node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
EPM2A | GYG1 | ENSP00000356489 | ENSP00000340736 | Laforin; Plays an important role in preventing glycogen hyperphosphorylation and the formation of insoluble aggregates, via its activity as glycogen phosphatase, and by promoting the ubiquitination of proteins involved in glycogen metabolism via its interaction with the E3 ubiquitin ligase NHLRC1/malin. Shows strong phosphatase activity towards complex carbohydrates in vitro, avoiding glycogen hyperphosphorylation which is associated with reduced branching and formation of insoluble aggregates. Dephosphorylates phosphotyrosine and synthetic substrates, such as para- nitrophenylphosphat [...] | Glycogenin-1; Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase. Belongs to the glycosyltransferase 8 family. Glycogenin subfamily. | 0.773 |
EPM2A | GYS1 | ENSP00000356489 | ENSP00000317904 | Laforin; Plays an important role in preventing glycogen hyperphosphorylation and the formation of insoluble aggregates, via its activity as glycogen phosphatase, and by promoting the ubiquitination of proteins involved in glycogen metabolism via its interaction with the E3 ubiquitin ligase NHLRC1/malin. Shows strong phosphatase activity towards complex carbohydrates in vitro, avoiding glycogen hyperphosphorylation which is associated with reduced branching and formation of insoluble aggregates. Dephosphorylates phosphotyrosine and synthetic substrates, such as para- nitrophenylphosphat [...] | Glycogen [starch] synthase, muscle; Transfers the glycosyl residue from UDP-Glc to the non- reducing end of alpha-1,4-glucan. | 0.965 |
EPM2A | GYS2 | ENSP00000356489 | ENSP00000261195 | Laforin; Plays an important role in preventing glycogen hyperphosphorylation and the formation of insoluble aggregates, via its activity as glycogen phosphatase, and by promoting the ubiquitination of proteins involved in glycogen metabolism via its interaction with the E3 ubiquitin ligase NHLRC1/malin. Shows strong phosphatase activity towards complex carbohydrates in vitro, avoiding glycogen hyperphosphorylation which is associated with reduced branching and formation of insoluble aggregates. Dephosphorylates phosphotyrosine and synthetic substrates, such as para- nitrophenylphosphat [...] | Glycogen [starch] synthase, liver; Transfers the glycosyl residue from UDP-Glc to the non- reducing end of alpha-1,4-glucan. | 0.744 |
EPM2A | NHLRC1 | ENSP00000356489 | ENSP00000345464 | Laforin; Plays an important role in preventing glycogen hyperphosphorylation and the formation of insoluble aggregates, via its activity as glycogen phosphatase, and by promoting the ubiquitination of proteins involved in glycogen metabolism via its interaction with the E3 ubiquitin ligase NHLRC1/malin. Shows strong phosphatase activity towards complex carbohydrates in vitro, avoiding glycogen hyperphosphorylation which is associated with reduced branching and formation of insoluble aggregates. Dephosphorylates phosphotyrosine and synthetic substrates, such as para- nitrophenylphosphat [...] | E3 ubiquitin-protein ligase NHLRC1; E3 ubiquitin-protein ligase. Together with the phosphatase EPM2A/laforin, appears to be involved in the clearance of toxic polyglucosan and protein aggregates via multiple pathways. In complex with EPM2A/laforin and HSP70, suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system (UPS). Ubiquitinates the glycogen-targeting protein phosphatase subunits PPP1R3C/PTG and PPP1R3D in a laforin- dependent manner and targets them for proteasome-dependent degradation, thus decreasing glycogen [...] | 0.999 |
