node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
PIIN_00922 | PIIN_02671 | G4T6Y0 | G4TBU7 | Probable t-complex-type molecular chaperone, epsilon subunit. | Uncharacterized protein. | 0.747 |
PIIN_00922 | PIIN_03742 | G4T6Y0 | G4TEQ4 | Probable t-complex-type molecular chaperone, epsilon subunit. | T-complex protein 1 subunit eta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. | 0.999 |
PIIN_00922 | PIIN_04503 | G4T6Y0 | G4TGX4 | Probable t-complex-type molecular chaperone, epsilon subunit. | T-complex protein 1 subunit delta. | 0.999 |
PIIN_00922 | PIIN_07636 | G4T6Y0 | G4TQU0 | Probable t-complex-type molecular chaperone, epsilon subunit. | Probable CCT2-chaperonin of the TCP1 ring complex, cytosolic. | 0.999 |
PIIN_02671 | PIIN_00922 | G4TBU7 | G4T6Y0 | Uncharacterized protein. | Probable t-complex-type molecular chaperone, epsilon subunit. | 0.747 |
PIIN_02671 | PIIN_03742 | G4TBU7 | G4TEQ4 | Uncharacterized protein. | T-complex protein 1 subunit eta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. | 0.637 |
PIIN_02671 | PIIN_04503 | G4TBU7 | G4TGX4 | Uncharacterized protein. | T-complex protein 1 subunit delta. | 0.478 |
PIIN_02671 | PIIN_07636 | G4TBU7 | G4TQU0 | Uncharacterized protein. | Probable CCT2-chaperonin of the TCP1 ring complex, cytosolic. | 0.467 |
PIIN_03742 | PIIN_00922 | G4TEQ4 | G4T6Y0 | T-complex protein 1 subunit eta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. | Probable t-complex-type molecular chaperone, epsilon subunit. | 0.999 |
PIIN_03742 | PIIN_02671 | G4TEQ4 | G4TBU7 | T-complex protein 1 subunit eta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. | Uncharacterized protein. | 0.637 |
PIIN_03742 | PIIN_04503 | G4TEQ4 | G4TGX4 | T-complex protein 1 subunit eta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. | T-complex protein 1 subunit delta. | 0.999 |
PIIN_03742 | PIIN_07636 | G4TEQ4 | G4TQU0 | T-complex protein 1 subunit eta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. | Probable CCT2-chaperonin of the TCP1 ring complex, cytosolic. | 0.999 |
PIIN_04503 | PIIN_00922 | G4TGX4 | G4T6Y0 | T-complex protein 1 subunit delta. | Probable t-complex-type molecular chaperone, epsilon subunit. | 0.999 |
PIIN_04503 | PIIN_02671 | G4TGX4 | G4TBU7 | T-complex protein 1 subunit delta. | Uncharacterized protein. | 0.478 |
PIIN_04503 | PIIN_03742 | G4TGX4 | G4TEQ4 | T-complex protein 1 subunit delta. | T-complex protein 1 subunit eta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. | 0.999 |
PIIN_04503 | PIIN_07636 | G4TGX4 | G4TQU0 | T-complex protein 1 subunit delta. | Probable CCT2-chaperonin of the TCP1 ring complex, cytosolic. | 0.999 |
PIIN_07636 | PIIN_00922 | G4TQU0 | G4T6Y0 | Probable CCT2-chaperonin of the TCP1 ring complex, cytosolic. | Probable t-complex-type molecular chaperone, epsilon subunit. | 0.999 |
PIIN_07636 | PIIN_02671 | G4TQU0 | G4TBU7 | Probable CCT2-chaperonin of the TCP1 ring complex, cytosolic. | Uncharacterized protein. | 0.467 |
PIIN_07636 | PIIN_03742 | G4TQU0 | G4TEQ4 | Probable CCT2-chaperonin of the TCP1 ring complex, cytosolic. | T-complex protein 1 subunit eta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. | 0.999 |
PIIN_07636 | PIIN_04503 | G4TQU0 | G4TGX4 | Probable CCT2-chaperonin of the TCP1 ring complex, cytosolic. | T-complex protein 1 subunit delta. | 0.999 |