| + |
CDK2 | down-regulates 
phosphorylation
|
TK1 |
0.301 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-95578 |
Ser13 |
LPTVLPGsPSKTRGQ |
Homo sapiens |
|
| pmid |
sentence |
| 12435275 |
Given that the dimeric form of tk1 is less active than the tetrameric, we propose that mitotic phosphorylation of serine-13 is of physiological importance, in that it may counteract atp-dependent activation of tk1 by affecting its quaternary structure, thus attenuating its enzymatic function at the g2/m phase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120372 |
Ser13 |
LPTVLPGsPSKTRGQ |
Homo sapiens |
|
| pmid |
sentence |
| 14697231 |
Given that the dimeric form of tk1 is less active than the tetrameric, we propose that mitotic phosphorylation of serine-13 is of physiological importance, in that it may counteract atp-dependent activation of tk1 by affecting its quaternary structure, thus attenuating its enzymatic function at the g2/m phase. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CDK1 | down-regulates
phosphorylation
|
TK1 |
0.521 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120368 |
Ser13 |
LPTVLPGsPSKTRGQ |
Homo sapiens |
|
| pmid |
sentence |
| 14697231 |
Given that the dimeric form of tk1 is less active than the tetrameric, we propose that mitotic phosphorylation of serine-13 is of physiological importance, in that it may counteract atp-dependent activation of tk1 by affecting its quaternary structure, thus attenuating its enzymatic function at the g2/m phase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-95574 |
Ser13 |
LPTVLPGsPSKTRGQ |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 12435275 |
Given that the dimeric form of tk1 is less active than the tetrameric, we propose that mitotic phosphorylation of serine-13 is of physiological importance, in that it may counteract atp-dependent activation of tk1 by affecting its quaternary structure, thus attenuating its enzymatic function at the g2/m phase. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
FZR1 | down-regulates quantity by destabilization
binding
|
TK1 |
0.348 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272945 |
|
|
in vitro |
|
| pmid |
sentence |
| 14701726 |
We show that hTK1 is degraded via a ubiquitin-proteasome pathway in mammalian cells and that anaphase-promoting complex/cyclosome (APC/C) activator Cdh1 is not only a necessary but also a rate-limiting factor for mitotic degradation of hTK1. By in vitro ubiquitinylation assays, we demonstrated that hTK1 is targeted for degradation by the APC/C-Cdh1 ubiquitin ligase dependent on this KEN box motif. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
APC-c | down-regulates quantity by destabilization
polyubiquitination
|
TK1 |
0.25 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272946 |
|
|
in vitro |
|
| pmid |
sentence |
| 14701726 |
We show that hTK1 is degraded via a ubiquitin-proteasome pathway in mammalian cells and that anaphase-promoting complex/cyclosome (APC/C) activator Cdh1 is not only a necessary but also a rate-limiting factor for mitotic degradation of hTK1. By in vitro ubiquitinylation assays, we demonstrated that hTK1 is targeted for degradation by the APC/C-Cdh1 ubiquitin ligase dependent on this KEN box motif. |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
TK1
- 
- 