| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Ryr1 | S100a1 | ENSMUSP00000137123 | ENSMUSP00000058237 | Ryanodine receptor 1; Calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm and thereby plays a key role in triggering muscle contraction following depolarization of T-tubules. Repeated very high-level exercise increases the open probability of the channel and leads to Ca(2+) leaking into the cytoplasm. Can also mediate the release of Ca(2+) from intracellular stores in neurons, and may thereby promote prolonged Ca(2+) signaling in the brain. Required for normal embryonic development of muscle fibers and skeletal muscle. Required for nor [...] | Protein S100-A1; Probably acts as a Ca(2+) signal transducer. In response to an increase in intracellular Ca(2+) levels, binds calcium which triggers a conformational change. This conformational change allows interaction of S1001A with specific target proteins, such as TPR- containing proteins, and the modulation of their activity. | 0.871 |
| S100a1 | Ryr1 | ENSMUSP00000058237 | ENSMUSP00000137123 | Protein S100-A1; Probably acts as a Ca(2+) signal transducer. In response to an increase in intracellular Ca(2+) levels, binds calcium which triggers a conformational change. This conformational change allows interaction of S1001A with specific target proteins, such as TPR- containing proteins, and the modulation of their activity. | Ryanodine receptor 1; Calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm and thereby plays a key role in triggering muscle contraction following depolarization of T-tubules. Repeated very high-level exercise increases the open probability of the channel and leads to Ca(2+) leaking into the cytoplasm. Can also mediate the release of Ca(2+) from intracellular stores in neurons, and may thereby promote prolonged Ca(2+) signaling in the brain. Required for normal embryonic development of muscle fibers and skeletal muscle. Required for nor [...] | 0.871 |
| S100a1 | S100a10 | ENSMUSP00000058237 | ENSMUSP00000036949 | Protein S100-A1; Probably acts as a Ca(2+) signal transducer. In response to an increase in intracellular Ca(2+) levels, binds calcium which triggers a conformational change. This conformational change allows interaction of S1001A with specific target proteins, such as TPR- containing proteins, and the modulation of their activity. | Protein S100-A10; Because S100A10 induces the dimerization of ANXA2/p36, it may function as a regulator of protein phosphorylation in that the ANXA2 monomer is the preferred target (in vitro) of tyrosine-specific kinase; Belongs to the S-100 family. | 0.848 |
| S100a1 | S100a13 | ENSMUSP00000058237 | ENSMUSP00000047737 | Protein S100-A1; Probably acts as a Ca(2+) signal transducer. In response to an increase in intracellular Ca(2+) levels, binds calcium which triggers a conformational change. This conformational change allows interaction of S1001A with specific target proteins, such as TPR- containing proteins, and the modulation of their activity. | Protein S100-A13; Plays a role in the export of proteins that lack a signal peptide and are secreted by an alternative pathway. Binds two calcium ions per subunit. Binds one copper ion. Binding of one copper ion does not interfere with calcium binding. Required for the copper-dependent stress-induced export of IL1A and FGF1. The calcium-free protein binds to lipid vesicles containing phosphatidylserine, but not to vesicles containing phosphatidylcholine. | 0.901 |
| S100a1 | S100a14 | ENSMUSP00000058237 | ENSMUSP00000126821 | Protein S100-A1; Probably acts as a Ca(2+) signal transducer. In response to an increase in intracellular Ca(2+) levels, binds calcium which triggers a conformational change. This conformational change allows interaction of S1001A with specific target proteins, such as TPR- containing proteins, and the modulation of their activity. | Protein S100-A14; Modulates P53/TP53 protein levels, and thereby plays a role in the regulation of cell survival and apoptosis. Depending on the context, it can promote cell proliferation or apoptosis. Plays a role in the regulation of cell migration by modulating the levels of MMP2, a matrix protease that is under transcriptional control of P53/TP53. Does not bind calcium (By similarity). | 0.893 |
