| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ATP5F1 | DNAJC28 | ENSP00000358737 | ENSP00000479716 | ATP synthase F(0) complex subunit B1, mitochondrial; Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechani [...] | DnaJ homolog subfamily C member 28; May have a role in protein folding or as a chaperone; DNAJ heat shock proteins | 0.795 |
| DNAJB14 | DNAJC28 | ENSP00000404381 | ENSP00000479716 | DnaJ homolog subfamily B member 14; Acts as a co-chaperone with HSPA8/Hsc70; required to promote protein folding and trafficking, prevent aggregation of client proteins, and promote unfolded proteins to endoplasmic reticulum-associated degradation (ERAD) pathway. Acts by determining HSPA8/Hsc70’s ATPase and polypeptide-binding activities. Can also act independently of HSPA8/Hsc70- together with DNAJB12, acts as a chaperone that promotes maturation of potassium channels KCND2 and KCNH2 by stabilizing nascent channel subunits and assembling them into tetramers. While stabilization of nas [...] | DnaJ homolog subfamily C member 28; May have a role in protein folding or as a chaperone; DNAJ heat shock proteins | 0.656 |
| DNAJC18 | DNAJC24 | ENSP00000302843 | ENSP00000417548 | DnaJ heat shock protein family member C18 | DnaJ homolog subfamily C member 24; Stimulates the ATPase activity of several Hsp70-type chaperones. This ability is enhanced by iron-binding. The iron- bound form is redox-active and can function as electron carrier. Plays a role in the diphthamide biosynthesis, a post-translational modification of histidine which occurs in translation elongation factor 2 (EEF2) which can be ADP-ribosylated by diphtheria toxin and by Pseudomonas exotoxin A (Eta); Belongs to the DPH4 family | 0.676 |
| DNAJC18 | DNAJC28 | ENSP00000302843 | ENSP00000479716 | DnaJ heat shock protein family member C18 | DnaJ homolog subfamily C member 28; May have a role in protein folding or as a chaperone; DNAJ heat shock proteins | 0.675 |
| DNAJC18 | DNAJC8 | ENSP00000302843 | ENSP00000263697 | DnaJ heat shock protein family member C18 | DnaJ homolog subfamily C member 8; Suppresses polyglutamine (polyQ) aggregation of ATXN3 in neuronal cells; DNAJ heat shock proteins | 0.806 |
| DNAJC24 | DNAJC18 | ENSP00000417548 | ENSP00000302843 | DnaJ homolog subfamily C member 24; Stimulates the ATPase activity of several Hsp70-type chaperones. This ability is enhanced by iron-binding. The iron- bound form is redox-active and can function as electron carrier. Plays a role in the diphthamide biosynthesis, a post-translational modification of histidine which occurs in translation elongation factor 2 (EEF2) which can be ADP-ribosylated by diphtheria toxin and by Pseudomonas exotoxin A (Eta); Belongs to the DPH4 family | DnaJ heat shock protein family member C18 | 0.676 |
| DNAJC24 | DNAJC28 | ENSP00000417548 | ENSP00000479716 | DnaJ homolog subfamily C member 24; Stimulates the ATPase activity of several Hsp70-type chaperones. This ability is enhanced by iron-binding. The iron- bound form is redox-active and can function as electron carrier. Plays a role in the diphthamide biosynthesis, a post-translational modification of histidine which occurs in translation elongation factor 2 (EEF2) which can be ADP-ribosylated by diphtheria toxin and by Pseudomonas exotoxin A (Eta); Belongs to the DPH4 family | DnaJ homolog subfamily C member 28; May have a role in protein folding or as a chaperone; DNAJ heat shock proteins | 0.651 |
| DNAJC24 | DNAJC8 | ENSP00000417548 | ENSP00000263697 | DnaJ homolog subfamily C member 24; Stimulates the ATPase activity of several Hsp70-type chaperones. This ability is enhanced by iron-binding. The iron- bound form is redox-active and can function as electron carrier. Plays a role in the diphthamide biosynthesis, a post-translational modification of histidine which occurs in translation elongation factor 2 (EEF2) which can be ADP-ribosylated by diphtheria toxin and by Pseudomonas exotoxin A (Eta); Belongs to the DPH4 family | DnaJ homolog subfamily C member 8; Suppresses polyglutamine (polyQ) aggregation of ATXN3 in neuronal cells; DNAJ heat shock proteins | 0.597 |
