Inpp5d
entrez
16331
canonical
uniprot
Q9ES52
canonical
ensembl
ENSMUSG00000026288
resolver
ensp
ENSMUSP00000044647
resolver
ensp
ENSMUSP00000127941
resolver
ensp
ENSMUSP00000131244
resolver
genesymbol
Inpp5d
resolver
genesymbol_syn
7a33
resolver
genesymbol_syn
Ship
resolver
genesymbol_syn
Ship1
resolver
uniprot
Q3UPF9
resolver
uniprot
Q4U212
resolver
uniprot
Q61034
resolver
uniprot
Q61173
resolver
uniprot
Q61181
resolver
uniprot
Q9JKR7
resolver
uniprot
Q9JLF9
resolver
uniprot
Q9JLG0
resolver
uniprot
Q9QVN8
resolver
uniprot
Q9WUC2
resolver
uniprot_entry
SHIP1_MOUSE
resolver
uniprot_sec
Q3UPF9
resolver
uniprot_sec
Q4U212
resolver
uniprot_sec
Q61034
resolver
uniprot_sec
Q61173
resolver
uniprot_sec
Q61181
resolver
uniprot_sec
Q9JKR7
resolver
uniprot_sec
Q9JLF9
resolver
uniprot_sec
Q9JLG0
resolver
uniprot_sec
Q9QVN8
resolver
uniprot_sec
Q9WUC2
resolver
activity_regulation
ACTIVITY REGULATION: Activated upon translocation to the sites of synthesis of PtdIns(3,4,5)P3 in the membrane.
uniprot
proteins
amino_acid_sequence
MPAMVPGWNHGNITRSKAEELLSRAGKDGSFLVRASESIPRAYALCVLFRNCVYTYRILPNEDDKFTVQASEGVPMRFFTKLDQLIDFYKKENMGLVTHLQYPVPLEEEDAIDEAEEDTVESVMSPPELPPRNIPMSAGPSEAKDLPLATENPRAPEVTRLSLSETLFQRLQSMDTSGLPEEHLKAIQDYLSTQLLLDSDFLKTGSSNLPHLKKLMSLLCKELHGEVIRTLPSLESLQRLFDQQLSPGLRPRPQVPGEASPITMVAKLSQLTSLLSSIEDKVKSLLHEGSESTNRRSLIPPVTFEVKSESLGIPQKMHLKVDVESGKLIVKKSKDGSEDKFYSHKKILQLIKSQKFLNKLVILVETEKEKILRKEYVFADSKKREGFCQLLQQMKNKHSEQPEPDMITIFIGTWNMGNAPPPKKITSWFLSKGQGKTRDDSADYIPHDIYVIGTQEDPLGEKEWLELLRHSLQEVTSMTFKTVAIHTLWNIRIVVLAKPEHENRISHICTDNVKTGIANTLGNKGAVGVSFMFNGTSLGFVNSHLTSGSEKKLRRNQNYMNILRFLALGDKKLSPFNITHRFTHLFWLGDLNYRVELPTWEAEAIIQKIKQQQYSDLLAHDQLLLERKDQKVFLHFEEEEITFAPTYRFERLTRDKYAYTKQKATGMKYNLPSWCDRVLWKSYPLVHVVCQSYGSTSDIMTSDHSPVFATFEAGVTSQFVSKNGPGTVDSQGQIEFLACYATLKTKSQTKFYLEFHSSCLESFVKSQEGENEEGSEGELVVRFGETLPKLKPIISDPEYLLDQHILISIKSSDSDESYGEGCIALRLETTEAQHPIYTPLTHHGEMTGHFRGEIKLQTSQGKMREKLYDFVKTERDESSGMKCLKNLTSHDPMRQWEPSGRVPACGVSSLNEMINPNYIGMGPFGQPLHGKSTLSPDQQLTAWSYDQLPKDSSLGPGRGEGPPTPPSQPPLSPKKFSSSTANRGPCPRVQEARPGDLGKVEALLQEDLLLTKPEMFENPLYGSVSSFPKLVPRKEQESPKMLRKEPPPCPDPGISSPSIVLPKAQEVESVKGTSKQAPVPVLGPTPRIRSFTCSSSAEGRMTSGDKSQGKPKASASSQAPVPVKRPVKPSRSEMSQQTTPIPAPRPPLPVKSPAVLQLQHSKGRDYRDNTELPHHGKHRQEEGLLGRTAMQ
uniprot
proteins
ec_number
3.1.3.36
uniprot
proteins
ec_number
3.1.3.56
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 (By similarity). Also, is able to hydrolyze the 5-phosphate of phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P3), 1D-myo-inositol 1,4,5-trisphosphate and inositol 1,3,4,5-tetrakisphosphate (PubMed:9367159). Acts as a negative regulator of B-cell antigen receptor signaling. Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Acts as a negative regulator of myeloid cell proliferation/survival and chemotaxis, mast cell degranulation, immune cells homeostasis, integrin alpha-IIb/beta-3 signaling in platelets and JNK signaling in B-cells. Regulates proliferation of osteoclast precursors, macrophage programming, phagocytosis and activation and is required for endotoxin tolerance. Involved in the control of cell-cell junctions, CD32a signaling in neutrophils and modulation of EGF-induced phospholipase C activity. Key regulator of neutrophil migration, by governing the formation of the leading edge and polarization required for chemotaxis. Modulates FCGR3/CD16-mediated cytotoxicity in NK cells. Mediates the activin/TGF-beta-induced apoptosis through its Smad-dependent expression. {ECO:0000250|UniProtKB:Q92835, ECO:0000269|PubMed:11136821, ECO:0000269|PubMed:11222379, ECO:0000269|PubMed:11359765, ECO:0000269|PubMed:11896575, ECO:0000269|PubMed:12161749, ECO:0000269|PubMed:12370370, ECO:0000269|PubMed:12447389, ECO:0000269|PubMed:12882960, ECO:0000269|PubMed:14993273, ECO:0000269|PubMed:15166241, ECO:0000269|PubMed:17142780, ECO:0000269|PubMed:17173042, ECO:0000269|PubMed:8654924, ECO:0000269|PubMed:8805703, ECO:0000269|PubMed:9244303, ECO:0000269|PubMed:9367159, ECO:0000269|PubMed:9620849, ECO:0000269|PubMed:9736736, ECO:0000269|PubMed:9763612, ECO:0000269|PubMed:9857188}.
