| Gene Symbol |
Inppl1
|
| Entrez Gene |
65038
|
| Alt Symbol |
Ship2
|
| Species |
Rat
|
| Gene Type |
protein-coding
|
| Description |
inositol polyphosphate phosphatase-like 1
|
| Other Description |
INPPL-1|SH2 domain-containing inositol 5'-phosphatase 2|SH2 domain-containing inositol phosphatase 2|SH2 domain-containing inositol-5'-phosphatase 2|SH2-containing inositol phosphatase 2|SHIP-2|inositol polyphosphate phosphatase-like protein 1|phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2|phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2
|
| Swissprots |
Q9R1V2 Q9WVR3
|
| Accessions |
EDM18265 EDM18266 EDM18267 EDM18268 EDM18269 EDM18270 EDM18271 EDM18272 Q9WVR3 AB011439 BAA81818 AB025794 BAA82308 BQ199460 CA506674 CK653108 FQ139232 NM_001270843 NP_001257772 NM_022944 NP_075233
|
| Function |
Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol- 3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Plays a central role in regulation of PI3K-dependent insulin signaling, although the precise molecular mechanisms and signaling pathways remain unclear. While overexpression reduces both insulin-stimulated MAP kinase and Akt activation, its absence does not affect insulin signaling or GLUT4 trafficking. Confers resistance to dietary obesity. May act by regulating AKT2, but not AKT1, phosphorylation at the plasma membrane. Part of a signaling pathway that regulates actin cytoskeleton remodeling. Required for the maintenance and dynamic remodeling of actin structures as well as in endocytosis, having a major impact on ligand-induced EGFR internalization and degradation. Participates in regulation of cortical and submembraneous actin by hyd
|
| Subcellular Location |
Cytoplasm, cytosol {ECO:0000269|PubMed:12351701}. Cytoplasm, cytoskeleton {ECO:0000250}. Membrane {ECO:0000269|PubMed:12351701}; Peripheral membrane protein {ECO:0000269|PubMed:12351701}. Cell projection, filopodium {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Note=Translocates to membrane ruffles when activated, translocation is probably due to different mechanisms depending on the stimulus and cell type. Partly translocated via its SH2 domain which mediates interaction with tyrosine phosphorylated receptors such as the FC-gamma-RIIB receptor (FCGR2B). Tyrosine phosphorylation may also participate in membrane localization. Insulin specifically stimulates its redistribution from the cytosol to the plasma membrane. Recruited to the membrane following M-CSF stimulation. In activated spreading platelets, localizes with actin at filopodia, lamellipodia and the central actin ring.
|
| Top Pathways |
B cell receptor signaling pathway, Insulin signaling pathway, Fc gamma R-mediated phagocytosis, Inositol phosphate metabolism, Phosphatidylinositol signaling system
|