| + |
MRE11 | up-regulates activity 
binding
|
PIH1D1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265898 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28436950 |
Here we show that MRE11 directly interacts with PIH1D1, a subunit of heat-shock protein 90 cochaperone R2TP complex, which is required for the assembly of large protein complexes, such as RNA polymerase II, small nucleolar ribonucleoproteins and mammalian target of rapamycin complex 1. The MRE11-PIH1D1 interaction is dependent on casein kinase 2 (CK2) phosphorylation of two acidic sequences within the MRE11 C terminus containing serines 558/561 and 688/689. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PIH1D1 | up-regulates quantity by stabilization
binding
|
mTORC1 |
0.344 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265897 |
|
|
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 24036451 |
PIH1D1 interacts with mTOR complex 1 and enhances ribosome RNA transcription.PIH1D1 is important for mTORC1 assembly |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PIH1D1 | form complex 
binding
|
R2TP core co-chaperone |
0.838 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270926 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29662061 |
Here we use cryo-EM and biochemical studies on the human R2TP core (RUVBL1-RUVBL2-RPAP3-PIH1D1) which reveal the distinctive role of RPAP3, distinguishing metazoan R2TP from the smaller yeast equivalent. RPAP3 spans both faces of a single RUVBL ring, providing an extended scaffold that recruits clients and provides a flexible tether for HSP90. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
PIH1D1
- 
- 