| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| DNAJC18 | GRPEL1 | ENSP00000302843 | ENSP00000264954 | DnaJ (Hsp40) homolog, subfamily C, member 18 | GrpE-like 1, mitochondrial (E. coli); 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 | 0.863 |
| DNAJC18 | GRPEL2 | ENSP00000302843 | ENSP00000329558 | DnaJ (Hsp40) homolog, subfamily C, member 18 | GrpE-like 2, mitochondrial (E. coli); 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. Stimulates ATPase activity of mt-HSP70. May also serve to modulate the interconversion of oligomeric (inactive) and monomeric (active) forms of mt-HSP70 (By similarity) | 0.863 |
| DNAJC18 | HSPA13 | ENSP00000302843 | ENSP00000285667 | DnaJ (Hsp40) homolog, subfamily C, member 18 | heat shock protein 70kDa family, member 13; Has peptide-independent ATPase activity | 0.877 |
| DNAJC18 | HSPA1A | ENSP00000302843 | ENSP00000364802 | DnaJ (Hsp40) homolog, subfamily C, member 18 | heat shock 70kDa protein 1A | 0.871 |
| DNAJC18 | HSPA1B | ENSP00000302843 | ENSP00000364801 | DnaJ (Hsp40) homolog, subfamily C, member 18 | heat shock 70kDa protein 1B | 0.871 |
| DNAJC18 | HSPA1L | ENSP00000302843 | ENSP00000364805 | DnaJ (Hsp40) homolog, subfamily C, member 18 | heat shock 70kDa protein 1-like | 0.870 |
| DNAJC18 | HSPA2 | ENSP00000302843 | ENSP00000247207 | DnaJ (Hsp40) homolog, subfamily C, member 18 | 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 | 0.870 |
| DNAJC18 | HSPA5 | ENSP00000302843 | ENSP00000324173 | DnaJ (Hsp40) homolog, subfamily C, member 18 | heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa); Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER | 0.876 |
| DNAJC18 | HSPA6 | ENSP00000302843 | ENSP00000310219 | DnaJ (Hsp40) homolog, subfamily C, member 18 | 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) | 0.875 |
| DNAJC18 | HSPA8 | ENSP00000302843 | ENSP00000227378 | DnaJ (Hsp40) homolog, subfamily C, member 18 | 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 | 0.886 |
| GRPEL1 | DNAJC18 | ENSP00000264954 | ENSP00000302843 | GrpE-like 1, mitochondrial (E. coli); 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 | DnaJ (Hsp40) homolog, subfamily C, member 18 | 0.863 |
| GRPEL1 | GRPEL2 | ENSP00000264954 | ENSP00000329558 | GrpE-like 1, mitochondrial (E. coli); 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 | GrpE-like 2, mitochondrial (E. coli); 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. Stimulates ATPase activity of mt-HSP70. May also serve to modulate the interconversion of oligomeric (inactive) and monomeric (active) forms of mt-HSP70 (By similarity) | 0.908 |
| GRPEL1 | HSPA13 | ENSP00000264954 | ENSP00000285667 | GrpE-like 1, mitochondrial (E. coli); 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 | heat shock protein 70kDa family, member 13; Has peptide-independent ATPase activity | 0.987 |
| GRPEL1 | HSPA1A | ENSP00000264954 | ENSP00000364802 | GrpE-like 1, mitochondrial (E. coli); 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 | heat shock 70kDa protein 1A | 0.993 |
| GRPEL1 | HSPA1B | ENSP00000264954 | ENSP00000364801 | GrpE-like 1, mitochondrial (E. coli); 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 | heat shock 70kDa protein 1B | 0.988 |
| GRPEL1 | HSPA1L | ENSP00000264954 | ENSP00000364805 | GrpE-like 1, mitochondrial (E. coli); 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 | heat shock 70kDa protein 1-like | 0.987 |
| GRPEL1 | HSPA2 | ENSP00000264954 | ENSP00000247207 | GrpE-like 1, mitochondrial (E. coli); 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 | 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 | 0.987 |
| GRPEL1 | HSPA5 | ENSP00000264954 | ENSP00000324173 | GrpE-like 1, mitochondrial (E. coli); 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 | heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa); Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER | 0.987 |
| GRPEL1 | HSPA6 | ENSP00000264954 | ENSP00000310219 | GrpE-like 1, mitochondrial (E. coli); 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 | 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) | 0.987 |
| GRPEL1 | HSPA8 | ENSP00000264954 | ENSP00000227378 | GrpE-like 1, mitochondrial (E. coli); 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 | 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 | 0.991 |
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