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Literature summary extracted from

  • Satir, B.H.; Srisomsap, C.; Reichman, M.; Marchase, R.B.
    Parafusin, an exocytic-sensitive phosphoprotein, is the primary acceptor for the glucosylphosphotransferase in Paramecium tetraurelia and rat liver (1990), J. Cell Biol., 111, 901-907.
    View publication on PubMedView publication on EuropePMC

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.8.19 membrane
-
 Rattus norvegicus 16020
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2.7.8.19 membrane membrane-associated enzyme, faces the cytosol Paramecium tetraurelia 16020
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.8.19 UDP-glucose + parafusin Paramecium tetraurelia reversible phosphoglycosylation of parafusin could play an important role in signal transduction during secretion in Paramecium tetraurelia, a protein evidently associated with membrane fusion during exocytosis ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.8.19 Paramecium tetraurelia
-
-
-
2.7.8.19 Rattus norvegicus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.8.19 UDP-glucose + glycoprotein D-mannose the 35S-labeled phosphorothioate analogue of UDP-glucose is used by this enzyme with high efficiency Rattus norvegicus UMP + glycoprotein 6-(D-glucose-1-phospho)-D-mannose
-
 ?
2.7.8.19 UDP-glucose + glycoprotein D-mannose the 35S-labeled phosphorothioate analogue of UDP-glucose is used by this enzyme with high efficiency Paramecium tetraurelia UMP + glycoprotein 6-(D-glucose-1-phospho)-D-mannose
-
 ?
2.7.8.19 UDP-glucose + parafusin parafusin is the principal acceptor for GlcPTase in Paramecium tetraurelia and it is evidently associated with membrane fusion during exocytosis, its cytoplasmic glycosylation by GlcPTase has a regulatory role Paramecium tetraurelia ?
-
 ?
2.7.8.19 UDP-glucose + parafusin reversible phosphoglycosylation of parafusin could play an important role in signal transduction during secretion in Paramecium tetraurelia, a protein evidently associated with membrane fusion during exocytosis Paramecium tetraurelia ?
-
 ?