| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| DNAJB12 | HSP90AA1 | ENSP00000345575 | ENSP00000335153 | DnaJ (Hsp40) homolog, subfamily B, member 12 | heat shock protein 90kDa alpha (cytosolic), class A member 1; 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 | 0.873 |
| DNAJB12 | HSPA13 | ENSP00000345575 | ENSP00000285667 | DnaJ (Hsp40) homolog, subfamily B, member 12 | heat shock protein 70kDa family, member 13; Has peptide-independent ATPase activity | 0.884 |
| DNAJB12 | HSPA1A | ENSP00000345575 | ENSP00000364802 | DnaJ (Hsp40) homolog, subfamily B, member 12 | heat shock 70kDa protein 1A | 0.883 |
| DNAJB12 | HSPA1B | ENSP00000345575 | ENSP00000364801 | DnaJ (Hsp40) homolog, subfamily B, member 12 | heat shock 70kDa protein 1B | 0.870 |
| DNAJB12 | HSPA1L | ENSP00000345575 | ENSP00000364805 | DnaJ (Hsp40) homolog, subfamily B, member 12 | heat shock 70kDa protein 1-like | 0.896 |
| DNAJB12 | HSPA5 | ENSP00000345575 | ENSP00000324173 | DnaJ (Hsp40) homolog, subfamily B, member 12 | heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa); Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER | 0.870 |
| DNAJB12 | HSPA6 | ENSP00000345575 | ENSP00000310219 | DnaJ (Hsp40) homolog, subfamily B, member 12 | 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) | 0.870 |
| DNAJB12 | HSPA8 | ENSP00000345575 | ENSP00000227378 | DnaJ (Hsp40) homolog, subfamily B, member 12 | 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 | 0.973 |
| DNAJB12 | R3HCC1L | ENSP00000345575 | ENSP00000298999 | DnaJ (Hsp40) homolog, subfamily B, member 12 | R3H domain and coiled-coil containing 1-like | 0.890 |
| DNAJB12 | UBC | ENSP00000345575 | ENSP00000344818 | DnaJ (Hsp40) homolog, subfamily B, member 12 | ubiquitin C | 0.940 |
| HSP90AA1 | DNAJB12 | ENSP00000335153 | ENSP00000345575 | heat shock protein 90kDa alpha (cytosolic), class A member 1; 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 | DnaJ (Hsp40) homolog, subfamily B, member 12 | 0.873 |
| HSP90AA1 | HSPA13 | ENSP00000335153 | ENSP00000285667 | heat shock protein 90kDa alpha (cytosolic), class A member 1; 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 | heat shock protein 70kDa family, member 13; Has peptide-independent ATPase activity | 0.957 |
| HSP90AA1 | HSPA1A | ENSP00000335153 | ENSP00000364802 | heat shock protein 90kDa alpha (cytosolic), class A member 1; 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 | heat shock 70kDa protein 1A | 0.984 |
| HSP90AA1 | HSPA1B | ENSP00000335153 | ENSP00000364801 | heat shock protein 90kDa alpha (cytosolic), class A member 1; 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 | heat shock 70kDa protein 1B | 0.975 |
| HSP90AA1 | HSPA1L | ENSP00000335153 | ENSP00000364805 | heat shock protein 90kDa alpha (cytosolic), class A member 1; 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 | heat shock 70kDa protein 1-like | 0.980 |
| HSP90AA1 | HSPA5 | ENSP00000335153 | ENSP00000324173 | heat shock protein 90kDa alpha (cytosolic), class A member 1; 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 | heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa); Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER | 0.992 |
| HSP90AA1 | HSPA6 | ENSP00000335153 | ENSP00000310219 | heat shock protein 90kDa alpha (cytosolic), class A member 1; 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 | 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) | 0.999 |
| HSP90AA1 | HSPA8 | ENSP00000335153 | ENSP00000227378 | heat shock protein 90kDa alpha (cytosolic), class A member 1; 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 | 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 | 0.999 |
| HSP90AA1 | UBC | ENSP00000335153 | ENSP00000344818 | heat shock protein 90kDa alpha (cytosolic), class A member 1; 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 | ubiquitin C | 0.999 |
| HSPA13 | DNAJB12 | ENSP00000285667 | ENSP00000345575 | heat shock protein 70kDa family, member 13; Has peptide-independent ATPase activity | DnaJ (Hsp40) homolog, subfamily B, member 12 | 0.884 |
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