EC Number |
General Information |
Reference |
---|
3.1.3.86 | malfunction |
apoptosis in MDA-MB-231 cells is increased in SHIP2-depleted cells as compared to control cells |
751180 |
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 | 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 | malfunction |
disruption of the enzyme-Mena interaction in cancer cells leads to attenuated capacity for extracellular matrix degradation and invasion in vitro, as well as reduced metastasis in vivo |
751174 |
3.1.3.86 | malfunction |
enzyme deficiency leads to myeloproliferation and B-cell lymphoma in mice |
751768 |
3.1.3.86 | malfunction |
enzyme depletion inhibits cell migration of glioblastoma cells |
751179 |
3.1.3.86 | malfunction |
enzyme mutations are associated with opsismodysplasia. Mice expressing a germline catalytically inactive SHIP2 mutant protein are viable, but have defects in the development of muscle, adipose tissue and the female genital tract, as well as in somatic growth |
750315 |
3.1.3.86 | malfunction |
isoform SHIP2 inhibition or knockdown inhibits cell migration and reduces phosphorylated protein kinase B levels, resulting in sensitivity to chemotherapeutics |
751770 |
3.1.3.86 | metabolism |
the enzyme participates in the insulin signalling pathway in vivo |
679146 |
3.1.3.86 | physiological function |
high glucose induces SHIP2 mRNA and protein levels in HepG2 cells. Overexpression of a dominant negative mutant SHIP2 ameliorates high glucose-induced de novo lipogenesis and secretion of apoB containing lipoprotein in HepG2 cells. Overexpression of the SHIP2 dominant negative mutant decreases high glucose-induced apoB containing lipoproteins secretion via reduction in reactive oxygen species generation, JNK phosphorylation and Akt activation. AMPK/mTOR/SREBP1 is the signaling pathway that mediates the effects of SHIP2 modulation on hepatic de novo lipogenesis |
750611 |