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Literature summary for 1.2.1.12 extracted from

  • Park, J.; Han, D.; Kim, K.; Kang, Y.; Kim, Y.
    O-GlcNAcylation disrupts glyceraldehyde-3-phosphate dehydrogenase homo-tetramer formation and mediates its nuclear translocation (2009), Biochim. Biophys. Acta, 1794, 254-262.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in INS-1 cells Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
T227A mutation at site of O-GlcNAcylation. Mutation induces the cytoplasmic accumulation of glyceraldehyde 3-phosphate dehydrogenase Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm O-GlcNAcylation at residue T227 interrupts the hydrophobic interfaces formed between the enzyme monomers in its terameric state and allows for nucleic translocation of the cytoplasmic enzyme Rattus norvegicus 5737
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nucleus O-GlcNAcylation at residue T227 interrupts the hydrophobic interfaces formed between the enzyme monomers in its terameric state and allows for nucleic translocation of the cytoplasmic enzyme Rattus norvegicus 5634
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Organism

Organism UniProt Comment Textmining
Rattus norvegicus P04797
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-

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information O-GlcNAcylation at residue T227 interrupts the hydrophobic interfaces formed between the enzyme monomers in its terameric state and allows for nucleic translocation of the cytoplasmic enzyme Rattus norvegicus