| + |
PRKDC | down-regulates quantity by destabilization 
phosphorylation
|
TOP1 |
0.46 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277352 |
Ser10 |
GDHLHNDsQIEADFR |
Homo sapiens |
HCT-15 Cell |
| pmid |
sentence |
| 28415827 |
Here, we show that the Ku70/Ku80 heterodimer binds with topoI, and that the DNA-dependent protein kinase (DNA-PKcs) phosphorylates topoI on serine 10 (topoI-pS10), which is subsequently ubiquitinated by BRCA1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKDC | down-regulates activity
phosphorylation
|
RPA2 |
0.598 |
| 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 |
| + |
PRKDC | up-regulates 
phosphorylation
|
PNKP |
0.636 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176016 |
Ser114 |
EETRTPEsQPDTPPG |
Homo sapiens |
|
| pmid |
sentence |
| 21824916 |
We demonstrate that pnkp is phosphorylated by the dna-dependent protein kinase (dna-pk) and ataxia-telangiectasia mutated (atm) in vitro. The major phosphorylation site for both kinases was serine 114, with serine 126 being a minor site. Purified pnkp protein with mutation of serines 114 and 126 had decreased dna kinase and dna phosphatase activities and reduced affinity for dna in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176020 |
Ser126 |
PPGTPLVsQDEKRDA |
Homo sapiens |
|
| pmid |
sentence |
| 21824916 |
We demonstrate that pnkp is phosphorylated by the dna-dependent protein kinase (dna-pk) and ataxia-telangiectasia mutated (atm) in vitro. The major phosphorylation site for both kinases was serine 114, with serine 126 being a minor site. Purified pnkp protein with mutation of serines 114 and 126 had decreased dna kinase and dna phosphatase activities and reduced affinity for dna in vitro. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKDC | up-regulates activity
phosphorylation
|
MCC |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273530 |
Ser118 |
SELRSELsQSQHEVN |
Homo sapiens |
HCT-116 Cell |
| pmid |
sentence |
| 21779472 |
MCC is phosphorylated at the ATM/ATR consensus sites Ser118 and Ser120. Finally, mutation of S118/120 to alanine did not affect MCC nuclear shuttling following UV but did impair MCC G2/M checkpoint activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273531 |
Ser120 |
LRSELSQsQHEVNED |
Homo sapiens |
HCT-116 Cell |
| pmid |
sentence |
| 21779472 |
MCC is phosphorylated at the ATM/ATR consensus sites Ser118 and Ser120. Finally, mutation of S118/120 to alanine did not affect MCC nuclear shuttling following UV but did impair MCC G2/M checkpoint activity. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKDC | up-regulates
phosphorylation
|
CASP2 |
0.302 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183895 |
Ser139 |
LSCDYDLsLPFPVCE |
Homo sapiens |
|
| pmid |
sentence |
| 19203584 |
Here we show that dna damage induced by gamma-radiation triggers the phosphorylation of nuclear caspase-2 at the s122 site within its prodomain, leading to its cleavage and activation. This phosphorylation is carried out by the nuclear serine/threonine protein kinase dna-pkcs |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKDC | up-regulates
phosphorylation
|
TP53 |
0.785 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-53030 |
Ser15 |
PSVEPPLsQETFSDL |
Homo sapiens |
|
| pmid |
sentence |
| 9363941 |
We demonstrate that phosphorylation of p53 at serines 15 and 37 impairs the ability of mdm2 to inhibit p53-dependent transactivation. We present evidence that these effects are most likely due to a conformational change induced upon phosphorylation of p53. Our studies provide a plausible mechanism by which the induction of p53 can be modulated by dna-pk (or other protein kinases with similar specificity) in response to dna damage. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Cell cycle: G2/M phase transition |
| + |
PRKDC | up-regulates activity
phosphorylation
|
PRKAG1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277503 |
Ser192 |
KPEFMSKsLEELQIG |
in vitro |
|
| pmid |
sentence |
| 31983282 |
PRKDC interacted with the AMPK complex and phosphorylated its nucleotide-sensing γ1 subunit PRKAG1/AMPKγ1 at Ser192 and Thr284, both events being significantly reduced upon the activation of the AMPK complex. Alanine substitutions of PRKDC phosphorylation sites in PRKAG1 reduced AMPK complex activation without affecting its nucleotide sensing capacity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277504 |
Thr284 |
LKCYLHEtLETIINR |
in vitro |
|
| pmid |
sentence |
| 31983282 |
PRKDC interacted with the AMPK complex and phosphorylated its nucleotide-sensing γ1 subunit PRKAG1/AMPKγ1 at Ser192 and Thr284, both events being significantly reduced upon the activation of the AMPK complex. Alanine substitutions of PRKDC phosphorylation sites in PRKAG1 reduced AMPK complex activation without affecting its nucleotide sensing capacity. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PRKDC | up-regulates
phosphorylation
|
PRKDC |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-151445 |
Ser2056 |
VQSYSYSsQDPRPAT |
Homo sapiens |
|
| pmid |
sentence |
| 17189255 |
Ir-induced dna-pkcs phosphorylation at thr-2609 and ser-2056, however, exhibits distinct kinetics indicating that they are differentially regulated. Although dna-pkcs autophosphorylates itself at ser-2056 after ir, in addition, our data suggest that dna-pkcs- and atm-mediated dna-pkcs phosphorylations are cooperative and required for the full activation of dna-pkcs and the subsequent dsb repair. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-151449 |
Thr2609 |
LTPMFVEtQASQGTL |
Homo sapiens |
|
| pmid |
sentence |
| 17189255 |
Ir-induced dna-pkcs phosphorylation at thr-2609 and ser-2056, however, exhibits distinct kinetics indicating that they are differentially regulated. Although dna-pkcs autophosphorylates itself at ser-2056 after ir, we have reported here that atm mediates dna-pkcs phosphorylation at thr-2609 as well as at the adjacent (s/t)q motifs within the thr-2609 cluster. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Cell cycle: G2/M phase transition |
| + |
PRKDC | down-regulates
phosphorylation
|
POU2F1 |
0.335 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-53258 |
Ser232 |
LTQLPQQsQANLLQS |
Homo sapiens |
|
| pmid |
sentence |
| 9368058 |
Through a similar strategy, t226 and s232 were characterized as the dna-pk phosphorylation sites |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-53262 |
Thr226 |
LQAQNLLtQLPQQSQ |
Homo sapiens |
|
| pmid |
sentence |
| 9368058 |
Through a similar strategy, t226 and s232 were characterized as the dna-pk phosphorylation sites |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKDC |
phosphorylation
|
NHEJ1 |
0.654 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179532 |
Ser245 |
PHTSNSAsLQGIDSQ |
Homo sapiens |
|
| pmid |
sentence |
| 18644470 |
Here, we have identified two major in vitro dna-pk phosphorylation sites in the c-terminal region of xlf, serines 245 and 251. We show that these represent the major phosphorylation sites in xlf in vivo and that serine 245 is phosphorylated in vivo by dna-pk, while serine 251 is phosphorylated by ataxia-telangiectasia mutated (atm). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKDC |
phosphorylation
|
JUN |
0.415 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248934 |
Ser249 |
LSPIDMEsQERIKAE |
in vitro |
|
| pmid |
sentence |
| 8464713 |
Here, we show that the DNA-PK modifies c-Jun in vitro and that serine residue 249 (Ser-249) is required for phosphorylation to occur. This residue corresponds to one of three sites of c-Jun that are phosphorylated in vivo and which negatively regulate c-Jun DNA binding in vitro. However, we find that phosphorylation of c-Jun by the DNA-PK does not interfere with DNA binding, indicating that phosphorylation at other sites is required for this effect. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKDC | up-regulates activity
phosphorylation
|
PRKDC |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249155 |
Ser2612 |
MFVETQAsQGTLQTR |
Homo sapiens |
Lymphoblastoid Cell Line |
| pmid |
sentence |
| 12186630 |
We have identified seven in vitro autophosphorylation sites in DNA-PKcs. Six of these sites (Thr2609, Ser2612, Thr2620, Ser2624, Thr2638 and Thr2647) are clustered in a region of 38 amino acids in the central region of the protein. Five of these sites (Thr2609, Ser2612, Thr2638, Thr2647 and Ser3205) are conserved between six vertebrate species. Moreover, we show that DNA-PKcs is phosphorylated in vivo at Thr2609, Ser2612, Thr2638 and Thr2647 in okadaic acid-treated human cells. | Thus phosphorylation of DNA-PKcs at one or more of the autophosphorylation sites identified in this study is likely to be required for DNA-PKcs function. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249156 |
Ser2624 |
QTRTQEGsLSARWPV |
in vitro |
|
| pmid |
sentence |
| 12186630 |
We have identified seven in vitro autophosphorylation sites in DNA-PKcs. Six of these sites (Thr2609, Ser2612, Thr2620, Ser2624, Thr2638 and Thr2647) are clustered in a region of 38 amino acids in the central region of the protein. Five of these sites (Thr2609, Ser2612, Thr2638, Thr2647 and Ser3205) are conserved between six vertebrate species. Moreover, we show that DNA-PKcs is phosphorylated in vivo at Thr2609, Ser2612, Thr2638 and Thr2647 in okadaic acid-treated human cells. | Thus phosphorylation of DNA-PKcs at one or more of the autophosphorylation sites identified in this study is likely to be required for DNA-PKcs function. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249157 |
Ser3205 |
TPLPEDNsMNVDQDG |
Homo sapiens |
Lymphoblastoid Cell Line |
| pmid |
sentence |
| 12186630 |
We have identified seven in vitro autophosphorylation sites in DNA-PKcs. Six of these sites (Thr2609, Ser2612, Thr2620, Ser2624, Thr2638 and Thr2647) are clustered in a region of 38 amino acids in the central region of the protein. Five of these sites (Thr2609, Ser2612, Thr2638, Thr2647 and Ser3205) are conserved between six vertebrate species. Moreover, we show that DNA-PKcs is phosphorylated in vivo at Thr2609, Ser2612, Thr2638 and Thr2647 in okadaic acid-treated human cells. | Thus phosphorylation of DNA-PKcs at one or more of the autophosphorylation sites identified in this study is likely to be required for DNA-PKcs function. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249154 |
Thr2609 |
LTPMFVEtQASQGTL |
Homo sapiens |
|
| pmid |
sentence |
| 12186630 |
We have identified seven in vitro autophosphorylation sites in DNA-PKcs. Six of these sites (Thr2609, Ser2612, Thr2620, Ser2624, Thr2638 and Thr2647) are clustered in a region of 38 amino acids in the central region of the protein. Five of these sites (Thr2609, Ser2612, Thr2638, Thr2647 and Ser3205) are conserved between six vertebrate species. Moreover, we show that DNA-PKcs is phosphorylated in vivo at Thr2609, Ser2612, Thr2638 and Thr2647 in okadaic acid-treated human cells. | Thus phosphorylation of DNA-PKcs at one or more of the autophosphorylation sites identified in this study is likely to be required for DNA-PKcs function. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249158 |
Thr2620 |
QGTLQTRtQEGSLSA |
in vitro |
|
| pmid |
sentence |
| 12186630 |
We have identified seven in vitro autophosphorylation sites in DNA-PKcs. Six of these sites (Thr2609, Ser2612, Thr2620, Ser2624, Thr2638 and Thr2647) are clustered in a region of 38 amino acids in the central region of the protein. Five of these sites (Thr2609, Ser2612, Thr2638, Thr2647 and Ser3205) are conserved between six vertebrate species. Moreover, we show that DNA-PKcs is phosphorylated in vivo at Thr2609, Ser2612, Thr2638 and Thr2647 in okadaic acid-treated human cells. | Thus phosphorylation of DNA-PKcs at one or more of the autophosphorylation sites identified in this study is likely to be required for DNA-PKcs function. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249159 |
Thr2638 |
VAGQIRAtQQQHDFT |
Homo sapiens |
Lymphoblastoid Cell Line |
| pmid |
sentence |
| 12186630 |
We have identified seven in vitro autophosphorylation sites in DNA-PKcs. Six of these sites (Thr2609, Ser2612, Thr2620, Ser2624, Thr2638 and Thr2647) are clustered in a region of 38 amino acids in the central region of the protein. Five of these sites (Thr2609, Ser2612, Thr2638, Thr2647 and Ser3205) are conserved between six vertebrate species. Moreover, we show that DNA-PKcs is phosphorylated in vivo at Thr2609, Ser2612, Thr2638 and Thr2647 in okadaic acid-treated human cells. | Thus phosphorylation of DNA-PKcs at one or more of the autophosphorylation sites identified in this study is likely to be required for DNA-PKcs function. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249160 |
Thr2647 |
QQHDFTLtQTADGRS |
Homo sapiens |
Lymphoblastoid Cell Line |
| pmid |
sentence |
| 12186630 |
We have identified seven in vitro autophosphorylation sites in DNA-PKcs. Six of these sites (Thr2609, Ser2612, Thr2620, Ser2624, Thr2638 and Thr2647) are clustered in a region of 38 amino acids in the central region of the protein. Five of these sites (Thr2609, Ser2612, Thr2638, Thr2647 and Ser3205) are conserved between six vertebrate species. Moreover, we show that DNA-PKcs is phosphorylated in vivo at Thr2609, Ser2612, Thr2638 and Thr2647 in okadaic acid-treated human cells. | Thus phosphorylation of DNA-PKcs at one or more of the autophosphorylation sites identified in this study is likely to be required for DNA-PKcs function. |
|
| Publications: |
7 |
Organism: |
Homo Sapiens, In Vitro |
| Pathways: | Cell cycle: G2/M phase transition |
| + |
PRKDC | up-regulates activity
phosphorylation
|
XRCC6 |
0.939 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274022 |
Ser27 |
QEENLEAsGDYKYSG |
Homo sapiens |
Chronic Lymphocytic Leukemia Cell |
| pmid |
sentence |
| 26337656 |
Ku70 phosphorylation occurs within minutes of genotoxic stress and involves DNA-PKcs and/or ATM kinase activities.By using specific vectors enabling the simultaneous shRNA-mediated inhibition of endogenous Ku70 and the expression of exogenous Ku70 resistant to shRNA (i.e. S27-S33-Ku70 and A27-A33-Ku70 expressing cells), we showed that phospho-Ku70 contributes to faster but error-prone DNA repair resulting in higher levels of chromosomal breaks. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274023 |
