node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
A0A287BQU9_PIG | BAG3 | ENSSSCP00000058891 | ENSSSCP00000011385 | Uncharacterized protein. | BCL2 associated athanogene 3. | 0.965 |
A0A287BQU9_PIG | CRYAB | ENSSSCP00000058891 | ENSSSCP00000047187 | Uncharacterized protein. | Alpha-crystallin B chain; May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. | 0.598 |
A0A287BQU9_PIG | HSP90AA1 | ENSSSCP00000058891 | ENSSSCP00000046159 | Uncharacterized protein. | 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 [...] | 0.900 |
A0A287BQU9_PIG | HSPB1 | ENSSSCP00000058891 | ENSSSCP00000008215 | Uncharacterized protein. | Heat shock protein beta-1; Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding- competent state. Plays a role in stress resistance and actin organization. Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins. | 0.780 |
A0A287BQU9_PIG | TP53 | ENSSSCP00000058891 | ENSSSCP00000050664 | Uncharacterized protein. | Cellular tumor antigen p53; Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. Its pro-apoptotic activity is activated via its intera [...] | 0.459 |
BAG3 | A0A287BQU9_PIG | ENSSSCP00000011385 | ENSSSCP00000058891 | BCL2 associated athanogene 3. | Uncharacterized protein. | 0.965 |
BAG3 | CRYAB | ENSSSCP00000011385 | ENSSSCP00000047187 | BCL2 associated athanogene 3. | Alpha-crystallin B chain; May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. | 0.622 |
BAG3 | HSP90AA1 | ENSSSCP00000011385 | ENSSSCP00000046159 | BCL2 associated athanogene 3. | 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 [...] | 0.681 |
BAG3 | HSPA6 | ENSSSCP00000011385 | ENSSSCP00000073047 | BCL2 associated athanogene 3. | Heat shock 70 kDa protein 6; Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP [...] | 0.881 |
BAG3 | HSPB1 | ENSSSCP00000011385 | ENSSSCP00000008215 | BCL2 associated athanogene 3. | Heat shock protein beta-1; Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding- competent state. Plays a role in stress resistance and actin organization. Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins. | 0.773 |
CRYAB | A0A287BQU9_PIG | ENSSSCP00000047187 | ENSSSCP00000058891 | Alpha-crystallin B chain; May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. | Uncharacterized protein. | 0.598 |
CRYAB | BAG3 | ENSSSCP00000047187 | ENSSSCP00000011385 | Alpha-crystallin B chain; May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. | BCL2 associated athanogene 3. | 0.622 |
CRYAB | DAXX | ENSSSCP00000047187 | ENSSSCP00000001638 | Alpha-crystallin B chain; May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. | Death domain associated protein. | 0.448 |
CRYAB | HSP90AA1 | ENSSSCP00000047187 | ENSSSCP00000046159 | Alpha-crystallin B chain; May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. | 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 [...] | 0.642 |
CRYAB | HSPA6 | ENSSSCP00000047187 | ENSSSCP00000073047 | Alpha-crystallin B chain; May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. | Heat shock 70 kDa protein 6; Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP [...] | 0.932 |
CRYAB | HSPB1 | ENSSSCP00000047187 | ENSSSCP00000008215 | Alpha-crystallin B chain; May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. | Heat shock protein beta-1; Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding- competent state. Plays a role in stress resistance and actin organization. Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins. | 0.783 |
DAXX | CRYAB | ENSSSCP00000001638 | ENSSSCP00000047187 | Death domain associated protein. | Alpha-crystallin B chain; May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. | 0.448 |
DAXX | HSPB1 | ENSSSCP00000001638 | ENSSSCP00000008215 | Death domain associated protein. | Heat shock protein beta-1; Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding- competent state. Plays a role in stress resistance and actin organization. Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins. | 0.765 |
DAXX | TP53 | ENSSSCP00000001638 | ENSSSCP00000050664 | Death domain associated protein. | Cellular tumor antigen p53; Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. Its pro-apoptotic activity is activated via its intera [...] | 0.987 |
HSP90AA1 | A0A287BQU9_PIG | ENSSSCP00000046159 | ENSSSCP00000058891 | 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 [...] | Uncharacterized protein. | 0.900 |