node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ERV41 | KAR2 | YML067C | YJL034W | Protein localized to COPII-coated vesicles, forms a complex with Erv46p; involved in the membrane fusion stage of transport; has homology to human ERGIC2 (PTX1) protein; Constituent of COPII-coated endoplasmic reticulum- derived transport vesicles. Required for efficient transport of a subset of secretory proteins to the Golgi. The C-terminal Ile-Leu motif is required for exit from the endoplasmic reticulum. Facilitates retrograde transport from the Golgi to the endoplasmic reticulum | ATPase involved in protein import into the ER, also acts as a chaperone to mediate protein folding in the ER and may play a role in ER export of soluble proteins; regulates the unfolded protein response via interaction with Ire1p; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis | 0.510 |
ERV41 | SPC1 | YML067C | YJR010C-A | Protein localized to COPII-coated vesicles, forms a complex with Erv46p; involved in the membrane fusion stage of transport; has homology to human ERGIC2 (PTX1) protein; Constituent of COPII-coated endoplasmic reticulum- derived transport vesicles. Required for efficient transport of a subset of secretory proteins to the Golgi. The C-terminal Ile-Leu motif is required for exit from the endoplasmic reticulum. Facilitates retrograde transport from the Golgi to the endoplasmic reticulum | Subunit of the signal peptidase complex (SPC), which cleaves the signal sequence from proteins targeted to the endoplasmic reticulum (ER), homolog of the SPC12 subunit of mammalian signal peptidase complex; Nonessential component of the signal peptidase complex (SPC), which catalyzes the cleavage of N-terminal signal sequences of proteins targeted to the endoplasmic reticulum. Signal peptide cleavage occurs during the translocation (cotranslationally or post-translationally) through the translocon pore into the endoplasmic reticulum. SPC3 is not required for signal peptidase activity | 0.971 |
KAR2 | ERV41 | YJL034W | YML067C | ATPase involved in protein import into the ER, also acts as a chaperone to mediate protein folding in the ER and may play a role in ER export of soluble proteins; regulates the unfolded protein response via interaction with Ire1p; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis | Protein localized to COPII-coated vesicles, forms a complex with Erv46p; involved in the membrane fusion stage of transport; has homology to human ERGIC2 (PTX1) protein; Constituent of COPII-coated endoplasmic reticulum- derived transport vesicles. Required for efficient transport of a subset of secretory proteins to the Golgi. The C-terminal Ile-Leu motif is required for exit from the endoplasmic reticulum. Facilitates retrograde transport from the Golgi to the endoplasmic reticulum | 0.510 |
KAR2 | SBH1 | YJL034W | YER087C-B | ATPase involved in protein import into the ER, also acts as a chaperone to mediate protein folding in the ER and may play a role in ER export of soluble proteins; regulates the unfolded protein response via interaction with Ire1p; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis | Beta subunit of the Sec61p ER translocation complex (Sec61p-Sss1p-Sbh1p); involved in protein translocation into the endoplasmic reticulum; interacts with the exocyst complex and also with Rtn1p; homologous to Sbh2p; Part of the Sec61 complex, which is the major component of a channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). The functional states of the translocon complex include co- and post- translational ER import, cotranslational membrane protein integration and retrograde transport of misfolded proteins out of the ER. In [...] | 0.709 |
KAR2 | SBH2 | YJL034W | YER019C-A | ATPase involved in protein import into the ER, also acts as a chaperone to mediate protein folding in the ER and may play a role in ER export of soluble proteins; regulates the unfolded protein response via interaction with Ire1p; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis | Ssh1p-Sss1p-Sbh2p complex component, involved in protein translocation into the endoplasmic reticulum; homologous to Sbh1p; Part of the Ssh1 complex, which probably is the major component of a channel-forming translocon complex that may function exclusively in the cotranslational pathway of protein endoplasmic reticulum (ER) import | 0.691 |
