| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Ank1 | Aqp1 | ENSMUSP00000113571 | ENSMUSP00000004774 | Ankyrin-1; Attaches integral membrane proteins to cytoskeletal elements; binds to the erythrocyte membrane protein band 4.2, to Na-K ATPase, to the lymphocyte membrane protein GP85, and to the cytoskeletal proteins fodrin, tubulin, vimentin and desmin. Erythrocyte ankyrins also link spectrin (beta chain) to the cytoplasmic domain of the erythrocytes anion exchange protein; they retain most or all of these binding functions. In skeletal muscle, isoform Mu7 together with obscurin may provide a molecular link between the sarcoplasmic reticulum and myofibrils. | Aquaporin-1; Forms a water-specific channel that provides the plasma membranes of red cells and kidney proximal tubules with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient. | 0.921 |
| Ank1 | Epb41 | ENSMUSP00000113571 | ENSMUSP00000030739 | Ankyrin-1; Attaches integral membrane proteins to cytoskeletal elements; binds to the erythrocyte membrane protein band 4.2, to Na-K ATPase, to the lymphocyte membrane protein GP85, and to the cytoskeletal proteins fodrin, tubulin, vimentin and desmin. Erythrocyte ankyrins also link spectrin (beta chain) to the cytoplasmic domain of the erythrocytes anion exchange protein; they retain most or all of these binding functions. In skeletal muscle, isoform Mu7 together with obscurin may provide a molecular link between the sarcoplasmic reticulum and myofibrils. | Protein 4.1; Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes. Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase. | 0.714 |
| Ank1 | Epb42 | ENSMUSP00000113571 | ENSMUSP00000099548 | Ankyrin-1; Attaches integral membrane proteins to cytoskeletal elements; binds to the erythrocyte membrane protein band 4.2, to Na-K ATPase, to the lymphocyte membrane protein GP85, and to the cytoskeletal proteins fodrin, tubulin, vimentin and desmin. Erythrocyte ankyrins also link spectrin (beta chain) to the cytoplasmic domain of the erythrocytes anion exchange protein; they retain most or all of these binding functions. In skeletal muscle, isoform Mu7 together with obscurin may provide a molecular link between the sarcoplasmic reticulum and myofibrils. | Erythrocyte membrane protein band 4.2; Probably plays an important role in the regulation of erythrocyte shape and mechanical properties; Belongs to the transglutaminase superfamily. Transglutaminase family. | 0.992 |
| Ank1 | Gypa | ENSMUSP00000113571 | ENSMUSP00000070836 | Ankyrin-1; Attaches integral membrane proteins to cytoskeletal elements; binds to the erythrocyte membrane protein band 4.2, to Na-K ATPase, to the lymphocyte membrane protein GP85, and to the cytoskeletal proteins fodrin, tubulin, vimentin and desmin. Erythrocyte ankyrins also link spectrin (beta chain) to the cytoplasmic domain of the erythrocytes anion exchange protein; they retain most or all of these binding functions. In skeletal muscle, isoform Mu7 together with obscurin may provide a molecular link between the sarcoplasmic reticulum and myofibrils. | Glycophorin-A; Glycophorin A is the major intrinsic membrane sialoglycoprotein of the erythrocyte. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane (By similarity). | 0.948 |
| Ank1 | Rhag | ENSMUSP00000113571 | ENSMUSP00000024721 | Ankyrin-1; Attaches integral membrane proteins to cytoskeletal elements; binds to the erythrocyte membrane protein band 4.2, to Na-K ATPase, to the lymphocyte membrane protein GP85, and to the cytoskeletal proteins fodrin, tubulin, vimentin and desmin. Erythrocyte ankyrins also link spectrin (beta chain) to the cytoplasmic domain of the erythrocytes anion exchange protein; they retain most or all of these binding functions. In skeletal muscle, isoform Mu7 together with obscurin may provide a molecular link between the sarcoplasmic reticulum and myofibrils. | Ammonium transporter Rh type A; May be part of an oligomeric complex which is likely to have a transport or channel function in the erythrocyte membrane. Involved in ammonia transport across the erythrocyte membrane. Seems to act in monovalent cation transport. | 0.963 |
