+ |
PDIK1L | form complex
binding
|
STK35/PDIK1L |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273771 |
|
|
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 |
+ |
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 |
+ |
CTDSPL2 | up-regulates quantity by stabilization
dephosphorylation
|
STK35/PDIK1L |
0.324 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273772 |
|
|
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.We provide evidence that SCP4 regulates STK35/PDIK1L through two distinct mechanisms: catalytic removal of inhibitory phosphorylation and by promoting kinase stability. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |