Comment Expression
3.2.1.183 Mus musculus treatment of knock-in Gne p.M712T mouse model with N-acetylmannosamine, the Gne transcript expression, in particular mGne2, increases significantly, likely resulting in increased Gne enzymatic activities, especially in kidney and skeletal muscle up
3.2.1.183 Mus musculus treatment of knock-in Gne p.M712T mouse model with N-acetylmannosamine, the Gne transcript expression, in particular mGne2, increases significantly, likely resulting in increased Gne enzymatic activities, especiallyin kidney and skeletal muscle up

General Information

EC Number General Information Comment Organism
2.7.1.60 evolution sequence comparion and modeling of human hGNE1 and mouse mGne1 isozymmess, overview Mus musculus
2.7.1.60 malfunction non-allosteric GNE gene mutations cause the muscular disorder GNE myopathy, i.e. hereditary inclusion body myopathy. Complete Gne knockout is embryonically lethal. Transgenic mice expressing the human GNE cDNA with the D176V mutation, common among Japanese patients, in a mouse background with a disrupted mouse Gne gene recapitulates the adult onset features of human GNE myopathy with hyposialylation in serum and different organs. M712T mouse mutants die within 72 h of birth from severe glomerular disease. Mouse isozyme mutant phenotypes, overview Mus musculus
2.7.1.60 metabolism the bifunctional enzyme UDP-GlcNAc 2-epimerase/ManNAc kinase, GNE, catalyzes the first two committed steps in sialic acid synthesis Mus musculus
2.7.1.60 physiological function the mGne2 encoding transcript is differentially expressed and may act as a tissue-specific regulator of sialylation. mGne2 expression appears significantly increased the first 2 days of life, possibly reflecting the high sialic acid demand during this period Mus musculus
3.2.1.183 malfunction GNE myopathy is autosomal recessive inherited and characterized by adult onset, slowly progressive muscle weakness and atrophy Mus musculus
3.2.1.183 physiological function mGne2 encoding transcript may act as a tissue-specific regulator of sialylation Mus musculus