| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CLDN12 | CLDN16 | ENSP00000287916 | ENSP00000264734 | Claudin-12; Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. | Claudin-16; Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. Involved in paracellular magnesium reabsorption. Required for a selective paracellular conductance. May form, alone or in partnership with other constituents, an intercellular pore permitting paracellular passage of magnesium and calcium ions down their electrochemical gradients. Alternatively, it could be a sensor of magnesium concentration that could alter paracellular permeability mediated by other factors. | 0.879 |
| CLDN12 | CLDN2 | ENSP00000287916 | ENSP00000336571 | Claudin-12; Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. | Claudin-2; Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. | 0.960 |
| CLDN12 | CLDN7 | ENSP00000287916 | ENSP00000353475 | Claudin-12; Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. | Claudin-7; Plays a major role in tight junction-specific obliteration of the intercellular space; Belongs to the claudin family. | 0.950 |
| CLDN12 | OCLN | ENSP00000287916 | ENSP00000347379 | Claudin-12; Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. | Occludin; May play a role in the formation and regulation of the tight junction (TJ) paracellular permeability barrier. It is able to induce adhesion when expressed in cells lacking tight junctions. | 0.924 |
| CLDN12 | PARD3 | ENSP00000287916 | ENSP00000363921 | Claudin-12; Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. | Partitioning defective 3 homolog; Adapter protein involved in asymmetrical cell division and cell polarization processes. Seems to play a central role in the formation of epithelial tight junctions. Targets the phosphatase PTEN to cell junctions (By similarity). Involved in Schwann cell peripheral myelination (By similarity). Association with PARD6B may prevent the interaction of PARD3 with F11R/JAM1, thereby preventing tight junction assembly (By similarity). The PARD6-PARD3 complex links GTP-bound Rho small GTPases to atypical protein kinase C proteins. Required for establishment of [...] | 0.713 |
| CLDN12 | TJP1 | ENSP00000287916 | ENSP00000348416 | Claudin-12; Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. | Tight junction protein ZO-1; TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton. The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Necessary for lumenogenesis, and particularly efficient epithelial polarization and barrier formation (By similarity). Plays a role i [...] | 0.927 |
| CLDN12 | TJP2 | ENSP00000287916 | ENSP00000438262 | Claudin-12; Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. | Tight junction protein ZO-2; Plays a role in tight junctions and adherens junctions. | 0.694 |
| CLDN12 | TJP3 | ENSP00000287916 | ENSP00000465419 | Claudin-12; Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. | Tight junction protein ZO-3; TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton. The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Binds and recruits PATJ to tight junctions where it connects and stabilizes apical and lateral components of tight junctions. Promote [...] | 0.850 |
| CLDN16 | CLDN12 | ENSP00000264734 | ENSP00000287916 | Claudin-16; Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. Involved in paracellular magnesium reabsorption. Required for a selective paracellular conductance. May form, alone or in partnership with other constituents, an intercellular pore permitting paracellular passage of magnesium and calcium ions down their electrochemical gradients. Alternatively, it could be a sensor of magnesium concentration that could alter paracellular permeability mediated by other factors. | Claudin-12; Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. | 0.879 |
| CLDN16 | CLDN2 | ENSP00000264734 | ENSP00000336571 | Claudin-16; Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. Involved in paracellular magnesium reabsorption. Required for a selective paracellular conductance. May form, alone or in partnership with other constituents, an intercellular pore permitting paracellular passage of magnesium and calcium ions down their electrochemical gradients. Alternatively, it could be a sensor of magnesium concentration that could alter paracellular permeability mediated by other factors. | Claudin-2; Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. | 0.741 |
| CLDN16 | CLDN7 | ENSP00000264734 | ENSP00000353475 | Claudin-16; Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. Involved in paracellular magnesium reabsorption. Required for a selective paracellular conductance. May form, alone or in partnership with other constituents, an intercellular pore permitting paracellular passage of magnesium and calcium ions down their electrochemical gradients. Alternatively, it could be a sensor of magnesium concentration that could alter paracellular permeability mediated by other factors. | Claudin-7; Plays a major role in tight junction-specific obliteration of the intercellular space; Belongs to the claudin family. | 0.727 |
