| + |
RPA1 | up-regulates activity 
binding
|
POLA1 |
0.671 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261272 |
|
|
in vitro |
|
| pmid |
sentence |
| 9214288 |
In our studies, we have shown that T antigen, DNA polymerase R, and the activation domain of VP16 all interact with overlapping regions of the 70-kDa subunit of RPA.| In the latter, both the direct protein-protein interaction and ssDNA-binding activities of RPA were needed for RPA to modulate polymerase processivity. We also found that SV40 T antigen inhibited the ability of RPA to increase processivity of DNA polymerase alpha, suggesting that this activity of RPA may be important for elongation but not during the initiation of DNA replication. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
ACD | down-regulates activity 
binding
|
RPA1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263328 |
|
|
|
|
| pmid |
sentence |
| 18680434 |
The current model for how telomeres repress ATR signaling proposes that POT1/TPP1 prevents the binding of RPA to the single-stranded telomeric DNA |
|
| Publications: |
1 |
| + |
RPA1 | up-regulates activity
binding
|
BRIP1 |
0.683 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259187 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17596542 |
Our data are consistent with a model in which FANCJ associates with RPA in a DNA damage-inducible manner and through the protein interaction RPA stimulates FANCJ helicase to better unwind duplex DNA substrates. These findings identify RPA as the first regulatory partner of FANCJ. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRPF19 | up-regulates activity
polyubiquitination
|
RPA1 |
0.48 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272076 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 24332808 |
PRP19 is a ubiquitin ligase involved in pre-mRNA splicing and the DNA damage response (DDR). PRP19 ubiquitylates RPA and promotes ATRIP recruitment. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RAD23B | up-regulates activity
binding
|
RPA1 |
0.552 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275698 |
|
|
|
|
| pmid |
sentence |
| 24086043 |
GG-NER is initiated by the GG-NER specific factor XPC-RAD23B, in some cases with the help of UV-DDB (UV-damaged DNA-binding protein). TC-NER is initiated by RNA polymerase stalled at a lesion with the help of TC-NER specific factors CSA, CSB, and XAB2. Both pathways require the core NER factors to complete the excision process|The core NER dual incision reaction has been reconstituted in vitro with purified factors using XPC-RAD23B, TFIIH, XPA, RPA, XPG, and ERCC1-XPF (Aboussekhra et al. 1995; Mu et al. 1995; Araujo et al. 2000).|The core NER dual incision reaction has been reconstituted in vitro with purified factors using XPC-RAD23B, TFIIH, XPA, RPA, XPG, and ERCC1-XPF (Aboussekhra et al. 1995; Mu et al. 1995; Araujo et al. 2000). Functional studies revealed that XPC-RAD23B is the initial damage recognition factor in this system, as the presence of XPC-RAD23B is required for assembly of the other core NER factors and progression through the NER pathway both in vitro and in vivo |
|
| Publications: |
1 |
| + |
RPA1 | up-regulates 
|
Nucleotide-excision_repair |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275705 |
|
|
|
|
| pmid |
sentence |
| 24086043 |
The core NER dual incision reaction has been reconstituted in vitro with purified factors using XPC-RAD23B, TFIIH, XPA, RPA, XPG, and ERCC1-XPF (Aboussekhra et al. 1995; Mu et al. 1995; Araujo et al. 2000). Functional studies revealed that XPC-RAD23B is the initial damage recognition factor in this system, as the presence of XPC-RAD23B is required for assembly of the other core NER factors and progression through the NER pathway both in vitro and in vivo |
|
| Publications: |
1 |
| + |
POT1 | down-regulates activity
binding
|
RPA1 |
0.302 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263325 |
|
|
|
|
| pmid |
sentence |
| 18680434 |
The current model for how telomeres repress ATR signaling proposes that POT1/TPP1 prevents the binding of RPA to the single-stranded telomeric DNA |
|
| Publications: |
1 |
3.0
RPA1
- 
- 