PI Metabolism (Homo sapiens)

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1, 15, 28, 31, 41...55, 7012, 82, 109, 110, 11313, 56, 58, 90, 104...14, 39, 54, 11111, 70, 1072, 3, 21, 43, 49...20, 22, 23, 73, 10648, 51, 5720, 22, 58, 7318, 49, 53, 9342, 47, 6520, 10638, 85, 100612933, 39, 54, 9642, 4729, 64, 74, 101, 1051720, 1067, 19, 34, 64, 7412, 86, 8820, 22, 58, 736118, 49, 931093210, 16, 40, 46, 68...14, 39, 54, 58, 11182, 86, 11020, 10630, 7314, 39, 54, 58, 11124, 25, 44, 60, 66...3, 58, 75, 104, 114294, 35, 1083, 13, 56, 58, 90...11, 70, 10710, 33, 40, 46, 54...81, 976, 9, 59, 62, 63, 782, 21, 43, 49, 50, 58...58, 104, 1148, 18, 26, 49, 53...5, 8, 26, 27, 37...324, 29, 35, 64, 74...82, 109, 1136, 9, 59, 62, 63, 786, 7836, 54616, 78Golgi lumenendoplasmic reticulum lumenlate endosome lumenearly endosome lumencytosolPIK3C2A:Ca2+/Mg2+VAC14 INPP4B PIK3C2A PIOCRL/INPP5EPI4PPIK3R4 PiPI3PPITPNB PIK3R3 MTM(2)ATPPI:PITPNBCa2+ PIOCRL PIP5K1C SYNJ1 Ca2+ PIP5K1B PIP5K1A-CPIP5K1A ATPMTMR1 ATPPIK3R5 ADPPC:PITPNBSACM1LMTMR4 PIK3R2 PIK3R4 ADPMg2+ PI(3,5)P2Mg2+ INPP5D Mg2+ ADPSYNJ/INPP5(1)ARF3 H2OADPATPPIP5K1B INPP5K H2OPI(4,5)P2PiMn2+ PIK3C2A SYNJPIK3CD PIK3C2A PIK3R6 PC PI4KA/2BPiMTMR7 ATPPIKFYVE:VAC14:FIG4MTM1 PiPIK3R6 SYNJPI5PSYNJ1 Ca2+ SYNJ2 PiPIK3C2A PiPCTPTE PIK3CA SYNJ2 ADPINPP4B ADPH2OH2OARF1/3:GTP:PI4KBPI(3,4)P2PI4KA MTM1 PI5PATPH2OPIK3C2A PIK3R1 ADPTPTE2-like proteinsPIP5K1A/BINPP5(2)PIKFYVE PI4K2A INPP5J PI4KB SYNJ2 ADPCa2+ PI4K2A/2BPI:PITPNBMTMR4 PI(3,4)P2H2OPIP5K1A PI5PPI3PPIK3CG Ca2+ ADPH2OMTMR14 PiMTMR7 INPP4A/BVAC14 MTMR2 ARF1 ARF1 ADPPIK3R4 FIG4 INPP5E PIK3C2G Ca2+ PIP4K2/5K1PIK3CD MTMR6 H2OFIG4 ADPH2OPIK3CA PI4K2B ARF1/3:GTPATPPI3PPIP4K2A PIK3C2A/GATPPI4K2A PI(3,4,5)P3PI3PPIP5K1C PIP4K2B ATPPIPI ADPINPP5(1) SYNJ1 PIP5K1B PiMTMR3 ADPPIP4K2A PI4KA/2A/2BPIP5K1A ADPPIKFYVE:VAC14:FIG4PI4K2B MTM1 INPPL1 ATPPI(4,5)P2PIP5K1B ADPATPPITPNB PTEN:Mg2+PIK3CB SACM1LH2OMg2+ H2OPIK3C3 PiPI4K2A MTM1 PI4PPIP5K1A/BSYNJ1 ATPPITPNB PI4PPI MTMR2 MTM(3)PIP5K1A PIKFYVE H2OPIK3C2A/3PIINPP4A/BATPPIP5K1C PIK3C2B PIP5K1B PIKFYVE Mn2+ SACM1LINPP4A MTMR2 PC:PITPNBSYNJ2 ATPPI(3,5)P2ADPPIK3C3 ADPH2OH2OPIP5K1A-CPIK3R1 PI(3,5)P2FIG4 ADPATPPiPCPiSYNJ/MTM(1)VAC14 PIKFYVE:VAC14:FIG4Mg2+ PIK3C3 PIK3R2 PI(3,5)P2Mg2+ PC PI4KA ADPPITPNB PI4K2B MTM(3)PIK3CB PI4K2B PIK3C2A PiPIP4K2B ATPPIK3C(1)PI4PPIK3(2)ADPPiPiPTEN INPP4A PI4KBPIK3C2G GTP GTP ATPPiPIK3CG PIP4K2A/BARF3 H2OPIPIP5K1A Mn2+ PIK3R3 MTMR4 PIMg2+ PIK3C2A/3PiPI4K2A/2BPiMn2+ PiPIK3R5 PI(3,4)P2TPTE2 PIK3C2A/3


Description

Phosphatidylinositol (PI), a membrane phospholipid, can be reversibly phosphorylated at the 3, 4, and 5 positions of the inositol ring to generate seven phosphoinositides: phosphatidylinositol 3-phosphate (PI3P), phosphatidylinositol 4-phosphate (PI4P), phosphatidylinositol 5-phosphate (PI5P), phosphatidylinositol 3,4-bisphosphate PI(3,4)P2, phosphatidylinositol 4,5-bisphosphate PI(4,5)P2, phosphatidylinositol 3,5-bisphosphate PI(3,5)P2, and phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3). These seven phosphoinositides, which are heterogeneously distributed within cells, can serve as signature components of different intracellular compartment membranes and so help to mediate specificity of membrane interactions. Phosphoinositide levels are tightly regulated spatially and temporally by the action of various kinases and phosphatases whilst PI(4,5)P2 is also a substrate for phospholipase C. The differential localisation of each of these enzymes on specific compartment membranes ensures maintenance of the heterogeneous distribution of phosphoinositides despite the continuous membrane flow from one compartment to another.

