node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Cct2 | Cct6a | ENSRNOP00000029234 | ENSRNOP00000001227 | T-complex protein 1 subunit beta; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin. | Chaperonin containing Tcp1, subunit 6A (Zeta 1). | 0.997 |
Cct2 | Dnaja1 | ENSRNOP00000029234 | ENSRNOP00000010061 | T-complex protein 1 subunit beta; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin. | DnaJ homolog subfamily A member 1; Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co- chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. | 0.463 |
Cct2 | Dnaja2 | ENSRNOP00000029234 | ENSRNOP00000022573 | T-complex protein 1 subunit beta; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin. | DnaJ homolog subfamily A member 2; Co-chaperone of Hsc70. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro). | 0.579 |
Cct2 | Dnaja4 | ENSRNOP00000029234 | ENSRNOP00000017053 | T-complex protein 1 subunit beta; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin. | DnaJ heat shock protein family (Hsp40) member A4. | 0.437 |
Cct2 | Hspa1l | ENSRNOP00000029234 | ENSRNOP00000063974 | T-complex protein 1 subunit beta; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin. | Heat shock 70 kDa protein 1-like; Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis an [...] | 0.840 |
Cct6a | Cct2 | ENSRNOP00000001227 | ENSRNOP00000029234 | Chaperonin containing Tcp1, subunit 6A (Zeta 1). | T-complex protein 1 subunit beta; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin. | 0.997 |
Cct6a | Dnaja1 | ENSRNOP00000001227 | ENSRNOP00000010061 | Chaperonin containing Tcp1, subunit 6A (Zeta 1). | DnaJ homolog subfamily A member 1; Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co- chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. | 0.416 |
Cct6a | Dnaja2 | ENSRNOP00000001227 | ENSRNOP00000022573 | Chaperonin containing Tcp1, subunit 6A (Zeta 1). | DnaJ homolog subfamily A member 2; Co-chaperone of Hsc70. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro). | 0.505 |
Cct6a | Dnaja4 | ENSRNOP00000001227 | ENSRNOP00000017053 | Chaperonin containing Tcp1, subunit 6A (Zeta 1). | DnaJ heat shock protein family (Hsp40) member A4. | 0.496 |
Cct6a | Dnajb1 | ENSRNOP00000001227 | ENSRNOP00000032313 | Chaperonin containing Tcp1, subunit 6A (Zeta 1). | DnaJ (Hsp40) homolog, subfamily B, member 1 (Predicted), isoform CRA_a. | 0.435 |
Cct6a | Hspa1l | ENSRNOP00000001227 | ENSRNOP00000063974 | Chaperonin containing Tcp1, subunit 6A (Zeta 1). | Heat shock 70 kDa protein 1-like; Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis an [...] | 0.840 |
Dnaja1 | Cct2 | ENSRNOP00000010061 | ENSRNOP00000029234 | DnaJ homolog subfamily A member 1; Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co- chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. | T-complex protein 1 subunit beta; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin. | 0.463 |
Dnaja1 | Cct6a | ENSRNOP00000010061 | ENSRNOP00000001227 | DnaJ homolog subfamily A member 1; Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co- chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. | Chaperonin containing Tcp1, subunit 6A (Zeta 1). | 0.416 |
Dnaja1 | Dnaja2 | ENSRNOP00000010061 | ENSRNOP00000022573 | DnaJ homolog subfamily A member 1; Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co- chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. | DnaJ homolog subfamily A member 2; Co-chaperone of Hsc70. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro). | 0.815 |
Dnaja1 | Dnaja4 | ENSRNOP00000010061 | ENSRNOP00000017053 | DnaJ homolog subfamily A member 1; Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co- chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. | DnaJ heat shock protein family (Hsp40) member A4. | 0.639 |
Dnaja1 | Dnajb1 | ENSRNOP00000010061 | ENSRNOP00000032313 | DnaJ homolog subfamily A member 1; Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co- chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. | DnaJ (Hsp40) homolog, subfamily B, member 1 (Predicted), isoform CRA_a. | 0.868 |
Dnaja1 | Hspa1l | ENSRNOP00000010061 | ENSRNOP00000063974 | DnaJ homolog subfamily A member 1; Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co- chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. | Heat shock 70 kDa protein 1-like; Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis an [...] | 0.898 |
Dnaja2 | Cct2 | ENSRNOP00000022573 | ENSRNOP00000029234 | DnaJ homolog subfamily A member 2; Co-chaperone of Hsc70. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro). | T-complex protein 1 subunit beta; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin. | 0.579 |
Dnaja2 | Cct6a | ENSRNOP00000022573 | ENSRNOP00000001227 | DnaJ homolog subfamily A member 2; Co-chaperone of Hsc70. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro). | Chaperonin containing Tcp1, subunit 6A (Zeta 1). | 0.505 |
Dnaja2 | Dnaja1 | ENSRNOP00000022573 | ENSRNOP00000010061 | DnaJ homolog subfamily A member 2; Co-chaperone of Hsc70. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro). | DnaJ homolog subfamily A member 1; Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co- chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. | 0.815 |