node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Bbs10 | Bbs12 | ENSRNOP00000037320 | ENSRNOP00000009898 | Bardet-Biedl syndrome 10 (Human). | Bardet-Biedl syndrome 12. | 0.991 |
Bbs10 | Bbs5 | ENSRNOP00000037320 | ENSRNOP00000009396 | Bardet-Biedl syndrome 10 (Human). | Bardet-Biedl syndrome 5 protein homolog; The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the gua [...] | 0.896 |
Bbs10 | Bbs7 | ENSRNOP00000037320 | ENSRNOP00000021453 | Bardet-Biedl syndrome 10 (Human). | Bardet-Biedl syndrome 7 protein homolog; The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. | 0.940 |
Bbs10 | Cct2 | ENSRNOP00000037320 | ENSRNOP00000029234 | Bardet-Biedl syndrome 10 (Human). | 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. | 0.968 |
Bbs10 | Cct3 | ENSRNOP00000037320 | ENSRNOP00000025824 | Bardet-Biedl syndrome 10 (Human). | T-complex protein 1 subunit gamma; 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. | 0.919 |
Bbs10 | Cct4 | ENSRNOP00000037320 | ENSRNOP00000012847 | Bardet-Biedl syndrome 10 (Human). | T-complex protein 1 subunit delta; 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. | 0.967 |
Bbs10 | Cct5 | ENSRNOP00000037320 | ENSRNOP00000015886 | Bardet-Biedl syndrome 10 (Human). | T-complex protein 1 subunit epsilon; 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. | 0.966 |
Bbs10 | Cct7 | ENSRNOP00000037320 | ENSRNOP00000021030 | Bardet-Biedl syndrome 10 (Human). | 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. | 0.965 |
Bbs10 | Cct8l1 | ENSRNOP00000037320 | ENSRNOP00000067222 | Bardet-Biedl syndrome 10 (Human). | Chaperonin containing TCP1, subunit 8 (theta)-like 1. | 0.960 |
Bbs10 | LOC102553845 | ENSRNOP00000037320 | ENSRNOP00000066908 | Bardet-Biedl syndrome 10 (Human). | Chaperonin-containing TCP1, subunit 8 (theta)-like 1. | 0.960 |
Bbs12 | Bbs10 | ENSRNOP00000009898 | ENSRNOP00000037320 | Bardet-Biedl syndrome 12. | Bardet-Biedl syndrome 10 (Human). | 0.991 |
Bbs12 | Bbs5 | ENSRNOP00000009898 | ENSRNOP00000009396 | Bardet-Biedl syndrome 12. | Bardet-Biedl syndrome 5 protein homolog; The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the gua [...] | 0.806 |
Bbs12 | Bbs7 | ENSRNOP00000009898 | ENSRNOP00000021453 | Bardet-Biedl syndrome 12. | Bardet-Biedl syndrome 7 protein homolog; The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. | 0.952 |
Bbs5 | Bbs10 | ENSRNOP00000009396 | ENSRNOP00000037320 | Bardet-Biedl syndrome 5 protein homolog; The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the gua [...] | Bardet-Biedl syndrome 10 (Human). | 0.896 |
Bbs5 | Bbs12 | ENSRNOP00000009396 | ENSRNOP00000009898 | Bardet-Biedl syndrome 5 protein homolog; The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the gua [...] | Bardet-Biedl syndrome 12. | 0.806 |
Bbs5 | Bbs7 | ENSRNOP00000009396 | ENSRNOP00000021453 | Bardet-Biedl syndrome 5 protein homolog; The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the gua [...] | Bardet-Biedl syndrome 7 protein homolog; The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. | 0.999 |
Bbs7 | Bbs10 | ENSRNOP00000021453 | ENSRNOP00000037320 | Bardet-Biedl syndrome 7 protein homolog; The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. | Bardet-Biedl syndrome 10 (Human). | 0.940 |
Bbs7 | Bbs12 | ENSRNOP00000021453 | ENSRNOP00000009898 | Bardet-Biedl syndrome 7 protein homolog; The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. | Bardet-Biedl syndrome 12. | 0.952 |
Bbs7 | Bbs5 | ENSRNOP00000021453 | ENSRNOP00000009396 | Bardet-Biedl syndrome 7 protein homolog; The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. | Bardet-Biedl syndrome 5 protein homolog; The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the gua [...] | 0.999 |
Cct2 | Bbs10 | ENSRNOP00000029234 | ENSRNOP00000037320 | 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. | Bardet-Biedl syndrome 10 (Human). | 0.968 |