| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Cad | Dnaja1 | ENSRNOP00000030030 | ENSRNOP00000010061 | CAD protein | DnaJ homolog subfamily A member 1 ; Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co- chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone (PubMed-10816573) | 0.808 |
| Cad | Dnajb11 | ENSRNOP00000030030 | ENSRNOP00000002462 | CAD protein | DnaJ homolog subfamily B member 11 ; Serves as a co-chaperone for HSPA5. Binds directly to both unfolded proteins that are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed. May help recruiting HSPA5 and other chaperones to the substrate. Stimulates HSPA5 ATPase activity (By similarity) | 0.808 |
| Cad | Dnajb9 | ENSRNOP00000030030 | ENSRNOP00000005363 | CAD protein | DnaJ homolog subfamily B member 9 ; Involved in endoplasmic reticulum-associated degradation (ERAD) of misfolded proteins. Acts as a co-chaperone with an Hsp70 protein (By similarity) | 0.808 |
| Cad | Dnajc10 | ENSRNOP00000030030 | ENSRNOP00000009839 | CAD protein | DnaJ homolog subfamily C member 10 ; Endoplasmic reticulum disulfide reductase involved both in the correct folding of proteins and degradation of misfolded proteins. Required for efficient folding of proteins in the endoplasmic reticulum by catalyzing the removal of non-native disulfide bonds formed during the folding of proteins, such as LDLR. Also involved in endoplasmic reticulum-associated degradation (ERAD) by reducing incorrect disulfide bonds in misfolded glycoproteins recognized by EDEM1. Interaction with HSPA5 is required its activity, not for the disulfide reductase activity [...] | 0.701 |
| Cad | Hsp90aa1 | ENSRNOP00000030030 | ENSRNOP00000009556 | CAD 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. 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 (By similarity). Binds bacterial lipopolysaccharide (LPS) et me [...] | 0.866 |
| Cad | Hsp90ab1 | ENSRNOP00000030030 | ENSRNOP00000026920 | CAD protein | Heat shock protein HSP 90-beta ; 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. 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 (By similarity) | 0.866 |
| Cad | Hsp90b1 | ENSRNOP00000030030 | ENSRNOP00000034846 | CAD protein | 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 (By similarity) | 0.866 |
| Cad | Hspa5 | ENSRNOP00000030030 | ENSRNOP00000025064 | CAD protein | 78 kDa glucose-regulated protein ; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the endoplasmic reticulum. Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10, probably to facilitate the release of DNAJC10 from its substrate (By similarity) | 0.955 |
| Dnaja1 | Cad | ENSRNOP00000010061 | ENSRNOP00000030030 | DnaJ homolog subfamily A member 1 ; Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co- chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone (PubMed-10816573) | CAD protein | 0.808 |
| Dnaja1 | Dnajb9 | ENSRNOP00000010061 | ENSRNOP00000005363 | DnaJ homolog subfamily A member 1 ; Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co- chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone (PubMed-10816573) | DnaJ homolog subfamily B member 9 ; Involved in endoplasmic reticulum-associated degradation (ERAD) of misfolded proteins. Acts as a co-chaperone with an Hsp70 protein (By similarity) | 0.400 |
| Dnaja1 | Dnajc6 | ENSRNOP00000010061 | ENSRNOP00000059262 | DnaJ homolog subfamily A member 1 ; Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co- chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone (PubMed-10816573) | Putative tyrosine-protein phosphatase auxilin | 0.491 |
| Dnaja1 | Hsp90aa1 | ENSRNOP00000010061 | ENSRNOP00000009556 | DnaJ homolog subfamily A member 1 ; Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co- chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone (PubMed-10816573) | 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. 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 (By similarity). Binds bacterial lipopolysaccharide (LPS) et me [...] | 0.986 |
| Dnaja1 | Hsp90ab1 | ENSRNOP00000010061 | ENSRNOP00000026920 | DnaJ homolog subfamily A member 1 ; Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co- chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone (PubMed-10816573) | Heat shock protein HSP 90-beta ; 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. 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 (By similarity) | 0.981 |
| Dnaja1 | Hsp90b1 | ENSRNOP00000010061 | ENSRNOP00000034846 | DnaJ homolog subfamily A member 1 ; Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co- chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone (PubMed-10816573) | 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 (By similarity) | 0.916 |
| Dnaja1 | Hspa5 | ENSRNOP00000010061 | ENSRNOP00000025064 | DnaJ homolog subfamily A member 1 ; Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co- chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone (PubMed-10816573) | 78 kDa glucose-regulated protein ; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the endoplasmic reticulum. Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10, probably to facilitate the release of DNAJC10 from its substrate (By similarity) | 0.962 |
| Dnajb11 | Cad | ENSRNOP00000002462 | ENSRNOP00000030030 | DnaJ homolog subfamily B member 11 ; Serves as a co-chaperone for HSPA5. Binds directly to both unfolded proteins that are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed. May help recruiting HSPA5 and other chaperones to the substrate. Stimulates HSPA5 ATPase activity (By similarity) | CAD protein | 0.808 |
| Dnajb11 | Dnajb9 | ENSRNOP00000002462 | ENSRNOP00000005363 | DnaJ homolog subfamily B member 11 ; Serves as a co-chaperone for HSPA5. Binds directly to both unfolded proteins that are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed. May help recruiting HSPA5 and other chaperones to the substrate. Stimulates HSPA5 ATPase activity (By similarity) | DnaJ homolog subfamily B member 9 ; Involved in endoplasmic reticulum-associated degradation (ERAD) of misfolded proteins. Acts as a co-chaperone with an Hsp70 protein (By similarity) | 0.491 |
| Dnajb11 | Dnajc10 | ENSRNOP00000002462 | ENSRNOP00000009839 | DnaJ homolog subfamily B member 11 ; Serves as a co-chaperone for HSPA5. Binds directly to both unfolded proteins that are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed. May help recruiting HSPA5 and other chaperones to the substrate. Stimulates HSPA5 ATPase activity (By similarity) | DnaJ homolog subfamily C member 10 ; Endoplasmic reticulum disulfide reductase involved both in the correct folding of proteins and degradation of misfolded proteins. Required for efficient folding of proteins in the endoplasmic reticulum by catalyzing the removal of non-native disulfide bonds formed during the folding of proteins, such as LDLR. Also involved in endoplasmic reticulum-associated degradation (ERAD) by reducing incorrect disulfide bonds in misfolded glycoproteins recognized by EDEM1. Interaction with HSPA5 is required its activity, not for the disulfide reductase activity [...] | 0.772 |
| Dnajb11 | Hsp90aa1 | ENSRNOP00000002462 | ENSRNOP00000009556 | DnaJ homolog subfamily B member 11 ; Serves as a co-chaperone for HSPA5. Binds directly to both unfolded proteins that are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed. May help recruiting HSPA5 and other chaperones to the substrate. Stimulates HSPA5 ATPase activity (By similarity) | 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. 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 (By similarity). Binds bacterial lipopolysaccharide (LPS) et me [...] | 0.676 |
| Dnajb11 | Hsp90ab1 | ENSRNOP00000002462 | ENSRNOP00000026920 | DnaJ homolog subfamily B member 11 ; Serves as a co-chaperone for HSPA5. Binds directly to both unfolded proteins that are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed. May help recruiting HSPA5 and other chaperones to the substrate. Stimulates HSPA5 ATPase activity (By similarity) | Heat shock protein HSP 90-beta ; 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. 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 (By similarity) | 0.666 |
Share
