| + |
ATM | up-regulates activity 
phosphorylation
|
RAD9A |
0.759 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-105243 |
Ser272 |
LSDTDSHsQDLGSPE |
Homo sapiens |
|
| pmid |
sentence |
| 11278446 |
Hyperphosphorylation of hrad9 induced by ir is dependent on atm. Ser(272) of hrad9 is phosphorylated directly by atm in vitro. / our results suggest that the atm-mediated phosphorylation of hrad9 is required for ir-induced checkpoint activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Lung |
| + |
CDK1 | up-regulates activity
phosphorylation
|
RAD9A |
0.37 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-101043 |
Ser277 |
SHSQDLGsPERHQPV |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 12734188 |
Here we present evidence that thr292 of hrad9 is subject to cdc2-dependent phosphorylation in mitosis. Furthermore, our data are also consistent with four other hrad9 phosphorylation sites (ser277, ser328, ser336, and thr355) being regulated in part by cdc2. We also identify ser387 as a novel site of hrad9 constitutive phosphorylation and show that phosphorylation at ser387 is a prerequisite for one form of dna damage-induced hyperphosphorylation of hrad9. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-101047 |
Ser328 |
VLPSISLsPGPQPPK |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 12734188 |
Here we present evidence that thr292 of hrad9 is subject to cdc2-dependent phosphorylation in mitosis. Furthermore, our data are also consistent with four other hrad9 phosphorylation sites (ser277, ser328, ser336, and thr355) being regulated in part by cdc2. We also identify ser387 as a novel site of hrad9 constitutive phosphorylation and show that phosphorylation at ser387 is a prerequisite for one form of dna damage-induced hyperphosphorylation of hrad9. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-101051 |
Ser336 |
PGPQPPKsPGPHSEE |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 12734188 |
Here we present evidence that thr292 of hrad9 is subject to cdc2-dependent phosphorylation in mitosis. Furthermore, our data are also consistent with four other hrad9 phosphorylation sites (ser277, ser328, ser336, and thr355) being regulated in part by cdc2. We also identify ser387 as a novel site of hrad9 constitutive phosphorylation and show that phosphorylation at ser387 is a prerequisite for one form of dna damage-induced hyperphosphorylation of hrad9. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-101055 |
Thr292 |
PQLQAHStPHPDDFA |
Homo sapiens |
|
| pmid |
sentence |
| 12734188 |
Here we present evidence that thr292 of hrad9 is subject to cdc2-dependent phosphorylation in mitosis. Furthermore, our data are also consistent with four other hrad9 phosphorylation sites (ser277, ser328, ser336, and thr355) being regulated in part by cdc2. We also identify ser387 as a novel site of hrad9 constitutive phosphorylation and show that phosphorylation at ser387 is a prerequisite for one form of dna damage-induced hyperphosphorylation of hrad9. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-101059 |
Thr355 |
EPSTVPGtPPPKKFR |
Homo sapiens |
|
| pmid |
sentence |
| 12734188 |
Here we present evidence that thr292 of hrad9 is subject to cdc2-dependent phosphorylation in mitosis. Furthermore, our data are also consistent with four other hrad9 phosphorylation sites (ser277, ser328, ser336, and thr355) being regulated in part by cdc2. We also identify ser387 as a novel site of hrad9 constitutive phosphorylation and show that phosphorylation at ser387 is a prerequisite for one form of dna damage-induced hyperphosphorylation of hrad9. |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| + |
TLK1 |
phosphorylation
|
RAD9A |
0.462 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203499 |
Ser328 |
VLPSISLsPGPQPPK |
Homo sapiens |
|
| pmid |
sentence |
| 24376897 |
Here we show that rad9 is phosphorylated in a tlk-dependent manner in vitro and in vivo, and that t355 within the c-terminal tail is the primary targeted residue. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203503 |
Thr355 |
EPSTVPGtPPPKKFR |
Homo sapiens |
|
| pmid |
sentence |
| 24376897 |
Here we show that rad9 is phosphorylated in a tlk-dependent manner in vitro and in vivo, and that t355 within the c-terminal tail is the primary targeted residue. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CyclinA2/CDK2 |
phosphorylation
|
RAD9A |
0.411 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217268 |
Ser328 |
VLPSISLsPGPQPPK |
Homo sapiens |
|
| pmid |
sentence |
| 23028682 |
The forced activation of cyclin a-cdk2 in these cells by the overexpression of cyclin a,triggered rad9 phosphorylation at serine 328 and thereby promoted the interaction of rad9 with bcl-xl and the subsequent initiation of the apoptotic program. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TLK1 | up-regulates
phosphorylation
|
RAD9A |
0.462 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-181748 |
Ser328 |
VLPSISLsPGPQPPK |
Homo sapiens |
|
| pmid |
sentence |
| 18940270 |
Tlk1b phosphorylates hrad9 at s328 after the induction of dsb, occupancy of rad9 adjacent to the break increased during repair while that of asf1 decreased, and the effect was more pronounced in tlk1b-overexpressing cells. We propose that following genotoxic stress, tlk1/1b is first recruited to the dsb in a complex with rad9. It then exchanges with asf1 to promote nucleosomes eviction at the dsb and access of the repair machinery to unencumbered dna. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK2 |
phosphorylation
|
RAD9A |
0.41 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-199020 |
Ser328 |
VLPSISLsPGPQPPK |
Homo sapiens |
|
| pmid |
sentence |
| 23028682 |
The forced activation of cyclin a-cdk2 in these cells by the overexpression of cyclin a,triggered rad9 phosphorylation at serine 328 and thereby promoted the interaction of rad9 with bcl-xl and the subsequent initiation of the apoptotic program. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ABL1 | up-regulates
phosphorylation
|
RAD9A |
0.491 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-86186 |
Tyr28 |
SRIGDELyLEPLEDG |
Homo sapiens |
|
| pmid |
sentence |
| 11971963 |
C-abl phosphorylates the rad9 bcl-2 homology 3 domain (tyr-28) in vitro and in cells exposed to dna-damaging agents. The results also demonstrate that c-abl-mediated phosphorylation of rad9 induces binding of rad9 to the antiapototic bcl-x(l) protein |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ABL1 | up-regulates activity
phosphorylation
|
RAD9A |
0.491 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260843 |
Tyr28 |
AVHSLSRiGDELYLE |
Homo sapiens |
|
| pmid |
sentence |
| 11971963 |
The SH3 domain of c-Abl interacts directly with the C-terminal region of Rad9. c-Abl phosphorylates the Rad9 Bcl-2 homology 3 domain (Tyr-28) in vitro and in cells exposed to DNA-damaging agents. | c-Abl-mediated phosphorylation of Rad9 induces binding of Rad9 to Bcl-xL |these findings indicate that Rad9 is regulated by a c-Abl-dependent mechanism in the apoptotic response to genotoxic stress. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RAD9A | up-regulates
binding
|
TOPBP1 |
0.82 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179382 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18594563 |
The 9-1-1 complex functions as a clamp, encircling the dna, and recruits the brct domain-containing protein topbp1 in a phospho-dependent manner |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
RAD9A
- 
- 