| + |
SEC61A2 | form complex 
binding
|
SEC61 complex |
0.654 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267728 |
|
|
in vitro |
|
| pmid |
sentence |
| 33925740 |
The heterotrimeric Sec61 complex of the ER membrane represents the major entry point for precursor polypeptides into the membrane or lumen of the ER |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
SEC61 complex | up-regulates activity 
binding
|
SEC63 |
0.891 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265274 |
|
|
|
|
| pmid |
sentence |
| 33925740 |
This is where allosteric effectors of the Sec61 complex (BiP together with Sec62/Sec63 complex or TRAP complex) (Figure 2 and Figure 5) and auxiliary membrane protein insertases (EMC and TMCO1 complex) join the game |
|
| Publications: |
1 |
| + |
Signal peptidase complex, SEC11A variant | up-regulates
|
SEC61 complex |
0.499 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280780 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9585408 |
Using chemical cross-linking we show that Sec61beta not only interacts with subunits of the Sec61 complex but also with the 25-kD subunit of the signal peptidase complex (SPC25), thus demonstrating for the first time a tight interaction between the SPC and the Sec61 complex. Interestingly, the cross-links between Sec61beta and SPC25 and between Sec61beta and Sec61alpha depend on the presence of membrane-bound ribosomes, suggesting that these interactions are induced when translocation is initiated. We propose that the SPC is transiently recruited to the translocation site, thus enhancing its activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Signal peptidase complex, SEC11C variant | up-regulates
|
SEC61 complex |
0.507 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280781 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9585408 |
Using chemical cross-linking we show that Sec61beta not only interacts with subunits of the Sec61 complex but also with the 25-kD subunit of the signal peptidase complex (SPC25), thus demonstrating for the first time a tight interaction between the SPC and the Sec61 complex. Interestingly, the cross-links between Sec61beta and SPC25 and between Sec61beta and Sec61alpha depend on the presence of membrane-bound ribosomes, suggesting that these interactions are induced when translocation is initiated. We propose that the SPC is transiently recruited to the translocation site, thus enhancing its activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SEC61 complex | up-regulates 
|
Protein_maturation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280795 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 35940906 |
The endoplasmic reticulum (ER) is a major site for protein synthesis, folding, and maturation in eukaryotic cells, responsible for production of secretory proteins and most integral membrane proteins. The universally conserved protein-conducting channel Sec61 complex mediates core steps in these processes by translocating hydrophilic polypeptide segments of client proteins across the ER membrane and integrating hydrophobic transmembrane segments into the membrane. The Sec61 complex associates with several other molecular machines and enzymes to enable substrate engagement with the channel and coordination of protein translocation with translation, protein folding, and/or post-translational modifications. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BOS complex, NOMO1 variant | up-regulates quantity by stabilization
binding
|
SEC61 complex |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280796 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 38896445 |
The protein translocon at the endoplasmic reticulum comprises the Sec61 translocation channel and numerous accessory factors that collectively facilitate the biogenesis of secretory and membrane proteins. The PAT, GEL, and BOS complexes are recruited to the ribosome-Sec61 complex at a later stage of multipass biogenesis to form the multipass translocon (MPT). The function of the BOS complex is unclear, but its contacts with Sec61 and the ribosome may facilitate multipass translocon (MPT) assembly or stability |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BOS complex, NOMO3 variant | up-regulates quantity by stabilization
binding
|
SEC61 complex |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280797 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 38896445 |
The protein translocon at the endoplasmic reticulum comprises the Sec61 translocation channel and numerous accessory factors that collectively facilitate the biogenesis of secretory and membrane proteins. The PAT, GEL, and BOS complexes are recruited to the ribosome-Sec61 complex at a later stage of multipass biogenesis to form the multipass translocon (MPT). The function of the BOS complex is unclear, but its contacts with Sec61 and the ribosome may facilitate multipass translocon (MPT) assembly or stability |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BOS complex, NOMO2 variant | up-regulates quantity by stabilization
binding
|
SEC61 complex |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280798 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 38896445 |
The protein translocon at the endoplasmic reticulum comprises the Sec61 translocation channel and numerous accessory factors that collectively facilitate the biogenesis of secretory and membrane proteins. The PAT, GEL, and BOS complexes are recruited to the ribosome-Sec61 complex at a later stage of multipass biogenesis to form the multipass translocon (MPT). The function of the BOS complex is unclear, but its contacts with Sec61 and the ribosome may facilitate multipass translocon (MPT) assembly or stability |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TRAP complex | up-regulates quantity by stabilization
binding
|
SEC61 complex |
0.525 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280799 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28218252 |
In eukaryotic cells, one-third of all proteins must be transported across or inserted into the endoplasmic reticulum (ER) membrane by the ER protein translocon. The translocon-associated protein (TRAP) complex is an integral component of the translocon, assisting the Sec61 protein-conducting channel by regulating signal sequence and transmembrane helix insertion in a substrate-dependent manner. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SEC61 complex | up-regulates quantity
relocalization
|
calcium(2+) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265284 |
|
|
|
|
| pmid |
sentence |
| 33925740 |
The Sec61 complex in the ER membrane represents the major entry point for precursor polypeptides into the membrane or lumen of the ER and provides a conduit for Ca2+ ions from the ER lumen to the cytosol. |
|
| Publications: |
1 |
| + |
SEC61G | form complex
binding
|
SEC61 complex |
0.891 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265278 |
|
|
in vitro |
|
| pmid |
sentence |
| 33925740 |
The heterotrimeric Sec61 complex of the ER membrane represents the major entry point for precursor polypeptides into the membrane or lumen of the ER |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
SEC61B | form complex
binding
|
SEC61 complex |
0.908 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265277 |
|
|
in vitro |
|
| pmid |
sentence |
| 33925740 |
The heterotrimeric Sec61 complex of the ER membrane represents the major entry point for precursor polypeptides into the membrane or lumen of the ER |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
SEC61 complex | up-regulates activity
binding
|
SEC62 |
0.749 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265275 |
|
|
|
|
| pmid |
sentence |
| 33925740 |
This is where allosteric effectors of the Sec61 complex (BiP together with Sec62/Sec63 complex or TRAP complex) (Figure 2 and Figure 5) and auxiliary membrane protein insertases (EMC and TMCO1 complex) join the game |
|
| Publications: |
1 |
| + |
SEC61A1 | form complex
binding
|
SEC61 complex |
0.765 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265279 |
|
|
in vitro |
|
| pmid |
sentence |
| 33925740 |
The heterotrimeric Sec61 complex of the ER membrane represents the major entry point for precursor polypeptides into the membrane or lumen of the ER |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
SEC61 complex | up-regulates activity
binding
|
HSPA5 |
0.452 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265276 |
|
|
|
|
| pmid |
sentence |
| 33925740 |
This is where allosteric effectors of the Sec61 complex (BiP together with Sec62/Sec63 complex or TRAP complex) (Figure 2 and Figure 5) and auxiliary membrane protein insertases (EMC and TMCO1 complex) join the game |
|
| Publications: |
1 |
4.0
SEC61 complex