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Literature summary for 3.1.3.86 extracted from

  • Paternotte, N.; Zhang, J.; Vandenbroere, I.; Backers, K.; Blero, D.; Kioka, N.; Vanderwinden, J.M.; Pirson, I.; Erneux, C.
    SHIP2 interaction with the cytoskeletal protein Vinexin (2005), FEBS J., 272, 6052-6066.
    View publication on PubMed
Search for more literature for 3.1.3.86

Activating Compound

Activating Compound Comment Organism Structure
additional information vinexin beta does not affect PtdIns(3,4,5)P3 5-phosphatase activity of SHIP2 Mus musculus

Cloned(Commentary)

Cloned (Comment) Organism
expression in COS-7 cells Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Mus musculus 16020
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
150000
-
 gel filtration Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
MEF cell
-
 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
PtdIns(3,4,5)P3 5-phosphatase
-
 Mus musculus
SH2 domain-containing inositol 5-phosphatase 2
-
 Mus musculus
SHIP2
-
 Mus musculus
src homology 2 domain-containing inositol 5-phosphatase 2
-
 Mus musculus

General Information

General Information Comment Organism
malfunction cell adhesion to collagen-I-coated dishes is decreased in SHIP2-deicient MEF cells compared with wild type cells Mus musculus
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 Mus musculus