+ |
CSNK2A1 | up-regulates
phosphorylation
|
PIP4K2A |
0.43 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-71014 |
Ser304 |
DGEEEGEsDGTHPVG |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
10508590 |
Here, we demonstrate the partial purification of a protein kinase that phosphorylates the type iialpha pip kinase at a single site unique to that isoform - ser304. This kinase was identified as protein kinase ck2 (formerly casein kinase 2). Mutation of ser304 to aspartate to mimic its phosphorylation had no effect on pip kinase activity, but promoted both redistribution of the green fluorescent protein (gfp)-tagged enzyme in hela cells from the cytosol to the plasma membrane, and membrane ruffling. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRKD1 | down-regulates
phosphorylation
|
PIP4K2A |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-145370 |
Thr376 |
KAAHAAKtVKHGAGA |
Homo sapiens |
|
pmid |
sentence |
16563698 |
We conclude that the type ii pip kinases are physiological targets for pkd phosphorylation, and that this modification is likely to regulate inositol lipid turnover by inhibition of these lipid kinases. |
|
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 |
+ |
ARF6 | up-regulates activity
|
PIP4K2A |
0.344 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264911 |
|
|
Rattus norvegicus |
Pyramidal Neuron |
pmid |
sentence |
14565977 |
Effects of ARF6 upon Axonogenesis Are Mediated by Phosphatidyl-inositol-4-phosphate 5-Kinase α. activated ARF6 stimulates the lipid-modifying enzyme PI(4)P 5-Kinase, leading to local increases in plasma membrane PIP2 and changes in actin dynamics. Alternatively, activation of Rac1 by upstream Rac1 activators or indirectly by ARF6-GTP results in stimulation of actin polymerization. |
|
Publications: |
1 |
Organism: |
Rattus Norvegicus |
+ |
PIP4K2A | up-regulates quantity
chemical modification
|
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate(5-) |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-268864 |
|
|
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 |