Inppl1
entrez
16332
canonical
uniprot
Q6P549
canonical
ensembl
ENSMUSG00000032737
resolver
ensp
ENSMUSP00000048057
resolver
ensp
ENSMUSP00000132883
resolver
ensp
ENSMUSP00000139910
resolver
ensp
ENSMUSP00000197587
resolver
ensp
ENSMUSP00000197593
resolver
ensp
ENSMUSP00000197608
resolver
enst
ENSMUST00000035836
resolver
enst
ENSMUST00000165052
resolver
genesymbol
Inppl1
resolver
genesymbol_syn
Ship2
resolver
uniprot
O08611
resolver
uniprot
Q0VDX5
resolver
uniprot
Q80YB9
resolver
uniprot
Q9JLL7
resolver
uniprot_entry
SHIP2_MOUSE
resolver
uniprot_sec
O08611
resolver
uniprot_sec
Q0VDX5
resolver
uniprot_sec
Q80YB9
resolver
uniprot_sec
Q9JLL7
resolver
activity_regulation
ACTIVITY REGULATION: Activated upon translocation to the sites of synthesis of PtdIns(3,4,5)P3 in the membrane. Enzymatic activity is enhanced in the presence of phosphatidylserine (By similarity). {ECO:0000250}.
uniprot
proteins
amino_acid_sequence
MASVCGTPSPGGALGSPAPAWYHRDLSRAAAEELLARAGRDGSFLVRDSESVAGAFALCVLYQKHVHTYRILPDGEDFLAVQTSQGVPVRRFQTLGELIGLYAQPNQGLVCALLLPVEGEREPDPPDDRDASDVEDEKPPLPPRSGSTSISAPVGPSSPLPTPETPTTPAAESTPNGLSTVSHEYLKGSYGLDLEAVRGGASNLPHLTRTLVTSCRRLHSEVDKVLSGLEILSKVFDQQSSPMVTRLLQQQSLPQTGEQELESLVLKLSVLKDFLSGIQKKALKALQDMSSTAPPAPLQPSIRKAKTIPVQAFEVKLDVTLGDLTKIGKSQKFTLSVDVEGGRLVLLRRQRDSQEDWTTFTHDRIRQLIKSQRVQNKLGVVFEKEKDRTQRKDFIFVSARKREAFCQLLQLMKNRHSKQDEPDMISVFIGTWNMGSVPPPKNVTSWFTSKGLGKALDEVTVTIPHDIYVFGTQENSVGDREWLDLLRGGLKELTDLDYRPIAMQSLWNIKVAVLVKPEHENRISHVSTSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNCHLTSGNEKTTRRNQNYLDILRLLSLGDRQLSAFDISLRFTHLFWFGDLNYRLDMDIQEILNYISRREFEPLLRVDQLNLEREKHKVFLRFSEEEISFPPTYRYERGSRDTYAWHKQKPTGVRTNVPSWCDRILWKSYPETHIICNSYGCTDDIVTSDHSPVFGTFEVGVTSQFISKKGLSKTSDQAYIEFESIEAIVKTASRTKFFIEFYSTCLEEYKKSFENDAQSSDNINFLKVQWSSRQLPTLKPILADIEYLQDQHLLLTVKSMDGYESYGECVVALKSMIGSTAQQFLTFLSHRGEETGNIRGSMKVRVPTERLGTRERLYEWISIDKDDTGAKSKVPSVSRGSQEHRSGSRKPASTETSCPLSKLFEEPEKPPPTGRPPAPPRAVPREEPLNPRLKSEGTSEQEGVAAPPPKNSFNNPAYYVLEGVPHQLLPLEPPSLARAPLPPATKNKVAITVPAPQLGRHRTPRVGEGSSSDEDSGGTLPPPDFPPPPLPDSAIFLPPNLDPLSMPVVRGRSGGEARGPPPPKAHPRPPLPPGTSPASTFLGEVASGDDRSCSVLQMAKTLSEVDYAPGPGRSALLPNPLELQPPRGPSDYGRPLSFPPPRIRESIQEDLAEEAPCPQGGRASGLGEAGMGAWLRAIGLERYEEGLVHNGWDDLEFLSDITEEDLEEAGVQDPAHKRLLLDTLQLSK
uniprot
proteins
ec_number
3.1.3.86
uniprot
proteins
function
FUNCTION: Phosphatidylinositol (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 (PubMed:10958682). Required for correct mitotic spindle orientation and therefore progression of mitosis (By similarity). Plays a central role in regulation of PI3K-dependent insulin signaling, although the precise molecular mechanisms and signaling pathways remain unclear (PubMed:11343120). While overexpression reduces both insulin-stimulated MAP kinase and Akt activation, its absence does not affect insulin signaling or GLUT4 trafficking (PubMed:14744864). Confers resistance to dietary obesity (PubMed:15654325). May act by regulating AKT2, but not AKT1, phosphorylation at the plasma membrane (PubMed:14744864). Part of a signaling pathway that regulates actin cytoskeleton remodeling (By similarity). 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 (By similarity). Participates in regulation of cortical and submembraneous actin by hydrolyzing PtdIns(3,4,5)P3 thereby regulating membrane ruffling (By similarity). Regulates cell adhesion and cell spreading (PubMed:29749928). Required for HGF-mediated lamellipodium formation, cell scattering and spreading (By similarity). Acts as a negative regulator of EPHA2 receptor endocytosis by inhibiting via PI3K-dependent Rac1 activation (By similarity). Acts as a regulator of neuritogenesis by regulating PtdIns(3,4,5)P3 level and is required to form an initial protrusive pattern, and later, maintain proper neurite outgrowth (By similarity). Acts as a negative regulator of the FC-gamma-RIIA receptor (FCGR2A) (By similarity). Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems (PubMed:10789675, PubMed:15456754). Upon stimulation by EGF, it is recruited by EGFR and dephosphorylates PtdIns(3,4,5)P3 (By similarity). Plays a negative role in regulating the PI3K-PKB pathway, possibly by inhibiting PKB activity (By similarity). Down-regulates Fc-gamma-R-mediated phagocytosis in macrophages independently of INPP5D/SHIP1 (PubMed:15557176, PubMed:16179375). In macrophages, down-regulates NF-kappa-B-dependent gene transcription by regulating macrophage colony-stimulating factor (M-CSF)-induced signaling (PubMed:15557176, PubMed:16179375). Plays a role in the localization of AURKA and NEDD9/HEF1 to the basolateral membrane at interphase in polarized cysts, thereby mediates cell cycle homeostasis, cell polarization and cilia assembly (By similarity). Additionally promotion of cilia growth is also facilitated by hydrolysis of (PtdIns(3,4,5)P3) to PtdIns(3,4)P2 (By similarity). Promotes formation of apical membrane-initiation sites during the initial stages of lumen formation via Rho family-induced actin filament organization and CTNNB1 localization to cell-cell contacts (By similarity). May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6. Involved in endochondral ossification (By similarity). {ECO:0000250|UniProtKB:F1PNY0, ECO:0000250|UniProtKB:O15357, ECO:0000250|UniProtKB:Q9WVR3, ECO:0000269|PubMed:10789675, ECO:0000269|PubMed:10958682, ECO:0000269|PubMed:11343120, ECO:0000269|PubMed:14744864, ECO:0000269|PubMed:15456754, ECO:0000269|PubMed:15557176, ECO:0000269|PubMed:15654325, ECO:0000269|PubMed:16179375, ECO:0000269|PubMed:29749928}.
uniprot
proteins
mass_dalton
138973
uniprot
proteins
mutagenesis
MUTAGEN 47; /note="R->A: Does not affect the ability to inhibit PKB activity."; /evidence="ECO:0000269|PubMed:10958682"; MUTAGEN 608; /note="D->A: Abolishes both enzyme activity and ability to inhibit PKB activity."; /evidence="ECO:0000269|PubMed:10958682"; MUTAGEN 690; /note="C->A: Induces little effect."; /evidence="ECO:0000269|PubMed:10958682"; MUTAGEN 692; /note="R->A: Still partially active."; /evidence="ECO:0000269|PubMed:10958682"; MUTAGEN 987; /note="Y->F: Does not affect the ability to inhibit PKB activity."; /evidence="ECO:0000269|PubMed:10958682"; MUTAGEN 1222; /note="D->A: Abolishes interaction with EPHA2 SAM domain."; /evidence="ECO:0000269|PubMed:29749928"; MUTAGEN 1226; /note="F->A,L: Abolishes interaction with EPHA2 SAM domain."; /evidence="ECO:0000269|PubMed:29749928
uniprot
proteins
post_translational_modification
PTM: Tyrosine phosphorylated by the members of the SRC family after exposure to a diverse array of extracellular stimuli such as insulin, growth factors such as EGF or PDGF, chemokines, integrin ligands and hypertonic and oxidative stress. May be phosphorylated upon IgG receptor FCGR2B-binding. Phosphorylated at Tyr-987 following cell attachment and spreading. Phosphorylated at Tyr-1161 following EGF signaling pathway stimulation (By similarity). {ECO:0000250}.
uniprot
proteins
protein_family
4
uniprot
proteins
protein_family
5-trisphosphate 5-phosphatase family
uniprot
proteins
protein_family
Inositol 1
uniprot
proteins
pubmed
10610720
uniprot
proteins
pubmed
10789675
uniprot
proteins
pubmed
10958682
uniprot
proteins
pubmed
11343120
uniprot
proteins
pubmed
12145149
uniprot
proteins
pubmed
14744864
uniprot
proteins
pubmed
15456754
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15492005
uniprot
proteins
pubmed
15557176
uniprot
proteins
pubmed
15654325
uniprot
proteins
pubmed
16179375
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21624956
uniprot
proteins
pubmed
29749928
uniprot
proteins
pubmed
9126384
uniprot
proteins
pubmed
9485206
uniprot
proteins
sequence_length
1257
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9WVR3}. Cytoplasm, cytoskeleton {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:Q9WVR3}; Peripheral membrane protein. Cell projection, filopodium {ECO:0000250|UniProtKB:O15357}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:O15357}. Basal cell membrane {ECO:0000250|UniProtKB:F1PNY0}. Nucleus {ECO:0000250|UniProtKB:D7PF45}. Nucleus speckle {ECO:0000250|UniProtKB:D7PF45}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:F1PNY0}. Note=Translocates to membrane ruffles when activated, translocation is probably due to different mechanisms depending on the stimulus and cell type. Partly translocated via its SH2 domain which mediates interaction with tyrosine phosphorylated receptors such as the FC-gamma-RIIB receptor (FCGR2B). Tyrosine phosphorylation may also participate in membrane localization. Insulin specifically stimulates its redistribution from the cytosol to the plasma membrane. Recruited to the membrane following M-CSF stimulation. In activated spreading platelets, localizes with actin at filopodia, lamellipodia and the central actin ring.
uniprot
proteins