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Literature summary for 3.1.3.36 extracted from

  • Kato, K.; Yazawa, T.; Taki, K.; Mori, K.; Wang, S.; Nishioka, T.; Hamaguchi, T.; Itoh, T.; Takenawa, T.; Kataoka, C.; Matsuura, Y.; Amano, M.; Murohara, T.; Kaibuchi, K.
    The inositol 5-phosphatase SHIP2 is an effector of RhoA and is involved in cell polarity and migration (2012), Mol. Biol. Cell, 23, 2593-2604.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
D193/E195A binding activity is much lower compared to wild-type fragment consisting of amino acids 124-314. Binding activity for active RhoA is dramatically reduced compared to wild-type Homo sapiens
D223/K224A binding activity is much lower compared to wild-type fragment consisting of amino acids 124-314 Homo sapiens
additional information using different fragments of SHIP2 it is shown that the SHIP2-NDELTASH2-4 fragment (124-314 amino acids) is sufficient to bind to RhoA. These results indicate that active RhoA directly interacts with SHIP2 at the N-terminal region between the SH2 and catalytic domains Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens SHIP2 interacts with RhoA in a GTP-dependent manner ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
glioblastoma cell line U-251 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information SHIP2 interacts with RhoA in a GTP-dependent manner Homo sapiens ?
-
?

Synonyms

Synonyms Comment Organism
SHIP2
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Homo sapiens

General Information

General Information Comment Organism
malfunction depletion of SHIP2 attenuates cell polarization and migration, which is rescued by wild-type SHIP2 but not by a mutant defective in RhoA binding. In addition, the depletion of SHIP2 impairs the proper localization of phosphatidylinositol 3,4,5-trisphosphate, which is not restored by a mutant defective in RhoA binding Homo sapiens
physiological function SHIP2 restricts PI(3,4,5)P3 localization at the leading edge in migrating cells to thereby control the cell polarity downstream of RhoA Homo sapiens