+ |
PLK1 |
phosphorylation
|
PKMYT1 |
0.707 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249207 |
Ser426 |
CSLLLDSsLSSNWDD |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
12738781 |
These results suggest that Ser-426 is a major phosphorylation site by Plk1, and Thr-495 is a second major site. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249208 |
Thr495 |
LLSLFEDtLDPT |
Homo sapiens |
|
pmid |
sentence |
12738781 |
These results suggest that Ser-426 is a major phosphorylation site by Plk1, and Thr-495 is a second major site. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
PLK1 | down-regulates activity
phosphorylation
|
PKMYT1 |
0.707 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263096 |
Ser426 |
CSLLLDSsLSSNWDD |
in vitro |
|
pmid |
sentence |
12738781 |
Here, we have shown that Plk1 is responsible for part of the phosphorylation of Myt1 during M phase. The kinase activity of human Myt1 is reported to be decreased during M phase, and the decreased activity correlates with hyperphosphorylated forms of Myt1 (35, 37). We then tested the ability of these mutant forms of Myt1 (GST fusion proteins), to serve as a substrate for Plk1 in vitro. Quantification of the result (Fig. 5C) showed that Ser-426 is the major phosphorylation site by Plk1 in vitro and Thr-495 the second major site. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263097 |
Thr495 |
LLSLFEDtLDPT |
in vitro |
|
pmid |
sentence |
12738781 |
Here, we have shown that Plk1 is responsible for part of the phosphorylation of Myt1 during M phase. The kinase activity of human Myt1 is reported to be decreased during M phase, and the decreased activity correlates with hyperphosphorylated forms of Myt1 (35, 37). We then tested the ability of these mutant forms of Myt1 (GST fusion proteins), to serve as a substrate for Plk1 in vitro. Quantification of the result (Fig. 5C) showed that Ser-426 is the major phosphorylation site by Plk1 in vitro and Thr-495 the second major site. |
|
Publications: |
2 |
Organism: |
In Vitro |
+ |
PKMYT1 | down-regulates
phosphorylation
|
CDK1 |
0.739 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-45725 |
Thr14 |
IEKIGEGtYGVVYKG |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
9001210 |
Myt1hu preferentially phosphorylates cdc2 on threonine 14 in a cyclin-dependent manner;phosphorylation of threonine 14 and tyrosine 15 is inhibitory. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-45729 |
Tyr15 |
EKIGEGTyGVVYKGR |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
9001210 |
Myt1hu preferentially phosphorylates cdc2 on threonine 14 in a cyclin-dependent manner;phosphorylation of threonine 14 and tyrosine 15 is inhibitory. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
MAPK8 | up-regulates
phosphorylation
|
PKMYT1 |
0.342 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-183899 |
|
|
Homo sapiens |
Skin Cancer Cell |
pmid |
sentence |
19204086 |
A kinase assay using gst-myt1 revealed that active jnk1 or jnk3, but not jnk2, phosphorylated myt1 in vitro. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |