+ |
HUWE1 | down-regulates quantity by destabilization
polyubiquitination
|
POLL |
0.313 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272904 |
Lys27 |
ASSKVLAkIPRREEG |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
22203964 |
We found that Pol λ can be ubiquitinated by the E3 ligase Mule in vitro and in vivo and that this interaction is functionally connected to the phosphorylation-dependent stabilization of Pol λ by Cdk2/cyclinA. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272905 |
Lys273 |
AYSVQGDkWRALGYA |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
22203964 |
We found that Pol λ can be ubiquitinated by the E3 ligase Mule in vitro and in vivo and that this interaction is functionally connected to the phosphorylation-dependent stabilization of Pol λ by Cdk2/cyclinA. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272920 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
22203964 |
Identification of Mule as an E3 ubiquitin ligase regulating cellular protein levels of DNA polymerase λ.Here, we show that the E3 ligase Mule mediates the degradation of Pol λ and that the control of Pol λ levels by Mule has functional consequences for the ability of mammalian cells to deal with 8-oxo-G lesions. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
ATM | up-regulates activity
phosphorylation
|
POLL |
0.361 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273510 |
Thr204 |
EASDGEEtQVSAADL |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
28109743 |
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. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273836 |
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: |
2 |
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 |
+ |
CyclinA2/CDK2 | up-regulates quantity by stabilization
phosphorylation
|
POLL |
0.341 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273595 |
Thr553 |
GPGRVLPtPTEKDVF |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
18688254 |
Pol λ phosphorylation prevents degradation. Recently, we identified Pol λ as an interaction partner of cyclin-dependent kinase 2 (CDK2) that is central to the cell cycle G1/S transition and S-phase progression. This interaction leads to in vitro phosphorylation of Pol λ, and its in vivo phosphorylation pattern during cell cycle progression mimics the modulation of CDK2/cyclin A. Experiments with phosphorylation-defective mutants suggest that phosphorylation of Thr 553 is important for maintaining Pol λ stability, |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK2 | up-regulates quantity by stabilization
phosphorylation
|
POLL |
0.341 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276169 |
Thr553 |
GPGRVLPtPTEKDVF |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
18688254 |
Phosphorylation of DNA polymerase λ is required to maintain its stability. Recently, we identified Pol lambda as an interaction partner of cyclin-dependent kinase 2 (CDK2) that is central to the cell cycle G1/S transition and S-phase progression. Experiments with phosphorylation-defective mutants suggest that phosphorylation of Thr 553 is important for maintaining Pol lambda stability, as it is targeted to the proteasomal degradation pathway through ubiquitination unless this residue is phosphorylated. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |