| Rank |
PPI partner |
STRING score |
Description |
| 1 |
9601.ENSPPYP00000017643 |
0.871 |
Pongo abelii heat shock 70kDa protein 4 (HSPA4), mRNA |
| 2 |
9601.ENSPPYP00000004564 |
0.834 |
Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chap [...] |
| 3 |
9601.ENSPPYP00000005659 |
0.834 |
Uncharacterized protein |
| 4 |
9601.ENSPPYP00000024459 |
0.834 |
Uncharacterized protein |
| 5 |
9601.ENSPPYP00000018408 |
0.827 |
Heat shock 70 kDa protein 1 |
| 6 |
9601.ENSPPYP00000018406 |
0.773 |
Belongs to the heat shock protein 70 family. |
| 7 |
9601.ENSPPYP00000014577 |
0.759 |
Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and asso [...] |
| 8 |
9601.ENSPPYP00000016819 |
0.749 |
Heat shock 70kDa protein 4-like |
| 9 |
9601.ENSPPYP00000006709 |
0.719 |
Belongs to the heat shock protein 70 family. |
| 10 |
9601.ENSPPYP00000002443 |
0.705 |
Component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding- competent state. In the RAC complex, binds to the nascent polypeptide chain, while DNAJC2 stimulates its ATPase activity (By similarity). |
| 11 |
9601.ENSPPYP00000003135 |
0.705 |
Heat shock 70kDa protein 12A |
| 12 |
9601.ENSPPYP00000012078 |
0.705 |
Heat shock 70kD protein 12B |
| 13 |
9601.ENSPPYP00000012608 |
0.705 |
Heat shock protein 70kDa family, member 13 |
| 14 |
9601.ENSPPYP00000005987 |
0.689 |
Acts as a nucleotide-exchange factor (NEF) for chaperone proteins HSPA1A and HSPA1B, promoting the release of ADP from HSPA1A/B thereby triggering substrate release. Prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. Inhibits HSPA8/HSC70 ATPase and chaperone activities |
| 15 |
9601.ENSPPYP00000015201 |
0.672 |
TRK-fused gene |
| 16 |
9601.ENSPPYP00000000695 |
0.664 |
Heat shock 70kDa protein 6 (HSP70B') |
| 17 |
9601.ENSPPYP00000021973 |
0.662 |
Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to disrupt the dimerization of ERN1/IRE1, t [...] |
| 18 |
9601.ENSPPYP00000017699 |
0.623 |
Chaperone protein which plays an important role in mitochondrial iron-sulfur cluster (ISC) biogenesis. Interacts with and stabilizes ISC cluster assembly proteins FXN, NFU1, NFS1 and ISCU. Regulates erythropoiesis via stabilization of ISC assembly. May play a role in the control of cell proliferation and cellular aging. |
| 19 |
9601.ENSPPYP00000024257 |
0.623 |
Uncharacterized protein |
| 20 |
9601.ENSPPYP00000009818 |
0.622 |
This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modif [...] |