PI is primarily synthesised in the endoplasmic reticulum from where the phospholipid is exported to other compartments via membrane traffic or via cytosolic phospholipid transfer proteins. Phosphorylation of PI to PI4P primarily occurs in the Golgi, where PI4P plays an important role in the biogenesis of transport vesicles such as the secretory vesicle involved in its transport to the plasma membrane. At this place, PI4P has a major function acting as a precursor of PI(4,5)P2, which is located predominantly at this membrane. PI(4,5)P2 binds and regulates a wide range of proteins that function on the cell surface and serves as a precursor for second messengers. Additionally, it helps define this membrane as a target for secretory vesicles, functions as a coreceptor in endocytic processes, and functions as a cofactor for actin nucleation.

At the plasma membrane, PI(4,5)P2 is further phosphorylated to PI(3,4,5)P3, another phosphoinositide with important signalling functions including stimulating cell survival and proliferation. The inositol 3-phosphatase, phosphatase and tensin homolog (PTEN) regenerates PI (4,5)P2, while the 5-phosphatases convert PI(3,4,5)P3 into the phosphoinositide, PI(3,4)P2, propagating the signal initiated by PI(3,4,5)P3. PI(3,4)P2 is further dephosphorylated in the endocytic pathway by inositol 4-phosphatases to PI3P, the signature phosphoinositide of the early endosomal compartment and a ligand for numerous endosomal proteins. However, the bulk of PI3P is generated directly in the endosomes by phosphorylation of PI. The subsequent endosomal phosphorylation of PI3P to PI(3,5)P2 is believed to generate docking sites for recruitment of cytosolic factors responsible for the control of outgoing traffic from the endosomes. The main localisation and function of the low abundance phosphoinositide PI5P, that can be generated by several pathways, remains to be determined (Krauss & Haucke 2007, Leventis & Grinstein 2010, Roth 2004, Gees et al. 2010, De Matteis & Godi 2004, van Meer et al. 2008, Vicinanza et al. 2008, Lemmon 2008, Kutaleladze 2010, Robinson & Dixon 2006, Blero et al. 2007, Liu & Bankaitis 2010, McCrea & De Camilli 2009, Vicinanza et al. 2008, Di Paolo & De Camilli, 2006). View original pathway at:Reactome.

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Bibliography

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  92. Rudd CE.; ''Adaptors and molecular scaffolds in immune cell signaling.''; PubMed Europe PMC Scholia
  93. Zhao R, Qi Y, Chen J, Zhao ZJ.; ''FYVE-DSP2, a FYVE domain-containing dual specificity protein phosphatase that dephosphorylates phosphotidylinositol 3-phosphate.''; PubMed Europe PMC Scholia
  94. Dowler S, Currie RA, Campbell DG, Deak M, Kular G, Downes CP, Alessi DR.; ''Identification of pleckstrin-homology-domain-containing proteins with novel phosphoinositide-binding specificities.''; PubMed Europe PMC Scholia
  95. Gupta VA, Hnia K, Smith LL, Gundry SR, McIntire JE, Shimazu J, Bass JR, Talbot EA, Amoasii L, Goldman NE, Laporte J, Beggs AH.; ''Loss of catalytically inactive lipid phosphatase myotubularin-related protein 12 impairs myotubularin stability and promotes centronuclear myopathy in zebrafish.''; PubMed Europe PMC Scholia
  96. Sakagami H, Aoki J, Natori Y, Nishikawa K, Kakehi Y, Natori Y, Arai H.; ''Biochemical and molecular characterization of a novel choline-specific glycerophosphodiester phosphodiesterase belonging to the nucleotide pyrophosphatase/phosphodiesterase family.''; PubMed Europe PMC Scholia
  97. Mochizuki Y, Majerus PW.; ''Characterization of myotubularin-related protein 7 and its binding partner, myotubularin-related protein 9.''; PubMed Europe PMC Scholia
  98. Kienesberger PC, Lass A, Preiss-Landl K, Wolinski H, Kohlwein SD, Zimmermann R, Zechner R.; ''Identification of an insulin-regulated lysophospholipase with homology to neuropathy target esterase.''; PubMed Europe PMC Scholia
  99. Myers MP, Pass I, Batty IH, Van der Kaay J, Stolarov JP, Hemmings BA, Wigler MH, Downes CP, Tonks NK.; ''The lipid phosphatase activity of PTEN is critical for its tumor supressor function.''; PubMed Europe PMC Scholia
  100. Misawa H, Ohtsubo M, Copeland NG, Gilbert DJ, Jenkins NA, Yoshimura A.; ''Cloning and characterization of a novel class II phosphoinositide 3-kinase containing C2 domain.''; PubMed Europe PMC Scholia
  101. Zhang X, Loijens JC, Boronenkov IV, Parker GJ, Norris FA, Chen J, Thum O, Prestwich GD, Majerus PW, Anderson RA.; ''Phosphatidylinositol-4-phosphate 5-kinase isozymes catalyze the synthesis of 3-phosphate-containing phosphatidylinositol signaling molecules.''; PubMed Europe PMC Scholia
  102. Sbrissa D, Ikonomov OC, Fu Z, Ijuin T, Gruenberg J, Takenawa T, Shisheva A.; ''Core protein machinery for mammalian phosphatidylinositol 3,5-bisphosphate synthesis and turnover that regulates the progression of endosomal transport. Novel Sac phosphatase joins the ArPIKfyve-PIKfyve complex.''; PubMed Europe PMC Scholia
  103. Ivetac I, Munday AD, Kisseleva MV, Zhang XM, Luff S, Tiganis T, Whisstock JC, Rowe T, Majerus PW, Mitchell CA.; ''The type Ialpha inositol polyphosphate 4-phosphatase generates and terminates phosphoinositide 3-kinase signals on endosomes and the plasma membrane.''; PubMed Europe PMC Scholia
  104. Ciruela A, Hinchliffe KA, Divecha N, Irvine RF.; ''Nuclear targeting of the beta isoform of type II phosphatidylinositol phosphate kinase (phosphatidylinositol 5-phosphate 4-kinase) by its alpha-helix 7.''; PubMed Europe PMC Scholia
  105. Clarke JH, Emson PC, Irvine RF.; ''Localization of phosphatidylinositol phosphate kinase IIgamma in kidney to a membrane trafficking compartment within specialized cells of the nephron.''; PubMed Europe PMC Scholia
  106. Rokudai S, Laptenko O, Arnal SM, Taya Y, Kitabayashi I, Prives C.; ''MOZ increases p53 acetylation and premature senescence through its complex formation with PML.''; PubMed Europe PMC Scholia
  107. Lorenzo O, Urbé S, Clague MJ.; ''Systematic analysis of myotubularins: heteromeric interactions, subcellular localisation and endosome related functions.''; PubMed Europe PMC Scholia
  108. Arcaro A, Volinia S, Zvelebil MJ, Stein R, Watton SJ, Layton MJ, Gout I, Ahmadi K, Downward J, Waterfield MD.; ''Human phosphoinositide 3-kinase C2beta, the role of calcium and the C2 domain in enzyme activity.''; PubMed Europe PMC Scholia
  109. Berger P, Schaffitzel C, Berger I, Ban N, Suter U.; ''Membrane association of myotubularin-related protein 2 is mediated by a pleckstrin homology-GRAM domain and a coiled-coil dimerization module.''; PubMed Europe PMC Scholia
  110. Fayngerts SA, Wu J, Oxley CL, Liu X, Vourekas A, Cathopoulis T, Wang Z, Cui J, Liu S, Sun H, Lemmon MA, Zhang L, Shi Y, Chen YH.; ''TIPE3 is the transfer protein of lipid second messengers that promote cancer.''; PubMed Europe PMC Scholia
  111. Das S, Dixon JE, Cho W.; ''Membrane-binding and activation mechanism of PTEN.''; PubMed Europe PMC Scholia
  112. Blero D, Payrastre B, Schurmans S, Erneux C.; ''Phosphoinositide phosphatases in a network of signalling reactions.''; PubMed Europe PMC Scholia
  113. Jiang L, Kon N, Li T, Wang SJ, Su T, Hibshoosh H, Baer R, Gu W.; ''Ferroptosis as a p53-mediated activity during tumour suppression.''; PubMed Europe PMC Scholia
  114. Kim SA, Taylor GS, Torgersen KM, Dixon JE.; ''Myotubularin and MTMR2, phosphatidylinositol 3-phosphatases mutated in myotubular myopathy and type 4B Charcot-Marie-Tooth disease.''; PubMed Europe PMC Scholia
  115. Haynes LP, Sherwood MW, Dolman NJ, Burgoyne RD.; ''Specificity, promiscuity and localization of ARF protein interactions with NCS-1 and phosphatidylinositol-4 kinase-III beta.''; PubMed Europe PMC Scholia
  116. Walker DM, Urbé S, Dove SK, Tenza D, Raposo G, Clague MJ.; ''Characterization of MTMR3. an inositol lipid 3-phosphatase with novel substrate specificity.''; PubMed Europe PMC Scholia
  117. Choudhury P, Srivastava S, Li Z, Ko K, Albaqumi M, Narayan K, Coetzee WA, Lemmon MA, Skolnik EY.; ''Specificity of the myotubularin family of phosphatidylinositol-3-phosphatase is determined by the PH/GRAM domain.''; PubMed Europe PMC Scholia
  118. Guo S, Stolz LE, Lemrow SM, York JD.; ''SAC1-like domains of yeast SAC1, INP52, and INP53 and of human synaptojanin encode polyphosphoinositide phosphatases.''; PubMed Europe PMC Scholia
  119. Schaletzky J, Dove SK, Short B, Lorenzo O, Clague MJ, Barr FA.; ''Phosphatidylinositol-5-phosphate activation and conserved substrate specificity of the myotubularin phosphatidylinositol 3-phosphatases.''; PubMed Europe PMC Scholia
  120. Bensaad K, Tsuruta A, Selak MA, Vidal MN, Nakano K, Bartrons R, Gottlieb E, Vousden KH.; ''TIGAR, a p53-inducible regulator of glycolysis and apoptosis.''; PubMed Europe PMC Scholia
  121. Fouraux MA, Deneka M, Ivan V, van der Heijden A, Raymackers J, van Suylekom D, van Venrooij WJ, van der Sluijs P, Pruijn GJ.; ''Rabip4' is an effector of rab5 and rab4 and regulates transport through early endosomes.''; PubMed Europe PMC Scholia
  122. Voigt P, Dorner MB, Schaefer M.; ''Characterization of p87PIKAP, a novel regulatory subunit of phosphoinositide 3-kinase gamma that is highly expressed in heart and interacts with PDE3B.''; PubMed Europe PMC Scholia
  123. Marshall AJ, Krahn AK, Ma K, Duronio V, Hou S.; ''TAPP1 and TAPP2 are targets of phosphatidylinositol 3-kinase signaling in B cells: sustained plasma membrane recruitment triggered by the B-cell antigen receptor.''; PubMed Europe PMC Scholia
  124. De Matteis MA, Godi A.; ''PI-loting membrane traffic.''; PubMed Europe PMC Scholia
  125. Tosch V, Rohde HM, Tronchère H, Zanoteli E, Monroy N, Kretz C, Dondaine N, Payrastre B, Mandel JL, Laporte J.; ''A novel PtdIns3P and PtdIns(3,5)P2 phosphatase with an inactivating variant in centronuclear myopathy.''; PubMed Europe PMC Scholia
  126. Gehrmann T, Gülkan H, Suer S, Herberg FW, Balla A, Vereb G, Mayr GW, Heilmeyer LM.; ''Functional expression and characterisation of a new human phosphatidylinositol 4-kinase PI4K230.''; PubMed Europe PMC Scholia
  127. Lou Y, Liu S.; ''The TIPE (TNFAIP8) family in inflammation, immunity, and cancer.''; PubMed Europe PMC Scholia
  128. Choudhury R, Noakes CJ, McKenzie E, Kox C, Lowe M.; ''Differential clathrin binding and subcellular localization of OCRL1 splice isoforms.''; PubMed Europe PMC Scholia
  129. Malecz N, McCabe PC, Spaargaren C, Qiu R, Chuang Y, Symons M.; ''Synaptojanin 2, a novel Rac1 effector that regulates clathrin-mediated endocytosis.''; PubMed Europe PMC Scholia
  130. Cao C, Backer JM, Laporte J, Bedrick EJ, Wandinger-Ness A.; ''Sequential actions of myotubularin lipid phosphatases regulate endosomal PI(3)P and growth factor receptor trafficking.''; PubMed Europe PMC Scholia
  131. van Meer G, Voelker DR, Feigenson GW.; ''Membrane lipids: where they are and how they behave.''; PubMed Europe PMC Scholia
  132. Tang Y, Luo J, Zhang W, Gu W.; ''Tip60-dependent acetylation of p53 modulates the decision between cell-cycle arrest and apoptosis.''; PubMed Europe PMC Scholia
  133. Caldwell KK, Lips DL, Bansal VS, Majerus PW.; ''Isolation and characterization of two 3-phosphatases that hydrolyze both phosphatidylinositol 3-phosphate and inositol 1,3-bisphosphate.''; PubMed Europe PMC Scholia
  134. Oude Weernink PA, Schmidt M, Jakobs KH.; ''Regulation and cellular roles of phosphoinositide 5-kinases.''; PubMed Europe PMC Scholia
  135. Godi A, Pertile P, Meyers R, Marra P, Di Tullio G, Iurisci C, Luini A, Corda D, De Matteis MA.; ''ARF mediates recruitment of PtdIns-4-OH kinase-beta and stimulates synthesis of PtdIns(4,5)P2 on the Golgi complex.''; PubMed Europe PMC Scholia
  136. Wong K, Meyers ddR, Cantley LC.; ''Subcellular locations of phosphatidylinositol 4-kinase isoforms.''; PubMed Europe PMC Scholia
  137. Rohde HM, Cheong FY, Konrad G, Paiha K, Mayinger P, Boehmelt G.; ''The human phosphatidylinositol phosphatase SAC1 interacts with the coatomer I complex.''; PubMed Europe PMC Scholia
  138. Suchy SF, Olivos-Glander IM, Nussabaum RL.; ''Lowe syndrome, a deficiency of phosphatidylinositol 4,5-bisphosphate 5-phosphatase in the Golgi apparatus.''; PubMed Europe PMC Scholia
  139. Lemmon MA.; ''Membrane recognition by phospholipid-binding domains.''; PubMed Europe PMC Scholia
  140. Mani M, Lee SY, Lucast L, Cremona O, Di Paolo G, De Camilli P, Ryan TA.; ''The dual phosphatase activity of synaptojanin1 is required for both efficient synaptic vesicle endocytosis and reavailability at nerve terminals.''; PubMed Europe PMC Scholia
  141. Bachmann AS, Duennebier FF, Mocz G.; ''Genomic organization, characterization, and molecular 3D model of GDE1, a novel mammalian glycerophosphoinositol phosphodiesterase.''; PubMed Europe PMC Scholia
  142. Habib T, Hejna JA, Moses RE, Decker SJ.; ''Growth factors and insulin stimulate tyrosine phosphorylation of the 51C/SHIP2 protein.''; PubMed Europe PMC Scholia
  143. Li W, Ouyang Z, Zhang Q, Wang L, Shen Y, Wu X, Gu Y, Shu Y, Yu B, Wu X, Sun Y, Xu Q.; ''SBF-1 exerts strong anticervical cancer effect through inducing endoplasmic reticulum stress-associated cell death via targeting sarco/endoplasmic reticulum Ca(2+)-ATPase 2.''; PubMed Europe PMC Scholia
  144. Yang J, Kim O, Wu J, Qiu Y.; ''Interaction between tyrosine kinase Etk and a RUN domain- and FYVE domain-containing protein RUFY1. A possible role of ETK in regulation of vesicle trafficking.''; PubMed Europe PMC Scholia
  145. Leventis PA, Grinstein S.; ''The distribution and function of phosphatidylserine in cellular membranes.''; PubMed Europe PMC Scholia
  146. Mari M, Monzo P, Kaddai V, Keslair F, Gonzalez T, Le Marchand-Brustel Y, Cormont M.; ''The Rab4 effector Rabip4 plays a role in the endocytotic trafficking of Glut 4 in 3T3-L1 adipocytes.''; PubMed Europe PMC Scholia
  147. Krag C, Malmberg EK, Salcini AE.; ''PI3KC2α, a class II PI3K, is required for dynamin-independent internalization pathways.''; PubMed Europe PMC Scholia
  148. Kavanaugh WM, Pot DA, Chin SM, Deuter-Reinhard M, Jefferson AB, Norris FA, Masiarz FR, Cousens LS, Majerus PW, Williams LT.; ''Multiple forms of an inositol polyphosphate 5-phosphatase form signaling complexes with Shc and Grb2.''; PubMed Europe PMC Scholia
  149. Kisseleva MV, Wilson MP, Majerus PW.; ''The isolation and characterization of a cDNA encoding phospholipid-specific inositol polyphosphate 5-phosphatase.''; PubMed Europe PMC Scholia
  150. Tronchère H, Laporte J, Pendaries C, Chaussade C, Liaubet L, Pirola L, Mandel JL, Payrastre B.; ''Production of phosphatidylinositol 5-phosphate by the phosphoinositide 3-phosphatase myotubularin in mammalian cells.''; PubMed Europe PMC Scholia
  151. Rozycka M, Lu YJ, Brown RA, Lau MR, Shipley JM, Fry MJ.; ''cDNA cloning of a third human C2-domain-containing class II phosphoinositide 3-kinase, PI3K-C2gamma, and chromosomal assignment of this gene (PIK3C2G) to 12p12.''; PubMed Europe PMC Scholia
  152. Drost J, Mantovani F, Tocco F, Elkon R, Comel A, Holstege H, Kerkhoven R, Jonkers J, Voorhoeve PM, Agami R, Del Sal G.; ''BRD7 is a candidate tumour suppressor gene required for p53 function.''; PubMed Europe PMC Scholia
  153. Guo X, Ghalayini AJ, Chen H, Anderson RE.; ''Phosphatidylinositol 3-kinase in bovine photoreceptor rod outer segments.''; PubMed Europe PMC Scholia
  154. Hammond GR, Schiavo G, Irvine RF.; ''Immunocytochemical techniques reveal multiple, distinct cellular pools of PtdIns4P and PtdIns(4,5)P(2).''; PubMed Europe PMC Scholia
  155. Vordtriede PB, Doan CN, Tremblay JM, Helmkamp GM, Yoder MD.; ''Structure of PITPbeta in complex with phosphatidylcholine: comparison of structure and lipid transfer to other PITP isoforms.''; PubMed Europe PMC Scholia
  156. Mochizuki Y, Takenawa T.; ''Novel inositol polyphosphate 5-phosphatase localizes at membrane ruffles.''; PubMed Europe PMC Scholia
  157. Nakatsu F, Messa M, Nández R, Czapla H, Zou Y, Strittmatter SM, De Camilli P.; ''Sac2/INPP5F is an inositol 4-phosphatase that functions in the endocytic pathway.''; PubMed Europe PMC Scholia
  158. McCrea HJ, De Camilli P.; ''Mutations in phosphoinositide metabolizing enzymes and human disease.''; PubMed Europe PMC Scholia
  159. Moniz LS, Vanhaesebroeck B.; ''A new TIPE of phosphoinositide regulator in cancer.''; PubMed Europe PMC Scholia
  160. Berger P, Berger I, Schaffitzel C, Tersar K, Volkmer B, Suter U.; ''Multi-level regulation of myotubularin-related protein-2 phosphatase activity by myotubularin-related protein-13/set-binding factor-2.''; PubMed Europe PMC Scholia
  161. Li T, Kon N, Jiang L, Tan M, Ludwig T, Zhao Y, Baer R, Gu W.; ''Tumor suppression in the absence of p53-mediated cell-cycle arrest, apoptosis, and senescence.''; PubMed Europe PMC Scholia
  162. Zheng B, Berrie CP, Corda D, Farquhar MG.; ''GDE1/MIR16 is a glycerophosphoinositol phosphodiesterase regulated by stimulation of G protein-coupled receptors.''; PubMed Europe PMC Scholia
  163. Meier TI, Cook JA, Thomas JE, Radding JA, Horn C, Lingaraj T, Smith MC.; ''Cloning, expression, purification, and characterization of the human Class Ia phosphoinositide 3-kinase isoforms.''; PubMed Europe PMC Scholia
  164. Cabezas A, Pattni K, Stenmark H.; ''Cloning and subcellular localization of a human phosphatidylinositol 3-phosphate 5-kinase, PIKfyve/Fab1.''; PubMed Europe PMC Scholia
  165. Sbrissa D, Ikonomov OC, Deeb R, Shisheva A.; ''Phosphatidylinositol 5-phosphate biosynthesis is linked to PIKfyve and is involved in osmotic response pathway in mammalian cells.''; PubMed Europe PMC Scholia
  166. Robinson FL, Dixon JE.; ''Myotubularin phosphatases: policing 3-phosphoinositides.''; PubMed Europe PMC Scholia
  167. Sykes SM, Mellert HS, Holbert MA, Li K, Marmorstein R, Lane WS, McMahon SB.; ''Acetylation of the p53 DNA-binding domain regulates apoptosis induction.''; PubMed Europe PMC Scholia
  168. Wenk MR, Pellegrini L, Klenchin VA, Di Paolo G, Chang S, Daniell L, Arioka M, Martin TF, De Camilli P.; ''PIP kinase Igamma is the major PI(4,5)P(2) synthesizing enzyme at the synapse.''; PubMed Europe PMC Scholia
  169. Johenning FW, Wenk MR, Uhlén P, Degray B, Lee E, De Camilli P, Ehrlich BE.; ''InsP3-mediated intracellular calcium signalling is altered by expression of synaptojanin-1.''; PubMed Europe PMC Scholia
  170. Yamada K, Nomura N, Yamano A, Yamada Y, Wakamatsu N.; ''Identification and characterization of splicing variants of PLEKHA5 (Plekha5) during brain development.''; PubMed Europe PMC Scholia
  171. Kitagishi Y, Matsuda S.; ''RUFY, Rab and Rap Family Proteins Involved in a Regulation of Cell Polarity and Membrane Trafficking.''; PubMed Europe PMC Scholia
  172. Drayer AL, Pesesse X, De Smedt F, Woscholski R, Parker P, Erneux C.; ''Cloning and expression of a human placenta inositol 1,3,4,5-tetrakisphosphate and phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase.''; PubMed Europe PMC Scholia

History

View all...
CompareRevisionActionTimeUserComment
114955view16:48, 25 January 2021ReactomeTeamReactome version 75
113399view11:47, 2 November 2020ReactomeTeamReactome version 74
112603view15:58, 9 October 2020ReactomeTeamReactome version 73
101519view11:38, 1 November 2018ReactomeTeamreactome version 66
101055view21:20, 31 October 2018ReactomeTeamreactome version 65
100586view19:54, 31 October 2018ReactomeTeamreactome version 64
100135view16:39, 31 October 2018ReactomeTeamreactome version 63
99685view15:08, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
93921view13:45, 16 August 2017ReactomeTeamreactome version 61
93500view11:25, 9 August 2017ReactomeTeamreactome version 61
88092view09:25, 26 July 2016RyanmillerOntology Term : 'lipid metabolic pathway' added !
88091view09:23, 26 July 2016RyanmillerOntology Term : 'classic metabolic pathway' added !
86595view09:21, 11 July 2016ReactomeTeamreactome version 56
83160view10:14, 18 November 2015ReactomeTeamVersion54
81516view13:03, 21 August 2015ReactomeTeamVersion53
76987view08:27, 17 July 2014ReactomeTeamFixed remaining interactions
76692view12:05, 16 July 2014ReactomeTeamFixed remaining interactions
76018view10:08, 11 June 2014ReactomeTeamRe-fixing comment source
75727view11:20, 10 June 2014ReactomeTeamReactome 48 Update
75077view14:02, 8 May 2014AnweshaFixing comment source for displaying WikiPathways description
74724view08:48, 30 April 2014ReactomeTeamNew pathway

External references

DataNodes

View all...
NameTypeDatabase referenceComment
ADPMetaboliteCHEBI:16761 (ChEBI)
ARF1 ProteinP84077 (Uniprot-TrEMBL)
ARF1/3:GTP:PI4KBComplexR-HSA-1806287 (Reactome)
ARF1/3:GTPComplexR-HSA-1806258 (Reactome)
ARF3 ProteinP61204 (Uniprot-TrEMBL)
ATPMetaboliteCHEBI:15422 (ChEBI)
Ca2+ MetaboliteCHEBI:29108 (ChEBI)
FIG4 ProteinQ92562 (Uniprot-TrEMBL)
GTP MetaboliteCHEBI:15996 (ChEBI)
H2OMetaboliteCHEBI:15377 (ChEBI)
INPP4A ProteinQ96PE3 (Uniprot-TrEMBL)
INPP4A/BComplexR-HSA-1806281 (Reactome)
INPP4B ProteinO15327 (Uniprot-TrEMBL)
INPP5(1) R-HSA-1806201 (Reactome)
INPP5(2)ComplexR-HSA-1806186 (Reactome)
INPP5D ProteinQ92835 (Uniprot-TrEMBL)
INPP5E ProteinQ9NRR6 (Uniprot-TrEMBL)
INPP5J ProteinQ15735 (Uniprot-TrEMBL)
INPP5K ProteinQ9BT40 (Uniprot-TrEMBL)
INPPL1 ProteinO15357 (Uniprot-TrEMBL)
MTM(2)ComplexR-HSA-1806263 (Reactome)
MTM(3)ComplexR-HSA-1806231 (Reactome)
MTM1 ProteinQ13496 (Uniprot-TrEMBL)
MTMR1 ProteinQ13613 (Uniprot-TrEMBL)
MTMR14 ProteinQ8NCE2 (Uniprot-TrEMBL)
MTMR2 ProteinQ13614 (Uniprot-TrEMBL)
MTMR3 ProteinQ13615 (Uniprot-TrEMBL)
MTMR4 ProteinQ9NYA4 (Uniprot-TrEMBL)
MTMR6 ProteinQ9Y217 (Uniprot-TrEMBL)
MTMR7 ProteinQ9Y216 (Uniprot-TrEMBL)
Mg2+ MetaboliteCHEBI:18420 (ChEBI)
Mn2+ MetaboliteCHEBI:29035 (ChEBI)
OCRL ProteinQ01968 (Uniprot-TrEMBL)
OCRL/INPP5EComplexR-HSA-1806215 (Reactome)
PC MetaboliteCHEBI:16110 (ChEBI)
PC:PITPNBComplexR-HSA-1524110 (Reactome)
PC:PITPNBComplexR-HSA-1524122 (Reactome)
PCMetaboliteCHEBI:16110 (ChEBI)
PI MetaboliteCHEBI:16749 (ChEBI)
PI(3,4)P2MetaboliteCHEBI:16152 (ChEBI)
PI(3,4,5)P3MetaboliteCHEBI:16618 (ChEBI)
PI(3,5)P2MetaboliteCHEBI:16851 (ChEBI)
PI(4,5)P2MetaboliteCHEBI:18348 (ChEBI)
PI3PMetaboliteCHEBI:17283 (ChEBI)
PI4K2A ProteinQ9BTU6 (Uniprot-TrEMBL)
PI4K2A/2BComplexR-HSA-1806167 (Reactome)
PI4K2B ProteinQ8TCG2 (Uniprot-TrEMBL)
PI4KA ProteinP42356 (Uniprot-TrEMBL)
PI4KA/2A/2BComplexR-HSA-1806171 (Reactome)
PI4KA/2BComplexR-HSA-1806271 (Reactome)
PI4KB ProteinQ9UBF8 (Uniprot-TrEMBL)
PI4KBProteinQ9UBF8 (Uniprot-TrEMBL)
PI4PMetaboliteCHEBI:17526 (ChEBI)
PI5PMetaboliteCHEBI:16500 (ChEBI)
PI:PITPNBComplexR-HSA-1524117 (Reactome)
PI:PITPNBComplexR-HSA-1524150 (Reactome)
PIMetaboliteCHEBI:16749 (ChEBI)
PIK3(2)ComplexR-HSA-1806189 (Reactome)
PIK3C(1)ComplexR-HSA-1806233 (Reactome)
PIK3C2A ProteinO00443 (Uniprot-TrEMBL)
PIK3C2A/3ComplexR-HSA-1806185 (Reactome)
PIK3C2A/GComplexR-HSA-1806247 (Reactome)
PIK3C2A:Ca2+/Mg2+ComplexR-HSA-1604655 (Reactome)
PIK3C2B ProteinO00750 (Uniprot-TrEMBL)
PIK3C2G ProteinO75747 (Uniprot-TrEMBL)
PIK3C3 ProteinQ8NEB9 (Uniprot-TrEMBL)
PIK3CA ProteinP42336 (Uniprot-TrEMBL)
PIK3CB ProteinP42338 (Uniprot-TrEMBL)
PIK3CD ProteinO00329 (Uniprot-TrEMBL)
PIK3CG ProteinP48736 (Uniprot-TrEMBL)
PIK3R1 ProteinP27986 (Uniprot-TrEMBL)
PIK3R2 ProteinO00459 (Uniprot-TrEMBL)
PIK3R3 ProteinQ92569 (Uniprot-TrEMBL)
PIK3R4 ProteinQ99570 (Uniprot-TrEMBL)
PIK3R5 ProteinQ8WYR1 (Uniprot-TrEMBL)
PIK3R6 ProteinQ5UE93 (Uniprot-TrEMBL)
PIKFYVE ProteinQ9Y2I7 (Uniprot-TrEMBL)
PIKFYVE:VAC14:FIG4ComplexR-HSA-1806169 (Reactome)
PIKFYVE:VAC14:FIG4ComplexR-HSA-1806187 (Reactome)
PIKFYVE:VAC14:FIG4ComplexR-HSA-1806269 (Reactome)
PIP4K2/5K1ComplexR-HSA-1806163 (Reactome)
PIP4K2A ProteinP48426 (Uniprot-TrEMBL)
PIP4K2A/BComplexR-HSA-1806229 (Reactome)
PIP4K2B ProteinP78356 (Uniprot-TrEMBL)
PIP5K1A ProteinQ99755 (Uniprot-TrEMBL)
PIP5K1A-CComplexR-HSA-1806157 (Reactome)
PIP5K1A/BComplexR-HSA-1806245 (Reactome)
PIP5K1B ProteinO14986 (Uniprot-TrEMBL)
PIP5K1C ProteinO60331 (Uniprot-TrEMBL)
PITPNB ProteinP48739 (Uniprot-TrEMBL)
PTEN ProteinP60484 (Uniprot-TrEMBL)
PTEN:Mg2+ComplexR-HSA-199426 (Reactome)
PiMetaboliteCHEBI:18367 (ChEBI)
SACM1LProteinQ9NTJ5 (Uniprot-TrEMBL)
SYNJ/INPP5(1)ComplexR-HSA-1806214 (Reactome)
SYNJ/MTM(1)ComplexR-HSA-1806223 (Reactome)
SYNJ1 ProteinO43426 (Uniprot-TrEMBL)
SYNJ2 ProteinO15056 (Uniprot-TrEMBL)
SYNJComplexR-HSA-1806173 (Reactome)
TPTE ProteinP56180 (Uniprot-TrEMBL)
TPTE2 ProteinQ6XPS3 (Uniprot-TrEMBL)
TPTE2-like proteinsComplexR-HSA-3968346 (Reactome) This CandidateSet contains sequences identified by William Pearson's analysis of Reactome catalyst entities. Catalyst entity sequences were used to identify analagous sequences that shared overall homology and active site homology. Sequences in this Candidate set were identified in an April 24, 2012 analysis.
VAC14 ProteinQ08AM6 (Uniprot-TrEMBL)

Annotated Interactions

View all...
