| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| DENND4B | ENSPPYP00000008352 | ENSPPYP00000000930 | ENSPPYP00000008352 | DENND4B isoform 2. | annotation not available | 0.691 |
| DENND4B | TMEM129 | ENSPPYP00000000930 | ENSPPYP00000016237 | DENND4B isoform 2. | Transmembrane protein 129. | 0.684 |
| DERL1 | DERL2 | ENSPPYP00000021151 | ENSPPYP00000008861 | Derlin-1; Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. May act by forming a channel that allows the retrotranslocation of misfolded proteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and the misfolded protein. Also involved in endoplasmic reticulum stress-induced pre- emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for pro [...] | Derlin-2; Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal glycoproteins, but not that of misfolded nonglycoproteins. May act by forming a channel that allows the retrotranslocation of misfolded glycoproteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and misfolded glycoproteins. May also be involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the [...] | 0.999 |
| DERL1 | SEL1L | ENSPPYP00000021151 | ENSPPYP00000006873 | Derlin-1; Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. May act by forming a channel that allows the retrotranslocation of misfolded proteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and the misfolded protein. Also involved in endoplasmic reticulum stress-induced pre- emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for pro [...] | SEL1L isoform 1. | 0.987 |
| DERL1 | TMEM129 | ENSPPYP00000021151 | ENSPPYP00000016237 | Derlin-1; Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. May act by forming a channel that allows the retrotranslocation of misfolded proteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and the misfolded protein. Also involved in endoplasmic reticulum stress-induced pre- emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for pro [...] | Transmembrane protein 129. | 0.916 |
| DERL1 | UBE2J2 | ENSPPYP00000021151 | ENSPPYP00000002333 | Derlin-1; Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. May act by forming a channel that allows the retrotranslocation of misfolded proteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and the misfolded protein. Also involved in endoplasmic reticulum stress-induced pre- emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for pro [...] | Ubiquitin conjugating enzyme E2 J2. | 0.633 |
| DERL1 | VCP | ENSPPYP00000021151 | ENSPPYP00000021408 | Derlin-1; Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. May act by forming a channel that allows the retrotranslocation of misfolded proteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and the misfolded protein. Also involved in endoplasmic reticulum stress-induced pre- emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for pro [...] | Transitional endoplasmic reticulum ATPase isoform X1. | 0.993 |
| DERL2 | DERL1 | ENSPPYP00000008861 | ENSPPYP00000021151 | Derlin-2; Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal glycoproteins, but not that of misfolded nonglycoproteins. May act by forming a channel that allows the retrotranslocation of misfolded glycoproteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and misfolded glycoproteins. May also be involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the [...] | Derlin-1; Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. May act by forming a channel that allows the retrotranslocation of misfolded proteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and the misfolded protein. Also involved in endoplasmic reticulum stress-induced pre- emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for pro [...] | 0.999 |
| DERL2 | SEL1L | ENSPPYP00000008861 | ENSPPYP00000006873 | Derlin-2; Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal glycoproteins, but not that of misfolded nonglycoproteins. May act by forming a channel that allows the retrotranslocation of misfolded glycoproteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and misfolded glycoproteins. May also be involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the [...] | SEL1L isoform 1. | 0.998 |
| DERL2 | TMEM129 | ENSPPYP00000008861 | ENSPPYP00000016237 | Derlin-2; Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal glycoproteins, but not that of misfolded nonglycoproteins. May act by forming a channel that allows the retrotranslocation of misfolded glycoproteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and misfolded glycoproteins. May also be involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the [...] | Transmembrane protein 129. | 0.619 |
| DERL2 | UBE2J2 | ENSPPYP00000008861 | ENSPPYP00000002333 | Derlin-2; Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal glycoproteins, but not that of misfolded nonglycoproteins. May act by forming a channel that allows the retrotranslocation of misfolded glycoproteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and misfolded glycoproteins. May also be involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the [...] | Ubiquitin conjugating enzyme E2 J2. | 0.610 |
| DERL2 | VCP | ENSPPYP00000008861 | ENSPPYP00000021408 | Derlin-2; Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal glycoproteins, but not that of misfolded nonglycoproteins. May act by forming a channel that allows the retrotranslocation of misfolded glycoproteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and misfolded glycoproteins. May also be involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the [...] | Transitional endoplasmic reticulum ATPase isoform X1. | 0.984 |
| ENSPPYP00000008352 | DENND4B | ENSPPYP00000008352 | ENSPPYP00000000930 | annotation not available | DENND4B isoform 2. | 0.691 |
| ENSPPYP00000008352 | TMEM129 | ENSPPYP00000008352 | ENSPPYP00000016237 | annotation not available | Transmembrane protein 129. | 0.684 |
| FAM53A | SLBP | ENSPPYP00000016235 | ENSPPYP00000016236 | Family with sequence similarity 53 member A. | Stem-loop binding protein. | 0.485 |
| FAM53A | TMEM129 | ENSPPYP00000016235 | ENSPPYP00000016237 | Family with sequence similarity 53 member A. | Transmembrane protein 129. | 0.569 |
| RNFT2 | TMEM129 | ENSPPYP00000005700 | ENSPPYP00000016237 | RING finger and transmembrane domain-containing protein 2. | Transmembrane protein 129. | 0.568 |
| SEL1L | DERL1 | ENSPPYP00000006873 | ENSPPYP00000021151 | SEL1L isoform 1. | Derlin-1; Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. May act by forming a channel that allows the retrotranslocation of misfolded proteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and the misfolded protein. Also involved in endoplasmic reticulum stress-induced pre- emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for pro [...] | 0.987 |
| SEL1L | DERL2 | ENSPPYP00000006873 | ENSPPYP00000008861 | SEL1L isoform 1. | Derlin-2; Functional component of endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal glycoproteins, but not that of misfolded nonglycoproteins. May act by forming a channel that allows the retrotranslocation of misfolded glycoproteins into the cytosol where they are ubiquitinated and degraded by the proteasome. May mediate the interaction between VCP and misfolded glycoproteins. May also be involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the [...] | 0.998 |
| SEL1L | TMEM129 | ENSPPYP00000006873 | ENSPPYP00000016237 | SEL1L isoform 1. | Transmembrane protein 129. | 0.584 |
