node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AHSA1 | CLPB | ENSP00000216479 | ENSP00000294053 | Activator of 90 kDa heat shock protein ATPase homolog 1; Acts as a co-chaperone of HSP90AA1. Activates the ATPase activity of HSP90AA1 leading to increase in its chaperone activity. Competes with the inhibitory co-chaperone FNIP1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins | Caseinolytic peptidase B protein homolog; May function as a regulatory ATPase and be related to secretion/protein trafficking process; AAA ATPases | 0.699 |
AHSA1 | HSP90AA1 | ENSP00000216479 | ENSP00000335153 | Activator of 90 kDa heat shock protein ATPase homolog 1; Acts as a co-chaperone of HSP90AA1. Activates the ATPase activity of HSP90AA1 leading to increase in its chaperone activity. Competes with the inhibitory co-chaperone FNIP1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins | Heat shock protein HSP 90-alpha; 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 which is essential for its chaperone 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 ra [...] | 0.996 |
AHSA1 | HSP90AB1 | ENSP00000216479 | ENSP00000360609 | Activator of 90 kDa heat shock protein ATPase homolog 1; Acts as a co-chaperone of HSP90AA1. Activates the ATPase activity of HSP90AA1 leading to increase in its chaperone activity. Competes with the inhibitory co-chaperone FNIP1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins | 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 interacti [...] | 0.980 |
AHSA1 | HSPD1 | ENSP00000216479 | ENSP00000373620 | Activator of 90 kDa heat shock protein ATPase homolog 1; Acts as a co-chaperone of HSP90AA1. Activates the ATPase activity of HSP90AA1 leading to increase in its chaperone activity. Competes with the inhibitory co-chaperone FNIP1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins | 60 kDa heat shock protein, mitochondrial; 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 rin [...] | 0.801 |
AHSA1 | TRAP1 | ENSP00000216479 | ENSP00000246957 | Activator of 90 kDa heat shock protein ATPase homolog 1; Acts as a co-chaperone of HSP90AA1. Activates the ATPase activity of HSP90AA1 leading to increase in its chaperone activity. Competes with the inhibitory co-chaperone FNIP1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins | Heat shock protein 75 kDa, mitochondrial; Chaperone that expresses an ATPase activity. Involved in maintaining mitochondrial function and polarization, downstream of PINK1 and mitochondrial complex I. Is a negative regulator of mitochondrial respiration able to modulate the balance between oxidative phosphorylation and aerobic glycolysis. The impact of TRAP1 on mitochondrial respiration is probably mediated by modulation of mitochondrial SRC and inhibition of SDHA; Belongs to the heat shock protein 90 family | 0.900 |
AHSA1 | TTC28 | ENSP00000216479 | ENSP00000381003 | Activator of 90 kDa heat shock protein ATPase homolog 1; Acts as a co-chaperone of HSP90AA1. Activates the ATPase activity of HSP90AA1 leading to increase in its chaperone activity. Competes with the inhibitory co-chaperone FNIP1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins | Tetratricopeptide repeat protein 28; During mitosis, may be involved in the condensation of spindle midzone microtubules, leading to the formation of midbody; Tetratricopeptide repeat domain containing | 0.651 |
AHSA2 | CLPB | ENSP00000377970 | ENSP00000294053 | Activator of 90 kDa heat shock protein ATPase homolog 2; Co-chaperone that stimulates HSP90 ATPase activity | Caseinolytic peptidase B protein homolog; May function as a regulatory ATPase and be related to secretion/protein trafficking process; AAA ATPases | 0.569 |
AHSA2 | HSP90AA1 | ENSP00000377970 | ENSP00000335153 | Activator of 90 kDa heat shock protein ATPase homolog 2; Co-chaperone that stimulates HSP90 ATPase activity | Heat shock protein HSP 90-alpha; 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 which is essential for its chaperone 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 ra [...] | 0.967 |
AHSA2 | HSP90AB1 | ENSP00000377970 | ENSP00000360609 | Activator of 90 kDa heat shock protein ATPase homolog 2; Co-chaperone that stimulates HSP90 ATPase activity | 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 interacti [...] | 0.943 |
AHSA2 | HSPD1 | ENSP00000377970 | ENSP00000373620 | Activator of 90 kDa heat shock protein ATPase homolog 2; Co-chaperone that stimulates HSP90 ATPase activity | 60 kDa heat shock protein, mitochondrial; 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 rin [...] | 0.677 |
AHSA2 | TRAP1 | ENSP00000377970 | ENSP00000246957 | Activator of 90 kDa heat shock protein ATPase homolog 2; Co-chaperone that stimulates HSP90 ATPase activity | Heat shock protein 75 kDa, mitochondrial; Chaperone that expresses an ATPase activity. Involved in maintaining mitochondrial function and polarization, downstream of PINK1 and mitochondrial complex I. Is a negative regulator of mitochondrial respiration able to modulate the balance between oxidative phosphorylation and aerobic glycolysis. The impact of TRAP1 on mitochondrial respiration is probably mediated by modulation of mitochondrial SRC and inhibition of SDHA; Belongs to the heat shock protein 90 family | 0.872 |
AHSA2 | TTC28 | ENSP00000377970 | ENSP00000381003 | Activator of 90 kDa heat shock protein ATPase homolog 2; Co-chaperone that stimulates HSP90 ATPase activity | Tetratricopeptide repeat protein 28; During mitosis, may be involved in the condensation of spindle midzone microtubules, leading to the formation of midbody; Tetratricopeptide repeat domain containing | 0.651 |
CLPB | AHSA1 | ENSP00000294053 | ENSP00000216479 | Caseinolytic peptidase B protein homolog; May function as a regulatory ATPase and be related to secretion/protein trafficking process; AAA ATPases | Activator of 90 kDa heat shock protein ATPase homolog 1; Acts as a co-chaperone of HSP90AA1. Activates the ATPase activity of HSP90AA1 leading to increase in its chaperone activity. Competes with the inhibitory co-chaperone FNIP1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins | 0.699 |
CLPB | AHSA2 | ENSP00000294053 | ENSP00000377970 | Caseinolytic peptidase B protein homolog; May function as a regulatory ATPase and be related to secretion/protein trafficking process; AAA ATPases | Activator of 90 kDa heat shock protein ATPase homolog 2; Co-chaperone that stimulates HSP90 ATPase activity | 0.569 |
CLPB | HSP90AA1 | ENSP00000294053 | ENSP00000335153 | Caseinolytic peptidase B protein homolog; May function as a regulatory ATPase and be related to secretion/protein trafficking process; AAA ATPases | Heat shock protein HSP 90-alpha; 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 which is essential for its chaperone 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 ra [...] | 0.894 |
CLPB | HSP90AB1 | ENSP00000294053 | ENSP00000360609 | Caseinolytic peptidase B protein homolog; May function as a regulatory ATPase and be related to secretion/protein trafficking process; AAA ATPases | 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 interacti [...] | 0.775 |
CLPB | HSPD1 | ENSP00000294053 | ENSP00000373620 | Caseinolytic peptidase B protein homolog; May function as a regulatory ATPase and be related to secretion/protein trafficking process; AAA ATPases | 60 kDa heat shock protein, mitochondrial; 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 rin [...] | 0.934 |
CLPB | TRAP1 | ENSP00000294053 | ENSP00000246957 | Caseinolytic peptidase B protein homolog; May function as a regulatory ATPase and be related to secretion/protein trafficking process; AAA ATPases | Heat shock protein 75 kDa, mitochondrial; Chaperone that expresses an ATPase activity. Involved in maintaining mitochondrial function and polarization, downstream of PINK1 and mitochondrial complex I. Is a negative regulator of mitochondrial respiration able to modulate the balance between oxidative phosphorylation and aerobic glycolysis. The impact of TRAP1 on mitochondrial respiration is probably mediated by modulation of mitochondrial SRC and inhibition of SDHA; Belongs to the heat shock protein 90 family | 0.725 |
CLPB | TTC28 | ENSP00000294053 | ENSP00000381003 | Caseinolytic peptidase B protein homolog; May function as a regulatory ATPase and be related to secretion/protein trafficking process; AAA ATPases | Tetratricopeptide repeat protein 28; During mitosis, may be involved in the condensation of spindle midzone microtubules, leading to the formation of midbody; Tetratricopeptide repeat domain containing | 0.638 |
HSP90AA1 | AHSA1 | ENSP00000335153 | ENSP00000216479 | Heat shock protein HSP 90-alpha; 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 which is essential for its chaperone 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 ra [...] | Activator of 90 kDa heat shock protein ATPase homolog 1; Acts as a co-chaperone of HSP90AA1. Activates the ATPase activity of HSP90AA1 leading to increase in its chaperone activity. Competes with the inhibitory co-chaperone FNIP1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins | 0.996 |