| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| DNAJC10 | ERO1LB | ENSP00000264065 | ENSP00000346635 | DnaJ (Hsp40) homolog, subfamily C, member 10 | ERO1-like beta (S. cerevisiae); Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly P4HB/PDI isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on P4HB/PDI to transfer oxidizing equivalent. Associates with ERP44 but not with GRP54, demonstrating that it does not oxidize all PDI related proteins and can discriminate between PDI and related proteins. Its reoxidation probably involves electron transfer to molecular oxygen via FAD. Acts independently [...] | 0.735 |
| DNAJC10 | ERP29 | ENSP00000264065 | ENSP00000261735 | DnaJ (Hsp40) homolog, subfamily C, member 10 | endoplasmic reticulum protein 29; Does not seem to be a disulfide isomerase. Plays an important role in the processing of secretory proteins within the endoplasmic reticulum (ER), possibly by participating in the folding of proteins in the ER | 0.592 |
| DNAJC10 | P4HB | ENSP00000264065 | ENSP00000327801 | DnaJ (Hsp40) homolog, subfamily C, member 10 | prolyl 4-hydroxylase, beta polypeptide; This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with [...] | 0.521 |
| DNAJC10 | PDIA2 | ENSP00000264065 | ENSP00000219406 | DnaJ (Hsp40) homolog, subfamily C, member 10 | protein disulfide isomerase family A, member 2; Acts as an intracellular estrogen-binding protein. May be involved in modulating cellular levels and biological functions of estrogens in the pancreas. May act as a chaperone that inhibits aggregation of misfolded proteins | 0.548 |
| DNAJC10 | PDIA3 | ENSP00000264065 | ENSP00000300289 | DnaJ (Hsp40) homolog, subfamily C, member 10 | protein disulfide isomerase family A, member 3 | 0.552 |
| DNAJC10 | PDIA4 | ENSP00000264065 | ENSP00000286091 | DnaJ (Hsp40) homolog, subfamily C, member 10 | protein disulfide isomerase family A, member 4 | 0.542 |
| ERGIC3 | ERO1LB | ENSP00000349970 | ENSP00000346635 | ERGIC and golgi 3; Possible role in transport between endoplasmic reticulum and Golgi (By similarity) | ERO1-like beta (S. cerevisiae); Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly P4HB/PDI isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on P4HB/PDI to transfer oxidizing equivalent. Associates with ERP44 but not with GRP54, demonstrating that it does not oxidize all PDI related proteins and can discriminate between PDI and related proteins. Its reoxidation probably involves electron transfer to molecular oxygen via FAD. Acts independently [...] | 0.758 |
| ERO1LB | DNAJC10 | ENSP00000346635 | ENSP00000264065 | ERO1-like beta (S. cerevisiae); Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly P4HB/PDI isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on P4HB/PDI to transfer oxidizing equivalent. Associates with ERP44 but not with GRP54, demonstrating that it does not oxidize all PDI related proteins and can discriminate between PDI and related proteins. Its reoxidation probably involves electron transfer to molecular oxygen via FAD. Acts independently [...] | DnaJ (Hsp40) homolog, subfamily C, member 10 | 0.735 |
| ERO1LB | ERGIC3 | ENSP00000346635 | ENSP00000349970 | ERO1-like beta (S. cerevisiae); Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly P4HB/PDI isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on P4HB/PDI to transfer oxidizing equivalent. Associates with ERP44 but not with GRP54, demonstrating that it does not oxidize all PDI related proteins and can discriminate between PDI and related proteins. Its reoxidation probably involves electron transfer to molecular oxygen via FAD. Acts independently [...] | ERGIC and golgi 3; Possible role in transport between endoplasmic reticulum and Golgi (By similarity) | 0.758 |
| ERO1LB | ERP29 | ENSP00000346635 | ENSP00000261735 | ERO1-like beta (S. cerevisiae); Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly P4HB/PDI isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on P4HB/PDI to transfer oxidizing equivalent. Associates with ERP44 but not with GRP54, demonstrating that it does not oxidize all PDI related proteins and can discriminate between PDI and related proteins. Its reoxidation probably involves electron transfer to molecular oxygen via FAD. Acts independently [...] | endoplasmic reticulum protein 29; Does not seem to be a disulfide isomerase. Plays an important role in the processing of secretory proteins within the endoplasmic reticulum (ER), possibly by participating in the folding of proteins in the ER | 0.806 |
| ERO1LB | ERP44 | ENSP00000346635 | ENSP00000262455 | ERO1-like beta (S. cerevisiae); Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly P4HB/PDI isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on P4HB/PDI to transfer oxidizing equivalent. Associates with ERP44 but not with GRP54, demonstrating that it does not oxidize all PDI related proteins and can discriminate between PDI and related proteins. Its reoxidation probably involves electron transfer to molecular oxygen via FAD. Acts independently [...] | endoplasmic reticulum protein 44; Mediates thiol-dependent retention in the early secretory pathway, forming mixed disulfides with substrate proteins through its conserved CRFS motif. Inhibits the calcium channel activity of ITPR1. May have a role in the control of oxidative protein folding in the endoplasmic reticulum. Required to retain ERO1L and ERO1LB in the endoplasmic reticulum | 0.772 |