EPM2A | PPP1R3C | ENSP00000356489 | ENSP00000238994 | Laforin; Plays an important role in preventing glycogen hyperphosphorylation and the formation of insoluble aggregates, via its activity as glycogen phosphatase, and by promoting the ubiquitination of proteins involved in glycogen metabolism via its interaction with the E3 ubiquitin ligase NHLRC1/malin. Shows strong phosphatase activity towards complex carbohydrates in vitro, avoiding glycogen hyperphosphorylation which is associated with reduced branching and formation of insoluble aggregates. Dephosphorylates phosphotyrosine and synthetic substrates, such as para- nitrophenylphosphat [...] | Protein phosphatase 1 regulatory subunit 3C; Acts as a glycogen-targeting subunit for PP1 and regulates its activity. Activates glycogen synthase, reduces glycogen phosphorylase activity and limits glycogen breakdown. Dramatically increases basal and insulin-stimulated glycogen synthesis upon overexpression in a variety of cell types. | 0.987 |
EPM2A | PPP1R3D | ENSP00000356489 | ENSP00000360035 | Laforin; Plays an important role in preventing glycogen hyperphosphorylation and the formation of insoluble aggregates, via its activity as glycogen phosphatase, and by promoting the ubiquitination of proteins involved in glycogen metabolism via its interaction with the E3 ubiquitin ligase NHLRC1/malin. Shows strong phosphatase activity towards complex carbohydrates in vitro, avoiding glycogen hyperphosphorylation which is associated with reduced branching and formation of insoluble aggregates. Dephosphorylates phosphotyrosine and synthetic substrates, such as para- nitrophenylphosphat [...] | Protein phosphatase 1 regulatory subunit 3D; Seems to act as a glycogen-targeting subunit for PP1. PP1 is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. | 0.742 |
GYG1 | EPM2A | ENSP00000340736 | ENSP00000356489 | Glycogenin-1; Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase. Belongs to the glycosyltransferase 8 family. Glycogenin subfamily. | Laforin; Plays an important role in preventing glycogen hyperphosphorylation and the formation of insoluble aggregates, via its activity as glycogen phosphatase, and by promoting the ubiquitination of proteins involved in glycogen metabolism via its interaction with the E3 ubiquitin ligase NHLRC1/malin. Shows strong phosphatase activity towards complex carbohydrates in vitro, avoiding glycogen hyperphosphorylation which is associated with reduced branching and formation of insoluble aggregates. Dephosphorylates phosphotyrosine and synthetic substrates, such as para- nitrophenylphosphat [...] | 0.773 |
GYG1 | GYS1 | ENSP00000340736 | ENSP00000317904 | Glycogenin-1; Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase. Belongs to the glycosyltransferase 8 family. Glycogenin subfamily. | Glycogen [starch] synthase, muscle; Transfers the glycosyl residue from UDP-Glc to the non- reducing end of alpha-1,4-glucan. | 0.999 |
GYG1 | GYS2 | ENSP00000340736 | ENSP00000261195 | Glycogenin-1; Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase. Belongs to the glycosyltransferase 8 family. Glycogenin subfamily. | Glycogen [starch] synthase, liver; Transfers the glycosyl residue from UDP-Glc to the non- reducing end of alpha-1,4-glucan. | 0.987 |
GYG1 | NHLRC1 | ENSP00000340736 | ENSP00000345464 | Glycogenin-1; Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase. Belongs to the glycosyltransferase 8 family. Glycogenin subfamily. | E3 ubiquitin-protein ligase NHLRC1; E3 ubiquitin-protein ligase. Together with the phosphatase EPM2A/laforin, appears to be involved in the clearance of toxic polyglucosan and protein aggregates via multiple pathways. In complex with EPM2A/laforin and HSP70, suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system (UPS). Ubiquitinates the glycogen-targeting protein phosphatase subunits PPP1R3C/PTG and PPP1R3D in a laforin- dependent manner and targets them for proteasome-dependent degradation, thus decreasing glycogen [...] | 0.720 |
GYG1 | PPP1R3C | ENSP00000340736 | ENSP00000238994 | Glycogenin-1; Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase. Belongs to the glycosyltransferase 8 family. Glycogenin subfamily. | Protein phosphatase 1 regulatory subunit 3C; Acts as a glycogen-targeting subunit for PP1 and regulates its activity. Activates glycogen synthase, reduces glycogen phosphorylase activity and limits glycogen breakdown. Dramatically increases basal and insulin-stimulated glycogen synthesis upon overexpression in a variety of cell types. | 0.969 |
