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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
glioblastoma cell line | U-251 | Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | SHIP2 interacts with RhoA in a GTP-dependent manner | Homo sapiens | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
SHIP2 | - |
Homo sapiens |
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 |