| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ATXN10 | SPTBN2 | ENSP00000252934 | ENSP00000432568 | Ataxin-10; Necessary for the survival of cerebellar neurons. Induces neuritogenesis by activating the Ras-MAP kinase pathway. May play a role in the maintenance of a critical intracellular glycosylation level and homeostasis. | Spectrin beta chain, non-erythrocytic 2; Probably plays an important role in neuronal membrane skeleton; Belongs to the spectrin family. | 0.917 |
| EPB41L2 | GRM1 | ENSP00000357110 | ENSP00000282753 | Band 4.1-like protein 2; Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase. | Metabotropic glutamate receptor 1; G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling activates a phosphatidylinositol- calcium second messenger system. May participate in the central action of glutamate in the CNS, such as long-term potentiation in the hippocampus and long-term depression in the cerebellum. May function in the light response in the retina (By similarity). | 0.487 |
| EPB41L2 | SPTA1 | ENSP00000357110 | ENSP00000495214 | Band 4.1-like protein 2; Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase. | Spectrin alpha chain, erythrocytic 1; Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane. | 0.910 |
| EPB41L2 | SPTAN1 | ENSP00000357110 | ENSP00000487444 | Band 4.1-like protein 2; Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase. | Spectrin alpha chain, non-erythrocytic 1; Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane. | 0.929 |
| EPB41L2 | SPTB | ENSP00000357110 | ENSP00000495909 | Band 4.1-like protein 2; Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase. | Spectrin beta chain, erythrocytic; Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane. | 0.914 |
| EPB41L2 | SPTBN1 | ENSP00000357110 | ENSP00000349259 | Band 4.1-like protein 2; Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase. | Spectrin beta chain, non-erythrocytic 1; Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane. | 0.933 |
| EPB41L2 | SPTBN2 | ENSP00000357110 | ENSP00000432568 | Band 4.1-like protein 2; Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase. | Spectrin beta chain, non-erythrocytic 2; Probably plays an important role in neuronal membrane skeleton; Belongs to the spectrin family. | 0.906 |
| EPB41L2 | SPTBN4 | ENSP00000357110 | ENSP00000469242 | Band 4.1-like protein 2; Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase. | Spectrin beta chain, non-erythrocytic 4. | 0.932 |
| EPB41L2 | SPTBN5 | ENSP00000357110 | ENSP00000317790 | Band 4.1-like protein 2; Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase. | Spectrin beta, non-erythrocytic 5. | 0.908 |
| GRM1 | EPB41L2 | ENSP00000282753 | ENSP00000357110 | Metabotropic glutamate receptor 1; G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling activates a phosphatidylinositol- calcium second messenger system. May participate in the central action of glutamate in the CNS, such as long-term potentiation in the hippocampus and long-term depression in the cerebellum. May function in the light response in the retina (By similarity). | Band 4.1-like protein 2; Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase. | 0.487 |
| GRM1 | SLC1A6 | ENSP00000282753 | ENSP00000221742 | Metabotropic glutamate receptor 1; G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling activates a phosphatidylinositol- calcium second messenger system. May participate in the central action of glutamate in the CNS, such as long-term potentiation in the hippocampus and long-term depression in the cerebellum. May function in the light response in the retina (By similarity). | Excitatory amino acid transporter 4; Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate. Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions and one proton, in parallel with the counter-transport of one K(+) ion. Mediates Cl(-) flux that is not coupled to amino acid transport; this avoids the accumulation of negative charges due to aspartate and Na(+) symport (By similarity). Plays a redundant role in the rapid removal of released glutamate from the synapt [...] | 0.593 |
| GRM1 | SPTBN2 | ENSP00000282753 | ENSP00000432568 | Metabotropic glutamate receptor 1; G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling activates a phosphatidylinositol- calcium second messenger system. May participate in the central action of glutamate in the CNS, such as long-term potentiation in the hippocampus and long-term depression in the cerebellum. May function in the light response in the retina (By similarity). | Spectrin beta chain, non-erythrocytic 2; Probably plays an important role in neuronal membrane skeleton; Belongs to the spectrin family. | 0.939 |
| SLC1A6 | GRM1 | ENSP00000221742 | ENSP00000282753 | Excitatory amino acid transporter 4; Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate. Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions and one proton, in parallel with the counter-transport of one K(+) ion. Mediates Cl(-) flux that is not coupled to amino acid transport; this avoids the accumulation of negative charges due to aspartate and Na(+) symport (By similarity). Plays a redundant role in the rapid removal of released glutamate from the synapt [...] | Metabotropic glutamate receptor 1; G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling activates a phosphatidylinositol- calcium second messenger system. May participate in the central action of glutamate in the CNS, such as long-term potentiation in the hippocampus and long-term depression in the cerebellum. May function in the light response in the retina (By similarity). | 0.593 |
| SLC1A6 | SPTB | ENSP00000221742 | ENSP00000495909 | Excitatory amino acid transporter 4; Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate. Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions and one proton, in parallel with the counter-transport of one K(+) ion. Mediates Cl(-) flux that is not coupled to amino acid transport; this avoids the accumulation of negative charges due to aspartate and Na(+) symport (By similarity). Plays a redundant role in the rapid removal of released glutamate from the synapt [...] | Spectrin beta chain, erythrocytic; Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane. | 0.596 |
| SLC1A6 | SPTBN1 | ENSP00000221742 | ENSP00000349259 | Excitatory amino acid transporter 4; Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate. Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions and one proton, in parallel with the counter-transport of one K(+) ion. Mediates Cl(-) flux that is not coupled to amino acid transport; this avoids the accumulation of negative charges due to aspartate and Na(+) symport (By similarity). Plays a redundant role in the rapid removal of released glutamate from the synapt [...] | Spectrin beta chain, non-erythrocytic 1; Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane. | 0.608 |
| SLC1A6 | SPTBN2 | ENSP00000221742 | ENSP00000432568 | Excitatory amino acid transporter 4; Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate. Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions and one proton, in parallel with the counter-transport of one K(+) ion. Mediates Cl(-) flux that is not coupled to amino acid transport; this avoids the accumulation of negative charges due to aspartate and Na(+) symport (By similarity). Plays a redundant role in the rapid removal of released glutamate from the synapt [...] | Spectrin beta chain, non-erythrocytic 2; Probably plays an important role in neuronal membrane skeleton; Belongs to the spectrin family. | 0.915 |
| SPTA1 | EPB41L2 | ENSP00000495214 | ENSP00000357110 | Spectrin alpha chain, erythrocytic 1; Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane. | Band 4.1-like protein 2; Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase. | 0.910 |
| SPTA1 | SPTAN1 | ENSP00000495214 | ENSP00000487444 | Spectrin alpha chain, erythrocytic 1; Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane. | Spectrin alpha chain, non-erythrocytic 1; Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane. | 0.909 |
| SPTA1 | SPTB | ENSP00000495214 | ENSP00000495909 | Spectrin alpha chain, erythrocytic 1; Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane. | Spectrin beta chain, erythrocytic; Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane. | 0.999 |
| SPTA1 | SPTBN1 | ENSP00000495214 | ENSP00000349259 | Spectrin alpha chain, erythrocytic 1; Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane. | Spectrin beta chain, non-erythrocytic 1; Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane. | 0.972 |
