| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| A0A287BQU9_PIG | DNAJB13 | ENSSSCP00000058891 | ENSSSCP00000015751 | Uncharacterized protein. | DnaJ heat shock protein family (Hsp40) member B13. | 0.724 |
| A0A287BQU9_PIG | HSPA1L | ENSSSCP00000058891 | ENSSSCP00000020097 | Uncharacterized protein. | Heat shock 70 kDa protein 1-like; 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 an [...] | 0.406 |
| A0A287BQU9_PIG | HSPA4 | ENSSSCP00000058891 | ENSSSCP00000052080 | Uncharacterized protein. | Heat shock protein family A (Hsp70) member 4. | 0.799 |
| A0A287BQU9_PIG | HSPA5 | ENSSSCP00000058891 | ENSSSCP00000055982 | Uncharacterized protein. | Endoplasmic reticulum chaperone BiP; 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 dis [...] | 0.753 |
| A0A287BQU9_PIG | HSPA8 | ENSSSCP00000058891 | ENSSSCP00000036002 | Uncharacterized protein. | Uncharacterized protein; Belongs to the heat shock protein 70 family. | 0.799 |
| A0A287BQU9_PIG | HSPH1 | ENSSSCP00000058891 | ENSSSCP00000065843 | Uncharacterized protein. | Heat shock protein family H (Hsp110) member 1. | 0.766 |
| DNAJB13 | A0A287BQU9_PIG | ENSSSCP00000015751 | ENSSSCP00000058891 | DnaJ heat shock protein family (Hsp40) member B13. | Uncharacterized protein. | 0.724 |
| DNAJB13 | HSPA1L | ENSSSCP00000015751 | ENSSSCP00000020097 | DnaJ heat shock protein family (Hsp40) member B13. | Heat shock 70 kDa protein 1-like; 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 an [...] | 0.724 |
| DNAJB13 | HSPA4 | ENSSSCP00000015751 | ENSSSCP00000052080 | DnaJ heat shock protein family (Hsp40) member B13. | Heat shock protein family A (Hsp70) member 4. | 0.750 |
| DNAJB13 | HSPA5 | ENSSSCP00000015751 | ENSSSCP00000055982 | DnaJ heat shock protein family (Hsp40) member B13. | Endoplasmic reticulum chaperone BiP; 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 dis [...] | 0.747 |
| DNAJB13 | HSPA6 | ENSSSCP00000015751 | ENSSSCP00000073047 | DnaJ heat shock protein family (Hsp40) member B13. | Heat shock 70 kDa protein 6; 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 [...] | 0.764 |
| DNAJB13 | HSPA8 | ENSSSCP00000015751 | ENSSSCP00000036002 | DnaJ heat shock protein family (Hsp40) member B13. | Uncharacterized protein; Belongs to the heat shock protein 70 family. | 0.791 |
| DNAJB13 | HSPH1 | ENSSSCP00000015751 | ENSSSCP00000065843 | DnaJ heat shock protein family (Hsp40) member B13. | Heat shock protein family H (Hsp110) member 1. | 0.740 |
| DNAJB13 | RSPH3 | ENSSSCP00000015751 | ENSSSCP00000004381 | DnaJ heat shock protein family (Hsp40) member B13. | Radial spoke head 3. | 0.750 |
| DNAJB13 | RSPH9 | ENSSSCP00000015751 | ENSSSCP00000001841 | DnaJ heat shock protein family (Hsp40) member B13. | Radial spoke head protein 9 homolog isoform 1. | 0.734 |
| DNAJB13 | ZMYND11 | ENSSSCP00000015751 | ENSSSCP00000042458 | DnaJ heat shock protein family (Hsp40) member B13. | Zinc finger MYND domain-containing protein 11 isoform X1. | 0.711 |
| HSPA1L | A0A287BQU9_PIG | ENSSSCP00000020097 | ENSSSCP00000058891 | Heat shock 70 kDa protein 1-like; 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 an [...] | Uncharacterized protein. | 0.406 |
| HSPA1L | DNAJB13 | ENSSSCP00000020097 | ENSSSCP00000015751 | Heat shock 70 kDa protein 1-like; 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 an [...] | DnaJ heat shock protein family (Hsp40) member B13. | 0.724 |
| HSPA1L | HSPA4 | ENSSSCP00000020097 | ENSSSCP00000052080 | Heat shock 70 kDa protein 1-like; 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 an [...] | Heat shock protein family A (Hsp70) member 4. | 0.790 |
| HSPA1L | HSPA5 | ENSSSCP00000020097 | ENSSSCP00000055982 | Heat shock 70 kDa protein 1-like; 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 an [...] | Endoplasmic reticulum chaperone BiP; 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 dis [...] | 0.753 |
STRING v12.5 is now available!
