node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
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 | HSP90B1 | ENSP00000349525 | ENSP00000299767 | AHA1, activator of heat shock 90kDa protein ATPase homolog 2 (yeast); Co-chaperone that stimulates HSP90 ATPase activity (By similarity) | heat shock protein 90kDa beta (Grp94), member 1; Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity | 0.966 |
AHSA2 | NKTR | ENSP00000349525 | ENSP00000232978 | AHA1, activator of heat shock 90kDa protein ATPase homolog 2 (yeast); Co-chaperone that stimulates HSP90 ATPase activity (By similarity) | natural killer-tumor recognition sequence; Component of a putative tumor-recognition complex. Involved in the function of NK cells | 0.954 |
AHSA2 | PPID | ENSP00000349525 | ENSP00000303754 | AHA1, activator of heat shock 90kDa protein ATPase homolog 2 (yeast); Co-chaperone that stimulates HSP90 ATPase activity (By similarity) | peptidylprolyl isomerase D; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Proposed to act as a co-chaperone in HSP90 complexes such as in unligated steroid receptors heterocomplexes. Different co-chaperones seem to compete for association with HSP90 thus establishing distinct HSP90-co-chaperone-receptor complexes with the potential to exert tissue-specific receptor activity control. May have a preference for estrogen receptor complexes and is not found in glucocorticoid receptor complexes. May be i [...] | 0.964 |
AHSA2 | PPIG | ENSP00000349525 | ENSP00000260970 | AHA1, activator of heat shock 90kDa protein ATPase homolog 2 (yeast); Co-chaperone that stimulates HSP90 ATPase activity (By similarity) | peptidylprolyl isomerase G (cyclophilin G); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be implicated in the folding, transport, and assembly of proteins. May play an important role in the regulation of pre-mRNA splicing | 0.954 |
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 |
AHSA2 | SUGT1 | ENSP00000349525 | ENSP00000367208 | AHA1, activator of heat shock 90kDa protein ATPase homolog 2 (yeast); Co-chaperone that stimulates HSP90 ATPase activity (By similarity) | SGT1, suppressor of G2 allele of SKP1 (S. cerevisiae); May play a role in ubiquitination and subsequent proteasomal degradation of target proteins | 0.951 |
AHSA2 | TRAP1 | ENSP00000349525 | ENSP00000246957 | AHA1, activator of heat shock 90kDa protein ATPase homolog 2 (yeast); Co-chaperone that stimulates HSP90 ATPase activity (By similarity) | TNF receptor-associated protein 1; Chaperone that expresses an ATPase activity | 0.943 |
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 | 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 | HSP90B1 | ENSP00000335153 | ENSP00000299767 | 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 beta (Grp94), member 1; Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity | 0.655 |
HSP90AA1 | NKTR | ENSP00000335153 | ENSP00000232978 | 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 | natural killer-tumor recognition sequence; Component of a putative tumor-recognition complex. Involved in the function of NK cells | 0.990 |
HSP90AA1 | PPID | ENSP00000335153 | ENSP00000303754 | 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 D; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Proposed to act as a co-chaperone in HSP90 complexes such as in unligated steroid receptors heterocomplexes. Different co-chaperones seem to compete for association with HSP90 thus establishing distinct HSP90-co-chaperone-receptor complexes with the potential to exert tissue-specific receptor activity control. May have a preference for estrogen receptor complexes and is not found in glucocorticoid receptor complexes. May be i [...] | 0.999 |
HSP90AA1 | PPIG | ENSP00000335153 | ENSP00000260970 | 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 G (cyclophilin G); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be implicated in the folding, transport, and assembly of proteins. May play an important role in the regulation of pre-mRNA splicing | 0.992 |
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 | SUGT1 | ENSP00000335153 | ENSP00000367208 | 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 | SGT1, suppressor of G2 allele of SKP1 (S. cerevisiae); May play a role in ubiquitination and subsequent proteasomal degradation of target proteins | 0.999 |
HSP90AA1 | TRAP1 | ENSP00000335153 | ENSP00000246957 | 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 | TNF receptor-associated protein 1; Chaperone that expresses an ATPase activity | 0.723 |