node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AHSA1 | HSP90AA1 | ENSP00000216479 | ENSP00000335153 | AHA1, activator of heat shock 90kDa protein ATPase homolog 1 (yeast); Cochaperone that stimulates HSP90 ATPase activity (By similarity). May affect a step in the endoplasmic reticulum to Golgi trafficking | heat shock protein 90kDa alpha (cytosolic), class A member 1; 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 | 0.999 |
AHSA1 | HSP90AB1 | ENSP00000216479 | ENSP00000325875 | AHA1, activator of heat shock 90kDa protein ATPase homolog 1 (yeast); Cochaperone that stimulates HSP90 ATPase activity (By similarity). May affect a step in the endoplasmic reticulum to Golgi trafficking | heat shock protein 90kDa alpha (cytosolic), class B member 1; 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 | 0.999 |
AHSA1 | PPIH | ENSP00000216479 | ENSP00000306614 | AHA1, activator of heat shock 90kDa protein ATPase homolog 1 (yeast); Cochaperone that stimulates HSP90 ATPase activity (By similarity). May affect a step in the endoplasmic reticulum to Golgi trafficking | peptidylprolyl isomerase H (cyclophilin H); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Participates in pre-mRNA splicing. May play a role in the assembly of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome. May act as a chaperone | 0.954 |
AHSA1 | STIP1 | ENSP00000216479 | ENSP00000305958 | AHA1, activator of heat shock 90kDa protein ATPase homolog 1 (yeast); Cochaperone that stimulates HSP90 ATPase activity (By similarity). May affect a step in the endoplasmic reticulum to Golgi trafficking | stress-induced-phosphoprotein 1; Mediates the association of the molecular chaperones HSC70 and HSP90 (HSPCA and HSPCB) | 0.996 |
AHSA1 | UBC | ENSP00000216479 | ENSP00000344818 | AHA1, activator of heat shock 90kDa protein ATPase homolog 1 (yeast); Cochaperone that stimulates HSP90 ATPase activity (By similarity). May affect a step in the endoplasmic reticulum to Golgi trafficking | ubiquitin C | 0.858 |
AHSA2 | HSP90AA1 | ENSP00000349525 | ENSP00000335153 | AHA1, activator of heat shock 90kDa protein ATPase homolog 2 (yeast); Co-chaperone that stimulates HSP90 ATPase activity (By similarity) | heat shock protein 90kDa alpha (cytosolic), class A member 1; 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 | 0.999 |
AHSA2 | HSP90AB1 | ENSP00000349525 | ENSP00000325875 | AHA1, activator of heat shock 90kDa protein ATPase homolog 2 (yeast); Co-chaperone that stimulates HSP90 ATPase activity (By similarity) | heat shock protein 90kDa alpha (cytosolic), class B member 1; 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 | 0.997 |
AHSA2 | PPIH | ENSP00000349525 | ENSP00000306614 | AHA1, activator of heat shock 90kDa protein ATPase homolog 2 (yeast); Co-chaperone that stimulates HSP90 ATPase activity (By similarity) | peptidylprolyl isomerase H (cyclophilin H); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Participates in pre-mRNA splicing. May play a role in the assembly of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome. May act as a chaperone | 0.954 |
AHSA2 | STIP1 | ENSP00000349525 | ENSP00000305958 | AHA1, activator of heat shock 90kDa protein ATPase homolog 2 (yeast); Co-chaperone that stimulates HSP90 ATPase activity (By similarity) | stress-induced-phosphoprotein 1; Mediates the association of the molecular chaperones HSC70 and HSP90 (HSPCA and HSPCB) | 0.996 |
BAG2 | HSP90AA1 | ENSP00000359727 | ENSP00000335153 | BCL2-associated athanogene 2; Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release | heat shock protein 90kDa alpha (cytosolic), class A member 1; 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 | 0.681 |
BAG2 | PPIH | ENSP00000359727 | ENSP00000306614 | BCL2-associated athanogene 2; Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release | peptidylprolyl isomerase H (cyclophilin H); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Participates in pre-mRNA splicing. May play a role in the assembly of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome. May act as a chaperone | 0.944 |
BAG2 | UBC | ENSP00000359727 | ENSP00000344818 | BCL2-associated athanogene 2; Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release | ubiquitin C | 0.973 |
HSP90AA1 | AHSA1 | ENSP00000335153 | ENSP00000216479 | heat shock protein 90kDa alpha (cytosolic), class A member 1; 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 | AHA1, activator of heat shock 90kDa protein ATPase homolog 1 (yeast); Cochaperone that stimulates HSP90 ATPase activity (By similarity). May affect a step in the endoplasmic reticulum to Golgi trafficking | 0.999 |
HSP90AA1 | AHSA2 | ENSP00000335153 | ENSP00000349525 | heat shock protein 90kDa alpha (cytosolic), class A member 1; 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 | AHA1, activator of heat shock 90kDa protein ATPase homolog 2 (yeast); Co-chaperone that stimulates HSP90 ATPase activity (By similarity) | 0.999 |
HSP90AA1 | BAG2 | ENSP00000335153 | ENSP00000359727 | heat shock protein 90kDa alpha (cytosolic), class A member 1; 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 | BCL2-associated athanogene 2; Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release | 0.681 |
HSP90AA1 | HSP90AB1 | ENSP00000335153 | ENSP00000325875 | heat shock protein 90kDa alpha (cytosolic), class A member 1; 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 | heat shock protein 90kDa alpha (cytosolic), class B member 1; 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 | 0.999 |
HSP90AA1 | PPIH | ENSP00000335153 | ENSP00000306614 | heat shock protein 90kDa alpha (cytosolic), class A member 1; 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 | peptidylprolyl isomerase H (cyclophilin H); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Participates in pre-mRNA splicing. May play a role in the assembly of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome. May act as a chaperone | 0.991 |
HSP90AA1 | STIP1 | ENSP00000335153 | ENSP00000305958 | heat shock protein 90kDa alpha (cytosolic), class A member 1; 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 | stress-induced-phosphoprotein 1; Mediates the association of the molecular chaperones HSC70 and HSP90 (HSPCA and HSPCB) | 0.999 |
HSP90AA1 | UBC | ENSP00000335153 | ENSP00000344818 | heat shock protein 90kDa alpha (cytosolic), class A member 1; 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 | ubiquitin C | 0.999 |
HSP90AB1 | AHSA1 | ENSP00000325875 | ENSP00000216479 | heat shock protein 90kDa alpha (cytosolic), class B member 1; 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 | AHA1, activator of heat shock 90kDa protein ATPase homolog 1 (yeast); Cochaperone that stimulates HSP90 ATPase activity (By similarity). May affect a step in the endoplasmic reticulum to Golgi trafficking | 0.999 |