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Literature summary for 6.3.1.2 extracted from

  • Matthews, G.D.; Gur, N.; Koopman, W.J.; Pines, O.; Vardimon, L.
    Weak mitochondrial targeting sequence determines tissue-specific subcellular localization of glutamine synthetase in liver and brain cells (2010), J. Cell Sci., 123, 351-359.
    View publication on PubMed
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Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion the N-terminus of glutamine synthetase, which constitutes a weak mitochondrial targeting signal, is sufficient to direct a chimeric protein to the mitochondria in hepatocytes and to the cytoplasm in astrocytes. The mitochondrial membrane potential in hepatocytes is more negative than in astrocytes Gallus gallus 5739
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Organism

Organism UniProt Comment Textmining
Gallus gallus
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Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification the N-terminus of glutamine synthetase, which constitutes a weak mitochondrial targeting signal, is sufficient to direct a chimeric protein to the mitochondria in hepatocytes and to the cytoplasm in astrocytes Gallus gallus

Source Tissue

Source Tissue Comment Organism Textmining
brain glutamine synthetase transcripts of liver and brain cells are identical, no difference in the amino acid sequence of the protein. The N-terminus of glutamine synthetase, which constitutes a weak mitochondrial targeting signal, is sufficient to direct a chimeric protein to the mitochondria in hepatocytes and to the cytoplasm in astrocytes Gallus gallus
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liver glutamine synthetase transcripts of liver and brain cells are identical, no difference in the amino acid sequence of the protein. The N-terminus of glutamine synthetase, which constitutes a weak mitochondrial targeting signal, is sufficient to direct a chimeric protein to the mitochondria in hepatocytes and to the cytoplasm in astrocytes Gallus gallus
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