node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
KAR2 | Q6FRI9_CANGA | Q6FW50 | Q6FRI9 | Endoplasmic reticulum chaperone BiP; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis; Belongs to the heat shock protein 70 family. | Uncharacterized protein. | 0.590 |
KAR2 | Q6FRN9_CANGA | Q6FW50 | Q6FRN9 | Endoplasmic reticulum chaperone BiP; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis; Belongs to the heat shock protein 70 family. | TPR_REGION domain-containing protein. | 0.935 |
KAR2 | Q6FS39_CANGA | Q6FW50 | Q6FS39 | Endoplasmic reticulum chaperone BiP; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis; Belongs to the heat shock protein 70 family. | J domain-containing protein. | 0.864 |
KAR2 | Q6FTS3_CANGA | Q6FW50 | Q6FTS3 | Endoplasmic reticulum chaperone BiP; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis; Belongs to the heat shock protein 70 family. | J domain-containing protein. | 0.744 |
KAR2 | Q6FW89_CANGA | Q6FW50 | Q6FW89 | Endoplasmic reticulum chaperone BiP; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis; Belongs to the heat shock protein 70 family. | WD_REPEATS_REGION domain-containing protein. | 0.495 |
KAR2 | SSA1 | Q6FW50 | Q6FTB5 | Endoplasmic reticulum chaperone BiP; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis; Belongs to the heat shock protein 70 family. | Uncharacterized protein; Belongs to the heat shock protein 70 family. | 0.779 |
KAR2 | SSA3 | Q6FW50 | Q6FTD8 | Endoplasmic reticulum chaperone BiP; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis; Belongs to the heat shock protein 70 family. | Uncharacterized protein; Belongs to the heat shock protein 70 family. | 0.684 |
KAR2 | SSB1 | Q6FW50 | Q876N3 | Endoplasmic reticulum chaperone BiP; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis; Belongs to the heat shock protein 70 family. | Ribosome-associated molecular chaperone SSB; Ribosome-bound, Hsp70-type chaperone that assists in the cotranslational folding of newly synthesized proteins in the cytosol. Stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated, and aggregation- prone nascent polypeptides and domains that cannot fold stably until fully synthesized. The Hsp70-protein substrate interaction depends on ATP-binding and on allosteric regulation between the NBD and the SBD. The ATP-b [...] | 0.968 |
Q6FRI9_CANGA | KAR2 | Q6FRI9 | Q6FW50 | Uncharacterized protein. | Endoplasmic reticulum chaperone BiP; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis; Belongs to the heat shock protein 70 family. | 0.590 |
Q6FRI9_CANGA | Q6FS39_CANGA | Q6FRI9 | Q6FS39 | Uncharacterized protein. | J domain-containing protein. | 0.947 |
Q6FRI9_CANGA | SSA1 | Q6FRI9 | Q6FTB5 | Uncharacterized protein. | Uncharacterized protein; Belongs to the heat shock protein 70 family. | 0.874 |
Q6FRI9_CANGA | SSA3 | Q6FRI9 | Q6FTD8 | Uncharacterized protein. | Uncharacterized protein; Belongs to the heat shock protein 70 family. | 0.856 |
Q6FRI9_CANGA | SSB1 | Q6FRI9 | Q876N3 | Uncharacterized protein. | Ribosome-associated molecular chaperone SSB; Ribosome-bound, Hsp70-type chaperone that assists in the cotranslational folding of newly synthesized proteins in the cytosol. Stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated, and aggregation- prone nascent polypeptides and domains that cannot fold stably until fully synthesized. The Hsp70-protein substrate interaction depends on ATP-binding and on allosteric regulation between the NBD and the SBD. The ATP-b [...] | 0.850 |
Q6FRN9_CANGA | KAR2 | Q6FRN9 | Q6FW50 | TPR_REGION domain-containing protein. | Endoplasmic reticulum chaperone BiP; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis; Belongs to the heat shock protein 70 family. | 0.935 |
Q6FRN9_CANGA | Q6FS39_CANGA | Q6FRN9 | Q6FS39 | TPR_REGION domain-containing protein. | J domain-containing protein. | 0.610 |
Q6FRN9_CANGA | Q6FTS3_CANGA | Q6FRN9 | Q6FTS3 | TPR_REGION domain-containing protein. | J domain-containing protein. | 0.667 |
Q6FRN9_CANGA | SSA1 | Q6FRN9 | Q6FTB5 | TPR_REGION domain-containing protein. | Uncharacterized protein; Belongs to the heat shock protein 70 family. | 0.925 |
Q6FRN9_CANGA | SSA3 | Q6FRN9 | Q6FTD8 | TPR_REGION domain-containing protein. | Uncharacterized protein; Belongs to the heat shock protein 70 family. | 0.925 |
Q6FRN9_CANGA | SSB1 | Q6FRN9 | Q876N3 | TPR_REGION domain-containing protein. | Ribosome-associated molecular chaperone SSB; Ribosome-bound, Hsp70-type chaperone that assists in the cotranslational folding of newly synthesized proteins in the cytosol. Stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated, and aggregation- prone nascent polypeptides and domains that cannot fold stably until fully synthesized. The Hsp70-protein substrate interaction depends on ATP-binding and on allosteric regulation between the NBD and the SBD. The ATP-b [...] | 0.925 |
Q6FS39_CANGA | KAR2 | Q6FS39 | Q6FW50 | J domain-containing protein. | Endoplasmic reticulum chaperone BiP; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis; Belongs to the heat shock protein 70 family. | 0.864 |