+ |
MAPK6 | up-regulates activity
phosphorylation
|
TDP2 |
0.386 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277188 |
Ser60 |
EMERALNsYFEPPVE |
in vitro |
|
pmid |
sentence |
26701725 |
In the current study, we have found that ERK3, an atypical MAPK, phosphorylates TDP2 at S60 and regulates TDP2's phosphodiesterase activity, thereby cooperatively protecting lung cancer cells against Top2 inhibitors-induced DNA damage and growth inhibition. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
ACVR1B | up-regulates activity
phosphorylation
|
TDP2 |
0.285 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262611 |
Thr88 |
PKTYVDLtNEETTDS |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
18039968 |
ALK4 phosphorylated TTRAP in vitro (Fig. 6A). The band migrating at the position of TTRAP was excised and analyzed by LC-MS/MS. One TTRAP peptide was phosphorylated either on T88 and T92, or on T92 only (Fig. 6B). |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262612 |
Thr92 |
VDLTNEEtTDSTTSK |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
18039968 |
ALK4 phosphorylated TTRAP in vitro (Fig. 6A). The band migrating at the position of TTRAP was excised and analyzed by LC-MS/MS. One TTRAP peptide was phosphorylated either on T88 and T92, or on T92 only (Fig. 6B).We tested in vivo phosphorylation of Strep-TTRAP by co-expression with mouse Alk4 in HEK293T cells, and affinity-purified TTRAP. In this preparation TTRAP-specific peptides were reproducibly found in both the singly (T92) and doubly phosphorylated form (T88/T92). mutant TTRAPT88A,T92A is not able to rescue the TtrapMO phenotype, suggesting that phosphorylation of Ttrap on Thr88 and Thr92 is essential for Ttrap function. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
TDP2 | up-regulates activity
binding
|
TRAF6 |
0.386 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277189 |
|
|
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
21980489 |
TTRAP associates with TRAF6.The TAK1-TTRAP-TRAF6 complex is stabilized by ubiquitylation and recruited to TβRI. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |