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Literature summary for 3.1.3.36 extracted from

  • Mondal, S.; Subramanian, K.K.; Sakai, J.; Bajrami, B.; Luo, H.R.
    Phosphoinositide lipid phosphatase SHIP1 and PTEN coordinate to regulate cell migration and adhesion (2012), Mol. Biol. Cell, 23, 1219-1230.
    View publication on PubMedView publication on EuropePMC

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Mus musculus 5829
-
plasma membrane SHIP1 is localized to the membrane during cell adhesion Mus musculus 5886
-

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein SHIP1 is localized to the membrane and is tyrosine phosphorylated during cell adhesion Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
neutrophil
-
Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate + H2O
-
Mus musculus 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate + phosphate
-
?

Synonyms

Synonyms Comment Organism
SHIP1
-
Mus musculus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Mus musculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Mus musculus

General Information

General Information Comment Organism
malfunction SHIP1-/- neutrophils are extremely adherent, which results in impaired cell migration. Reduction in cell adhesion can rescue the defect in cell migration in SHIP1-/- neutrophils. Cell adhesion results in excessive Akt activation in SHIP1-/- cells Mus musculus
physiological function during cell migration SHIP1 acts a negative regulator of PtdIns(3,4,5)P3 formation at the cell-substratum interface, preventing the formation of top-down PtdIns(3,4,5) P3 polarity and facilitating proper cell attachment and detachment during chemotaxis Mus musculus