| + |
MTMR1 | up-regulates quantity 
chemical modification
|
1-phosphatidyl-1D-myo-inositol 5-phosphate(3-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269805 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18429927 |
PtdIns(3,5)P2 can be dephosphorylated by the 3-phosphatase myotubularins (MTMs), leading to the production of PtdIns5P. Myotubularins also dephosphorylate PtdIns3P into PtdIns |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
1-phosphatidyl-1D-myo-inositol 5-phosphate(3-) | up-regulates quantity
precursor of
|
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate(5-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268865 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9367159 |
The enzymes that produce PtdIns-4,5-P2 in vitro fall into two related subfamilies (type I and type II PtdInsP-5-OH kinases, or PIP(5)Ks) based on their enzymatic properties and sequence similarities'. Here we have reinvestigated the substrate specificities of these enzymes. As expected, the type I enzyme phosphorylates PtdIns-4-P at the D-5 position of the inositol ring. Surprisingly, the type II enzyme, which is abundant in some tissues, phosphorylates PtdIns-5-P at the D-4 position, and thus should be considered as a 4-OH kinase, or PIP(4)K |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PIP4K2A | down-regulates quantity 
chemical modification
|
1-phosphatidyl-1D-myo-inositol 5-phosphate(3-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268866 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9367159 |
The enzymes that produce PtdIns-4,5-P2 in vitro fall into two related subfamilies (type I and type II PtdInsP-5-OH kinases, or PIP(5)Ks) based on their enzymatic properties and sequence similarities'. Here we have reinvestigated the substrate specificities of these enzymes. As expected, the type I enzyme phosphorylates PtdIns-4-P at the D-5 position of the inositol ring. Surprisingly, the type II enzyme, which is abundant in some tissues, phosphorylates PtdIns-5-P at the D-4 position, and thus should be considered as a 4-OH kinase, or PIP(4)K |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
1-phosphatidyl-1D-myo-inositol 5-phosphate(3-) | up-regulates activity
binding
|
SPOP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268863 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 18218622 |
Taken together, these data define a novel mechanism whereby the phosphoinositide PI5P leads to stimulation of Cul3-SPOP ubiquitin ligase activity and also implicate PIPKIIbeta as a key regulator of this signaling pathway through its association with the Cul3-SPOP complex. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate(5-) | up-regulates quantity
precursor of
|
1-phosphatidyl-1D-myo-inositol 5-phosphate(3-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269806 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18429927 |
PtdIns(3,5)P2 can be dephosphorylated by the 3-phosphatase myotubularins (MTMs), leading to the production of PtdIns5P. Myotubularins also dephosphorylate PtdIns3P into PtdIns |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
1-phosphatidyl-1D-myo-inositol 5-phosphate(3-)