| + |
PRKDC | down-regulates activity 
phosphorylation
|
RPA2 |
0.605 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248980 |
Ser11 |
SGFESYGsSSYGGAG |
in vitro |
|
| pmid |
sentence |
| 9295339 |
We showed previously that UV irradiation increases phosphorylation of the p34 subunit of human replication protein A (RPA) and that this hyperphosphorylation correlated with loss of activity of the DNA replication complex. | we detected phosphorylation of the RPA complex by DNA-PK on RPA-p34 sites Ser-23, Ser-29, and Ser-11, -12, or -13 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248981 |
Ser12 |
GFESYGSsSYGGAGG |
in vitro |
|
| pmid |
sentence |
| 9295339 |
We showed previously that UV irradiation increases phosphorylation of the p34 subunit of human replication protein A (RPA) and that this hyperphosphorylation correlated with loss of activity of the DNA replication complex. | we detected phosphorylation of the RPA complex by DNA-PK on RPA-p34 sites Ser-23, Ser-29, and Ser-11, -12, or -13 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248982 |
Ser13 |
FESYGSSsYGGAGGY |
in vitro |
|
| pmid |
sentence |
| 9295339 |
We showed previously that UV irradiation increases phosphorylation of the p34 subunit of human replication protein A (RPA) and that this hyperphosphorylation correlated with loss of activity of the DNA replication complex. | we detected phosphorylation of the RPA complex by DNA-PK on RPA-p34 sites Ser-23, Ser-29, and Ser-11, -12, or -13 |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
CDK1 | up-regulates activity 
phosphorylation
|
RPA2 |
0.523 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-16971 |
Ser23 |
GAGGYTQsPGGFGSP |
Homo sapiens |
|
| pmid |
sentence |
| 1318195 |
Cdc2 family kinases phosphorylate a human cell dna replication factor, rpa, and activate dna replication. therefore, the serines on rpa p34 that were necessary for phosphorylation by cdc2 kinase were also necessary for phosphorylation in the cell |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-16975 |
Ser29 |
QSPGGFGsPAPSQAE |
Homo sapiens |
|
| pmid |
sentence |
| 1318195 |
Cdc2 family kinases phosphorylate a human cell dna replication factor, rpa, and activate dna replication. therefore, the serines on rpa p34 that were necessary for phosphorylation by cdc2 kinase were also necessary for phosphorylation in the cell |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ATR |
phosphorylation
|
RPA2 |
0.746 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-188666 |
Ser33 |
GFGSPAPsQAEKKSR |
Homo sapiens |
|
| pmid |
sentence |
| 19843584 |
Atr phosphorylates s33 in response to replication stress |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKDC |
phosphorylation
|
RPA2 |
0.605 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248971 |
Ser33 |
GFGSPAPsQAEKKSR |
in vitro |
|
| pmid |
sentence |
| 9139719 |
In this study, we show that efficient phosphorylation of HSSB-p34 by DNA-PK requires Ku as well as DNA. The DNA-PK phosphorylation sites in HSSB-p34 have been mapped at Thr-21 and Ser-33. Kinetic studies demonstrated that a phosphate residue is first incorporated at Thr-21 followed by the incorporation of a second phosphate residue at Ser-33. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248972 |
Thr21 |
YGGAGGYtQSPGGFG |
in vitro |
|
| pmid |
sentence |
| 9139719 |
In this study, we show that efficient phosphorylation of HSSB-p34 by DNA-PK requires Ku as well as DNA. The DNA-PK phosphorylation sites in HSSB-p34 have been mapped at Thr-21 and Ser-33. Kinetic studies demonstrated that a phosphate residue is first incorporated at Thr-21 followed by the incorporation of a second phosphate residue at Ser-33. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-121873 |
Thr21 |
YGGAGGYtQSPGGFG |
Homo sapiens |
|
| pmid |
sentence |
| 14872059 |
We show that both dna-pk and atm phosphorylate rpa32 on thr21 in vitro. |
|
| Publications: |
3 |
Organism: |
In Vitro, Homo Sapiens |
| + |
PIAS4 | up-regulates
phosphorylation
|
RPA2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-162160 |
Ser4 |
sGFESYGS |
Homo sapiens |
|
| pmid |
sentence |
| 20016603 |
Pias1 and pias4 promote brca1 accumulation and sumoylation, rpa phosphorylation, and dsb repair furthermore, phosphorylation of the 34 kda subunit of rpa on ser-4 and ser-8 (ps4/ps8) in response to ir or camptothecin treatment was diminished by pias4 depletion, while pias1 depletion impaired ir-induced but not camptothecin-induced rpa phosphorylation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-162164 |
Ser8 |
MWNSGFEsYGSSSYG |
Homo sapiens |
|
| pmid |
sentence |
| 20016603 |
Pias1 and pias4 promote brca1 accumulation and sumoylation, rpa phosphorylation, and dsb repair furthermore, phosphorylation of the 34 kda subunit of rpa on ser-4 and ser-8 (ps4/ps8) in response to ir or camptothecin treatment was diminished by pias4 depletion, while pias1 depletion impaired ir-induced but not camptothecin-induced rpa phosphorylation |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ATM | up-regulates
phosphorylation
|
RPA2 |
0.803 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-121861 |
Thr21 |
YGGAGGYtQSPGGFG |
Homo sapiens |
|
| pmid |
sentence |
| 14872059 |
Replication protein a (rpa) is a single-stranded dna (ssdna) binding protein involved in various processes, including nucleotide excision repair and dna replication. The 32 kda subunit of rpa (rpa32) is phosphorylated in response to various dna-damaging agents, and two protein kinases, ataxia-telangiectasia mutated (atm) and the dna-dependent protein kinase (dna-pk) have been implicated in dna damage-induced phosphorylation of rpa32we show that both dna-pk and atm phosphorylate rpa32 on thr21 in vitro. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ATM |
phosphorylation
|
RPA2 |
0.803 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-121865 |
Thr21 |
YGGAGGYtQSPGGFG |
Homo sapiens |
|
| pmid |
sentence |
| 14872059 |
Atm and dna?PK Phosphorylate rpa32 thr21in vitro and in vivo |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKDC | up-regulates
phosphorylation
|
RPA2 |
0.605 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-121869 |
Thr21 |
YGGAGGYtQSPGGFG |
Homo sapiens |
|
| pmid |
sentence |
| 14872059 |
Replication protein a (rpa) is a single-stranded dna (ssdna) binding protein involved in various processes, including nucleotide excision repair and dna replication. The 32 kda subunit of rpa (rpa32) is phosphorylated in response to various dna-damaging agents, and two protein kinases, ataxia-telangiectasia mutated (atm) and the dna-dependent protein kinase (dna-pk) have been implicated in dna damage-induced phosphorylation of rpa32we show that both dna-pk and atm phosphorylate rpa32 on thr21 in vitro. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRPF19 | up-regulates activity
polyubiquitination
|
RPA2 |
0.453 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272075 |
|
|
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 |
| + |
ACD | down-regulates activity
binding
|
RPA2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263327 |
|
|
|
|
| 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 |
| + |
POT1 | down-regulates activity
binding
|
RPA2 |
0.419 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263324 |
|
|
|
|
| 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 |
| + |
RPA2 | up-regulates
binding
|
MRE11 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186648 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19586055 |
The response to replication stress requires the recruitment of rpa and the mre11-rad50-nbs1 (mrn) complex. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPA2 | up-regulates 
|
Nucleotide-excision_repair |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275706 |
|
|
|
|
| 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 |
| + |
RAD23B | up-regulates activity
binding
|
RPA2 |
0.5 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275699 |
|
|
|
|
| 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 |
| + |
RPA2 | up-regulates
binding
|
ATRIP |
0.673 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163176 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20068082 |
Ssdna lesions are then coated by replication protein a (rpa), recruiting atr/atrip (atr-interacting protein) complexes via recognition and association of rpa-ssdna by atrip. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PIAS1 | up-regulates
sumoylation
|
RPA2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-162153 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20016603 |
Pias1 and pias4 promote brca1 accumulation and sumoylation, rpa phosphorylation, and dsb repair |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPA2 | up-regulates
binding
|
NBN |
0.528 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186651 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19586055 |
The response to replication stress requires the recruitment of rpa and the mre11-rad50-nbs1 (mrn) complex. We observe a direct interaction between rpa with both nbs1 and mre11. By utilizing rpa bound to ssdna, we demonstrate that substituting rpa with phosphorylated rpa or a phosphomimetic weakens the interaction with the mrn complex. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
RPA2
- 
- 