| + |
HSPA14 | form complex
binding
|
Ribosome-associated complex |
0.798 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281107 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16002468 |
The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DNAJC2 | form complex
binding
|
Ribosome-associated complex |
0.798 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281108 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16002468 |
The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex. Here, we report that MPP11 is localized to the cytosol and associates with ribosomes. Purification of MPP11 revealed that it forms a stable complex with Hsp70L1, a distantly related homolog of Ssz1p. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Ribosome-associated complex | up-regulates activity
binding
|
80S_cytosolic_ribosome |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281109 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16002468 |
The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex. Here, we report that MPP11 is localized to the cytosol and associates with ribosomes. Purification of MPP11 revealed that it forms a stable complex with Hsp70L1, a distantly related homolog of Ssz1p. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |