node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Aqp11 | Aqp12 | ENSMUSP00000146215 | ENSMUSP00000060622 | Aquaporin-11; Channel protein that facilitates the transport of water, glycerol and hydrogen peroxide across membrane of cell or organelles guaranteeing intracellular homeostasis in several organes like liver, kidney and brain. In situation of stress, participates in endoplasmic reticulum (ER) homeostasis by regulating redox homeostasis through the transport of hydrogen peroxide across the endoplasmic reticulum membrane thereby regulating the oxidative stress through the NADPH oxidase 2 pathway. Plays a role by maintaining an environment suitable for translation or protein foldings in [...] | Aquaporin-12; Aquaporins facilitate the transport of water and small neutral solutes across cell membranes; Belongs to the MIP/aquaporin (TC 1.A.8) family. AQP11/AQP12 subfamily. | 0.617 |
Aqp11 | Mip | ENSMUSP00000146215 | ENSMUSP00000026455 | Aquaporin-11; Channel protein that facilitates the transport of water, glycerol and hydrogen peroxide across membrane of cell or organelles guaranteeing intracellular homeostasis in several organes like liver, kidney and brain. In situation of stress, participates in endoplasmic reticulum (ER) homeostasis by regulating redox homeostasis through the transport of hydrogen peroxide across the endoplasmic reticulum membrane thereby regulating the oxidative stress through the NADPH oxidase 2 pathway. Plays a role by maintaining an environment suitable for translation or protein foldings in [...] | Lens fiber major intrinsic protein; Water channel. Channel activity is down-regulated by CALM when cytoplasmic Ca(2+) levels are increased. May be responsible for regulating the osmolarity of the lens. Interactions between homotetramers from adjoining membranes may stabilize cell junctions in the eye lens core. Plays a role in cell-to-cell adhesion and facilitates gap junction coupling (By similarity). Belongs to the MIP/aquaporin (TC 1.A.8) family. | 0.933 |
Aqp12 | Aqp11 | ENSMUSP00000060622 | ENSMUSP00000146215 | Aquaporin-12; Aquaporins facilitate the transport of water and small neutral solutes across cell membranes; Belongs to the MIP/aquaporin (TC 1.A.8) family. AQP11/AQP12 subfamily. | Aquaporin-11; Channel protein that facilitates the transport of water, glycerol and hydrogen peroxide across membrane of cell or organelles guaranteeing intracellular homeostasis in several organes like liver, kidney and brain. In situation of stress, participates in endoplasmic reticulum (ER) homeostasis by regulating redox homeostasis through the transport of hydrogen peroxide across the endoplasmic reticulum membrane thereby regulating the oxidative stress through the NADPH oxidase 2 pathway. Plays a role by maintaining an environment suitable for translation or protein foldings in [...] | 0.617 |
Aqp12 | Mip | ENSMUSP00000060622 | ENSMUSP00000026455 | Aquaporin-12; Aquaporins facilitate the transport of water and small neutral solutes across cell membranes; Belongs to the MIP/aquaporin (TC 1.A.8) family. AQP11/AQP12 subfamily. | Lens fiber major intrinsic protein; Water channel. Channel activity is down-regulated by CALM when cytoplasmic Ca(2+) levels are increased. May be responsible for regulating the osmolarity of the lens. Interactions between homotetramers from adjoining membranes may stabilize cell junctions in the eye lens core. Plays a role in cell-to-cell adhesion and facilitates gap junction coupling (By similarity). Belongs to the MIP/aquaporin (TC 1.A.8) family. | 0.945 |
Bfsp1 | Cryaa | ENSMUSP00000096899 | ENSMUSP00000019192 | Filensin C-terminal fragment; Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity). Involved in altering the calcium regulation of MIP water permeability (By similarity). | Alpha-crystallin A chain; Contributes to the transparency and refractive index of the lens (By similarity). Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions (By similarity). Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity). | 0.834 |
Bfsp1 | Crygs | ENSMUSP00000096899 | ENSMUSP00000043588 | Filensin C-terminal fragment; Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity). Involved in altering the calcium regulation of MIP water permeability (By similarity). | Gamma-crystallin S; Crystallins are the dominant structural components of the vertebrate eye lens. | 0.794 |
Bfsp1 | Gja8 | ENSMUSP00000096899 | ENSMUSP00000049532 | Filensin C-terminal fragment; Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity). Involved in altering the calcium regulation of MIP water permeability (By similarity). | Gap junction alpha-8 protein; Structural component of eye lens gap junctions. Gap junctions are dodecameric channels that connect the cytoplasm of adjoining cells. They are formed by the docking of two hexameric hemichannels, one from each cell membrane (By similarity). Small molecules and ions diffuse from one cell to a neighboring cell via the central pore ; Belongs to the connexin family. Alpha-type (group II) subfamily. | 0.796 |