Ser33 |
ASGDYKYsGRDSLIF |
Homo sapiens |
Chronic Lymphocytic Leukemia Cell |
| pmid |
sentence |
| 26337656 |
Ku70 phosphorylation occurs within minutes of genotoxic stress and involves DNA-PKcs and/or ATM kinase activities.By using specific vectors enabling the simultaneous shRNA-mediated inhibition of endogenous Ku70 and the expression of exogenous Ku70 resistant to shRNA (i.e. S27-S33-Ku70 and A27-A33-Ku70 expressing cells), we showed that phospho-Ku70 contributes to faster but error-prone DNA repair resulting in higher levels of chromosomal breaks. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKDC | up-regulates activity
phosphorylation
|
XRCC4 |
0.905 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277198 |
Ser327 |
SLETLRNsSPEDLFD |
Homo sapiens |
MiaPaCa-2 Cell |
| pmid |
sentence |
| 26774286 |
In response to ionizing radiation, ATM phosphorylates FBXW7 at serine 26 to recruit it to DNA double-strand break (DSB) sites, whereas activated DNA-PKcs phosphorylates XRCC4 at serines 325/326, which promotes binding of XRCC4 to FBXW7. SCF(FBXW7) E3 ligase then promotes polyubiquitylation of XRCC4 at lysine 296 via lysine 63 linkage for enhanced association with the Ku70/80 complex to facilitate NHEJ repair. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277199 |
Ser328 |
LETLRNSsPEDLFDE |
Homo sapiens |
MiaPaCa-2 Cell |
| pmid |
sentence |
| 26774286 |
In response to ionizing radiation, ATM phosphorylates FBXW7 at serine 26 to recruit it to DNA double-strand break (DSB) sites, whereas activated DNA-PKcs phosphorylates XRCC4 at serines 325/326, which promotes binding of XRCC4 to FBXW7. SCF(FBXW7) E3 ligase then promotes polyubiquitylation of XRCC4 at lysine 296 via lysine 63 linkage for enhanced association with the Ku70/80 complex to facilitate NHEJ repair. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKDC |
phosphorylation
|
RPA2 |
0.598 |
| 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-121873 |
Thr21 |
YGGAGGYtQSPGGFG |
Homo sapiens |
|
| pmid |
sentence |
| 14872059 |
We show that both dna-pk and atm phosphorylate rpa32 on thr21 in vitro. |
|
| 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. |
|
| Publications: |
3 |
Organism: |
In Vitro, Homo Sapiens |
| + |
PRKDC | down-regulates activity
phosphorylation
|
IKBKG |
0.301 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277508 |
Ser43 |
PAMLHLPsEQGAPET |
in vitro |
|
| pmid |
sentence |
| 31932854 |
Here, we show that DNA-dependent protein kinase (DNA-PK), an enzyme involved in DNA double-strand break (DSB) repair, triggers the phosphorylation of NEMO by genotoxic stress, thereby enabling shuttling of NEMO through the nucleus with subsequent NF-κB activation. We identified serine 43 of NEMO as a DNA-PK phosphorylation site and point mutation of this serine to alanine led to a complete block of NF-κB activation by ionizing radiation (IR). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKDC | up-regulates activity
phosphorylation
|
SRF |
0.415 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248921 |
Ser435 |
LTVLNAFsQAPSTMQ |
in vitro |
|
| pmid |
sentence |
| 8407951 |
The carboxyl-terminal transcription activation domain was mapped within a 71-amino acid region that contains both DNA-PK phosphorylation sites. Amino acid substitutions that interfered with phosphorylation by DNA-PK at Ser-435/446 in GAL4-SRF fusion proteins were reduced in transactivation potency. From these data we suggest that DNA-PK phosphorylation may modulate SRF activity in vivo. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248922 |
Ser446 |
STMQVSHsQVQEPGG |
in vitro |
|
| pmid |
sentence |
| 8407951 |
The carboxyl-terminal transcription activation domain was mapped within a 71-amino acid region that contains both DNA-PK phosphorylation sites. Amino acid substitutions that interfered with phosphorylation by DNA-PK at Ser-435/446 in GAL4-SRF fusion proteins were reduced in transactivation potency. From these data we suggest that DNA-PK phosphorylation may modulate SRF activity in vivo. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PRKDC | up-regulates
phosphorylation
|
WRN |
0.662 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203737 |
Ser440 |
DTSYVIEsDEDLEME |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 24429382 |
Here, we identify ser-440 and -467 in wrn as major phosphorylation sites mediated by dna-pk our findings indicate that phosphorylation of ser-440 and -467 in wrn are important for relocalization of wrn to nucleoli, and that it is required for efficient dsb repair. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203741 |