GYG1 | PPP1R3D | ENSP00000340736 | ENSP00000360035 | Glycogenin-1; Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase. Belongs to the glycosyltransferase 8 family. Glycogenin subfamily. | Protein phosphatase 1 regulatory subunit 3D; Seems to act as a glycogen-targeting subunit for PP1. PP1 is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. | 0.470 |
GYS1 | EPM2A | ENSP00000317904 | ENSP00000356489 | Glycogen [starch] synthase, muscle; Transfers the glycosyl residue from UDP-Glc to the non- reducing end of alpha-1,4-glucan. | Laforin; Plays an important role in preventing glycogen hyperphosphorylation and the formation of insoluble aggregates, via its activity as glycogen phosphatase, and by promoting the ubiquitination of proteins involved in glycogen metabolism via its interaction with the E3 ubiquitin ligase NHLRC1/malin. Shows strong phosphatase activity towards complex carbohydrates in vitro, avoiding glycogen hyperphosphorylation which is associated with reduced branching and formation of insoluble aggregates. Dephosphorylates phosphotyrosine and synthetic substrates, such as para- nitrophenylphosphat [...] | 0.965 |
GYS1 | GYG1 | ENSP00000317904 | ENSP00000340736 | Glycogen [starch] synthase, muscle; Transfers the glycosyl residue from UDP-Glc to the non- reducing end of alpha-1,4-glucan. | Glycogenin-1; Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase. Belongs to the glycosyltransferase 8 family. Glycogenin subfamily. | 0.999 |
GYS1 | GYS2 | ENSP00000317904 | ENSP00000261195 | Glycogen [starch] synthase, muscle; Transfers the glycosyl residue from UDP-Glc to the non- reducing end of alpha-1,4-glucan. | Glycogen [starch] synthase, liver; Transfers the glycosyl residue from UDP-Glc to the non- reducing end of alpha-1,4-glucan. | 0.903 |
GYS1 | NHLRC1 | ENSP00000317904 | ENSP00000345464 | Glycogen [starch] synthase, muscle; Transfers the glycosyl residue from UDP-Glc to the non- reducing end of alpha-1,4-glucan. | E3 ubiquitin-protein ligase NHLRC1; E3 ubiquitin-protein ligase. Together with the phosphatase EPM2A/laforin, appears to be involved in the clearance of toxic polyglucosan and protein aggregates via multiple pathways. In complex with EPM2A/laforin and HSP70, suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system (UPS). Ubiquitinates the glycogen-targeting protein phosphatase subunits PPP1R3C/PTG and PPP1R3D in a laforin- dependent manner and targets them for proteasome-dependent degradation, thus decreasing glycogen [...] | 0.960 |
GYS1 | PPP1CA | ENSP00000317904 | ENSP00000326031 | Glycogen [starch] synthase, muscle; Transfers the glycosyl residue from UDP-Glc to the non- reducing end of alpha-1,4-glucan. | Serine/threonine-protein phosphatase PP1-alpha catalytic subunit; Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin de [...] | 0.973 |
GYS1 | PPP1CB | ENSP00000317904 | ENSP00000378769 | Glycogen [starch] synthase, muscle; Transfers the glycosyl residue from UDP-Glc to the non- reducing end of alpha-1,4-glucan. | Serine/threonine-protein phosphatase PP1-beta catalytic subunit; Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase (PP1) is essential for cell division, it participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progressi [...] | 0.970 |
GYS1 | PPP1CC | ENSP00000317904 | ENSP00000341779 | Glycogen [starch] synthase, muscle; Transfers the glycosyl residue from UDP-Glc to the non- reducing end of alpha-1,4-glucan. | Serine/threonine-protein phosphatase PP1-gamma catalytic subunit; Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Dephosphorylates RPS6KB1. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density- asso [...] | 0.986 |
GYS1 | PPP1R3A | ENSP00000317904 | ENSP00000284601 | Glycogen [starch] synthase, muscle; Transfers the glycosyl residue from UDP-Glc to the non- reducing end of alpha-1,4-glucan. | Protein phosphatase 1 regulatory subunit 3A; Seems to act as a glycogen-targeting subunit for PP1. PP1 is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Plays an important role in glycogen synthesis but is not essential for insulin activation of glycogen synthase (By similarity). | 0.952 |