Bfsp1 | Mip | ENSMUSP00000096899 | ENSMUSP00000026455 | Filensin C-terminal fragment; Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity). Involved in altering the calcium regulation of MIP water permeability (By similarity). | Lens fiber major intrinsic protein; Water channel. Channel activity is down-regulated by CALM when cytoplasmic Ca(2+) levels are increased. May be responsible for regulating the osmolarity of the lens. Interactions between homotetramers from adjoining membranes may stabilize cell junctions in the eye lens core. Plays a role in cell-to-cell adhesion and facilitates gap junction coupling (By similarity). Belongs to the MIP/aquaporin (TC 1.A.8) family. | 0.887 |
Calm4 | Calm5 | ENSMUSP00000041636 | ENSMUSP00000139342 | Calmodulin-4; Implicated in the early stage of ectopic ossification. | Skin calmodulin-related protein 2. | 0.955 |
Calm4 | Calml3 | ENSMUSP00000041636 | ENSMUSP00000076880 | Calmodulin-4; Implicated in the early stage of ectopic ossification. | Calmodulin-like protein 3; May function as a specific light chain of unconventional myosin-10 (MYO10), also enhances MYO10 translation, possibly by acting as a chaperone for the emerging MYO10 heavy chain protein. May compete with calmodulin by binding, with different affinities, to cellular substrates (By similarity). | 0.961 |
Calm4 | Calml4 | ENSMUSP00000041636 | ENSMUSP00000034777 | Calmodulin-4; Implicated in the early stage of ectopic ossification. | Calmodulin-like protein 4. | 0.953 |
Calm4 | Gja8 | ENSMUSP00000041636 | ENSMUSP00000049532 | Calmodulin-4; Implicated in the early stage of ectopic ossification. | Gap junction alpha-8 protein; Structural component of eye lens gap junctions. Gap junctions are dodecameric channels that connect the cytoplasm of adjoining cells. They are formed by the docking of two hexameric hemichannels, one from each cell membrane (By similarity). Small molecules and ions diffuse from one cell to a neighboring cell via the central pore ; Belongs to the connexin family. Alpha-type (group II) subfamily. | 0.515 |
Calm4 | Mip | ENSMUSP00000041636 | ENSMUSP00000026455 | Calmodulin-4; Implicated in the early stage of ectopic ossification. | Lens fiber major intrinsic protein; Water channel. Channel activity is down-regulated by CALM when cytoplasmic Ca(2+) levels are increased. May be responsible for regulating the osmolarity of the lens. Interactions between homotetramers from adjoining membranes may stabilize cell junctions in the eye lens core. Plays a role in cell-to-cell adhesion and facilitates gap junction coupling (By similarity). Belongs to the MIP/aquaporin (TC 1.A.8) family. | 0.936 |
Calm5 | Calm4 | ENSMUSP00000139342 | ENSMUSP00000041636 | Skin calmodulin-related protein 2. | Calmodulin-4; Implicated in the early stage of ectopic ossification. | 0.955 |
Calm5 | Calml3 | ENSMUSP00000139342 | ENSMUSP00000076880 | Skin calmodulin-related protein 2. | Calmodulin-like protein 3; May function as a specific light chain of unconventional myosin-10 (MYO10), also enhances MYO10 translation, possibly by acting as a chaperone for the emerging MYO10 heavy chain protein. May compete with calmodulin by binding, with different affinities, to cellular substrates (By similarity). | 0.953 |
Calm5 | Calml4 | ENSMUSP00000139342 | ENSMUSP00000034777 | Skin calmodulin-related protein 2. | Calmodulin-like protein 4. | 0.965 |
Calm5 | Gja8 | ENSMUSP00000139342 | ENSMUSP00000049532 | Skin calmodulin-related protein 2. | Gap junction alpha-8 protein; Structural component of eye lens gap junctions. Gap junctions are dodecameric channels that connect the cytoplasm of adjoining cells. They are formed by the docking of two hexameric hemichannels, one from each cell membrane (By similarity). Small molecules and ions diffuse from one cell to a neighboring cell via the central pore ; Belongs to the connexin family. Alpha-type (group II) subfamily. | 0.515 |
Calm5 | Mip | ENSMUSP00000139342 | ENSMUSP00000026455 | Skin calmodulin-related protein 2. | Lens fiber major intrinsic protein; Water channel. Channel activity is down-regulated by CALM when cytoplasmic Ca(2+) levels are increased. May be responsible for regulating the osmolarity of the lens. Interactions between homotetramers from adjoining membranes may stabilize cell junctions in the eye lens core. Plays a role in cell-to-cell adhesion and facilitates gap junction coupling (By similarity). Belongs to the MIP/aquaporin (TC 1.A.8) family. | 0.936 |
Calml3 | Calm4 | ENSMUSP00000076880 | ENSMUSP00000041636 | Calmodulin-like protein 3; May function as a specific light chain of unconventional myosin-10 (MYO10), also enhances MYO10 translation, possibly by acting as a chaperone for the emerging MYO10 heavy chain protein. May compete with calmodulin by binding, with different affinities, to cellular substrates (By similarity). | Calmodulin-4; Implicated in the early stage of ectopic ossification. | 0.961 |
Calml3 | Calm5 | ENSMUSP00000076880 | ENSMUSP00000139342 | Calmodulin-like protein 3; May function as a specific light chain of unconventional myosin-10 (MYO10), also enhances MYO10 translation, possibly by acting as a chaperone for the emerging MYO10 heavy chain protein. May compete with calmodulin by binding, with different affinities, to cellular substrates (By similarity). | Skin calmodulin-related protein 2. | 0.953 |