Ser467 |
DTSYVIEsDEDLEME |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 24429382 |
Here, we identify ser-440 and -467 in wrn as major phosphorylation sites mediated by dna-pk our findings indicate that phosphorylation of ser-440 and -467 in wrn are important for relocalization of wrn to nucleoli, and that it is required for efficient dsb repair. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKDC | up-regulates activity
phosphorylation
|
AKT1 |
0.745 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252431 |
Ser473 |
RPHFPQFsYSASGTA |
Homo sapiens |
HUVEC Cell |
| pmid |
sentence |
| 18439899 |
DNA-PK phosphorylates HM Ser473 of PKB. However, we also noted similar patterns in T loop Thr308 phosphorylation after _-IR []his function is apparently restricted to the PKBalpha isoform |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKDC | up-regulates activity
phosphorylation
|
AKT |
0.745 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252447 |
Ser473 |
RPHFPQFsYSASGTA |
Homo sapiens |
HUVEC Cell |
| pmid |
sentence |
| 18439899 |
DNA-PK phosphorylates HM Ser473 of PKB. However, we also noted similar patterns in T loop Thr308 phosphorylation after _-IR []his function is apparently restricted to the PKBalpha isoform |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Cell cycle: G2/M phase transition |
| + |
PRKDC | up-regulates
phosphorylation
|
DCLRE1C |
0.687 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-148327 |
Ser503 |
NDEITDEsLENFPSS |
Homo sapiens |
|
| pmid |
sentence |
| 16874298 |
Artemis is a nuclear phosphoprotein required for genomic integrity whose phosphorylation is increased subsequent to dna damage. Artemis phosphorylation by the dna-dependent protein kinase (dna-pk). However, regardless of its association with dna-pkcs, phosphorylation of artemis at both s516 and s645 was stimulated in response to the double-stranded dna-damaging agent bleomycin |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-145837 |
Ser516 |
SSTVAGGsQSPKLFS |
Homo sapiens |
|
| pmid |
sentence |
| 16600297 |
Artemis is a nuclear phosphoprotein required for genomic integrity whose phosphorylation is increased subsequent to dna damage. Artemis phosphorylation by the dna-dependent protein kinase (dna-pk). However, regardless of its association with dna-pkcs, phosphorylation of artemis at both s516 and s645 was stimulated in response to the double-stranded dna-damaging agent bleomycin |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-145841 |
Ser645 |
NLSTNADsQSSSDFE |
Homo sapiens |
|
| pmid |
sentence |
| 16600297 |
Artemis is a nuclear phosphoprotein required for genomic integrity whose phosphorylation is increased subsequent to dna damage. Artemis phosphorylation by the dna-dependent protein kinase (dna-pk). However, regardless of its association with dna-pkcs, phosphorylation of artemis at both s516 and s645 was stimulated in response to the double-stranded dna-damaging agent bleomycin |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PRKDC |
phosphorylation
|
NR3C1 |
0.355 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248965 |
Ser508 |
QQATTGVsQETSENP |
in vitro |
|
| pmid |
sentence |
| 9038175 |
Phosphorylation of the GR fusion protein by DNA-PK mapped to a single site, Ser-527. This site occurs adjacent the GR nuclear localization sequence between the DNA and ligand binding domains of GR, and thus its phosphorylation, if confirmed, has the potential to affect receptor function in vivo. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKDC | up-regulates
phosphorylation
|
HNRNPU |
0.385 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-185058 |
Ser59 |
AMEPGNGsLDLGGDS |
Homo sapiens |
|
| pmid |
sentence |
| 19351595 |
We identify heterogeneous nuclear ribonucleoprotein u (hnrnp-u), also termed scaffold attachment factor a (saf-a), as a specific substrate for dna-pk. We show that hnrnp-u is phosphorylated at ser59 by dna-pk in vitro and in cells in response to dna double-strand breaks |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKDC | down-regulates
phosphorylation
|
LIG4 |
0.801 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-125869 |
Ser668 |
DVEFCVMsGTDSQPK |
Homo sapiens |
|
| pmid |
sentence |
| 15194694 |
Using tandem mass spectrometry, we identified a dna-pk phosphorylation site at thr-650 in human lig4 and a potential second phosphorylation site at ser-668 or ser-672. Phosphorylation of lig4 per se was not required for lig4 dna end joining activity. Substitution of these amino acids with alanine, individually or in combination, led to changes in lig4 protein stability of mouse lig4. The phosphomimetic mutation s650d returned lig4 stability to that of the wild-type protein. Furthermore dna-pk was found to negatively regulate lig4 protein stability. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-125873 |
