node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ASNA1 | SEC61A1 | ENSP00000349887 | ENSP00000243253 | arsA arsenite transporter, ATP-binding, homolog 1 (bacterial); ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail- anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane pro [...] | Sec61 alpha 1 subunit (S. cerevisiae) | 0.807 |
ASNA1 | SEC61B | ENSP00000349887 | ENSP00000223641 | arsA arsenite transporter, ATP-binding, homolog 1 (bacterial); ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail- anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane pro [...] | Sec61 beta subunit; Necessary for protein translocation in the endoplasmic reticulum | 0.906 |
ASNA1 | SERP1 | ENSP00000349887 | ENSP00000239944 | arsA arsenite transporter, ATP-binding, homolog 1 (bacterial); ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail- anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane pro [...] | stress-associated endoplasmic reticulum protein 1; Interacts with target proteins during their translocation into the lumen of the endoplasmic reticulum. Protects unfolded target proteins against degradation during ER stress. May facilitate glycosylation of target proteins after termination of ER stress. May modulate the use of N-glycosylation sites on target proteins (By similarity) | 0.736 |
ASNA1 | SGTA | ENSP00000349887 | ENSP00000221566 | arsA arsenite transporter, ATP-binding, homolog 1 (bacterial); ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail- anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane pro [...] | small glutamine-rich tetratricopeptide repeat (TPR)-containing, alpha; Co-chaperone that binds directly to HSC70 and HSP70 and regulates their ATPase activity | 0.921 |
CANX | SEC61A1 | ENSP00000247461 | ENSP00000243253 | calnexin; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins. Associated with partial T-cell antigen receptor complexes that escape the ER of immature thymocytes, it may function as a signaling complex regulating thymocyte maturation. Additionally it may play a role in receptor- mediated endocytosis at [...] | Sec61 alpha 1 subunit (S. cerevisiae) | 0.922 |
CANX | SEC61A2 | ENSP00000247461 | ENSP00000298428 | calnexin; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins. Associated with partial T-cell antigen receptor complexes that escape the ER of immature thymocytes, it may function as a signaling complex regulating thymocyte maturation. Additionally it may play a role in receptor- mediated endocytosis at [...] | Sec61 alpha 2 subunit (S. cerevisiae); Appears to play a crucial role in the insertion of secretory and membrane polypeptides into the ER. It is required for assembly of membrane and secretory proteins. Found to be tightly associated with membrane-bound ribosomes, either directly or through adaptor proteins (By similarity) | 0.406 |
CANX | SEC61B | ENSP00000247461 | ENSP00000223641 | calnexin; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins. Associated with partial T-cell antigen receptor complexes that escape the ER of immature thymocytes, it may function as a signaling complex regulating thymocyte maturation. Additionally it may play a role in receptor- mediated endocytosis at [...] | Sec61 beta subunit; Necessary for protein translocation in the endoplasmic reticulum | 0.454 |
CANX | SEC62 | ENSP00000247461 | ENSP00000337688 | calnexin; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins. Associated with partial T-cell antigen receptor complexes that escape the ER of immature thymocytes, it may function as a signaling complex regulating thymocyte maturation. Additionally it may play a role in receptor- mediated endocytosis at [...] | SEC62 homolog (S. cerevisiae); Required for preprotein translocation (By similarity) | 0.420 |
CANX | SEC63 | ENSP00000247461 | ENSP00000357998 | calnexin; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins. Associated with partial T-cell antigen receptor complexes that escape the ER of immature thymocytes, it may function as a signaling complex regulating thymocyte maturation. Additionally it may play a role in receptor- mediated endocytosis at [...] | SEC63 homolog (S. cerevisiae); Required for integral membrane and secreted preprotein translocation across the endoplasmic reticulum membrane | 0.710 |
CANX | SERP1 | ENSP00000247461 | ENSP00000239944 | calnexin; Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins. Associated with partial T-cell antigen receptor complexes that escape the ER of immature thymocytes, it may function as a signaling complex regulating thymocyte maturation. Additionally it may play a role in receptor- mediated endocytosis at [...] | stress-associated endoplasmic reticulum protein 1; Interacts with target proteins during their translocation into the lumen of the endoplasmic reticulum. Protects unfolded target proteins against degradation during ER stress. May facilitate glycosylation of target proteins after termination of ER stress. May modulate the use of N-glycosylation sites on target proteins (By similarity) | 0.665 |
