| + |
CTDSPL2 | up-regulates quantity by stabilization 
dephosphorylation
|
STK35 |
0.284 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273775 |
Ser385 |
KVADFGLsKVCAGLA |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 35021089 |
We found that peptides corresponding to phosphoserines 194 and 216 of PDIK1L (S385 and S413 of STK35) were efficiently dephosphorylated by SCP4, whereas no activity was detected for the other two phosphopeptides (Figure 6D). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273776 |
Ser413 |
NVNKYWLsSACGSDF |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 35021089 |
We found that peptides corresponding to phosphoserines 194 and 216 of PDIK1L (S385 and S413 of STK35) were efficiently dephosphorylated by SCP4, whereas no activity was detected for the other two phosphopeptides (Figure 6D). |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
STK35 | form complex 
binding
|
STK35/PDIK1L |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273770 |
|
|
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 35021089 |
Through mass spectrometry analysis of affinity-purified complexes, we identify the kinase paralogs STK35 and PDIK1L as binding partners and substrates of the SCP4 phosphatase domain. We show that STK35 and PDIK1L function catalytically and redundantly in the same pathway as SCP4 to maintain AML proliferation and to support amino acid biosynthesis and transport. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
STK35
- 
- 