node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
BAG3 | DNAJB6 | ENSPPYP00000003157 | ENSPPYP00000020432 | BAG3 isoform 1. | DnaJ homolog subfamily B member 6; Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins (By similarity). Has a stimulatory effect on the ATPase activity of HSP70 in a dose- dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Also reduces cellular toxicity and caspase-3 activity (By similarity). | 0.834 |
BAG3 | ENSPPYP00000005659 | ENSPPYP00000003157 | ENSPPYP00000005659 | BAG3 isoform 1. | annotation not available | 0.934 |
BAG3 | ENSPPYP00000024257 | ENSPPYP00000003157 | ENSPPYP00000024257 | BAG3 isoform 1. | LOW QUALITY PROTEIN: stress-70 protein, mitochondrial-like. | 0.751 |
BAG3 | HSPA1A | ENSPPYP00000003157 | ENSPPYP00000018408 | BAG3 isoform 1. | Heat shock 70 kDa protein 1; 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 [...] | 0.895 |
BAG3 | HSPA4 | ENSPPYP00000003157 | ENSPPYP00000017643 | BAG3 isoform 1. | Heat shock 70 kDa protein 4; Belongs to the heat shock protein 70 family. | 0.990 |
BAG3 | HSPA5 | ENSPPYP00000003157 | ENSPPYP00000021973 | BAG3 isoform 1. | 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 [...] | 0.801 |
BAG3 | HSPA8 | ENSPPYP00000003157 | ENSPPYP00000004564 | BAG3 isoform 1. | Heat shock cognate 71 kDa protein; 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 a [...] | 0.934 |
BAG3 | HSPA9 | ENSPPYP00000003157 | ENSPPYP00000017699 | BAG3 isoform 1. | Stress-70 protein, mitochondrial; 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. | 0.751 |
BAG3 | MLF2 | ENSPPYP00000003157 | ENSPPYP00000004785 | BAG3 isoform 1. | Myeloid leukemia factor 2. | 0.440 |
BAG3 | STUB1 | ENSPPYP00000003157 | ENSPPYP00000007837 | BAG3 isoform 1. | STIP1 homology and U-box containing protein 1. | 0.967 |
DNAJB6 | BAG3 | ENSPPYP00000020432 | ENSPPYP00000003157 | DnaJ homolog subfamily B member 6; Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins (By similarity). Has a stimulatory effect on the ATPase activity of HSP70 in a dose- dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Also reduces cellular toxicity and caspase-3 activity (By similarity). | BAG3 isoform 1. | 0.834 |
DNAJB6 | ENSPPYP00000005659 | ENSPPYP00000020432 | ENSPPYP00000005659 | DnaJ homolog subfamily B member 6; Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins (By similarity). Has a stimulatory effect on the ATPase activity of HSP70 in a dose- dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Also reduces cellular toxicity and caspase-3 activity (By similarity). | annotation not available | 0.837 |
DNAJB6 | ENSPPYP00000024257 | ENSPPYP00000020432 | ENSPPYP00000024257 | DnaJ homolog subfamily B member 6; Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins (By similarity). Has a stimulatory effect on the ATPase activity of HSP70 in a dose- dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Also reduces cellular toxicity and caspase-3 activity (By similarity). | LOW QUALITY PROTEIN: stress-70 protein, mitochondrial-like. | 0.722 |
DNAJB6 | HSPA1A | ENSPPYP00000020432 | ENSPPYP00000018408 | DnaJ homolog subfamily B member 6; Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins (By similarity). Has a stimulatory effect on the ATPase activity of HSP70 in a dose- dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Also reduces cellular toxicity and caspase-3 activity (By similarity). | Heat shock 70 kDa protein 1; 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 [...] | 0.852 |
DNAJB6 | HSPA4 | ENSPPYP00000020432 | ENSPPYP00000017643 | DnaJ homolog subfamily B member 6; Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins (By similarity). Has a stimulatory effect on the ATPase activity of HSP70 in a dose- dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Also reduces cellular toxicity and caspase-3 activity (By similarity). | Heat shock 70 kDa protein 4; Belongs to the heat shock protein 70 family. | 0.896 |
DNAJB6 | HSPA5 | ENSPPYP00000020432 | ENSPPYP00000021973 | DnaJ homolog subfamily B member 6; Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins (By similarity). Has a stimulatory effect on the ATPase activity of HSP70 in a dose- dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Also reduces cellular toxicity and caspase-3 activity (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 [...] | 0.740 |
DNAJB6 | HSPA8 | ENSPPYP00000020432 | ENSPPYP00000004564 | DnaJ homolog subfamily B member 6; Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins (By similarity). Has a stimulatory effect on the ATPase activity of HSP70 in a dose- dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Also reduces cellular toxicity and caspase-3 activity (By similarity). | Heat shock cognate 71 kDa protein; 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 a [...] | 0.858 |
DNAJB6 | HSPA9 | ENSPPYP00000020432 | ENSPPYP00000017699 | DnaJ homolog subfamily B member 6; Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins (By similarity). Has a stimulatory effect on the ATPase activity of HSP70 in a dose- dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Also reduces cellular toxicity and caspase-3 activity (By similarity). | Stress-70 protein, mitochondrial; 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. | 0.724 |
DNAJB6 | MLF2 | ENSPPYP00000020432 | ENSPPYP00000004785 | DnaJ homolog subfamily B member 6; Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins (By similarity). Has a stimulatory effect on the ATPase activity of HSP70 in a dose- dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Also reduces cellular toxicity and caspase-3 activity (By similarity). | Myeloid leukemia factor 2. | 0.825 |
DNAJB6 | STUB1 | ENSPPYP00000020432 | ENSPPYP00000007837 | DnaJ homolog subfamily B member 6; Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. Suppresses aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins (By similarity). Has a stimulatory effect on the ATPase activity of HSP70 in a dose- dependent and time-dependent manner and hence acts as a co-chaperone of HSP70. Also reduces cellular toxicity and caspase-3 activity (By similarity). | STIP1 homology and U-box containing protein 1. | 0.840 |