| Ank1 | Rhd | ENSMUSP00000113571 | ENSMUSP00000030627 | Ankyrin-1; Attaches integral membrane proteins to cytoskeletal elements; binds to the erythrocyte membrane protein band 4.2, to Na-K ATPase, to the lymphocyte membrane protein GP85, and to the cytoskeletal proteins fodrin, tubulin, vimentin and desmin. Erythrocyte ankyrins also link spectrin (beta chain) to the cytoplasmic domain of the erythrocytes anion exchange protein; they retain most or all of these binding functions. In skeletal muscle, isoform Mu7 together with obscurin may provide a molecular link between the sarcoplasmic reticulum and myofibrils. | Blood group Rh(D) polypeptide; May be part of an oligomeric complex which is likely to have a transport or channel function in the erythrocyte membrane. | 0.946 |
| Ank1 | Slc4a1 | ENSMUSP00000113571 | ENSMUSP00000006749 | Ankyrin-1; Attaches integral membrane proteins to cytoskeletal elements; binds to the erythrocyte membrane protein band 4.2, to Na-K ATPase, to the lymphocyte membrane protein GP85, and to the cytoskeletal proteins fodrin, tubulin, vimentin and desmin. Erythrocyte ankyrins also link spectrin (beta chain) to the cytoplasmic domain of the erythrocytes anion exchange protein; they retain most or all of these binding functions. In skeletal muscle, isoform Mu7 together with obscurin may provide a molecular link between the sarcoplasmic reticulum and myofibrils. | Band 3 anion transport protein; Functions both as a transporter that mediates electroneutral anion exchange across the cell membrane and as a structural protein. Major integral membrane glycoprotein of the erythrocyte membrane; required for normal flexibility and stability of the erythrocyte membrane and for normal erythrocyte shape via the interactions of its cytoplasmic domain with cytoskeletal proteins, glycolytic enzymes, and hemoglobin. Functions as a transporter that mediates the 1:1 exchange of inorganic anions across the erythrocyte membrane. Mediates chloride- bicarbonate exch [...] | 0.994 |
| Ank1 | Spta1 | ENSMUSP00000113571 | ENSMUSP00000027817 | Ankyrin-1; Attaches integral membrane proteins to cytoskeletal elements; binds to the erythrocyte membrane protein band 4.2, to Na-K ATPase, to the lymphocyte membrane protein GP85, and to the cytoskeletal proteins fodrin, tubulin, vimentin and desmin. Erythrocyte ankyrins also link spectrin (beta chain) to the cytoplasmic domain of the erythrocytes anion exchange protein; they retain most or all of these binding functions. In skeletal muscle, isoform Mu7 together with obscurin may provide a molecular link between the sarcoplasmic reticulum and myofibrils. | 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. | 0.984 |
| Aqp1 | Ank1 | ENSMUSP00000004774 | ENSMUSP00000113571 | Aquaporin-1; Forms a water-specific channel that provides the plasma membranes of red cells and kidney proximal tubules with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient. | Ankyrin-1; Attaches integral membrane proteins to cytoskeletal elements; binds to the erythrocyte membrane protein band 4.2, to Na-K ATPase, to the lymphocyte membrane protein GP85, and to the cytoskeletal proteins fodrin, tubulin, vimentin and desmin. Erythrocyte ankyrins also link spectrin (beta chain) to the cytoplasmic domain of the erythrocytes anion exchange protein; they retain most or all of these binding functions. In skeletal muscle, isoform Mu7 together with obscurin may provide a molecular link between the sarcoplasmic reticulum and myofibrils. | 0.921 |
| Aqp1 | Epb42 | ENSMUSP00000004774 | ENSMUSP00000099548 | Aquaporin-1; Forms a water-specific channel that provides the plasma membranes of red cells and kidney proximal tubules with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient. | Erythrocyte membrane protein band 4.2; Probably plays an important role in the regulation of erythrocyte shape and mechanical properties; Belongs to the transglutaminase superfamily. Transglutaminase family. | 0.954 |
| Aqp1 | Gypa | ENSMUSP00000004774 | ENSMUSP00000070836 | Aquaporin-1; Forms a water-specific channel that provides the plasma membranes of red cells and kidney proximal tubules with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient. | Glycophorin-A; Glycophorin A is the major intrinsic membrane sialoglycoprotein of the erythrocyte. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane (By similarity). | 0.956 |
| Aqp1 | Rhag | ENSMUSP00000004774 | ENSMUSP00000024721 | Aquaporin-1; Forms a water-specific channel that provides the plasma membranes of red cells and kidney proximal tubules with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient. | Ammonium transporter Rh type A; May be part of an oligomeric complex which is likely to have a transport or channel function in the erythrocyte membrane. Involved in ammonia transport across the erythrocyte membrane. Seems to act in monovalent cation transport. | 0.976 |
