node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CASP3 | CASP7 | ENSP00000311032 | ENSP00000358327 | caspase 3, apoptosis-related cysteine peptidase; Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a ’216-Asp-|-Gly-217’ bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop- helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage | caspase 7, apoptosis-related cysteine peptidase | 0.933 |
CASP3 | CFLAR | ENSP00000311032 | ENSP00000312455 | caspase 3, apoptosis-related cysteine peptidase; Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a ’216-Asp-|-Gly-217’ bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop- helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage | CASP8 and FADD-like apoptosis regulator | 0.849 |
CASP3 | HSP90AB1 | ENSP00000311032 | ENSP00000325875 | caspase 3, apoptosis-related cysteine peptidase; Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a ’216-Asp-|-Gly-217’ bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop- helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage | 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 | 0.437 |
CASP7 | CASP3 | ENSP00000358327 | ENSP00000311032 | caspase 7, apoptosis-related cysteine peptidase | caspase 3, apoptosis-related cysteine peptidase; Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a ’216-Asp-|-Gly-217’ bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop- helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage | 0.933 |
CASP7 | CFLAR | ENSP00000358327 | ENSP00000312455 | caspase 7, apoptosis-related cysteine peptidase | CASP8 and FADD-like apoptosis regulator | 0.628 |
CDC37L1 | HSP90AB1 | ENSP00000371278 | ENSP00000325875 | cell division cycle 37 homolog (S. cerevisiae)-like 1; Co-chaperone that binds to numerous proteins and promotes their interaction with Hsp70 and Hsp90 (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 | 0.995 |
CDC37L1 | TTC4 | ENSP00000371278 | ENSP00000360329 | cell division cycle 37 homolog (S. cerevisiae)-like 1; Co-chaperone that binds to numerous proteins and promotes their interaction with Hsp70 and Hsp90 (By similarity) | tetratricopeptide repeat domain 4 | 0.521 |
CFLAR | CASP3 | ENSP00000312455 | ENSP00000311032 | CASP8 and FADD-like apoptosis regulator | caspase 3, apoptosis-related cysteine peptidase; Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a ’216-Asp-|-Gly-217’ bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop- helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage | 0.849 |
CFLAR | CASP7 | ENSP00000312455 | ENSP00000358327 | CASP8 and FADD-like apoptosis regulator | caspase 7, apoptosis-related cysteine peptidase | 0.628 |
HSP90AB1 | CASP3 | ENSP00000325875 | ENSP00000311032 | 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 | caspase 3, apoptosis-related cysteine peptidase; Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a ’216-Asp-|-Gly-217’ bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop- helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage | 0.437 |
HSP90AB1 | CDC37L1 | ENSP00000325875 | ENSP00000371278 | 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 | cell division cycle 37 homolog (S. cerevisiae)-like 1; Co-chaperone that binds to numerous proteins and promotes their interaction with Hsp70 and Hsp90 (By similarity) | 0.995 |
HSP90AB1 | TTC4 | ENSP00000325875 | ENSP00000360329 | 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 | tetratricopeptide repeat domain 4 | 0.996 |
NEB | TMOD4 | ENSP00000380505 | ENSP00000295314 | nebulin | tropomodulin 4 (muscle); Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton | 0.947 |
TMOD4 | NEB | ENSP00000295314 | ENSP00000380505 | tropomodulin 4 (muscle); Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton | nebulin | 0.947 |
TTC4 | CDC37L1 | ENSP00000360329 | ENSP00000371278 | tetratricopeptide repeat domain 4 | cell division cycle 37 homolog (S. cerevisiae)-like 1; Co-chaperone that binds to numerous proteins and promotes their interaction with Hsp70 and Hsp90 (By similarity) | 0.521 |
TTC4 | HSP90AB1 | ENSP00000360329 | ENSP00000325875 | tetratricopeptide repeat domain 4 | 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 | 0.996 |