EC Number   |
General Information |
Reference  |
|---|
   3.1.3.86 | metabolism |
the enzyme participates in the insulin signalling pathway in vivo |
679146 |
| 3.1.3.86 | physiological function |
isoforms SHIP2 and SHIP1 have a different hierarchy of binding SH3-domain containing proteins |
714601 |
| 3.1.3.86 | physiological function |
PR130/Balpha1 and SHIP2 partially colocalize in untreated HeLa cells, and both translocate to the cell membrane on epidermal growth factor stimulation. Protein phosphatase 2A PR130/Balpha1 subunit binds to the SH2 domain-containing inositol polyphosphate 5-phosphatase 2 and prevents epidermal growth factor-induced epidermal growth factor receptor degradation sustaining epidermal growth factor-mediated signaling |
714939 |
| 3.1.3.86 | malfunction |
cell adhesion to collagen-I-coated dishes is decreased in SHIP2-deicient MEF cells compared with wild type cells |
714946 |
| 3.1.3.86 | physiological function |
SHIP2 interaction with vinexin alpha promotes the localization of SHIP2 at the periphery of the cells leaving its catalytic site intact. SHIP2 is active both as a PtdIns(3,4,5)P3 5-phosphatase and as a modulator of focal contact formation |
714946 |
| 3.1.3.86 | physiological function |
SHIP is involved in platelet activation evoked by thrombin |
715430 |
| 3.1.3.86 | physiological function |
the Src homology 2 domain containing inositol 5-phosphatase SHIP2 is recruited to the epidermal growth factor receptor and dephosphorylates phosphatidylinositol 3,4,5-trisphosphate in epidermal growth factor-stimulated COS-7 cells |
715452 |
| 3.1.3.86 | malfunction |
depletion of SHIP 5'-phosphatases increases neutrophil wound attraction and random motility through a PI3K-dependent pathway. Ectopic expression of the SHIP1 phosphatase domain impairs neutrophil migration |
732045 |
| 3.1.3.86 | physiological function |
SHIP phosphatases serve as a brake that limit neutrophil motility and inflammation, at least in part through their effects on PI3K signaling |
732045 |
| 3.1.3.86 | physiological function |
overexpression of the wild-ype SHIP2 gene leads to a higher total lipid content (28%) compared to control, whereas overexpression of the dominant negative SHIP2 gene reduces total lipid content in oleate treated cells by 40%. Overexpression of SHIP2 wild-type also leads to a significant increase in both secretion of apoB100 containing lipoproteins and de novo lipogenesis. Overexpression of the SHIP2 dominant negative gene prevents oleate-induced de novo lipogenesis and secretion of apoB100 containing lipoproteins in HepG2 cells |
749802 |
