| + |
MAPK1 | down-regulates activity 
phosphorylation
|
TPPP |
0.368 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262928 |
Ser160 |
GVTKAISsPTVSRLT |
in vitro |
|
| pmid |
sentence |
| 17693641 |
Here we show that TPPP induces tubulin self-assembly into intact frequently bundled microtubules, and that the phosphorylation of specific sites distinctly affects the function of TPPP. The phosphorylation sites Thr(14), Ser(18), Ser(160) for Cdk5; Ser(18), Ser(160) for ERK2, and Ser(32) for PKA were identified by mass spectrometry. The phosphorylation by ERK2 or Cdk5 resulted in the loss of microtubule-assembling activity of TPPP. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262929 |
Ser18 |
ANRTPPKsPGDPSKD |
in vitro |
|
| pmid |
sentence |
| 17693641 |
Here we show that TPPP induces tubulin self-assembly into intact frequently bundled microtubules, and that the phosphorylation of specific sites distinctly affects the function of TPPP. The phosphorylation sites Thr(14), Ser(18), Ser(160) for Cdk5; Ser(18), Ser(160) for ERK2, and Ser(32) for PKA were identified by mass spectrometry. The phosphorylation by ERK2 or Cdk5 resulted in the loss of microtubule-assembling activity of TPPP. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
CDK5 | down-regulates activity
phosphorylation
|
TPPP |
0.421 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262931 |
Ser160 |
GVTKAISsPTVSRLT |
in vitro |
|
| pmid |
sentence |
| 17693641 |
Here we show that TPPP induces tubulin self-assembly into intact frequently bundled microtubules, and that the phosphorylation of specific sites distinctly affects the function of TPPP. The phosphorylation sites Thr(14), Ser(18), Ser(160) for Cdk5; Ser(18), Ser(160) for ERK2, and Ser(32) for PKA were identified by mass spectrometry. The phosphorylation by ERK2 or Cdk5 resulted in the loss of microtubule-assembling activity of TPPP. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262932 |
Ser18 |
ANRTPPKsPGDPSKD |
in vitro |
|
| pmid |
sentence |
| 17693641 |
Here we show that TPPP induces tubulin self-assembly into intact frequently bundled microtubules, and that the phosphorylation of specific sites distinctly affects the function of TPPP. The phosphorylation sites Thr(14), Ser(18), Ser(160) for Cdk5; Ser(18), Ser(160) for ERK2, and Ser(32) for PKA were identified by mass spectrometry. The phosphorylation by ERK2 or Cdk5 resulted in the loss of microtubule-assembling activity of TPPP. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262933 |
Thr14 |
PAKAANRtPPKSPGD |
in vitro |
|
| pmid |
sentence |
| 17693641 |
Here we show that TPPP induces tubulin self-assembly into intact frequently bundled microtubules, and that the phosphorylation of specific sites distinctly affects the function of TPPP. The phosphorylation sites Thr(14), Ser(18), Ser(160) for Cdk5; Ser(18), Ser(160) for ERK2, and Ser(32) for PKA were identified by mass spectrometry. The phosphorylation by ERK2 or Cdk5 resulted in the loss of microtubule-assembling activity of TPPP. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
PRKACA |
phosphorylation
|
TPPP |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262930 |
Ser32 |
DRAAKRLsLESEGAG |
in vitro |
|
| pmid |
sentence |
| 17693641 |
Here we show that TPPP induces tubulin self-assembly into intact frequently bundled microtubules, and that the phosphorylation of specific sites distinctly affects the function of TPPP. The phosphorylation sites Thr(14), Ser(18), Ser(160) for Cdk5; Ser(18), Ser(160) for ERK2, and Ser(32) for PKA were identified by mass spectrometry. The phosphorylation by ERK2 or Cdk5 resulted in the loss of microtubule-assembling activity of TPPP. Thus our data suggest that ERK2 or Cdk5 can perturb the interaction of TPPP with tubulin, in contrast to PKA that is ineffective in this respect. |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
TPPP
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