KAR2 | SEC11 | YJL034W | YIR022W | ATPase involved in protein import into the ER, also acts as a chaperone to mediate protein folding in the ER and may play a role in ER export of soluble proteins; regulates the unfolded protein response via interaction with Ire1p; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis | 18kDa catalytic subunit of the Signal Peptidase Complex (SPC; Spc1p, Spc2p, Spc3p, and Sec11p) which cleaves the signal sequence of proteins targeted to the endoplasmic reticulum; Catalytic component of the signal peptidase complex (SPC), which catalyzes the cleavage of N-terminal signal sequences of proteins targeted to the endoplasmic reticulum. Signal peptide cleavage occurs during the translocation (cotranslationally or post-translationally) through the translocon pore into the endoplasmic reticulum (By similarity) | 0.912 |
KAR2 | SEC62 | YJL034W | YPL094C | ATPase involved in protein import into the ER, also acts as a chaperone to mediate protein folding in the ER and may play a role in ER export of soluble proteins; regulates the unfolded protein response via interaction with Ire1p; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis | Essential subunit of Sec63 complex (Sec63p, Sec62p, Sec66p and Sec72p); with Sec61 complex, Kar2p/BiP and Lhs1p forms a channel competent for SRP-dependent and post-translational SRP-independent protein targeting and import into the ER; Acts as component of the Sec62/63 complex which is involved in SRP-independent post-translational translocation across the endoplasmic reticulum (ER) and functions together with the Sec61 complex and KAR2 in a channel-forming translocon complex. In an initial step, the signal sequence seems to bind simultaneously to SEC61 and SEC62. SEC62 and SEC63 are [...] | 0.893 |
KAR2 | SPC1 | YJL034W | YJR010C-A | ATPase involved in protein import into the ER, also acts as a chaperone to mediate protein folding in the ER and may play a role in ER export of soluble proteins; regulates the unfolded protein response via interaction with Ire1p; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis | Subunit of the signal peptidase complex (SPC), which cleaves the signal sequence from proteins targeted to the endoplasmic reticulum (ER), homolog of the SPC12 subunit of mammalian signal peptidase complex; Nonessential component of the signal peptidase complex (SPC), which catalyzes the cleavage of N-terminal signal sequences of proteins targeted to the endoplasmic reticulum. Signal peptide cleavage occurs during the translocation (cotranslationally or post-translationally) through the translocon pore into the endoplasmic reticulum. SPC3 is not required for signal peptidase activity | 0.918 |
KAR2 | SPC2 | YJL034W | YML055W | ATPase involved in protein import into the ER, also acts as a chaperone to mediate protein folding in the ER and may play a role in ER export of soluble proteins; regulates the unfolded protein response via interaction with Ire1p; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis | Subunit of signal peptidase complex (Spc1p, Spc2p, Spc3p, Sec11p), which catalyzes cleavage of N-terminal signal sequences of proteins targeted to the secretory pathway; homologous to mammalian SPC25; Nonessential component of the signal peptidase complex (SPC), which catalyzes the cleavage of N-terminal signal sequences of proteins targeted to the endoplasmic reticulum. Signal peptide cleavage occurs during the translocation (cotranslationally or post-translationally) through the translocon pore into the endoplasmic reticulum. SPC2 enhances the enzymatic activity of SPC and facilitate [...] | 0.959 |
KAR2 | SPC3 | YJL034W | YLR066W | ATPase involved in protein import into the ER, also acts as a chaperone to mediate protein folding in the ER and may play a role in ER export of soluble proteins; regulates the unfolded protein response via interaction with Ire1p; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis | Subunit of signal peptidase complex (Spc1p, Spc2p, Spc3p, Sec11p), which catalyzes cleavage of N-terminal signal sequences of proteins targeted to the secretory pathway; homologous to mammalian SPC22/23; Component of the signal peptidase complex (SPC), which catalyzes the cleavage of N-terminal signal sequences of proteins targeted to the endoplasmic reticulum. Signal peptide cleavage occurs during the translocation (cotranslationally or post- translationally) through the translocon pore into the endoplasmic reticulum. SPC3 is required for signal peptidase activity and is essential for [...] | 0.811 |
