node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
DSCR3 | HLCS | ENSP00000311399 | ENSP00000338387 | Down syndrome critical region gene 3 | holocarboxylase synthetase (biotin-(proprionyl-CoA-carboxylase (ATP-hydrolysing)) ligase); Post-translational modification of specific protein by attachment of biotin. Acts on various carboxylases such as acetyl- CoA-carboxylase, pyruvate carboxylase, propionyl CoA carboxylase, and 3-methylcrotonyl CoA carboxylase | 0.682 |
DSCR3 | KCNJ15 | ENSP00000311399 | ENSP00000331698 | Down syndrome critical region gene 3 | potassium inwardly-rectifying channel, subfamily J, member 15; Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium | 0.605 |
DSCR3 | PIGP | ENSP00000311399 | ENSP00000420037 | Down syndrome critical region gene 3 | phosphatidylinositol glycan anchor biosynthesis, class P | 0.680 |
HLCS | DSCR3 | ENSP00000338387 | ENSP00000311399 | holocarboxylase synthetase (biotin-(proprionyl-CoA-carboxylase (ATP-hydrolysing)) ligase); Post-translational modification of specific protein by attachment of biotin. Acts on various carboxylases such as acetyl- CoA-carboxylase, pyruvate carboxylase, propionyl CoA carboxylase, and 3-methylcrotonyl CoA carboxylase | Down syndrome critical region gene 3 | 0.682 |
HLCS | KCNJ15 | ENSP00000338387 | ENSP00000331698 | holocarboxylase synthetase (biotin-(proprionyl-CoA-carboxylase (ATP-hydrolysing)) ligase); Post-translational modification of specific protein by attachment of biotin. Acts on various carboxylases such as acetyl- CoA-carboxylase, pyruvate carboxylase, propionyl CoA carboxylase, and 3-methylcrotonyl CoA carboxylase | potassium inwardly-rectifying channel, subfamily J, member 15; Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium | 0.549 |
HLCS | PIGP | ENSP00000338387 | ENSP00000420037 | holocarboxylase synthetase (biotin-(proprionyl-CoA-carboxylase (ATP-hydrolysing)) ligase); Post-translational modification of specific protein by attachment of biotin. Acts on various carboxylases such as acetyl- CoA-carboxylase, pyruvate carboxylase, propionyl CoA carboxylase, and 3-methylcrotonyl CoA carboxylase | phosphatidylinositol glycan anchor biosynthesis, class P | 0.551 |
IL16 | KCNJ15 | ENSP00000302935 | ENSP00000331698 | interleukin 16; Interleukin-16 stimulates a migratory response in CD4+ lymphocytes, monocytes, and eosinophils. Primes CD4+ T-cells for IL-2 and IL-15 responsiveness. Also induces T-lymphocyte expression of interleukin 2 receptor. Ligand for CD4 | potassium inwardly-rectifying channel, subfamily J, member 15; Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium | 0.587 |
INADL | KCNJ15 | ENSP00000360200 | ENSP00000331698 | InaD-like (Drosophila) | potassium inwardly-rectifying channel, subfamily J, member 15; Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium | 0.824 |
KCNAB1 | KCNAB3 | ENSP00000419952 | ENSP00000302719 | potassium voltage-gated channel, shaker-related subfamily, beta member 1 | potassium voltage-gated channel, shaker-related subfamily, beta member 3; Accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. Alters the functional properties of Kv1.5 | 0.903 |
KCNAB1 | KCNJ15 | ENSP00000419952 | ENSP00000331698 | potassium voltage-gated channel, shaker-related subfamily, beta member 1 | potassium inwardly-rectifying channel, subfamily J, member 15; Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium | 0.484 |
KCNAB3 | KCNAB1 | ENSP00000302719 | ENSP00000419952 | potassium voltage-gated channel, shaker-related subfamily, beta member 3; Accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. Alters the functional properties of Kv1.5 | potassium voltage-gated channel, shaker-related subfamily, beta member 1 | 0.903 |
KCNAB3 | KCNJ15 | ENSP00000302719 | ENSP00000331698 | potassium voltage-gated channel, shaker-related subfamily, beta member 3; Accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. Alters the functional properties of Kv1.5 | potassium inwardly-rectifying channel, subfamily J, member 15; Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium | 0.488 |
KCNJ15 | DSCR3 | ENSP00000331698 | ENSP00000311399 | potassium inwardly-rectifying channel, subfamily J, member 15; Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium | Down syndrome critical region gene 3 | 0.605 |
KCNJ15 | HLCS | ENSP00000331698 | ENSP00000338387 | potassium inwardly-rectifying channel, subfamily J, member 15; Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium | holocarboxylase synthetase (biotin-(proprionyl-CoA-carboxylase (ATP-hydrolysing)) ligase); Post-translational modification of specific protein by attachment of biotin. Acts on various carboxylases such as acetyl- CoA-carboxylase, pyruvate carboxylase, propionyl CoA carboxylase, and 3-methylcrotonyl CoA carboxylase | 0.549 |
KCNJ15 | IL16 | ENSP00000331698 | ENSP00000302935 | potassium inwardly-rectifying channel, subfamily J, member 15; Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium | interleukin 16; Interleukin-16 stimulates a migratory response in CD4+ lymphocytes, monocytes, and eosinophils. Primes CD4+ T-cells for IL-2 and IL-15 responsiveness. Also induces T-lymphocyte expression of interleukin 2 receptor. Ligand for CD4 | 0.587 |
KCNJ15 | INADL | ENSP00000331698 | ENSP00000360200 | potassium inwardly-rectifying channel, subfamily J, member 15; Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium | InaD-like (Drosophila) | 0.824 |
KCNJ15 | KCNAB1 | ENSP00000331698 | ENSP00000419952 | potassium inwardly-rectifying channel, subfamily J, member 15; Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium | potassium voltage-gated channel, shaker-related subfamily, beta member 1 | 0.484 |
KCNJ15 | KCNAB3 | ENSP00000331698 | ENSP00000302719 | potassium inwardly-rectifying channel, subfamily J, member 15; Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium | potassium voltage-gated channel, shaker-related subfamily, beta member 3; Accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. Alters the functional properties of Kv1.5 | 0.488 |
KCNJ15 | KCNJ16 | ENSP00000331698 | ENSP00000283936 | potassium inwardly-rectifying channel, subfamily J, member 15; Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium | potassium inwardly-rectifying channel, subfamily J, member 16; Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. KCNJ16 may be involved in the regulation of fluid and pH balance | 0.648 |
KCNJ15 | MPDZ | ENSP00000331698 | ENSP00000370410 | potassium inwardly-rectifying channel, subfamily J, member 15; Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium | multiple PDZ domain protein | 0.899 |