uniprot
proteins
mass_dalton
133542
uniprot
proteins
mutagenesis
MUTAGEN 676; /note="D->G: Loss of function."; /evidence="ECO:0000269|PubMed:11222379"; MUTAGEN 918; /note="Y->F: Strongly impairs function, tyrosine phosphorylation, subcellular location and interaction with DOK1; when associated with F-1021."; /evidence="ECO:0000269|PubMed:11031258, ECO:0000269|PubMed:11222379, ECO:0000269|PubMed:9099679"; MUTAGEN 1021; /note="Y->F: Strongly impairs function, tyrosine phosphorylation, subcellular location and interaction with DOK1; when associated with F-918."; /evidence="ECO:0000269|PubMed:11031258, ECO:0000269|PubMed:11222379, ECO:0000269|PubMed:9099679
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 cytokines, growth factors, antibodies, chemokines, integrin ligands and hypertonic and oxidative stress. Phosphorylated upon IgG receptor FCGR2B-binding. {ECO:0000269|PubMed:10068665, ECO:0000269|PubMed:10395202, ECO:0000269|PubMed:10660611, ECO:0000269|PubMed:12370370, ECO:0000269|PubMed:8654924, ECO:0000269|PubMed:8805618, ECO:0000269|PubMed:9099679}.
uniprot
proteins
protein_family
4
uniprot
proteins
protein_family
5-trisphosphate 5-phosphatase family
uniprot
proteins
protein_family
Inositol 1
uniprot
proteins
pubmed
10068665
uniprot
proteins
pubmed
10395202
uniprot
proteins
pubmed
10660611
uniprot
proteins
pubmed
10779347
uniprot
proteins
pubmed
10794720
uniprot
proteins
pubmed
11013080
uniprot
proteins
pubmed
11016922
uniprot
proteins
pubmed
11031258
uniprot
proteins
pubmed
11136821
uniprot
proteins
pubmed
11222379
uniprot
proteins
pubmed
11247302
uniprot
proteins
pubmed
11359765
uniprot
proteins
pubmed
11567986
uniprot
proteins
pubmed
11896575
uniprot
proteins
pubmed
12161749
uniprot
proteins
pubmed
12370370
uniprot
proteins
pubmed
12393695
uniprot
proteins
pubmed
12447389
uniprot
proteins
pubmed
12882960
uniprot
proteins
pubmed
14993273
uniprot
proteins
pubmed
15166241
uniprot
proteins
pubmed
15456754
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15492005
uniprot
proteins
pubmed
16000869
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16406061
uniprot
proteins
pubmed
17105399
uniprot
proteins
pubmed
17142780
uniprot
proteins
pubmed
17173042
uniprot
proteins
pubmed
17947660
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
20526344
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
8632995
uniprot
proteins
pubmed
8643691
uniprot
proteins
pubmed
8654924
uniprot
proteins
pubmed
8723348
uniprot
proteins
pubmed
8805618
uniprot
proteins
pubmed
8805703
uniprot
proteins
pubmed
9027494
uniprot
proteins
pubmed
9083021
uniprot
proteins
pubmed
9099679
uniprot
proteins
pubmed
9110989
uniprot
proteins
pubmed
9244303
uniprot
proteins
pubmed
9341117
uniprot
proteins
pubmed
9367159
uniprot
proteins
pubmed
9393882
uniprot
proteins
pubmed
9485206
uniprot
proteins
pubmed
9531585
uniprot
proteins
pubmed
9620849
uniprot
proteins
pubmed
9694708
uniprot
proteins
pubmed
9736736
uniprot
proteins
pubmed
9763612
uniprot
proteins
pubmed
9857188
uniprot
proteins
sequence_length
1191
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16406061}. Cell membrane {ECO:0000269|PubMed:12393695}; Peripheral membrane protein {ECO:0000305|PubMed:12393695}. Membrane raft {ECO:0000269|PubMed:12393695}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9694708}. Note=Translocates to the plasma membrane when activated, translocation is probably due to different mechanisms depending on the stimulus and cell type (PubMed:12393695). Translocates from the cytoplasm to membrane ruffles in a FCGR3/CD16-dependent manner (PubMed:12393695). Colocalizes with FC-gamma-RIIB receptor (FCGR2B) or FCGR3/CD16 at membrane ruffles (PubMed:12393695). Tyrosine phosphorylation may also participate in membrane localization (PubMed:12393695). {ECO:0000269|PubMed:12393695}.; SUBCELLULAR LOCATION: [Isoform 5]: Cell membrane {ECO:0000269|PubMed:11567986}; Peripheral membrane protein {ECO:0000305|PubMed:11567986}. Note=Constitutively present at the cell membrane (PubMed:11567986). {ECO:0000269|PubMed:11567986}.
uniprot
proteins