| Aqp1 | Rhd | ENSMUSP00000004774 | ENSMUSP00000030627 | Aquaporin-1; Forms a water-specific channel that provides the plasma membranes of red cells and kidney proximal tubules with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient. | Blood group Rh(D) polypeptide; May be part of an oligomeric complex which is likely to have a transport or channel function in the erythrocyte membrane. | 0.956 |
| Aqp1 | Slc4a1 | ENSMUSP00000004774 | ENSMUSP00000006749 | Aquaporin-1; Forms a water-specific channel that provides the plasma membranes of red cells and kidney proximal tubules with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient. | Band 3 anion transport protein; Functions both as a transporter that mediates electroneutral anion exchange across the cell membrane and as a structural protein. Major integral membrane glycoprotein of the erythrocyte membrane; required for normal flexibility and stability of the erythrocyte membrane and for normal erythrocyte shape via the interactions of its cytoplasmic domain with cytoskeletal proteins, glycolytic enzymes, and hemoglobin. Functions as a transporter that mediates the 1:1 exchange of inorganic anions across the erythrocyte membrane. Mediates chloride- bicarbonate exch [...] | 0.974 |
| Epb41 | Ank1 | ENSMUSP00000030739 | ENSMUSP00000113571 | Protein 4.1; Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes. Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase. | Ankyrin-1; Attaches integral membrane proteins to cytoskeletal elements; binds to the erythrocyte membrane protein band 4.2, to Na-K ATPase, to the lymphocyte membrane protein GP85, and to the cytoskeletal proteins fodrin, tubulin, vimentin and desmin. Erythrocyte ankyrins also link spectrin (beta chain) to the cytoplasmic domain of the erythrocytes anion exchange protein; they retain most or all of these binding functions. In skeletal muscle, isoform Mu7 together with obscurin may provide a molecular link between the sarcoplasmic reticulum and myofibrils. | 0.714 |
| Epb41 | Epb42 | ENSMUSP00000030739 | ENSMUSP00000099548 | Protein 4.1; Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes. Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase. | Erythrocyte membrane protein band 4.2; Probably plays an important role in the regulation of erythrocyte shape and mechanical properties; Belongs to the transglutaminase superfamily. Transglutaminase family. | 0.616 |
| Epb41 | Gypa | ENSMUSP00000030739 | ENSMUSP00000070836 | Protein 4.1; Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes. Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase. | Glycophorin-A; Glycophorin A is the major intrinsic membrane sialoglycoprotein of the erythrocyte. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane (By similarity). | 0.571 |
| Epb41 | Rhag | ENSMUSP00000030739 | ENSMUSP00000024721 | Protein 4.1; Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes. Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase. | Ammonium transporter Rh type A; May be part of an oligomeric complex which is likely to have a transport or channel function in the erythrocyte membrane. Involved in ammonia transport across the erythrocyte membrane. Seems to act in monovalent cation transport. | 0.739 |
| Epb41 | Slc4a1 | ENSMUSP00000030739 | ENSMUSP00000006749 | Protein 4.1; Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes. Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase. | Band 3 anion transport protein; Functions both as a transporter that mediates electroneutral anion exchange across the cell membrane and as a structural protein. Major integral membrane glycoprotein of the erythrocyte membrane; required for normal flexibility and stability of the erythrocyte membrane and for normal erythrocyte shape via the interactions of its cytoplasmic domain with cytoskeletal proteins, glycolytic enzymes, and hemoglobin. Functions as a transporter that mediates the 1:1 exchange of inorganic anions across the erythrocyte membrane. Mediates chloride- bicarbonate exch [...] | 0.850 |
| Epb41 | Spta1 | ENSMUSP00000030739 | ENSMUSP00000027817 | Protein 4.1; Protein 4.1 is a major structural element of the erythrocyte membrane skeleton. It plays a key role in regulating membrane physical properties of mechanical stability and deformability by stabilizing spectrin-actin interaction. Recruits DLG1 to membranes. 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. | 0.728 |
