| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| A0A0G2JVI0_RAT | Hsp90aa1 | ENSRNOP00000069492 | ENSRNOP00000075715 | Uncharacterized protein; Belongs to the GroES chaperonin family. | Heat shock protein 90 alpha family class A member 1. | 0.537 |
| A0A0G2JVI0_RAT | Hsp90b1 | ENSRNOP00000069492 | ENSRNOP00000034846 | Uncharacterized protein; Belongs to the GroES chaperonin family. | Endoplasmin; Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity. | 0.557 |
| A0A0G2JVI0_RAT | Hspa1b | ENSRNOP00000069492 | ENSRNOP00000075599 | Uncharacterized protein; Belongs to the GroES chaperonin family. | Heat shock protein family A (Hsp70) member 1B. | 0.519 |
| A0A0G2JVI0_RAT | Hspa4 | ENSRNOP00000069492 | ENSRNOP00000023628 | Uncharacterized protein; Belongs to the GroES chaperonin family. | Heat shock 70 kDa protein 4; Belongs to the heat shock protein 70 family. | 0.518 |
| A0A0G2JVI0_RAT | Hspa5 | ENSRNOP00000069492 | ENSRNOP00000025064 | Uncharacterized protein; Belongs to the GroES chaperonin family. | Endoplasmic reticulum chaperone BiP; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to dis [...] | 0.505 |
| A0A0G2JVI0_RAT | Hspa9 | ENSRNOP00000069492 | ENSRNOP00000026696 | Uncharacterized protein; Belongs to the GroES chaperonin family. | Stress-70 protein, mitochondrial; Chaperone protein which plays an important role in mitochondrial iron-sulfur cluster (ISC) biogenesis. Interacts with and stabilizes ISC cluster assembly proteins FXN, NFU1, NFS1 and ISCU. Regulates erythropoiesis via stabilization of ISC assembly. May play a role in the control of cell proliferation and cellular aging. | 0.822 |
| A0A0G2JVI0_RAT | Hspd1 | ENSRNOP00000069492 | ENSRNOP00000063666 | Uncharacterized protein; Belongs to the GroES chaperonin family. | 60 kDa heat shock protein, mitochondrial; Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per rin [...] | 0.947 |
| Cd14 | Hspd1 | ENSRNOP00000023977 | ENSRNOP00000063666 | Monocyte differentiation antigen CD14; Coreceptor for bacterial lipopolysaccharide. In concert with LBP, binds to monomeric lipopolysaccharide and delivers it to the LY96/TLR4 complex, thereby mediating the innate immune response to bacterial lipopolysaccharide (LPS). Acts via MyD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Acts as a coreceptor for TLR2:TLR6 heterodimer in response to diacylated lipopeptides and for TLR2:TLR1 heterodimer in response to triacylated lipopeptides, these clusters trigger signaling from the cell su [...] | 60 kDa heat shock protein, mitochondrial; Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per rin [...] | 0.926 |
| Cd14 | Tlr4 | ENSRNOP00000023977 | ENSRNOP00000014020 | Monocyte differentiation antigen CD14; Coreceptor for bacterial lipopolysaccharide. In concert with LBP, binds to monomeric lipopolysaccharide and delivers it to the LY96/TLR4 complex, thereby mediating the innate immune response to bacterial lipopolysaccharide (LPS). Acts via MyD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Acts as a coreceptor for TLR2:TLR6 heterodimer in response to diacylated lipopeptides and for TLR2:TLR1 heterodimer in response to triacylated lipopeptides, these clusters trigger signaling from the cell su [...] | Toll-like receptor 4; Cooperates with LY96 and CD14 to mediate the innate immune response to bacterial lipopolysaccharide (LPS). Acts via MYD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Also involved in LPS-independent inflammatory responses triggered by free fatty acids, such as palmitate. In complex with TLR6, promotes sterile inflammation in monocytes/macrophages in response to oxidized low-density lipoprotein (oxLDL) or amyloid-beta 42. In this context, the initial signal is provided by oxLDL- or amyloid-beta 42-binding to [...] | 0.996 |
| Hsp90aa1 | A0A0G2JVI0_RAT | ENSRNOP00000075715 | ENSRNOP00000069492 | Heat shock protein 90 alpha family class A member 1. | Uncharacterized protein; Belongs to the GroES chaperonin family. | 0.537 |
| Hsp90aa1 | Hsp90b1 | ENSRNOP00000075715 | ENSRNOP00000034846 | Heat shock protein 90 alpha family class A member 1. | Endoplasmin; Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity. | 0.904 |
| Hsp90aa1 | Hspa1b | ENSRNOP00000075715 | ENSRNOP00000075599 | Heat shock protein 90 alpha family class A member 1. | Heat shock protein family A (Hsp70) member 1B. | 0.974 |
| Hsp90aa1 | Hspa4 | ENSRNOP00000075715 | ENSRNOP00000023628 | Heat shock protein 90 alpha family class A member 1. | Heat shock 70 kDa protein 4; Belongs to the heat shock protein 70 family. | 0.989 |
| Hsp90aa1 | Hspa5 | ENSRNOP00000075715 | ENSRNOP00000025064 | Heat shock protein 90 alpha family class A member 1. | Endoplasmic reticulum chaperone BiP; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to dis [...] | 0.897 |
| Hsp90aa1 | Hspa9 | ENSRNOP00000075715 | ENSRNOP00000026696 | Heat shock protein 90 alpha family class A member 1. | Stress-70 protein, mitochondrial; Chaperone protein which plays an important role in mitochondrial iron-sulfur cluster (ISC) biogenesis. Interacts with and stabilizes ISC cluster assembly proteins FXN, NFU1, NFS1 and ISCU. Regulates erythropoiesis via stabilization of ISC assembly. May play a role in the control of cell proliferation and cellular aging. | 0.875 |
| Hsp90aa1 | Hspd1 | ENSRNOP00000075715 | ENSRNOP00000063666 | Heat shock protein 90 alpha family class A member 1. | 60 kDa heat shock protein, mitochondrial; Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per rin [...] | 0.941 |
| Hsp90aa1 | Hspe1 | ENSRNOP00000075715 | ENSRNOP00000068700 | Heat shock protein 90 alpha family class A member 1. | 10 kDa heat shock protein, mitochondrial; Co-chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp60, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per [...] | 0.826 |
| Hsp90aa1 | Tlr4 | ENSRNOP00000075715 | ENSRNOP00000014020 | Heat shock protein 90 alpha family class A member 1. | Toll-like receptor 4; Cooperates with LY96 and CD14 to mediate the innate immune response to bacterial lipopolysaccharide (LPS). Acts via MYD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Also involved in LPS-independent inflammatory responses triggered by free fatty acids, such as palmitate. In complex with TLR6, promotes sterile inflammation in monocytes/macrophages in response to oxidized low-density lipoprotein (oxLDL) or amyloid-beta 42. In this context, the initial signal is provided by oxLDL- or amyloid-beta 42-binding to [...] | 0.608 |
| Hsp90b1 | A0A0G2JVI0_RAT | ENSRNOP00000034846 | ENSRNOP00000069492 | Endoplasmin; Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity. | Uncharacterized protein; Belongs to the GroES chaperonin family. | 0.557 |
| Hsp90b1 | Hsp90aa1 | ENSRNOP00000034846 | ENSRNOP00000075715 | Endoplasmin; Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity. | Heat shock protein 90 alpha family class A member 1. | 0.904 |
