| + |
SPCS3 | form complex 
binding
|
Signal peptidase complex, SEC11C variant |
0.735 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280770 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 34388369 |
The human SPC comprises the accessory proteins SPC12 (SPCS1), SPC22/23 (SPCS3), and SPC25 (SPCS2) and the two proteolytic subunits SEC11A (SPC18) and SEC11C (SPC21). The signal peptidase complex (SPC) is an essential membrane complex in the endoplasmic reticulum (ER), where it removes signal peptides (SPs) from a large variety of secretory pre-proteins with exquisite specificity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SPCS2 | form complex
binding
|
Signal peptidase complex, SEC11C variant |
0.815 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280771 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 34388369 |
The human SPC comprises the accessory proteins SPC12 (SPCS1), SPC22/23 (SPCS3), and SPC25 (SPCS2) and the two proteolytic subunits SEC11A (SPC18) and SEC11C (SPC21). The signal peptidase complex (SPC) is an essential membrane complex in the endoplasmic reticulum (ER), where it removes signal peptides (SPs) from a large variety of secretory pre-proteins with exquisite specificity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SEC11C | form complex
binding
|
Signal peptidase complex, SEC11C variant |
0.826 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280772 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 34388369 |
The human SPC comprises the accessory proteins SPC12 (SPCS1), SPC22/23 (SPCS3), and SPC25 (SPCS2) and the two proteolytic subunits SEC11A (SPC18) and SEC11C (SPC21). The signal peptidase complex (SPC) is an essential membrane complex in the endoplasmic reticulum (ER), where it removes signal peptides (SPs) from a large variety of secretory pre-proteins with exquisite specificity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SPCS1 | form complex
binding
|
Signal peptidase complex, SEC11C variant |
0.846 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280773 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 34388369 |
The human SPC comprises the accessory proteins SPC12 (SPCS1), SPC22/23 (SPCS3), and SPC25 (SPCS2) and the two proteolytic subunits SEC11A (SPC18) and SEC11C (SPC21). The signal peptidase complex (SPC) is an essential membrane complex in the endoplasmic reticulum (ER), where it removes signal peptides (SPs) from a large variety of secretory pre-proteins with exquisite specificity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Signal peptidase complex, SEC11C variant | up-regulates 
|
Protein_maturation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280779 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 34388369 |
Nascent SPs emerge from the ribosome and target the ribosome-nascent-chain complex to the ER membrane, where it is inserted into the protein-conducting channel Sec61 (Gemmer and Förster, 2020). For many proteins (approximated to exceed 3,000 different physiological protein substrates in humans (Uhlén et al., 2015)), the signal peptidase complex (SPC) cleaves off the SPs from their non-functional pre-forms. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Signal peptidase complex, SEC11C variant | up-regulates 
|
SEC61 complex |
0.505 |
| 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 |
4.0
Signal peptidase complex, SEC11C variant
CPX-7205