node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CDC16 | PPP5C | ENSP00000348554 | ENSP00000012443 | cell division cycle 16 homolog (S. cerevisiae); Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins- it mainly mediates the formation of ’Lys-11’-linked polyubiquitin chains and, to a lower extent, the formation of ’Lys-48’- and ’Lys-63’-linked polyubiquitin chains | protein phosphatase 5, catalytic subunit; May play a role in the regulation of RNA biogenesis and/or mitosis. In vitro, dephosphorylates serine residues of skeletal muscle phosphorylase and histone H1 | 0.955 |
CDC16 | UBC | ENSP00000348554 | ENSP00000344818 | cell division cycle 16 homolog (S. cerevisiae); Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins- it mainly mediates the formation of ’Lys-11’-linked polyubiquitin chains and, to a lower extent, the formation of ’Lys-48’- and ’Lys-63’-linked polyubiquitin chains | ubiquitin C | 0.980 |
CDC37 | FKBP5 | ENSP00000222005 | ENSP00000338160 | cell division cycle 37 homolog (S. cerevisiae); Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity | FK506 binding protein 5; Interacts with functionally mature heterooligomeric progesterone receptor complexes along with HSP90 and TEBP | 0.414 |
CDC37 | HSP90AA1 | ENSP00000222005 | ENSP00000335153 | cell division cycle 37 homolog (S. cerevisiae); Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity | 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 |
CDC37 | HSP90AB1 | ENSP00000222005 | ENSP00000325875 | cell division cycle 37 homolog (S. cerevisiae); Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity | 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 |
CDC37 | PPP5C | ENSP00000222005 | ENSP00000012443 | cell division cycle 37 homolog (S. cerevisiae); Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity | protein phosphatase 5, catalytic subunit; May play a role in the regulation of RNA biogenesis and/or mitosis. In vitro, dephosphorylates serine residues of skeletal muscle phosphorylase and histone H1 | 0.881 |
CDC37 | RAF1 | ENSP00000222005 | ENSP00000251849 | cell division cycle 37 homolog (S. cerevisiae); Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity | v-raf-1 murine leukemia viral oncogene homolog 1; Serine/threonine-protein kinase that acts as a regulatory link between the membrane-associated Ras GTPases and the MAPK/ERK cascade, and this critical regulatory link functions as a switch determining cell fate decisions including proliferation, differentiation, apoptosis, survival and oncogenic transformation. RAF1 activation initiates a mitogen-activated protein kinase (MAPK) cascade that comprises a sequential phosphorylation of the dual-specific MAPK kinases (MAP2K1/MEK1 and MAP2K2/MEK2) and the extracellular signal-regulated kinase [...] | 0.939 |
CDC37 | TRAP1 | ENSP00000222005 | ENSP00000246957 | cell division cycle 37 homolog (S. cerevisiae); Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity | TNF receptor-associated protein 1; Chaperone that expresses an ATPase activity | 0.805 |
CDC37 | UBC | ENSP00000222005 | ENSP00000344818 | cell division cycle 37 homolog (S. cerevisiae); Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity | ubiquitin C | 0.992 |
CHORDC1 | HSP90AA1 | ENSP00000319255 | ENSP00000335153 | cysteine and histidine-rich domain (CHORD) containing 1; Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2. Proposed to act as co-chaperone for HSP90. May play a role in the regulation of NOD1 via a HSP90 chaperone complex. In vitro, has intrinsic chaperone activity. This function may be achieved by inhibiting association of ROCK2 with NPM1. Involved in stress response. Prevents tumorigenesis | 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 | 0.989 |
CHORDC1 | HSP90AB1 | ENSP00000319255 | ENSP00000325875 | cysteine and histidine-rich domain (CHORD) containing 1; Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2. Proposed to act as co-chaperone for HSP90. May play a role in the regulation of NOD1 via a HSP90 chaperone complex. In vitro, has intrinsic chaperone activity. This function may be achieved by inhibiting association of ROCK2 with NPM1. Involved in stress response. Prevents tumorigenesis | 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 | 0.949 |
CHORDC1 | PPP5C | ENSP00000319255 | ENSP00000012443 | cysteine and histidine-rich domain (CHORD) containing 1; Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2. Proposed to act as co-chaperone for HSP90. May play a role in the regulation of NOD1 via a HSP90 chaperone complex. In vitro, has intrinsic chaperone activity. This function may be achieved by inhibiting association of ROCK2 with NPM1. Involved in stress response. Prevents tumorigenesis | protein phosphatase 5, catalytic subunit; May play a role in the regulation of RNA biogenesis and/or mitosis. In vitro, dephosphorylates serine residues of skeletal muscle phosphorylase and histone H1 | 0.865 |
CHORDC1 | UBC | ENSP00000319255 | ENSP00000344818 | cysteine and histidine-rich domain (CHORD) containing 1; Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2. Proposed to act as co-chaperone for HSP90. May play a role in the regulation of NOD1 via a HSP90 chaperone complex. In vitro, has intrinsic chaperone activity. This function may be achieved by inhibiting association of ROCK2 with NPM1. Involved in stress response. Prevents tumorigenesis | ubiquitin C | 0.795 |
FKBP5 | CDC37 | ENSP00000338160 | ENSP00000222005 | FK506 binding protein 5; Interacts with functionally mature heterooligomeric progesterone receptor complexes along with HSP90 and TEBP | cell division cycle 37 homolog (S. cerevisiae); Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity | 0.414 |
FKBP5 | HSP90AA1 | ENSP00000338160 | ENSP00000335153 | FK506 binding protein 5; Interacts with functionally mature heterooligomeric progesterone receptor complexes along with HSP90 and TEBP | 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 |
FKBP5 | HSP90AB1 | ENSP00000338160 | ENSP00000325875 | FK506 binding protein 5; Interacts with functionally mature heterooligomeric progesterone receptor complexes along with HSP90 and TEBP | 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 | 0.901 |
FKBP5 | PPP5C | ENSP00000338160 | ENSP00000012443 | FK506 binding protein 5; Interacts with functionally mature heterooligomeric progesterone receptor complexes along with HSP90 and TEBP | protein phosphatase 5, catalytic subunit; May play a role in the regulation of RNA biogenesis and/or mitosis. In vitro, dephosphorylates serine residues of skeletal muscle phosphorylase and histone H1 | 0.919 |
FKBP5 | TRAP1 | ENSP00000338160 | ENSP00000246957 | FK506 binding protein 5; Interacts with functionally mature heterooligomeric progesterone receptor complexes along with HSP90 and TEBP | TNF receptor-associated protein 1; Chaperone that expresses an ATPase activity | 0.779 |
FKBP5 | UBC | ENSP00000338160 | ENSP00000344818 | FK506 binding protein 5; Interacts with functionally mature heterooligomeric progesterone receptor complexes along with HSP90 and TEBP | ubiquitin C | 0.818 |
HSP90AA1 | CDC37 | ENSP00000335153 | ENSP00000222005 | 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 | cell division cycle 37 homolog (S. cerevisiae); Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity | 0.999 |