+ |
CTDSPL2 | up-regulates quantity by stabilization
dephosphorylation
|
PDIK1L |
0.361 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273773 |
Ser194 |
KVADFGLsKVCSASG |
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-273774 |
Ser216 |
SVNKCFLsTACGTDF |
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 |
+ |
CTDSPL2 | up-regulates quantity by stabilization
dephosphorylation
|
STK35 |
0.285 |
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 |
+ |
CTDSPL2 | up-regulates quantity by expression
transcriptional regulation
|
HBE1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251779 |
|
|
Homo sapiens |
|
pmid |
sentence |
20932329 |
CTD small phosphatase like 2 (CTDSPL2) can increase ε- and γ-globin gene expression in K562 cells and CD34+ cells derived from umbilical cord blood. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CTDSPL2 | up-regulates quantity by expression
transcriptional regulation
|
HBG1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251778 |
|
|
Homo sapiens |
K-562 Cell |
pmid |
sentence |
20932329 |
CTD small phosphatase like 2 (CTDSPL2) can increase ε- and γ-globin gene expression in K562 cells and CD34+ cells derived from umbilical cord blood. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CTDSPL2 | up-regulates quantity by expression
transcriptional regulation
|
HBG2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251777 |
|
|
Homo sapiens |
K-562 Cell |
pmid |
sentence |
20932329 |
CTD small phosphatase like 2 (CTDSPL2) can increase ε- and γ-globin gene expression in K562 cells and CD34+ cells derived from umbilical cord blood. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CTDSPL2 | up-regulates quantity by stabilization
dephosphorylation
|
STK35/PDIK1L |
0.323 |
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 |