node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
DNAJB9 | HSP90B1 | ENSP00000249356 | ENSP00000299767 | DnaJ (Hsp40) homolog, subfamily B, member 9; Acts as a co-chaperone with an Hsp70 protein (By similarity) | heat shock protein 90kDa beta (Grp94), member 1; Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity | 0.902 |
DNAJB9 | HSPA13 | ENSP00000249356 | ENSP00000285667 | DnaJ (Hsp40) homolog, subfamily B, member 9; Acts as a co-chaperone with an Hsp70 protein (By similarity) | heat shock protein 70kDa family, member 13; Has peptide-independent ATPase activity | 0.925 |
DNAJB9 | HSPA1A | ENSP00000249356 | ENSP00000364802 | DnaJ (Hsp40) homolog, subfamily B, member 9; Acts as a co-chaperone with an Hsp70 protein (By similarity) | heat shock 70kDa protein 1A | 0.902 |
DNAJB9 | HSPA1B | ENSP00000249356 | ENSP00000364801 | DnaJ (Hsp40) homolog, subfamily B, member 9; Acts as a co-chaperone with an Hsp70 protein (By similarity) | heat shock 70kDa protein 1B | 0.901 |
DNAJB9 | HSPA2 | ENSP00000249356 | ENSP00000247207 | DnaJ (Hsp40) homolog, subfamily B, member 9; Acts as a co-chaperone with an Hsp70 protein (By similarity) | heat shock 70kDa protein 2; In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage | 0.896 |
DNAJB9 | HSPA4 | ENSP00000249356 | ENSP00000302961 | DnaJ (Hsp40) homolog, subfamily B, member 9; Acts as a co-chaperone with an Hsp70 protein (By similarity) | heat shock 70kDa protein 4 | 0.894 |
DNAJB9 | HSPA5 | ENSP00000249356 | ENSP00000324173 | DnaJ (Hsp40) homolog, subfamily B, member 9; Acts as a co-chaperone with an Hsp70 protein (By similarity) | heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa); Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER | 0.979 |
DNAJB9 | HSPA6 | ENSP00000249356 | ENSP00000310219 | DnaJ (Hsp40) homolog, subfamily B, member 9; Acts as a co-chaperone with an Hsp70 protein (By similarity) | heat shock 70kDa protein 6 (HSP70B’); In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage (By similarity) | 0.902 |
DNAJB9 | HSPA8 | ENSP00000249356 | ENSP00000227378 | DnaJ (Hsp40) homolog, subfamily B, member 9; Acts as a co-chaperone with an Hsp70 protein (By similarity) | heat shock 70kDa protein 8; Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Chaperone. Component of the PRP19- CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex | 0.907 |
DNAJB9 | HYOU1 | ENSP00000249356 | ENSP00000384144 | DnaJ (Hsp40) homolog, subfamily B, member 9; Acts as a co-chaperone with an Hsp70 protein (By similarity) | hypoxia up-regulated 1; Has a pivotal role in cytoprotective cellular mechanisms triggered by oxygen deprivation. May play a role as a molecular chaperone and participate in protein folding | 0.922 |
HSP90B1 | DNAJB9 | ENSP00000299767 | ENSP00000249356 | heat shock protein 90kDa beta (Grp94), member 1; Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity | DnaJ (Hsp40) homolog, subfamily B, member 9; Acts as a co-chaperone with an Hsp70 protein (By similarity) | 0.902 |
HSP90B1 | HSPA13 | ENSP00000299767 | ENSP00000285667 | heat shock protein 90kDa beta (Grp94), member 1; Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity | heat shock protein 70kDa family, member 13; Has peptide-independent ATPase activity | 0.752 |
HSP90B1 | HSPA1A | ENSP00000299767 | ENSP00000364802 | heat shock protein 90kDa beta (Grp94), member 1; Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity | heat shock 70kDa protein 1A | 0.848 |
HSP90B1 | HSPA1B | ENSP00000299767 | ENSP00000364801 | heat shock protein 90kDa beta (Grp94), member 1; Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity | heat shock 70kDa protein 1B | 0.805 |
HSP90B1 | HSPA2 | ENSP00000299767 | ENSP00000247207 | heat shock protein 90kDa beta (Grp94), member 1; Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity | heat shock 70kDa protein 2; In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage | 0.825 |
HSP90B1 | HSPA4 | ENSP00000299767 | ENSP00000302961 | heat shock protein 90kDa beta (Grp94), member 1; Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity | heat shock 70kDa protein 4 | 0.943 |
HSP90B1 | HSPA5 | ENSP00000299767 | ENSP00000324173 | heat shock protein 90kDa beta (Grp94), member 1; Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity | heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa); Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER | 0.999 |
HSP90B1 | HSPA6 | ENSP00000299767 | ENSP00000310219 | heat shock protein 90kDa beta (Grp94), member 1; Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity | heat shock 70kDa protein 6 (HSP70B’); In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage (By similarity) | 0.818 |
HSP90B1 | HSPA8 | ENSP00000299767 | ENSP00000227378 | heat shock protein 90kDa beta (Grp94), member 1; Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity | heat shock 70kDa protein 8; Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Chaperone. Component of the PRP19- CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex | 0.925 |
HSP90B1 | HYOU1 | ENSP00000299767 | ENSP00000384144 | heat shock protein 90kDa beta (Grp94), member 1; Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity | hypoxia up-regulated 1; Has a pivotal role in cytoprotective cellular mechanisms triggered by oxygen deprivation. May play a role as a molecular chaperone and participate in protein folding | 0.983 |