| S100a1 | S100a16 | ENSMUSP00000058237 | ENSMUSP00000096510 | Protein S100-A1; Probably acts as a Ca(2+) signal transducer. In response to an increase in intracellular Ca(2+) levels, binds calcium which triggers a conformational change. This conformational change allows interaction of S1001A with specific target proteins, such as TPR- containing proteins, and the modulation of their activity. | Protein S100-A16; Calcium-binding protein. Binds one calcium ion per monomer. Can promote differentiation of adipocytes (in vitro). Overexpression in 3T3-L1 preadipocytes increases their proliferation, enhances adipogenesis and reduces insulin-stimulated glucose uptake. | 0.881 |
| S100a1 | S100a3 | ENSMUSP00000058237 | ENSMUSP00000001047 | Protein S100-A1; Probably acts as a Ca(2+) signal transducer. In response to an increase in intracellular Ca(2+) levels, binds calcium which triggers a conformational change. This conformational change allows interaction of S1001A with specific target proteins, such as TPR- containing proteins, and the modulation of their activity. | Protein S100-A3; Binds both calcium and zinc. May be involved in calcium- dependent cuticle cell differentiation, hair shaft and hair cuticular barrier formation (By similarity). | 0.850 |
| S100a1 | S100a4 | ENSMUSP00000058237 | ENSMUSP00000001046 | Protein S100-A1; Probably acts as a Ca(2+) signal transducer. In response to an increase in intracellular Ca(2+) levels, binds calcium which triggers a conformational change. This conformational change allows interaction of S1001A with specific target proteins, such as TPR- containing proteins, and the modulation of their activity. | Protein S100-A4; Belongs to the S-100 family. | 0.963 |
| S100a1 | S100a6 | ENSMUSP00000058237 | ENSMUSP00000001051 | Protein S100-A1; Probably acts as a Ca(2+) signal transducer. In response to an increase in intracellular Ca(2+) levels, binds calcium which triggers a conformational change. This conformational change allows interaction of S1001A with specific target proteins, such as TPR- containing proteins, and the modulation of their activity. | Protein S100-A6; May function as calcium sensor and modulator, contributing to cellular calcium signaling. May function by interacting with other proteins, such as TPR-containing proteins, and indirectly play a role in many physiological processes such as the reorganization of the actin cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium binding is cooperative (By similarity); Belongs to the S-100 family. | 0.870 |
| S100a1 | S100a7a | ENSMUSP00000058237 | ENSMUSP00000078268 | Protein S100-A1; Probably acts as a Ca(2+) signal transducer. In response to an increase in intracellular Ca(2+) levels, binds calcium which triggers a conformational change. This conformational change allows interaction of S1001A with specific target proteins, such as TPR- containing proteins, and the modulation of their activity. | Protein S100-A15A; Belongs to the S-100 family. | 0.872 |
| S100a1 | S100b | ENSMUSP00000058237 | ENSMUSP00000047968 | Protein S100-A1; Probably acts as a Ca(2+) signal transducer. In response to an increase in intracellular Ca(2+) levels, binds calcium which triggers a conformational change. This conformational change allows interaction of S1001A with specific target proteins, such as TPR- containing proteins, and the modulation of their activity. | Protein S100-B; Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. Binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase. Interaction with AGER after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling. Could assist ATAD3A cytoplasmic pr [...] | 0.951 |
| S100a10 | S100a1 | ENSMUSP00000036949 | ENSMUSP00000058237 | Protein S100-A10; Because S100A10 induces the dimerization of ANXA2/p36, it may function as a regulator of protein phosphorylation in that the ANXA2 monomer is the preferred target (in vitro) of tyrosine-specific kinase; Belongs to the S-100 family. | Protein S100-A1; Probably acts as a Ca(2+) signal transducer. In response to an increase in intracellular Ca(2+) levels, binds calcium which triggers a conformational change. This conformational change allows interaction of S1001A with specific target proteins, such as TPR- containing proteins, and the modulation of their activity. | 0.848 |
| S100a10 | S100a13 | ENSMUSP00000036949 | ENSMUSP00000047737 | Protein S100-A10; Because S100A10 induces the dimerization of ANXA2/p36, it may function as a regulator of protein phosphorylation in that the ANXA2 monomer is the preferred target (in vitro) of tyrosine-specific kinase; Belongs to the S-100 family. | Protein S100-A13; Plays a role in the export of proteins that lack a signal peptide and are secreted by an alternative pathway. Binds two calcium ions per subunit. Binds one copper ion. Binding of one copper ion does not interfere with calcium binding. Required for the copper-dependent stress-induced export of IL1A and FGF1. The calcium-free protein binds to lipid vesicles containing phosphatidylserine, but not to vesicles containing phosphatidylcholine. | 0.950 |