Ser672 |
CVMSGTDsQPKPDLE |
Homo sapiens |
|
| pmid |
sentence |
| 15194694 |
Using tandem mass spectrometry, we identified a dna-pk phosphorylation site at thr-650 in human lig4 and a potential second phosphorylation site at ser-668 or ser-672. Phosphorylation of lig4 per se was not required for lig4 dna end joining activity. Substitution of these amino acids with alanine, individually or in combination, led to changes in lig4 protein stability of mouse lig4. The phosphomimetic mutation s650d returned lig4 stability to that of the wild-type protein. Furthermore dna-pk was found to negatively regulate lig4 protein stability. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-125877 |
Thr650 |
HLKAPNLtNVNKISN |
Homo sapiens |
|
| pmid |
sentence |
| 15194694 |
Using tandem mass spectrometry, we identified a dna-pk phosphorylation site at thr-650 in human lig4 and a potential second phosphorylation site at ser-668 or ser-672. Phosphorylation of lig4 per se was not required for lig4 dna end joining activity. Substitution of these amino acids with alanine, individually or in combination, led to changes in lig4 protein stability of mouse lig4. The phosphomimetic mutation s650d returned lig4 stability to that of the wild-type protein. Furthermore dna-pk was found to negatively regulate lig4 protein stability. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PRKDC | up-regulates activity
phosphorylation
|
PNPT1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263182 |
Ser776 |
IVMGEPIsQSSSNSQ |
Homo sapiens |
|
| pmid |
sentence |
| 22815474 |
We also demonstrated that DNAPK phosphorylates PNPase at Ser-776, which is critical for its ribonuclease activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKDC | up-regulates
phosphorylation
|
TDP1 |
0.518 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-188776 |
Ser81 |
PKRQKSGsQEDLGWC |
Homo sapiens |
|
| pmid |
sentence |
| 19851285 |
Optimal function of the dna repair enzyme tdp1 requires its phosphorylation by atm and/or dna-pk. Here we show that top1-associated dna double-stranded breaks (dsbs) induce the phosphorylation of tdp1 at s81. This phosphorylation is mediated by the protein kinases: ataxia-telangiectasia-mutated (atm) and dna-dependent protein kinase (dna-pk) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKDC | down-regulates quantity by destabilization
phosphorylation
|
PDX1 |
0.311 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-225542 |
Thr11 |
EEQYYAAtQLYKDPC |
Mus musculus |
|
| pmid |
sentence |
| 16166097 |
The interaction of PDX-1 with Ku subunits and its phosphorylation on threonine 11 by the DNA-PK appear to be implicated in its degradation by the proteosome. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PRKDC | up-regulates
phosphorylation
|
IRF3 |
0.406 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-115331 |
Thr135 |
GGGSTSDtQEDILDE |
Homo sapiens |
|
| pmid |
sentence |
| 11867762 |
Phosphorylation of irf-3 by dna-pk after virus infection results in its nuclear retention and delayed proteolysis |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKDC | up-regulates activity
phosphorylation
|
GOLPH3 |
0.323 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253557 |
Thr143 |
ALKHVKEtQPPETVQ |
in vitro |
HeLa Cell |
| pmid |
sentence |
| 24485452 |
In response to DNA damage, DNA-PK phosphorylates GOLPH3, resulting in increased interaction with MYO18A, which applies a tensile force to the Golgi. Interference with the Golgi DNA damage response by depletion of DNA-PK, GOLPH3, or MYO18A reduces survival after DNA damage, whereas overexpression of GOLPH3, as is observed frequently in human cancers, confers resistance to killing by DNA-damaging agents |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253558 |
Thr148 |
KETQPPEtVQNWIEL |
in vitro |
HeLa Cell |
| pmid |
sentence |
| 24485452 |
In response to DNA damage, DNA-PK phosphorylates GOLPH3, resulting in increased interaction with MYO18A, which applies a tensile force to the Golgi. Interference with the Golgi DNA damage response by depletion of DNA-PK, GOLPH3, or MYO18A reduces survival after DNA damage, whereas overexpression of GOLPH3, as is observed frequently in human cancers, confers resistance to killing by DNA-damaging agents |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PRKDC | down-regulates activity
phosphorylation
|
H1-2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273834 |
Thr146 |
KKAAGGAtPKKSAKK |
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 22249259 |
