| + |
PAT intramembrane chaperone complex | up-regulates 
|
Protein_maturation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281081 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32814900 |
Here we identify the PAT complex, an abundant obligate heterodimer of the widely conserved ER-resident membrane proteins CCDC47 and Asterix. The PAT complex engages nascent TMDs that contain unshielded hydrophilic side chains within the lipid bilayer, and it disengages concomitant with substrate folding. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Signal peptidase complex, SEC11A variant | up-regulates
|
Protein_maturation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280778 |
|
|
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
|
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 |
| + |
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 |
4.0
Protein_maturation