OST2 | SBH1 | YOR103C | YER087C-B | Epsilon subunit of the oligosaccharyltransferase complex of the ER lumen, which catalyzes asparagine-linked glycosylation of newly synthesized proteins; Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation a [...] | Beta subunit of the Sec61p ER translocation complex (Sec61p-Sss1p-Sbh1p); involved in protein translocation into the endoplasmic reticulum; interacts with the exocyst complex and also with Rtn1p; homologous to Sbh2p; Part of the Sec61 complex, which is the major component of a channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). The functional states of the translocon complex include co- and post- translational ER import, cotranslational membrane protein integration and retrograde transport of misfolded proteins out of the ER. In [...] | 0.999 |
OST2 | SBH2 | YOR103C | YER019C-A | Epsilon subunit of the oligosaccharyltransferase complex of the ER lumen, which catalyzes asparagine-linked glycosylation of newly synthesized proteins; Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation a [...] | Ssh1p-Sss1p-Sbh2p complex component, involved in protein translocation into the endoplasmic reticulum; homologous to Sbh1p; Part of the Ssh1 complex, which probably is the major component of a channel-forming translocon complex that may function exclusively in the cotranslational pathway of protein endoplasmic reticulum (ER) import | 0.999 |
OST2 | SEC11 | YOR103C | YIR022W | Epsilon subunit of the oligosaccharyltransferase complex of the ER lumen, which catalyzes asparagine-linked glycosylation of newly synthesized proteins; Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation a [...] | 18kDa catalytic subunit of the Signal Peptidase Complex (SPC; Spc1p, Spc2p, Spc3p, and Sec11p) which cleaves the signal sequence of proteins targeted to the endoplasmic reticulum; Catalytic component of the signal peptidase complex (SPC), which catalyzes the cleavage of N-terminal signal sequences of proteins targeted to the endoplasmic reticulum. Signal peptide cleavage occurs during the translocation (cotranslationally or post-translationally) through the translocon pore into the endoplasmic reticulum (By similarity) | 0.407 |
OST2 | SEC62 | YOR103C | YPL094C | Epsilon subunit of the oligosaccharyltransferase complex of the ER lumen, which catalyzes asparagine-linked glycosylation of newly synthesized proteins; Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation a [...] | Essential subunit of Sec63 complex (Sec63p, Sec62p, Sec66p and Sec72p); with Sec61 complex, Kar2p/BiP and Lhs1p forms a channel competent for SRP-dependent and post-translational SRP-independent protein targeting and import into the ER; Acts as component of the Sec62/63 complex which is involved in SRP-independent post-translational translocation across the endoplasmic reticulum (ER) and functions together with the Sec61 complex and KAR2 in a channel-forming translocon complex. In an initial step, the signal sequence seems to bind simultaneously to SEC61 and SEC62. SEC62 and SEC63 are [...] | 0.599 |
OST2 | SPC1 | YOR103C | YJR010C-A | Epsilon subunit of the oligosaccharyltransferase complex of the ER lumen, which catalyzes asparagine-linked glycosylation of newly synthesized proteins; Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation a [...] | Subunit of the signal peptidase complex (SPC), which cleaves the signal sequence from proteins targeted to the endoplasmic reticulum (ER), homolog of the SPC12 subunit of mammalian signal peptidase complex; Nonessential component of the signal peptidase complex (SPC), which catalyzes the cleavage of N-terminal signal sequences of proteins targeted to the endoplasmic reticulum. Signal peptide cleavage occurs during the translocation (cotranslationally or post-translationally) through the translocon pore into the endoplasmic reticulum. SPC3 is not required for signal peptidase activity | 0.936 |
