ID:I5P2_HUMAN DESCRIPTION: RecName: Full=Type II inositol 1,4,5-trisphosphate 5-phosphatase; EC=3.1.3.36; AltName: Full=75 kDa inositol polyphosphate-5-phosphatase; AltName: Full=Phosphoinositide 5-phosphatase; Short=5PTase; FUNCTION: Hydrolyzes phosphatidylinositol 4,5-bisphosphate (PtIns(4,5)P2) and the signaling molecule phosphatidylinositol 1,4,5-trisphosphate (PtIns(1,4,5)P3), and thereby modulates cellular signaling events. CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 4,5- bisphosphate + H(2)O = 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate. SUBUNIT: Interacts with APPL1, FAM109A and FAM109B. Interacts with several Rab GTPases, at least RAB1A, RAB2A, RAB5A, RAB6A, RAB8A, RAB9A and RAB33B; these interactions may play a dual role in targeting INPP5B to the specific membranes and stimulating the phosphatase activity. SUBCELLULAR LOCATION: Cytoplasm, cytosol. Endoplasmic reticulum- Golgi intermediate compartment. Early endosome membrane. Membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle, phagosome membrane (By similarity). Golgi apparatus. TISSUE SPECIFICITY: Platelets. DOMAIN: The ASH (ASPM-SPD2-Hydin) and RhoGAP (Rho GTPase activating) domains form a single folding module. The ASH domain has an immunoglobulin-like fold, the Rho-GAP domain lacks the catalytic arginine and is catalytically inactive. The ASH-RhoGAP module regulates the majority of the protein-protein interactions currently described. The ASH domain mediates association with membrane-targeting Rab GTPases. The Rho-GAP domain interacts with the endocytic adapter APPL1, which is then displaced by FAM109A and FAM109B as endosomes mature, all three interactions relie on F&H motifs, an approximately 12-13 amino-acid sequence centered around Phe and His residues essential for binding (By similarity). PTM: Isoprenylation at Cys-990 may be required for localization at the membrane. PTM: May be proteolytically cleaved after Lys-320 as inferred from N-terminal protein sequence of the 75 kda form (PubMed:1718960). SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5- phosphatase type II family. SIMILARITY: Contains 1 PH domain. SIMILARITY: Contains 1 Rho-GAP domain. SEQUENCE CAUTION: Sequence=AAA79207.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on P32019
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Biological Process: GO:0001701 in utero embryonic development GO:0007165 signal transduction GO:0007283 spermatogenesis GO:0030317 flagellated sperm motility GO:0043547 positive regulation of GTPase activity GO:0043647 inositol phosphate metabolic process GO:0046856 phosphatidylinositol dephosphorylation GO:0051056 regulation of small GTPase mediated signal transduction GO:0070613 regulation of protein processing
Protein P32019 (Reactome details) participates in the following event(s):
R-HSA-194922 GAPs inactivate Rho GTPase:GTP by hydrolysis R-HSA-1855222 I(1,4,5)P3 is dephosphorylated to I(1,4)P2 by INPP5A/B at the plasma membrane R-HSA-1855213 I(1,3,4,5)P4 is dephosphorylated to I(1,3,4)P3 by INPP5B at the plasma membrane R-HSA-194840 Rho GTPase cycle R-HSA-1855183 Synthesis of IP2, IP, and Ins in the cytosol R-HSA-1855204 Synthesis of IP3 and IP4 in the cytosol R-HSA-194315 Signaling by Rho GTPases R-HSA-1483249 Inositol phosphate metabolism R-HSA-162582 Signal Transduction R-HSA-1430728 Metabolism
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Sequence and Links to Tools and Databases 
Common Gene Haplotype Alleles 
