| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| DNAJA1 | DNAJB1 | ENSPPYP00000021446 | ENSPPYP00000010811 | DnaJ homolog subfamily A member 1; Co-chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro). Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV (By similarity). | DnaJ heat shock protein family (Hsp40) member B1. | 0.779 |
| DNAJA1 | ENSPPYP00000005659 | ENSPPYP00000021446 | ENSPPYP00000005659 | DnaJ homolog subfamily A member 1; Co-chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro). Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV (By similarity). | annotation not available | 0.970 |
| DNAJA1 | ENSPPYP00000017062 | ENSPPYP00000021446 | ENSPPYP00000017062 | DnaJ homolog subfamily A member 1; Co-chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro). Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV (By similarity). | annotation not available | 0.801 |
| DNAJA1 | ENSPPYP00000024257 | ENSPPYP00000021446 | ENSPPYP00000024257 | DnaJ homolog subfamily A member 1; Co-chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro). Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV (By similarity). | LOW QUALITY PROTEIN: stress-70 protein, mitochondrial-like. | 0.725 |
| DNAJA1 | HSP90AA1 | ENSPPYP00000021446 | ENSPPYP00000006994 | DnaJ homolog subfamily A member 1; Co-chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro). Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV (By similarity). | HSP90AA1 isoform 6. | 0.801 |
| DNAJA1 | HSP90AB1 | ENSPPYP00000021446 | ENSPPYP00000018631 | DnaJ homolog subfamily A member 1; Co-chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro). Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV (By similarity). | Heat shock protein HSP 90-beta; 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. Engages with a range of client protein classes via its interact [...] | 0.832 |
| DNAJA1 | HSPA1L | ENSPPYP00000021446 | ENSPPYP00000018406 | DnaJ homolog subfamily A member 1; Co-chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro). Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV (By similarity). | Heat shock protein family A (Hsp70) member 1 like; Belongs to the heat shock protein 70 family. | 0.909 |
| DNAJA1 | HSPA2 | ENSPPYP00000021446 | ENSPPYP00000006709 | DnaJ homolog subfamily A member 1; Co-chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro). Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV (By similarity). | Heat shock protein family A (Hsp70) member 2; Belongs to the heat shock protein 70 family. | 0.928 |
| DNAJA1 | HSPA4 | ENSPPYP00000021446 | ENSPPYP00000017643 | DnaJ homolog subfamily A member 1; Co-chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro). Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV (By similarity). | Heat shock 70 kDa protein 4; Belongs to the heat shock protein 70 family. | 0.842 |
| DNAJA1 | HSPA5 | ENSPPYP00000021446 | ENSPPYP00000021973 | DnaJ homolog subfamily A member 1; Co-chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro). Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV (By similarity). | 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 [...] | 0.884 |
| DNAJB1 | DNAJA1 | ENSPPYP00000010811 | ENSPPYP00000021446 | DnaJ heat shock protein family (Hsp40) member B1. | DnaJ homolog subfamily A member 1; Co-chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro). Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV (By similarity). | 0.779 |
| DNAJB1 | ENSPPYP00000005659 | ENSPPYP00000010811 | ENSPPYP00000005659 | DnaJ heat shock protein family (Hsp40) member B1. | annotation not available | 0.952 |
| DNAJB1 | ENSPPYP00000017062 | ENSPPYP00000010811 | ENSPPYP00000017062 | DnaJ heat shock protein family (Hsp40) member B1. | annotation not available | 0.768 |
| DNAJB1 | ENSPPYP00000024257 | ENSPPYP00000010811 | ENSPPYP00000024257 | DnaJ heat shock protein family (Hsp40) member B1. | LOW QUALITY PROTEIN: stress-70 protein, mitochondrial-like. | 0.800 |
| DNAJB1 | HSP90AA1 | ENSPPYP00000010811 | ENSPPYP00000006994 | DnaJ heat shock protein family (Hsp40) member B1. | HSP90AA1 isoform 6. | 0.768 |
| DNAJB1 | HSP90AB1 | ENSPPYP00000010811 | ENSPPYP00000018631 | DnaJ heat shock protein family (Hsp40) member B1. | Heat shock protein HSP 90-beta; 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. Engages with a range of client protein classes via its interact [...] | 0.850 |
| DNAJB1 | HSPA1L | ENSPPYP00000010811 | ENSPPYP00000018406 | DnaJ heat shock protein family (Hsp40) member B1. | Heat shock protein family A (Hsp70) member 1 like; Belongs to the heat shock protein 70 family. | 0.952 |
| DNAJB1 | HSPA2 | ENSPPYP00000010811 | ENSPPYP00000006709 | DnaJ heat shock protein family (Hsp40) member B1. | Heat shock protein family A (Hsp70) member 2; Belongs to the heat shock protein 70 family. | 0.950 |
| DNAJB1 | HSPA4 | ENSPPYP00000010811 | ENSPPYP00000017643 | DnaJ heat shock protein family (Hsp40) member B1. | Heat shock 70 kDa protein 4; Belongs to the heat shock protein 70 family. | 0.989 |
| DNAJB1 | HSPA5 | ENSPPYP00000010811 | ENSPPYP00000021973 | DnaJ heat shock protein family (Hsp40) member B1. | 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 [...] | 0.864 |