Similarly, DNA-PK-mediated phosphorylation of H1.2 at T146 enhances p53 transcriptional activity by impeding H1.2 binding to p53 and thereby attenuating its suppressive effects on p53 transactivation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKDC | up-regulates activity
phosphorylation
|
POLL |
0.444 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273835 |
Thr204 |
EASDGEEtQVSAADL |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 28109743 |
We show that Polλ is efficiently phosphorylated by DNA-PKcs in vitro and predominantly by ATM after DSB induction with ionizing radiation (IR) in vivo. We identify threonine 204 (T204) as a main target for ATM/DNA-PKcs phosphorylation on human Polλ, and establish that its phosphorylation may facilitate the repair of a subset of IR-induced DSBs and the efficient Polλ-mediated gap-filling during NHEJ. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKDC | up-regulates
phosphorylation
|
RPA2 |
0.598 |
| 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 |
| + |
PRKDC | up-regulates activity
phosphorylation
|
FH |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266349 |
Thr236 |
IKIGRTHtQDAVPLT |
in vitro |
|
| pmid |
sentence |
| 26237645 |
We show that exposure to ionizing radiation induces DNA-PK-dependent phosphorylation of nuclear fumarase at Thr 236, which leads to an interaction between fumarase and the histone variant H2A.Z at DNA double-strand break (DSB) regions. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
ATR | up-regulates
phosphorylation
|
PRKDC |
0.316 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-148722 |
Thr2609 |
LTPMFVEtQASQGTL |
Homo sapiens |
|
| pmid |
sentence |
| 16908529 |
Finally, in vitro atr-mediated phosphorylation at the t2609 cluster was further confirmed by western blot analysis using phosphospecific antibodies against t2647 (fig. ?(Fig.7e),7e), suggesting that dna-pkcs could be the direct target of atr kinase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Cell cycle: G2/M phase transition |
| + |
ATM | up-regulates
phosphorylation
|
PRKDC |
0.689 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-151441 |
Thr2609 |
LTPMFVEtQASQGTL |
Homo sapiens |
|
| pmid |
sentence |
| 17189255 |
Atm mediates dna-pkcs phosphorylation at thr-2609 as well as at the adjacent (s/t)q motifs within the thr-2609 cluster. In addition, our data suggest that dna-pkcs- and atm-mediated dna-pkcs phosphorylations are cooperative and required for the full activation of dna-pkcs and the subsequent dsb repair. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Cell cycle: G2/M phase transition |
| + |
PRKDC | down-regulates
phosphorylation
|
PRKDC |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-151453 |
Thr3950 |
GHAFGSAtQFLPVPE |
Homo sapiens |
|
| pmid |
sentence |
| 17189255 |
Ir-induced dna-pkcs phosphorylation at thr-2609 and ser-2056, however, exhibits distinct kinetics indicating that they are differentially regulated. Although dna-pkcs autophosphorylates itself at ser-2056 after ir, we have reported here that atm mediates dna-pkcs phosphorylation at thr-2609 as well as at the adjacent (s/t)q motifs within the thr-2609 cluster. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Cell cycle: G2/M phase transition |
| + |
PRKDC |
phosphorylation
|
HSP90AA1 |
0.438 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248887 |
Thr5 |
tQTQDQPM |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 2507541 |
Here we show that the dsDNA-activated protein kinase from human HeLa cells phosphorylates 2 threonine residues in the sequence PEETQTQDQPME at the amino terminus of human hsp90 alpha. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248888 |
Thr7 |
tQDQPMEE |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 2507541 |
Here we show that the dsDNA-activated protein kinase from human HeLa cells phosphorylates 2 threonine residues in the sequence PEETQTQDQPME at the amino terminus of human hsp90 alpha. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKDC | up-regulates
phosphorylation
|
CHEK2 |
0.609 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-133384 |
Thr68 |
SSLETVStQELYSIP |
Homo sapiens |
|
| pmid |
sentence |
| 15668230 |
We have found that dna-pk is the major constituent of an activity present in extracts of mammalian cells that phosphorylates chk2. Our results suggest that hypophosphorylated chk2 can be phosphorylated at thr68 by dna-pk in vitro. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Cell cycle: G2/M phase transition |
| + |
PRKDC | up-regulates activity
phosphorylation
|
YBX1 |
0.343 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277611 |
Thr89 |
EDVFVHQtAIKKNNP |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 36475703 |
