LIPID MAPS® Gene/Proteome Database (LMPD)

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LMPD Record

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LMP011560

UniProt Annotations

Entry Information
Gene Nameinositol polyphosphate phosphatase-like 1a
Protein EntrySHP2A_DANRE
UniProt IDQ2I6J1
SpeciesZebrafish
Comments
Comment typeDescription
Catalytic Activity1-phosphatidyl-1D-myo-inositol 3,4,5- triphosphate + H(2)O = 1-phosphatidyl-1D-myo-inositol 3,4- diphosphate + phosphate.
DomainThe NPXY sequence motif found in many tyrosine- phosphorylated proteins is required for the specific binding of the PID domain. {ECO:0000250}.
DomainThe SH2 domain interacts with tyrosine phosphorylated forms of proteins. {ECO:0000250}.
FunctionPhosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol- 3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Plays a central role in regulation of PI3K-dependent insulin signaling, although the precise molecular mechanisms and signaling pathways remain unclear. Part of a signaling pathway that regulates actin cytoskeleton remodeling. Required for the maintenance and dynamic remodeling of actin structures as well as in endocytosis, having a major impact on ligand-induced EGFR internalization and degradation. Participates in regulation of cortical and submembraneous actin. Regulates cell adhesion and cell spreading. Acts as a negative regulator of the FC-gamma-RIIA receptor (FCGR2A). Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6 (By similarity). {ECO:0000250}.
PtmTyrosine phosphorylated by the members of the SRC family after exposure to a diverse array of extracellular stimuli.
SimilarityBelongs to the inositol 1,4,5-trisphosphate 5- phosphatase family. {ECO:0000305}.
SimilarityContains 1 SAM (sterile alpha motif) domain. {ECO:0000255|PROSITE-ProRule:PRU00184}.
SimilarityContains 1 SH2 domain. {ECO:0000255|PROSITE- ProRule:PRU00191}.
Subcellular LocationCytoplasm, cytosol {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell projection, filopodium {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Note=Translocates to membrane ruffles when activated, translocation is probably due to different mechanisms depending on the stimulus and cell type. {ECO:0000250}.