node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CNBD2 | EPYC | ENSP00000340954 | ENSP00000261172 | cyclic nucleotide binding domain containing 2 | epiphycan; May have a role in bone formation and also in establishing the ordered structure of cartilage through matrix organization | 0.760 |
CNBD2 | PRKG2 | ENSP00000340954 | ENSP00000264399 | cyclic nucleotide binding domain containing 2 | protein kinase, cGMP-dependent, type II | 0.787 |
EPYC | CNBD2 | ENSP00000261172 | ENSP00000340954 | epiphycan; May have a role in bone formation and also in establishing the ordered structure of cartilage through matrix organization | cyclic nucleotide binding domain containing 2 | 0.760 |
EPYC | HSP90AA1 | ENSP00000261172 | ENSP00000335153 | epiphycan; May have a role in bone formation and also in establishing the ordered structure of cartilage through matrix organization | 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 | 0.799 |
EPYC | HSP90AB1 | ENSP00000261172 | ENSP00000325875 | epiphycan; May have a role in bone formation and also in establishing the ordered structure of cartilage through matrix organization | 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 | 0.799 |
EPYC | HSP90B1 | ENSP00000261172 | ENSP00000299767 | epiphycan; May have a role in bone formation and also in establishing the ordered structure of cartilage through matrix organization | 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 | 0.684 |
EPYC | PLXNB3 | ENSP00000261172 | ENSP00000442736 | epiphycan; May have a role in bone formation and also in establishing the ordered structure of cartilage through matrix organization | plexin B3; Receptor for SEMA5A that plays a role in axon guidance, invasive growth and cell migration. Stimulates neurite outgrowth and mediates Ca(2+)/Mg(2+)-dependent cell aggregation. In glioma cells, SEMA5A stimulation of PLXNB3 results in the disassembly of F-actin stress fibers, disruption of focal adhesions and cellular collapse as well as inhibition of cell migration and invasion through ARHGDIA-mediated inactivation of RAC1 | 0.616 |
EPYC | PRKAR1A | ENSP00000261172 | ENSP00000351410 | epiphycan; May have a role in bone formation and also in establishing the ordered structure of cartilage through matrix organization | protein kinase, cAMP-dependent, regulatory, type I, alpha; Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells | 0.760 |
EPYC | PRKAR1B | ENSP00000261172 | ENSP00000353415 | epiphycan; May have a role in bone formation and also in establishing the ordered structure of cartilage through matrix organization | protein kinase, cAMP-dependent, regulatory, type I, beta; Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells | 0.760 |
EPYC | PRKAR2A | ENSP00000261172 | ENSP00000265563 | epiphycan; May have a role in bone formation and also in establishing the ordered structure of cartilage through matrix organization | protein kinase, cAMP-dependent, regulatory, type II, alpha; Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase | 0.760 |
EPYC | PRKAR2B | ENSP00000261172 | ENSP00000265717 | epiphycan; May have a role in bone formation and also in establishing the ordered structure of cartilage through matrix organization | protein kinase, cAMP-dependent, regulatory, type II, beta; Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase | 0.760 |
EPYC | PRKG2 | ENSP00000261172 | ENSP00000264399 | epiphycan; May have a role in bone formation and also in establishing the ordered structure of cartilage through matrix organization | protein kinase, cGMP-dependent, type II | 0.611 |
HSP90AA1 | EPYC | ENSP00000335153 | ENSP00000261172 | 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 | epiphycan; May have a role in bone formation and also in establishing the ordered structure of cartilage through matrix organization | 0.799 |
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 | PRKAR1A | ENSP00000335153 | ENSP00000351410 | 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 | protein kinase, cAMP-dependent, regulatory, type I, alpha; Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells | 0.727 |
HSP90AA1 | PRKAR2B | ENSP00000335153 | ENSP00000265717 | 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 | protein kinase, cAMP-dependent, regulatory, type II, beta; Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase | 0.916 |
HSP90AA1 | PRKG2 | ENSP00000335153 | ENSP00000264399 | 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 | protein kinase, cGMP-dependent, type II | 0.612 |
HSP90AB1 | EPYC | ENSP00000325875 | ENSP00000261172 | 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 | epiphycan; May have a role in bone formation and also in establishing the ordered structure of cartilage through matrix organization | 0.799 |
HSP90AB1 | HSP90AA1 | ENSP00000325875 | ENSP00000335153 | 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 | 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 |