The DNA-PK subunits and YB-1 phosphorylated at T89 were found colocalized suggesting their in vivo interaction.DNA-PK directly phosphorylates YB-1 and, this way, modulates YB-1 function. Point mutation of YB-1 at this residue abrogated the translocation of YB-1 into the nucleus. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
8-(4-dibenzothiophenyl)-2-(4-morpholinyl)-1-benzopyran-4-one | down-regulates
chemical inhibition
|
PRKDC |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-194865 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
XRCC6 | up-regulates
relocalization
|
PRKDC |
0.939 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183276 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19133841 |
Ku and dna-pkcs only interact in the presence of dna and recruitment of dna-pkcs to sites of dna damage in vivo is ku-dependent. Inward translocation of ku allows dna-pkcs to interact with the extreme termini of the dna, allowing two dna-pkcs molecules to interact across the dsb in a so-called synaptic complex . This interaction stimulates the kinase activity of dna-pkcs, promoting phosphorylation in trans across the dsb (discussed in more detail below). Once assembled at the dna ends, the dna-pkcs-ku-dsb complex serves to tether the ends of the dsb together and protects the dna ends from nuclease attack. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKDC | form complex 
binding
|
DNA-PK |
0.933 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-226026 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17308091 |
Complexes formed by interactions between Ku70, Ku80, and DNA-PKcs were well-established |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKDC | up-regulates
phosphorylation
|
H2AX |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-192443 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23620287 |
Dna-dependentprotein_ kinase_ (dna-pk) that phosphorylate h2ax at dsbs |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PIK-75 Hydrochloride | down-regulates
chemical inhibition
|
PRKDC |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-206214 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CTDSP1 | up-regulates activity
dephosphorylation
|
PRKDC |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277101 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32764831 |
CTDSP1 activates DNA-PKcs and enhances DNA-PKcs dependent topoI degradation in response to irinotecan .|Our novel finding indicates that CTDSP1 dephosphorylates DNA-PKcs, changes its kinase activity, and regulates irinotecan-induced topoI degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HOXB7 | up-regulates activity
binding
|
PRKDC |
0.338 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-226063 |
|
|
Homo sapiens |
SK-BR-3 Cell |
| pmid |
sentence |
| 17308091 |
Ku70 and Ku80 associated with HOXB7 in vivo. Ku70/Ku80 heterodimer formation is a prerequisite for HOXB7 binding. interaction between Ku70/80 and HOXB7 may affect the catalytic activity of DNA-PK. HOXB7 stimulates DNA-PK activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PI-103 | down-regulates
chemical inhibition
|
PRKDC |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-206175 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PP121 | down-regulates
chemical inhibition
|
PRKDC |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-206304 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKDC | up-regulates
phosphorylation
|
USF1 |
0.297 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-184849 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19303849 |
Feeding induces the recruitment of dna-pk to usf-1 and its phosphorylation, which then allows recruitment of p/caf, resulting in usf-1 acetylation and fas promoter activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP6C | up-regulates activity
dephosphorylation
|
PRKDC |
0.555 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277164 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19198648 |
In addition, siRNA knockdown of either PP6R1 or PP6 significantly decreased IR activation of DNA-PK, suggesting that PP6 activates DNA-PK by association and dephosphorylation.|PP6 may dephosphorylate sites in DNA-PKcs to reduce binding with heterodimer Ku proteins, because DNA-PK activation completely depends on Ku-mediated complex formation with DNA. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RNF144A | down-regulates quantity by destabilization
polyubiquitination
|
PRKDC |
0.548 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272213 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 24979766 |
We show that RNF144A induces ubiquitination of DNA-PKcs in vitro and in vivo and promotes its degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
PRKDC
- 
- 