EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.3.36 | Listeria monocytogenes | - |
- |
- |
3.1.3.86 | Danio rerio | - |
- |
- |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
3.1.3.86 | neutrophil | - |
Danio rerio | - |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.1.3.36 | OCRL | - |
Listeria monocytogenes |
3.1.3.86 | SH2-domain-containing 5-inositol phosphatase | - |
Danio rerio |
3.1.3.86 | SHIP | - |
Danio rerio |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.1.3.36 | malfunction | in cells knocked down for OCRL, transfection of enzymatically active EGFP-OCRL-a (but not of a phosphatase-dead enzyme) decreases the levels of intracellular Listeria monocytogenes and of actin associated with invading bacteria | Listeria monocytogenes |
3.1.3.36 | malfunction | inactivation of OCRL by siRNA leads to an increase in the internalization levels of Listeria monocytogenes in HeLa cells. OCRL depletion does not increase but rather decreases the surface expression of the receptor Met | Listeria monocytogenes |
3.1.3.36 | physiological function | by reducing the levels of PI(4,5)P2 and PI(3,4,5)P3 at the plasma membrane, OCRL restricts infection through modulation of actin dynamics at bacterial internalization sites | Listeria monocytogenes |
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 | Danio rerio |
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 | Danio rerio |