node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CACNA1H | CACNA1S | ENSGALP00000008367 | ENSGALP00000056760 | Calcium voltage-gated channel subunit alpha1 H. | Voltage-dependent L-type calcium channel subunit alpha-1S; Pore-forming, alpha-1S subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents in skeletal muscle. Calcium channels containing the alpha-1S subunit play an important role in excitation-contraction coupling in skeletal muscle via their interaction with RYR1, which triggers Ca(2+) release from the sarcplasmic reticulum and ultimately results in muscle contraction. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. | 0.727 |
CACNA1H | SCN1A | ENSGALP00000008367 | ENSGALP00000017793 | Calcium voltage-gated channel subunit alpha1 H. | Sodium channel protein; Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. | 0.704 |
CACNA1H | SCN2A | ENSGALP00000008367 | ENSGALP00000017912 | Calcium voltage-gated channel subunit alpha1 H. | Sodium channel protein; Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. | 0.708 |
CACNA1H | SCN2B | ENSGALP00000008367 | ENSGALP00000033652 | Calcium voltage-gated channel subunit alpha1 H. | Sodium voltage-gated channel beta subunit 2. | 0.562 |
CACNA1H | SCN3B | ENSGALP00000008367 | ENSGALP00000068170 | Calcium voltage-gated channel subunit alpha1 H. | Sodium voltage-gated channel beta subunit 3. | 0.695 |
CACNA1H | SCN4A | ENSGALP00000008367 | ENSGALP00000073837 | Calcium voltage-gated channel subunit alpha1 H. | Sodium channel protein; Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. | 0.687 |
CACNA1H | SCN4B | ENSGALP00000008367 | ENSGALP00000011971 | Calcium voltage-gated channel subunit alpha1 H. | Sodium voltage-gated channel beta subunit 4. | 0.661 |
CACNA1H | SCN5A | ENSGALP00000008367 | ENSGALP00000030644 | Calcium voltage-gated channel subunit alpha1 H. | Sodium channel protein; Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. | 0.691 |
CACNA1H | SCN8A | ENSGALP00000008367 | ENSGALP00000050098 | Calcium voltage-gated channel subunit alpha1 H. | Sodium channel protein; Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. | 0.707 |
CACNA1H | SCN9A | ENSGALP00000008367 | ENSGALP00000017788 | Calcium voltage-gated channel subunit alpha1 H. | Sodium channel protein; Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. | 0.721 |
CACNA1S | CACNA1H | ENSGALP00000056760 | ENSGALP00000008367 | Voltage-dependent L-type calcium channel subunit alpha-1S; Pore-forming, alpha-1S subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents in skeletal muscle. Calcium channels containing the alpha-1S subunit play an important role in excitation-contraction coupling in skeletal muscle via their interaction with RYR1, which triggers Ca(2+) release from the sarcplasmic reticulum and ultimately results in muscle contraction. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. | Calcium voltage-gated channel subunit alpha1 H. | 0.727 |
CACNA1S | SCN1A | ENSGALP00000056760 | ENSGALP00000017793 | Voltage-dependent L-type calcium channel subunit alpha-1S; Pore-forming, alpha-1S subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents in skeletal muscle. Calcium channels containing the alpha-1S subunit play an important role in excitation-contraction coupling in skeletal muscle via their interaction with RYR1, which triggers Ca(2+) release from the sarcplasmic reticulum and ultimately results in muscle contraction. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. | Sodium channel protein; Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. | 0.554 |
CACNA1S | SCN2A | ENSGALP00000056760 | ENSGALP00000017912 | Voltage-dependent L-type calcium channel subunit alpha-1S; Pore-forming, alpha-1S subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents in skeletal muscle. Calcium channels containing the alpha-1S subunit play an important role in excitation-contraction coupling in skeletal muscle via their interaction with RYR1, which triggers Ca(2+) release from the sarcplasmic reticulum and ultimately results in muscle contraction. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. | Sodium channel protein; Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. | 0.572 |
CACNA1S | SCN2B | ENSGALP00000056760 | ENSGALP00000033652 | Voltage-dependent L-type calcium channel subunit alpha-1S; Pore-forming, alpha-1S subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents in skeletal muscle. Calcium channels containing the alpha-1S subunit play an important role in excitation-contraction coupling in skeletal muscle via their interaction with RYR1, which triggers Ca(2+) release from the sarcplasmic reticulum and ultimately results in muscle contraction. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. | Sodium voltage-gated channel beta subunit 2. | 0.673 |
CACNA1S | SCN3B | ENSGALP00000056760 | ENSGALP00000068170 | Voltage-dependent L-type calcium channel subunit alpha-1S; Pore-forming, alpha-1S subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents in skeletal muscle. Calcium channels containing the alpha-1S subunit play an important role in excitation-contraction coupling in skeletal muscle via their interaction with RYR1, which triggers Ca(2+) release from the sarcplasmic reticulum and ultimately results in muscle contraction. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. | Sodium voltage-gated channel beta subunit 3. | 0.679 |
CACNA1S | SCN4A | ENSGALP00000056760 | ENSGALP00000073837 | Voltage-dependent L-type calcium channel subunit alpha-1S; Pore-forming, alpha-1S subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents in skeletal muscle. Calcium channels containing the alpha-1S subunit play an important role in excitation-contraction coupling in skeletal muscle via their interaction with RYR1, which triggers Ca(2+) release from the sarcplasmic reticulum and ultimately results in muscle contraction. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. | Sodium channel protein; Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. | 0.656 |
CACNA1S | SCN4B | ENSGALP00000056760 | ENSGALP00000011971 | Voltage-dependent L-type calcium channel subunit alpha-1S; Pore-forming, alpha-1S subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents in skeletal muscle. Calcium channels containing the alpha-1S subunit play an important role in excitation-contraction coupling in skeletal muscle via their interaction with RYR1, which triggers Ca(2+) release from the sarcplasmic reticulum and ultimately results in muscle contraction. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. | Sodium voltage-gated channel beta subunit 4. | 0.796 |
CACNA1S | SCN5A | ENSGALP00000056760 | ENSGALP00000030644 | Voltage-dependent L-type calcium channel subunit alpha-1S; Pore-forming, alpha-1S subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents in skeletal muscle. Calcium channels containing the alpha-1S subunit play an important role in excitation-contraction coupling in skeletal muscle via their interaction with RYR1, which triggers Ca(2+) release from the sarcplasmic reticulum and ultimately results in muscle contraction. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. | Sodium channel protein; Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. | 0.649 |
CACNA1S | SCN8A | ENSGALP00000056760 | ENSGALP00000050098 | Voltage-dependent L-type calcium channel subunit alpha-1S; Pore-forming, alpha-1S subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents in skeletal muscle. Calcium channels containing the alpha-1S subunit play an important role in excitation-contraction coupling in skeletal muscle via their interaction with RYR1, which triggers Ca(2+) release from the sarcplasmic reticulum and ultimately results in muscle contraction. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. | Sodium channel protein; Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. | 0.553 |
CACNA1S | SCN9A | ENSGALP00000056760 | ENSGALP00000017788 | Voltage-dependent L-type calcium channel subunit alpha-1S; Pore-forming, alpha-1S subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents in skeletal muscle. Calcium channels containing the alpha-1S subunit play an important role in excitation-contraction coupling in skeletal muscle via their interaction with RYR1, which triggers Ca(2+) release from the sarcplasmic reticulum and ultimately results in muscle contraction. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. | Sodium channel protein; Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. | 0.554 |