| CLDN16 | OCLN | ENSP00000264734 | ENSP00000347379 | Claudin-16; Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. Involved in paracellular magnesium reabsorption. Required for a selective paracellular conductance. May form, alone or in partnership with other constituents, an intercellular pore permitting paracellular passage of magnesium and calcium ions down their electrochemical gradients. Alternatively, it could be a sensor of magnesium concentration that could alter paracellular permeability mediated by other factors. | Occludin; May play a role in the formation and regulation of the tight junction (TJ) paracellular permeability barrier. It is able to induce adhesion when expressed in cells lacking tight junctions. | 0.887 |
| CLDN16 | PARD3 | ENSP00000264734 | ENSP00000363921 | Claudin-16; Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. Involved in paracellular magnesium reabsorption. Required for a selective paracellular conductance. May form, alone or in partnership with other constituents, an intercellular pore permitting paracellular passage of magnesium and calcium ions down their electrochemical gradients. Alternatively, it could be a sensor of magnesium concentration that could alter paracellular permeability mediated by other factors. | Partitioning defective 3 homolog; Adapter protein involved in asymmetrical cell division and cell polarization processes. Seems to play a central role in the formation of epithelial tight junctions. Targets the phosphatase PTEN to cell junctions (By similarity). Involved in Schwann cell peripheral myelination (By similarity). Association with PARD6B may prevent the interaction of PARD3 with F11R/JAM1, thereby preventing tight junction assembly (By similarity). The PARD6-PARD3 complex links GTP-bound Rho small GTPases to atypical protein kinase C proteins. Required for establishment of [...] | 0.669 |
| CLDN16 | TJP1 | ENSP00000264734 | ENSP00000348416 | Claudin-16; Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. Involved in paracellular magnesium reabsorption. Required for a selective paracellular conductance. May form, alone or in partnership with other constituents, an intercellular pore permitting paracellular passage of magnesium and calcium ions down their electrochemical gradients. Alternatively, it could be a sensor of magnesium concentration that could alter paracellular permeability mediated by other factors. | Tight junction protein ZO-1; TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton. The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Necessary for lumenogenesis, and particularly efficient epithelial polarization and barrier formation (By similarity). Plays a role i [...] | 0.890 |
| CLDN16 | TJP2 | ENSP00000264734 | ENSP00000438262 | Claudin-16; Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. Involved in paracellular magnesium reabsorption. Required for a selective paracellular conductance. May form, alone or in partnership with other constituents, an intercellular pore permitting paracellular passage of magnesium and calcium ions down their electrochemical gradients. Alternatively, it could be a sensor of magnesium concentration that could alter paracellular permeability mediated by other factors. | Tight junction protein ZO-2; Plays a role in tight junctions and adherens junctions. | 0.529 |
| CLDN16 | TJP3 | ENSP00000264734 | ENSP00000465419 | Claudin-16; Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. Involved in paracellular magnesium reabsorption. Required for a selective paracellular conductance. May form, alone or in partnership with other constituents, an intercellular pore permitting paracellular passage of magnesium and calcium ions down their electrochemical gradients. Alternatively, it could be a sensor of magnesium concentration that could alter paracellular permeability mediated by other factors. | Tight junction protein ZO-3; TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton. The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Binds and recruits PATJ to tight junctions where it connects and stabilizes apical and lateral components of tight junctions. Promote [...] | 0.791 |
| CLDN2 | CLDN12 | ENSP00000336571 | ENSP00000287916 | Claudin-2; Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. | Claudin-12; Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. | 0.960 |
| CLDN2 | CLDN16 | ENSP00000336571 | ENSP00000264734 | Claudin-2; Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. | Claudin-16; Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. Involved in paracellular magnesium reabsorption. Required for a selective paracellular conductance. May form, alone or in partnership with other constituents, an intercellular pore permitting paracellular passage of magnesium and calcium ions down their electrochemical gradients. Alternatively, it could be a sensor of magnesium concentration that could alter paracellular permeability mediated by other factors. | 0.741 |
| CLDN2 | CLDN7 | ENSP00000336571 | ENSP00000353475 | Claudin-2; Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. | Claudin-7; Plays a major role in tight junction-specific obliteration of the intercellular space; Belongs to the claudin family. | 0.729 |
| CLDN2 | HSP90AA1 | ENSP00000336571 | ENSP00000335153 | Claudin-2; Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. | Heat shock protein HSP 90-alpha; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a ra [...] | 0.807 |