| DNAJC24 | DNAJC9 | ENSP00000417548 | ENSP00000362041 | DnaJ homolog subfamily C member 24; Stimulates the ATPase activity of several Hsp70-type chaperones. This ability is enhanced by iron-binding. The iron- bound form is redox-active and can function as electron carrier. Plays a role in the diphthamide biosynthesis, a post-translational modification of histidine which occurs in translation elongation factor 2 (EEF2) which can be ADP-ribosylated by diphtheria toxin and by Pseudomonas exotoxin A (Eta); Belongs to the DPH4 family | DnaJ homolog subfamily C member 9; May play a role as co-chaperone of the Hsp70 family proteins HSPA1A, HSPA1B and HSPA8; DNAJ heat shock proteins | 0.619 |
| DNAJC28 | ATP5F1 | ENSP00000479716 | ENSP00000358737 | DnaJ homolog subfamily C member 28; May have a role in protein folding or as a chaperone; DNAJ heat shock proteins | ATP synthase F(0) complex subunit B1, mitochondrial; Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechani [...] | 0.795 |
| DNAJC28 | DNAJB14 | ENSP00000479716 | ENSP00000404381 | DnaJ homolog subfamily C member 28; May have a role in protein folding or as a chaperone; DNAJ heat shock proteins | DnaJ homolog subfamily B member 14; Acts as a co-chaperone with HSPA8/Hsc70; required to promote protein folding and trafficking, prevent aggregation of client proteins, and promote unfolded proteins to endoplasmic reticulum-associated degradation (ERAD) pathway. Acts by determining HSPA8/Hsc70’s ATPase and polypeptide-binding activities. Can also act independently of HSPA8/Hsc70- together with DNAJB12, acts as a chaperone that promotes maturation of potassium channels KCND2 and KCNH2 by stabilizing nascent channel subunits and assembling them into tetramers. While stabilization of nas [...] | 0.656 |
| DNAJC28 | DNAJC18 | ENSP00000479716 | ENSP00000302843 | DnaJ homolog subfamily C member 28; May have a role in protein folding or as a chaperone; DNAJ heat shock proteins | DnaJ heat shock protein family member C18 | 0.675 |
| DNAJC28 | DNAJC24 | ENSP00000479716 | ENSP00000417548 | DnaJ homolog subfamily C member 28; May have a role in protein folding or as a chaperone; DNAJ heat shock proteins | DnaJ homolog subfamily C member 24; Stimulates the ATPase activity of several Hsp70-type chaperones. This ability is enhanced by iron-binding. The iron- bound form is redox-active and can function as electron carrier. Plays a role in the diphthamide biosynthesis, a post-translational modification of histidine which occurs in translation elongation factor 2 (EEF2) which can be ADP-ribosylated by diphtheria toxin and by Pseudomonas exotoxin A (Eta); Belongs to the DPH4 family | 0.651 |
| DNAJC28 | DNAJC8 | ENSP00000479716 | ENSP00000263697 | DnaJ homolog subfamily C member 28; May have a role in protein folding or as a chaperone; DNAJ heat shock proteins | DnaJ homolog subfamily C member 8; Suppresses polyglutamine (polyQ) aggregation of ATXN3 in neuronal cells; DNAJ heat shock proteins | 0.666 |
| DNAJC28 | DNAJC9 | ENSP00000479716 | ENSP00000362041 | DnaJ homolog subfamily C member 28; May have a role in protein folding or as a chaperone; DNAJ heat shock proteins | DnaJ homolog subfamily C member 9; May play a role as co-chaperone of the Hsp70 family proteins HSPA1A, HSPA1B and HSPA8; DNAJ heat shock proteins | 0.668 |
| DNAJC28 | FAM120C | ENSP00000479716 | ENSP00000364324 | DnaJ homolog subfamily C member 28; May have a role in protein folding or as a chaperone; DNAJ heat shock proteins | Constitutive coactivator of PPAR-gamma-like protein 2; Family with sequence similarity 120C; Belongs to the constitutive coactivator of PPAR-gamma family | 0.731 |
| DNAJC28 | FAM3B | ENSP00000479716 | ENSP00000350673 | DnaJ homolog subfamily C member 28; May have a role in protein folding or as a chaperone; DNAJ heat shock proteins | Protein FAM3B; Induces apoptosis of alpha and beta cells in a dose- and time-dependent manner; Belongs to the FAM3 family | 0.703 |
| DNAJC28 | MPLKIP | ENSP00000479716 | ENSP00000304553 | DnaJ homolog subfamily C member 28; May have a role in protein folding or as a chaperone; DNAJ heat shock proteins | M-phase-specific PLK1-interacting protein; May play a role in maintenance of cell cycle integrity by regulating mitosis or cytokinesis | 0.705 |
| DNAJC28 | TADA1 | ENSP00000479716 | ENSP00000356848 | DnaJ homolog subfamily C member 28; May have a role in protein folding or as a chaperone; DNAJ heat shock proteins | Transcriptional adapter 1; Probably involved in transcriptional regulation; SAGA complex | 0.656 |
| DNAJC8 | DNAJC18 | ENSP00000263697 | ENSP00000302843 | DnaJ homolog subfamily C member 8; Suppresses polyglutamine (polyQ) aggregation of ATXN3 in neuronal cells; DNAJ heat shock proteins | DnaJ heat shock protein family member C18 | 0.806 |