SCNN1A | SCNN1B | ENSP00000353292 | ENSP00000345751 | sodium channel, non-voltage-gated 1 alpha subunit; Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Controls the reabsorption of sodium in kidney, colon, lung and sweat glands. Also plays a role in taste perception | sodium channel, non-voltage-gated 1, beta subunit; Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Controls the reabsorption of sodium in kidney, colon, lung and sweat glands. Also plays a role in taste perception | 0.983 |
SCNN1A | SCNN1G | ENSP00000353292 | ENSP00000300061 | sodium channel, non-voltage-gated 1 alpha subunit; Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Controls the reabsorption of sodium in kidney, colon, lung and sweat glands. Also plays a role in taste perception | sodium channel, non-voltage-gated 1, gamma subunit | 0.961 |
SCNN1A | SERP1 | ENSP00000353292 | ENSP00000239944 | sodium channel, non-voltage-gated 1 alpha subunit; Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Controls the reabsorption of sodium in kidney, colon, lung and sweat glands. Also plays a role in taste perception | stress-associated endoplasmic reticulum protein 1; Interacts with target proteins during their translocation into the lumen of the endoplasmic reticulum. Protects unfolded target proteins against degradation during ER stress. May facilitate glycosylation of target proteins after termination of ER stress. May modulate the use of N-glycosylation sites on target proteins (By similarity) | 0.566 |
SCNN1B | SCNN1A | ENSP00000345751 | ENSP00000353292 | sodium channel, non-voltage-gated 1, beta subunit; Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Controls the reabsorption of sodium in kidney, colon, lung and sweat glands. Also plays a role in taste perception | sodium channel, non-voltage-gated 1 alpha subunit; Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Controls the reabsorption of sodium in kidney, colon, lung and sweat glands. Also plays a role in taste perception | 0.983 |
SCNN1B | SCNN1G | ENSP00000345751 | ENSP00000300061 | sodium channel, non-voltage-gated 1, beta subunit; Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Controls the reabsorption of sodium in kidney, colon, lung and sweat glands. Also plays a role in taste perception | sodium channel, non-voltage-gated 1, gamma subunit | 0.982 |
SCNN1B | SERP1 | ENSP00000345751 | ENSP00000239944 | sodium channel, non-voltage-gated 1, beta subunit; Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Controls the reabsorption of sodium in kidney, colon, lung and sweat glands. Also plays a role in taste perception | stress-associated endoplasmic reticulum protein 1; Interacts with target proteins during their translocation into the lumen of the endoplasmic reticulum. Protects unfolded target proteins against degradation during ER stress. May facilitate glycosylation of target proteins after termination of ER stress. May modulate the use of N-glycosylation sites on target proteins (By similarity) | 0.566 |
SCNN1G | SCNN1A | ENSP00000300061 | ENSP00000353292 | sodium channel, non-voltage-gated 1, gamma subunit | sodium channel, non-voltage-gated 1 alpha subunit; Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Controls the reabsorption of sodium in kidney, colon, lung and sweat glands. Also plays a role in taste perception | 0.961 |
SCNN1G | SCNN1B | ENSP00000300061 | ENSP00000345751 | sodium channel, non-voltage-gated 1, gamma subunit | sodium channel, non-voltage-gated 1, beta subunit; Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Controls the reabsorption of sodium in kidney, colon, lung and sweat glands. Also plays a role in taste perception | 0.982 |
SCNN1G | SERP1 | ENSP00000300061 | ENSP00000239944 | sodium channel, non-voltage-gated 1, gamma subunit | stress-associated endoplasmic reticulum protein 1; Interacts with target proteins during their translocation into the lumen of the endoplasmic reticulum. Protects unfolded target proteins against degradation during ER stress. May facilitate glycosylation of target proteins after termination of ER stress. May modulate the use of N-glycosylation sites on target proteins (By similarity) | 0.566 |
SEC61A1 | ASNA1 | ENSP00000243253 | ENSP00000349887 | Sec61 alpha 1 subunit (S. cerevisiae) | arsA arsenite transporter, ATP-binding, homolog 1 (bacterial); ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors, where the tail- anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane pro [...] | 0.807 |