| + |
RUVBL2 | form complex 
binding
|
R2SP co-chaperone |
0.51 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270940 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29844425 |
Systematic interaction analyses show that one RPAP3-like protein, SPAG1, binds PIH1D2 and RUVBL1/2 to form an R2TP-like complex termed R2SP. This co-chaperone is enriched in testis and among 68 of the potential clients identified, some are expressed in testis and others are ubiquitous. One substrate is liprin-α2, which organizes large signaling complexes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
R2SP co-chaperone | up-regulates 
|
Chaperone-mediated protein folding |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270941 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29844425 |
Systematic interaction analyses show that one RPAP3-like protein, SPAG1, binds PIH1D2 and RUVBL1/2 to form an R2TP-like complex termed R2SP. This co-chaperone is enriched in testis and among 68 of the potential clients identified, some are expressed in testis and others are ubiquitous. One substrate is liprin-α2, which organizes large signaling complexes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PIH1D2 | form complex
binding
|
R2SP co-chaperone |
0.48 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270937 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29844425 |
Systematic interaction analyses show that one RPAP3-like protein, SPAG1, binds PIH1D2 and RUVBL1/2 to form an R2TP-like complex termed R2SP. This co-chaperone is enriched in testis and among 68 of the potential clients identified, some are expressed in testis and others are ubiquitous. One substrate is liprin-α2, which organizes large signaling complexes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RUVBL1 | form complex
binding
|
R2SP co-chaperone |
0.517 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270939 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29844425 |
Systematic interaction analyses show that one RPAP3-like protein, SPAG1, binds PIH1D2 and RUVBL1/2 to form an R2TP-like complex termed R2SP. This co-chaperone is enriched in testis and among 68 of the potential clients identified, some are expressed in testis and others are ubiquitous. One substrate is liprin-α2, which organizes large signaling complexes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
R2SP co-chaperone | up-regulates quantity by stabilization 
binding
|
PPFIA2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270942 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29844425 |
Systematic interaction analyses show that one RPAP3-like protein, SPAG1, binds PIH1D2 and RUVBL1/2 to form an R2TP-like complex termed R2SP. This co-chaperone is enriched in testis and among 68 of the potential clients identified, some are expressed in testis and others are ubiquitous. One substrate is liprin-α2, which organizes large signaling complexes. Remarkably, R2SP is required for liprin-α2 expression and for the assembly of liprin-α2 complexes, indicating that R2SP functions in quaternary protein folding. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SPAG1 | form complex
binding
|
R2SP co-chaperone |
0.393 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270938 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29844425 |
Systematic interaction analyses show that one RPAP3-like protein, SPAG1, binds PIH1D2 and RUVBL1/2 to form an R2TP-like complex termed R2SP. This co-chaperone is enriched in testis and among 68 of the potential clients identified, some are expressed in testis and others are ubiquitous. One substrate is liprin-α2, which organizes large signaling complexes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
R2SP co-chaperone
CPX-6150