| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| A0A0G2K9V8_RAT | Aco2 | ENSRNOP00000075149 | ENSRNOP00000029144 | Uncharacterized protein. | Aconitate hydratase, mitochondrial; Catalyzes the isomerization of citrate to isocitrate via cis- aconitate; Belongs to the aconitase/IPM isomerase family. | 0.483 |
| A0A0G2K9V8_RAT | Dnaja3 | ENSRNOP00000075149 | ENSRNOP00000073394 | Uncharacterized protein. | DnaJ heat shock protein family (Hsp40) member A3. | 0.451 |
| A0A0G2K9V8_RAT | Grpel1 | ENSRNOP00000075149 | ENSRNOP00000070967 | Uncharacterized protein. | GrpE protein homolog 1, mitochondrial; Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Seems to control the nucleotide-dependent binding of mitochondrial HSP70 to substrate proteins; Belongs to the GrpE family. | 0.755 |
| A0A0G2K9V8_RAT | Hspa5 | ENSRNOP00000075149 | ENSRNOP00000025064 | Uncharacterized protein. | 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 [...] | 0.880 |
| A0A0G2K9V8_RAT | Hspa9 | ENSRNOP00000075149 | ENSRNOP00000026696 | Uncharacterized protein. | 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. | 0.975 |
| A0A0G2K9V8_RAT | Hspe1 | ENSRNOP00000075149 | ENSRNOP00000068700 | Uncharacterized protein. | 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 [...] | 0.940 |
| A0A0G2K9V8_RAT | Trap1 | ENSRNOP00000075149 | ENSRNOP00000008966 | Uncharacterized protein. | Heat shock protein 75 kDa, mitochondrial; Chaperone that expresses an ATPase activity. Involved in maintaining mitochondrial function and polarization, downstream of PINK1 and mitochondrial complex I. Is a negative regulator of mitochondrial respiration able to modulate the balance between oxidative phosphorylation and aerobic glycolysis. The impact of TRAP1 on mitochondrial respiration is probably mediated by modulation of mitochondrial SRC and inhibition of SDHA. | 0.714 |
| Aco2 | A0A0G2K9V8_RAT | ENSRNOP00000029144 | ENSRNOP00000075149 | Aconitate hydratase, mitochondrial; Catalyzes the isomerization of citrate to isocitrate via cis- aconitate; Belongs to the aconitase/IPM isomerase family. | Uncharacterized protein. | 0.483 |
| Aco2 | Dnaja3 | ENSRNOP00000029144 | ENSRNOP00000073394 | Aconitate hydratase, mitochondrial; Catalyzes the isomerization of citrate to isocitrate via cis- aconitate; Belongs to the aconitase/IPM isomerase family. | DnaJ heat shock protein family (Hsp40) member A3. | 0.441 |
| Aco2 | Hspa5 | ENSRNOP00000029144 | ENSRNOP00000025064 | Aconitate hydratase, mitochondrial; Catalyzes the isomerization of citrate to isocitrate via cis- aconitate; Belongs to the aconitase/IPM isomerase 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 [...] | 0.417 |
| Aco2 | Hspa9 | ENSRNOP00000029144 | ENSRNOP00000026696 | Aconitate hydratase, mitochondrial; Catalyzes the isomerization of citrate to isocitrate via cis- aconitate; Belongs to the aconitase/IPM isomerase 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. | 0.947 |
| Aco2 | Hspd1 | ENSRNOP00000029144 | ENSRNOP00000063666 | Aconitate hydratase, mitochondrial; Catalyzes the isomerization of citrate to isocitrate via cis- aconitate; Belongs to the aconitase/IPM isomerase 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 [...] | 0.781 |
| Aco2 | Hspe1 | ENSRNOP00000029144 | ENSRNOP00000068700 | Aconitate hydratase, mitochondrial; Catalyzes the isomerization of citrate to isocitrate via cis- aconitate; Belongs to the aconitase/IPM isomerase family. | 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 [...] | 0.400 |
| Aco2 | Trap1 | ENSRNOP00000029144 | ENSRNOP00000008966 | Aconitate hydratase, mitochondrial; Catalyzes the isomerization of citrate to isocitrate via cis- aconitate; Belongs to the aconitase/IPM isomerase family. | Heat shock protein 75 kDa, mitochondrial; Chaperone that expresses an ATPase activity. Involved in maintaining mitochondrial function and polarization, downstream of PINK1 and mitochondrial complex I. Is a negative regulator of mitochondrial respiration able to modulate the balance between oxidative phosphorylation and aerobic glycolysis. The impact of TRAP1 on mitochondrial respiration is probably mediated by modulation of mitochondrial SRC and inhibition of SDHA. | 0.419 |
| Dnaja3 | A0A0G2K9V8_RAT | ENSRNOP00000073394 | ENSRNOP00000075149 | DnaJ heat shock protein family (Hsp40) member A3. | Uncharacterized protein. | 0.451 |
| Dnaja3 | Aco2 | ENSRNOP00000073394 | ENSRNOP00000029144 | DnaJ heat shock protein family (Hsp40) member A3. | Aconitate hydratase, mitochondrial; Catalyzes the isomerization of citrate to isocitrate via cis- aconitate; Belongs to the aconitase/IPM isomerase family. | 0.441 |
| Dnaja3 | Grpel1 | ENSRNOP00000073394 | ENSRNOP00000070967 | DnaJ heat shock protein family (Hsp40) member A3. | GrpE protein homolog 1, mitochondrial; Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Seems to control the nucleotide-dependent binding of mitochondrial HSP70 to substrate proteins; Belongs to the GrpE family. | 0.773 |
| Dnaja3 | Hspa5 | ENSRNOP00000073394 | ENSRNOP00000025064 | DnaJ heat shock protein family (Hsp40) member A3. | 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 [...] | 0.750 |
| Dnaja3 | Hspa9 | ENSRNOP00000073394 | ENSRNOP00000026696 | DnaJ heat shock protein family (Hsp40) member A3. | 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. | 0.966 |
| Dnaja3 | Hspd1 | ENSRNOP00000073394 | ENSRNOP00000063666 | DnaJ heat shock protein family (Hsp40) member A3. | 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 [...] | 0.562 |
