Search results for GYG2

Showing 22 results out of 31

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Types

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Protein (7 results from a total of 7)

Identifier: R-HSA-70205
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: GYG2: O15488
Identifier: R-HSA-70289
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: GYG2: O15488
Identifier: R-HSA-70176
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: GYG2: O15488
Identifier: R-HSA-3777097
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: GYG2: O15488
Identifier: R-HSA-70188
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: GYG2: O15488
Identifier: R-HSA-70300
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: GYG2: O15488
Identifier: R-HSA-70181
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: GYG2: O15488

Complex (7 results from a total of 14)

Identifier: R-HSA-70214
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-3781017
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-3777094
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-3780991
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-3322065
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-3322031
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-3777104
Species: Homo sapiens
Compartment: cytosol

Reaction (7 results from a total of 9)

Identifier: R-HSA-3322014
Species: Homo sapiens
Compartment: cytosol
Glycogenin 2 (GYG2) catalyzes its autoglycosylation reaction with UDP-glucose to form oligo (1,4)-alpha-D-glucosyl GYG2 (Mu et al. 1997). The oligosaccharide is annotated here as containing four glucose residues. Glycogenin occurs as a homodimer complexed with two molecules of glycogen synthase 1 (GYS2), here in a unphosphorylated (a) form (Roach et al. 2012).
Identifier: R-HSA-3322019
Species: Homo sapiens
Compartment: cytosol
Glycogenin 2 (GYG2) catalyzes its autoglycosylation reaction with UDP-glucose to form oligo (1,4)-alpha-D-glucosyl GYG2 (Mu et al. 1997). The oligosaccharide is annotated here as containing four glucose residues. Glycogenin occurs as a homodimer complexed with two molecules of glycogen synthase 1 (GYS2), here in a phosphorylated (b) form (Roach et al. 2012).
Identifier: R-HSA-3781011
Species: Homo sapiens
Compartment: cytosol
EPM2A (laforin), associated with PPP1R3C (protein phosphatase 1 regulatory subunit 3C, PTG) and phosphoglycogen-GYG2 in a cytosolic glycogen particle, catalyzes the dephosphorylation of phosphoglycogen (Tagliabracci et al. 2007). This reaction is inferred from the activity of EPM2A on phosphoglycogen-GYG1, and from the fact that in the absence of normal EPM2A activity, abnormally phosphorylated forms of both glycogen-GYG1 and glycogen-GYG2 accumulate in cells. The catalytically active form of EPM2A has been shown to be a homodimer (Raththagala et al. 2015; Sankhala et al. 2015).
Identifier: R-HSA-3322009
Species: Homo sapiens
Compartment: cytosol
Unphosphorylated glycogen synthase 2 (GYS2-a) complexed with oligo-D-glucose-GYG2 catalyzes the polyglucosylation of the latter. (Here the addition of four glucose residues is annotated.) (Orho et al. 1998; Roach et al. 2012).
Identifier: R-HSA-3781021
Species: Homo sapiens
Compartment: cytosol
EPM2A (laforin) dimer binds to the PPP1R3C:phosphoglycogen-GYG2 (glycogenin 2) complex, probably through interactions with the PPP1R3C (PTG) and glycogen moieties of the complex (Worby et al. 2008). This reaction is inferred from the properties of the better studied muscle glycogen particles containing GYG1 (glycogenin 1), and from the fact that in the absence of EMP2A (laforin) function, liver glycogen particles become abnormal in the same way as do muscle particles.
Identifier: R-HSA-3780994
Species: Homo sapiens
Compartment: cytosol
Glycogen synthase 2 (GYS2) catalyzes the incorporation of phosphoglucose into the glycogen-GYG1 molecules with which it is associated in a cytosolic glycogen granule. This reaction occurs at a low rate, yielding approximately one molecule of glucose phosphorylated at its C2, C3, or C6 positions incorporated into a growing glycogen polymer per ten thousand glucose molecules incorporated (DePaoli-Roach et al. 2015; Irimia et al. 2015; Nitschke et al. 2013; Tagliabracci et al. 2011). The function of these small amounts of phosphoglucose in normal glycogen remains to be established. This reaction has been characterized in muscle cells, where it is catalyzed by the homologous GYS1 enzyme. The occurrence of the reaction in liver, catalyzed by GYS2, can be inferred from the fact that in the absence of the enzyme EMP2A (laforin) that removes these phosphate groups, abnormally phosphorylated glycogen accumulates in both tissues (Worby et al. 2008).
Identifier: R-HSA-3322016
Species: Homo sapiens
Compartment: cytosol
Cytosolic glycogen branching enzyme (GBE1) associated with glycogen granules transfers terminal alpha(1,4) glucose blocks to form alpha(1,6) branches on growing glycogen molecules formed on glycogenin 2 (GYG2) complexed with unphosphorylated glycogen synthase 2 (GYS2-a) (Bao et al. 1996; Roach et al. 2012).

Icon (1 results from a total of 1)

GYG

Species: Homo sapiens
Graphic representation of Glycogenin-1 and/or Glycogenin-2.
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