OST2 | SPC3 | YOR103C | YLR066W | Epsilon subunit of the oligosaccharyltransferase complex of the ER lumen, which catalyzes asparagine-linked glycosylation of newly synthesized proteins; Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation a [...] | Subunit of signal peptidase complex (Spc1p, Spc2p, Spc3p, Sec11p), which catalyzes cleavage of N-terminal signal sequences of proteins targeted to the secretory pathway; homologous to mammalian SPC22/23; Component of the signal peptidase complex (SPC), which catalyzes the cleavage of N-terminal signal sequences of proteins targeted to the endoplasmic reticulum. Signal peptide cleavage occurs during the translocation (cotranslationally or post- translationally) through the translocon pore into the endoplasmic reticulum. SPC3 is required for signal peptidase activity and is essential for [...] | 0.672 |
SBH1 | KAR2 | YER087C-B | YJL034W | Beta subunit of the Sec61p ER translocation complex (Sec61p-Sss1p-Sbh1p); involved in protein translocation into the endoplasmic reticulum; interacts with the exocyst complex and also with Rtn1p; homologous to Sbh2p; Part of the Sec61 complex, which is the major component of a channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). The functional states of the translocon complex include co- and post- translational ER import, cotranslational membrane protein integration and retrograde transport of misfolded proteins out of the ER. In [...] | ATPase involved in protein import into the ER, also acts as a chaperone to mediate protein folding in the ER and may play a role in ER export of soluble proteins; regulates the unfolded protein response via interaction with Ire1p; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis | 0.709 |
SBH1 | OST2 | YER087C-B | YOR103C | Beta subunit of the Sec61p ER translocation complex (Sec61p-Sss1p-Sbh1p); involved in protein translocation into the endoplasmic reticulum; interacts with the exocyst complex and also with Rtn1p; homologous to Sbh2p; Part of the Sec61 complex, which is the major component of a channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). The functional states of the translocon complex include co- and post- translational ER import, cotranslational membrane protein integration and retrograde transport of misfolded proteins out of the ER. In [...] | Epsilon subunit of the oligosaccharyltransferase complex of the ER lumen, which catalyzes asparagine-linked glycosylation of newly synthesized proteins; Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation a [...] | 0.999 |
SBH1 | SBH2 | YER087C-B | YER019C-A | Beta subunit of the Sec61p ER translocation complex (Sec61p-Sss1p-Sbh1p); involved in protein translocation into the endoplasmic reticulum; interacts with the exocyst complex and also with Rtn1p; homologous to Sbh2p; Part of the Sec61 complex, which is the major component of a channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). The functional states of the translocon complex include co- and post- translational ER import, cotranslational membrane protein integration and retrograde transport of misfolded proteins out of the ER. In [...] | Ssh1p-Sss1p-Sbh2p complex component, involved in protein translocation into the endoplasmic reticulum; homologous to Sbh1p; Part of the Ssh1 complex, which probably is the major component of a channel-forming translocon complex that may function exclusively in the cotranslational pathway of protein endoplasmic reticulum (ER) import | 0.999 |
SBH1 | SEC11 | YER087C-B | YIR022W | Beta subunit of the Sec61p ER translocation complex (Sec61p-Sss1p-Sbh1p); involved in protein translocation into the endoplasmic reticulum; interacts with the exocyst complex and also with Rtn1p; homologous to Sbh2p; Part of the Sec61 complex, which is the major component of a channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). The functional states of the translocon complex include co- and post- translational ER import, cotranslational membrane protein integration and retrograde transport of misfolded proteins out of the ER. In [...] | 18kDa catalytic subunit of the Signal Peptidase Complex (SPC; Spc1p, Spc2p, Spc3p, and Sec11p) which cleaves the signal sequence of proteins targeted to the endoplasmic reticulum; Catalytic component of the signal peptidase complex (SPC), which catalyzes the cleavage of N-terminal signal sequences of proteins targeted to the endoplasmic reticulum. Signal peptide cleavage occurs during the translocation (cotranslationally or post-translationally) through the translocon pore into the endoplasmic reticulum (By similarity) | 0.999 |