| S100a10 | S100a14 | ENSMUSP00000036949 | ENSMUSP00000126821 | Protein S100-A10; Because S100A10 induces the dimerization of ANXA2/p36, it may function as a regulator of protein phosphorylation in that the ANXA2 monomer is the preferred target (in vitro) of tyrosine-specific kinase; Belongs to the S-100 family. | Protein S100-A14; Modulates P53/TP53 protein levels, and thereby plays a role in the regulation of cell survival and apoptosis. Depending on the context, it can promote cell proliferation or apoptosis. Plays a role in the regulation of cell migration by modulating the levels of MMP2, a matrix protease that is under transcriptional control of P53/TP53. Does not bind calcium (By similarity). | 0.868 |
| S100a10 | S100a16 | ENSMUSP00000036949 | ENSMUSP00000096510 | Protein S100-A10; Because S100A10 induces the dimerization of ANXA2/p36, it may function as a regulator of protein phosphorylation in that the ANXA2 monomer is the preferred target (in vitro) of tyrosine-specific kinase; Belongs to the S-100 family. | Protein S100-A16; Calcium-binding protein. Binds one calcium ion per monomer. Can promote differentiation of adipocytes (in vitro). Overexpression in 3T3-L1 preadipocytes increases their proliferation, enhances adipogenesis and reduces insulin-stimulated glucose uptake. | 0.958 |
| S100a10 | S100a3 | ENSMUSP00000036949 | ENSMUSP00000001047 | Protein S100-A10; Because S100A10 induces the dimerization of ANXA2/p36, it may function as a regulator of protein phosphorylation in that the ANXA2 monomer is the preferred target (in vitro) of tyrosine-specific kinase; Belongs to the S-100 family. | Protein S100-A3; Binds both calcium and zinc. May be involved in calcium- dependent cuticle cell differentiation, hair shaft and hair cuticular barrier formation (By similarity). | 0.915 |
| S100a10 | S100a4 | ENSMUSP00000036949 | ENSMUSP00000001046 | Protein S100-A10; Because S100A10 induces the dimerization of ANXA2/p36, it may function as a regulator of protein phosphorylation in that the ANXA2 monomer is the preferred target (in vitro) of tyrosine-specific kinase; Belongs to the S-100 family. | Protein S100-A4; Belongs to the S-100 family. | 0.946 |
| S100a10 | S100a6 | ENSMUSP00000036949 | ENSMUSP00000001051 | Protein S100-A10; Because S100A10 induces the dimerization of ANXA2/p36, it may function as a regulator of protein phosphorylation in that the ANXA2 monomer is the preferred target (in vitro) of tyrosine-specific kinase; Belongs to the S-100 family. | Protein S100-A6; May function as calcium sensor and modulator, contributing to cellular calcium signaling. May function by interacting with other proteins, such as TPR-containing proteins, and indirectly play a role in many physiological processes such as the reorganization of the actin cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium binding is cooperative (By similarity); Belongs to the S-100 family. | 0.992 |
| S100a10 | S100a7a | ENSMUSP00000036949 | ENSMUSP00000078268 | Protein S100-A10; Because S100A10 induces the dimerization of ANXA2/p36, it may function as a regulator of protein phosphorylation in that the ANXA2 monomer is the preferred target (in vitro) of tyrosine-specific kinase; Belongs to the S-100 family. | Protein S100-A15A; Belongs to the S-100 family. | 0.912 |
| S100a13 | S100a1 | ENSMUSP00000047737 | ENSMUSP00000058237 | Protein S100-A13; Plays a role in the export of proteins that lack a signal peptide and are secreted by an alternative pathway. Binds two calcium ions per subunit. Binds one copper ion. Binding of one copper ion does not interfere with calcium binding. Required for the copper-dependent stress-induced export of IL1A and FGF1. The calcium-free protein binds to lipid vesicles containing phosphatidylserine, but not to vesicles containing phosphatidylcholine. | Protein S100-A1; Probably acts as a Ca(2+) signal transducer. In response to an increase in intracellular Ca(2+) levels, binds calcium which triggers a conformational change. This conformational change allows interaction of S1001A with specific target proteins, such as TPR- containing proteins, and the modulation of their activity. | 0.901 |