node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
DERL2 | EDEM3 | ENSP00000158771 | ENSP00000318147 | 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 the degradation substrate. In contrast to DERL1, it is not involved in the degradation of MHC class I heavy chains following infection by cytomegaloviruses. May play a role in cell proliferation | ER degradation enhancer, mannosidase alpha-like 3; Involved in endoplasmic reticulum-associated degradation (ERAD). Accelerates the glycoprotein ERAD by proteasomes. This process depends on mannose-trimming from the N-glycans. Seems to have alpha 1,2-mannosidase activity (By similarity) | 0.653 |
DERL2 | ERLEC1 | ENSP00000158771 | ENSP00000185150 | 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 the degradation substrate. In contrast to DERL1, it is not involved in the degradation of MHC class I heavy chains following infection by cytomegaloviruses. May play a role in cell proliferation | endoplasmic reticulum lectin 1; Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins | 0.758 |
DERL2 | OS9 | ENSP00000158771 | ENSP00000318165 | 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 the degradation substrate. In contrast to DERL1, it is not involved in the degradation of MHC class I heavy chains following infection by cytomegaloviruses. May play a role in cell proliferation | osteosarcoma amplified 9, endoplasmic reticulum lectin | 0.995 |
DERL2 | SEL1L | ENSP00000158771 | ENSP00000337053 | 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 the degradation substrate. In contrast to DERL1, it is not involved in the degradation of MHC class I heavy chains following infection by cytomegaloviruses. May play a role in cell proliferation | sel-1 suppressor of lin-12-like (C. elegans); May play a role in Notch signaling (By similarity). May be involved in the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins | 0.999 |
DERL2 | SEL1L2 | ENSP00000158771 | ENSP00000284951 | 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 the degradation substrate. In contrast to DERL1, it is not involved in the degradation of MHC class I heavy chains following infection by cytomegaloviruses. May play a role in cell proliferation | sel-1 suppressor of lin-12-like 2 (C. elegans) | 0.608 |
DERL2 | SYVN1 | ENSP00000158771 | ENSP00000366395 | 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 the degradation substrate. In contrast to DERL1, it is not involved in the degradation of MHC class I heavy chains following infection by cytomegaloviruses. May play a role in cell proliferation | synovial apoptosis inhibitor 1, synoviolin; Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC7 E2 ligase and transfers it to substrates, promoting their degradation. Component of the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Also promotes the degradation of normal but naturally short-lived proteins such as SGK. Protects cells from ER stress-induced apoptosis. Protects neurons f [...] | 0.998 |
EDEM3 | DERL2 | ENSP00000318147 | ENSP00000158771 | ER degradation enhancer, mannosidase alpha-like 3; Involved in endoplasmic reticulum-associated degradation (ERAD). Accelerates the glycoprotein ERAD by proteasomes. This process depends on mannose-trimming from the N-glycans. Seems to have alpha 1,2-mannosidase activity (By similarity) | 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 the degradation substrate. In contrast to DERL1, it is not involved in the degradation of MHC class I heavy chains following infection by cytomegaloviruses. May play a role in cell proliferation | 0.653 |
EDEM3 | ERLEC1 | ENSP00000318147 | ENSP00000185150 | ER degradation enhancer, mannosidase alpha-like 3; Involved in endoplasmic reticulum-associated degradation (ERAD). Accelerates the glycoprotein ERAD by proteasomes. This process depends on mannose-trimming from the N-glycans. Seems to have alpha 1,2-mannosidase activity (By similarity) | endoplasmic reticulum lectin 1; Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins | 0.838 |
EDEM3 | MAN1B1 | ENSP00000318147 | ENSP00000360645 | ER degradation enhancer, mannosidase alpha-like 3; Involved in endoplasmic reticulum-associated degradation (ERAD). Accelerates the glycoprotein ERAD by proteasomes. This process depends on mannose-trimming from the N-glycans. Seems to have alpha 1,2-mannosidase activity (By similarity) | mannosidase, alpha, class 1B, member 1; Involved in glycoprotein quality control targeting of misfolded glycoproteins for degradation. It primarily trims a single alpha-1,2-linked mannose residue from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2), but at high enzyme concentrations, as found in the ER quality control compartment (ERQC), it further trims the carbohydrates to Man(5-6)GlcNAc(2) | 0.920 |
EDEM3 | MAN2A1 | ENSP00000318147 | ENSP00000261483 | ER degradation enhancer, mannosidase alpha-like 3; Involved in endoplasmic reticulum-associated degradation (ERAD). Accelerates the glycoprotein ERAD by proteasomes. This process depends on mannose-trimming from the N-glycans. Seems to have alpha 1,2-mannosidase activity (By similarity) | mannosidase, alpha, class 2A, member 1; Catalyzes the first committed step in the biosynthesis of complex N-glycans. It controls conversion of high mannose to complex N-glycans; the final hydrolytic step in the N-glycan maturation pathway | 0.769 |