| ERO1LB | P4HB | ENSP00000346635 | ENSP00000327801 | ERO1-like beta (S. cerevisiae); Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly P4HB/PDI isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on P4HB/PDI to transfer oxidizing equivalent. Associates with ERP44 but not with GRP54, demonstrating that it does not oxidize all PDI related proteins and can discriminate between PDI and related proteins. Its reoxidation probably involves electron transfer to molecular oxygen via FAD. Acts independently [...] | prolyl 4-hydroxylase, beta polypeptide; This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with [...] | 0.994 |
| ERO1LB | PDIA2 | ENSP00000346635 | ENSP00000219406 | ERO1-like beta (S. cerevisiae); Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly P4HB/PDI isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on P4HB/PDI to transfer oxidizing equivalent. Associates with ERP44 but not with GRP54, demonstrating that it does not oxidize all PDI related proteins and can discriminate between PDI and related proteins. Its reoxidation probably involves electron transfer to molecular oxygen via FAD. Acts independently [...] | protein disulfide isomerase family A, member 2; Acts as an intracellular estrogen-binding protein. May be involved in modulating cellular levels and biological functions of estrogens in the pancreas. May act as a chaperone that inhibits aggregation of misfolded proteins | 0.884 |
| ERO1LB | PDIA3 | ENSP00000346635 | ENSP00000300289 | ERO1-like beta (S. cerevisiae); Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly P4HB/PDI isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on P4HB/PDI to transfer oxidizing equivalent. Associates with ERP44 but not with GRP54, demonstrating that it does not oxidize all PDI related proteins and can discriminate between PDI and related proteins. Its reoxidation probably involves electron transfer to molecular oxygen via FAD. Acts independently [...] | protein disulfide isomerase family A, member 3 | 0.897 |
| ERO1LB | PDIA4 | ENSP00000346635 | ENSP00000286091 | ERO1-like beta (S. cerevisiae); Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly P4HB/PDI isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on P4HB/PDI to transfer oxidizing equivalent. Associates with ERP44 but not with GRP54, demonstrating that it does not oxidize all PDI related proteins and can discriminate between PDI and related proteins. Its reoxidation probably involves electron transfer to molecular oxygen via FAD. Acts independently [...] | protein disulfide isomerase family A, member 4 | 0.982 |
| ERO1LB | PDIA6 | ENSP00000346635 | ENSP00000272227 | ERO1-like beta (S. cerevisiae); Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly P4HB/PDI isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on P4HB/PDI to transfer oxidizing equivalent. Associates with ERP44 but not with GRP54, demonstrating that it does not oxidize all PDI related proteins and can discriminate between PDI and related proteins. Its reoxidation probably involves electron transfer to molecular oxygen via FAD. Acts independently [...] | protein disulfide isomerase family A, member 6; May function as a chaperone that inhibits aggregation of misfolded proteins. Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin | 0.935 |
| ERO1LB | TXNDC5 | ENSP00000346635 | ENSP00000369081 | ERO1-like beta (S. cerevisiae); Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly P4HB/PDI isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on P4HB/PDI to transfer oxidizing equivalent. Associates with ERP44 but not with GRP54, demonstrating that it does not oxidize all PDI related proteins and can discriminate between PDI and related proteins. Its reoxidation probably involves electron transfer to molecular oxygen via FAD. Acts independently [...] | thioredoxin domain containing 5 (endoplasmic reticulum); Possesses thioredoxin activity. Has been shown to reduce insulin disulfide bonds. Also complements protein disulfide- isomerase deficiency in yeast (By similarity) | 0.921 |
| ERP29 | DNAJC10 | ENSP00000261735 | ENSP00000264065 | endoplasmic reticulum protein 29; Does not seem to be a disulfide isomerase. Plays an important role in the processing of secretory proteins within the endoplasmic reticulum (ER), possibly by participating in the folding of proteins in the ER | DnaJ (Hsp40) homolog, subfamily C, member 10 | 0.592 |
| ERP29 | ERO1LB | ENSP00000261735 | ENSP00000346635 | endoplasmic reticulum protein 29; Does not seem to be a disulfide isomerase. Plays an important role in the processing of secretory proteins within the endoplasmic reticulum (ER), possibly by participating in the folding of proteins in the ER | ERO1-like beta (S. cerevisiae); Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly P4HB/PDI isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on P4HB/PDI to transfer oxidizing equivalent. Associates with ERP44 but not with GRP54, demonstrating that it does not oxidize all PDI related proteins and can discriminate between PDI and related proteins. Its reoxidation probably involves electron transfer to molecular oxygen via FAD. Acts independently [...] | 0.806 |
| ERP29 | ERP44 | ENSP00000261735 | ENSP00000262455 | endoplasmic reticulum protein 29; Does not seem to be a disulfide isomerase. Plays an important role in the processing of secretory proteins within the endoplasmic reticulum (ER), possibly by participating in the folding of proteins in the ER | endoplasmic reticulum protein 44; Mediates thiol-dependent retention in the early secretory pathway, forming mixed disulfides with substrate proteins through its conserved CRFS motif. Inhibits the calcium channel activity of ITPR1. May have a role in the control of oxidative protein folding in the endoplasmic reticulum. Required to retain ERO1L and ERO1LB in the endoplasmic reticulum | 0.652 |
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