EDEM3 | OS9 | ENSP00000318147 | ENSP00000318165 | ER degradation enhancer, mannosidase alpha-like 3; Involved in endoplasmic reticulum-associated degradation (ERAD). Accelerates the glycoprotein ERAD by proteasomes. This process depends on mannose-trimming from the N-glycans. Seems to have alpha 1,2-mannosidase activity (By similarity) | osteosarcoma amplified 9, endoplasmic reticulum lectin | 0.868 |
EDEM3 | PDIA3 | ENSP00000318147 | ENSP00000300289 | ER degradation enhancer, mannosidase alpha-like 3; Involved in endoplasmic reticulum-associated degradation (ERAD). Accelerates the glycoprotein ERAD by proteasomes. This process depends on mannose-trimming from the N-glycans. Seems to have alpha 1,2-mannosidase activity (By similarity) | protein disulfide isomerase family A, member 3 | 0.667 |
EDEM3 | SEL1L | ENSP00000318147 | ENSP00000337053 | ER degradation enhancer, mannosidase alpha-like 3; Involved in endoplasmic reticulum-associated degradation (ERAD). Accelerates the glycoprotein ERAD by proteasomes. This process depends on mannose-trimming from the N-glycans. Seems to have alpha 1,2-mannosidase activity (By similarity) | sel-1 suppressor of lin-12-like (C. elegans); May play a role in Notch signaling (By similarity). May be involved in the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins | 0.968 |
EDEM3 | SEL1L2 | ENSP00000318147 | ENSP00000284951 | ER degradation enhancer, mannosidase alpha-like 3; Involved in endoplasmic reticulum-associated degradation (ERAD). Accelerates the glycoprotein ERAD by proteasomes. This process depends on mannose-trimming from the N-glycans. Seems to have alpha 1,2-mannosidase activity (By similarity) | sel-1 suppressor of lin-12-like 2 (C. elegans) | 0.705 |
EDEM3 | SYVN1 | ENSP00000318147 | ENSP00000366395 | ER degradation enhancer, mannosidase alpha-like 3; Involved in endoplasmic reticulum-associated degradation (ERAD). Accelerates the glycoprotein ERAD by proteasomes. This process depends on mannose-trimming from the N-glycans. Seems to have alpha 1,2-mannosidase activity (By similarity) | synovial apoptosis inhibitor 1, synoviolin; Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC7 E2 ligase and transfers it to substrates, promoting their degradation. Component of the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Also promotes the degradation of normal but naturally short-lived proteins such as SGK. Protects cells from ER stress-induced apoptosis. Protects neurons f [...] | 0.729 |
EDEM3 | UGGT1 | ENSP00000318147 | ENSP00000259253 | ER degradation enhancer, mannosidase alpha-like 3; Involved in endoplasmic reticulum-associated degradation (ERAD). Accelerates the glycoprotein ERAD by proteasomes. This process depends on mannose-trimming from the N-glycans. Seems to have alpha 1,2-mannosidase activity (By similarity) | UDP-glucose glycoprotein glucosyltransferase 1; Recognizes glycoproteins with minor folding defects. Reglucosylates single N-glycans near the misfolded part of the protein, thus providing quality control for protein folding in the endoplasmic reticulum. Reglucosylated proteins are recognized by calreticulin for recycling to the endoplasmic reticulum and refolding or degradation | 0.650 |
ERLEC1 | DERL2 | ENSP00000185150 | ENSP00000158771 | endoplasmic reticulum lectin 1; Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins | 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 the degradation substrate. In contrast to DERL1, it is not involved in the degradation of MHC class I heavy chains following infection by cytomegaloviruses. May play a role in cell proliferation | 0.758 |
ERLEC1 | EDEM3 | ENSP00000185150 | ENSP00000318147 | endoplasmic reticulum lectin 1; Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins | ER degradation enhancer, mannosidase alpha-like 3; Involved in endoplasmic reticulum-associated degradation (ERAD). Accelerates the glycoprotein ERAD by proteasomes. This process depends on mannose-trimming from the N-glycans. Seems to have alpha 1,2-mannosidase activity (By similarity) | 0.838 |
ERLEC1 | MAN1B1 | ENSP00000185150 | ENSP00000360645 | endoplasmic reticulum lectin 1; Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins | mannosidase, alpha, class 1B, member 1; Involved in glycoprotein quality control targeting of misfolded glycoproteins for degradation. It primarily trims a single alpha-1,2-linked mannose residue from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2), but at high enzyme concentrations, as found in the ER quality control compartment (ERQC), it further trims the carbohydrates to Man(5-6)GlcNAc(2) | 0.461 |
ERLEC1 | OS9 | ENSP00000185150 | ENSP00000318165 | endoplasmic reticulum lectin 1; Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins | osteosarcoma amplified 9, endoplasmic reticulum lectin | 0.709 |