SourceTargetTypeDatabase referenceComment
ADPArrowR-HSA-1675773 (Reactome)
ADPArrowR-HSA-1675776 (Reactome)
ADPArrowR-HSA-1675780 (Reactome)
ADPArrowR-HSA-1675810 (Reactome)
ADPArrowR-HSA-1675813 (Reactome)
ADPArrowR-HSA-1675866 (Reactome)
ADPArrowR-HSA-1675883 (Reactome)
ADPArrowR-HSA-1675910 (Reactome)
ADPArrowR-HSA-1675921 (Reactome)
ADPArrowR-HSA-1675928 (Reactome)
ADPArrowR-HSA-1675939 (Reactome)
ADPArrowR-HSA-1675961 (Reactome)
ADPArrowR-HSA-1675974 (Reactome)
ADPArrowR-HSA-1676024 (Reactome)
ADPArrowR-HSA-1676048 (Reactome)
ADPArrowR-HSA-1676082 (Reactome)
ADPArrowR-HSA-1676109 (Reactome)
ADPArrowR-HSA-1676134 (Reactome)
ADPArrowR-HSA-1676145 (Reactome)
ADPArrowR-HSA-1676168 (Reactome)
ADPArrowR-HSA-1676185 (Reactome)
ADPArrowR-HSA-1676206 (Reactome)
ARF1/3:GTP:PI4KBArrowR-HSA-1676152 (Reactome)
ARF1/3:GTP:PI4KBmim-catalysisR-HSA-1675883 (Reactome)
ARF1/3:GTPR-HSA-1676152 (Reactome)
ATPR-HSA-1675773 (Reactome)
ATPR-HSA-1675776 (Reactome)
ATPR-HSA-1675780 (Reactome)
ATPR-HSA-1675810 (Reactome)
ATPR-HSA-1675813 (Reactome)
ATPR-HSA-1675866 (Reactome)
ATPR-HSA-1675883 (Reactome)
ATPR-HSA-1675910 (Reactome)
ATPR-HSA-1675921 (Reactome)
ATPR-HSA-1675928 (Reactome)
ATPR-HSA-1675939 (Reactome)
ATPR-HSA-1675961 (Reactome)
ATPR-HSA-1675974 (Reactome)
ATPR-HSA-1676024 (Reactome)
ATPR-HSA-1676048 (Reactome)
ATPR-HSA-1676082 (Reactome)
ATPR-HSA-1676109 (Reactome)
ATPR-HSA-1676134 (Reactome)
ATPR-HSA-1676145 (Reactome)
ATPR-HSA-1676168 (Reactome)
ATPR-HSA-1676185 (Reactome)
ATPR-HSA-1676206 (Reactome)
H2OR-HSA-1675795 (Reactome)
H2OR-HSA-1675824 (Reactome)
H2OR-HSA-1675836 (Reactome)
H2OR-HSA-1675949 (Reactome)
H2OR-HSA-1675988 (Reactome)
H2OR-HSA-1675994 (Reactome)
H2OR-HSA-1676005 (Reactome)
H2OR-HSA-1676020 (Reactome)
H2OR-HSA-1676065 (Reactome)
H2OR-HSA-1676105 (Reactome)
H2OR-HSA-1676114 (Reactome)
H2OR-HSA-1676124 (Reactome)
H2OR-HSA-1676141 (Reactome)
H2OR-HSA-1676149 (Reactome)
H2OR-HSA-1676162 (Reactome)
H2OR-HSA-1676164 (Reactome)
H2OR-HSA-1676174 (Reactome)
H2OR-HSA-1676177 (Reactome)
H2OR-HSA-1676191 (Reactome)
H2OR-HSA-1676203 (Reactome)
H2OR-HSA-1676204 (Reactome)
INPP4A/Bmim-catalysisR-HSA-1676162 (Reactome)
INPP4A/Bmim-catalysisR-HSA-1676164 (Reactome)
INPP5(2)mim-catalysisR-HSA-1675949 (Reactome)
MTM(2)mim-catalysisR-HSA-1676105 (Reactome)
MTM(2)mim-catalysisR-HSA-1676141 (Reactome)
MTM(3)mim-catalysisR-HSA-1675795 (Reactome)
MTM(3)mim-catalysisR-HSA-1676065 (Reactome)
OCRL/INPP5Emim-catalysisR-HSA-1675824 (Reactome)
PC:PITPNBArrowR-HSA-1483087 (Reactome)
PC:PITPNBArrowR-HSA-1483211 (Reactome)
PC:PITPNBR-HSA-1483211 (Reactome)
PC:PITPNBR-HSA-1483219 (Reactome)
PCArrowR-HSA-1483219 (Reactome)
PCR-HSA-1483087 (Reactome)
PI(3,4)P2ArrowR-HSA-1675834 (Reactome)
PI(3,4)P2ArrowR-HSA-1675928 (Reactome)
PI(3,4)P2ArrowR-HSA-1675949 (Reactome)
PI(3,4)P2ArrowR-HSA-1676109 (Reactome)
PI(3,4)P2ArrowR-HSA-1676145 (Reactome)
PI(3,4)P2ArrowR-HSA-1676206 (Reactome)
PI(3,4)P2R-HSA-1675773 (Reactome)
PI(3,4)P2R-HSA-1675834 (Reactome)
PI(3,4)P2R-HSA-1676149 (Reactome)
PI(3,4)P2R-HSA-1676162 (Reactome)
PI(3,4)P2R-HSA-1676164 (Reactome)
PI(3,4)P2R-HSA-1676204 (Reactome)
PI(3,4,5)P3ArrowR-HSA-1675773 (Reactome)
PI(3,4,5)P3ArrowR-HSA-1676048 (Reactome)
PI(3,4,5)P3R-HSA-1675949 (Reactome)
PI(3,4,5)P3R-HSA-1676191 (Reactome)
PI(3,5)P2ArrowR-HSA-1675896 (Reactome)
PI(3,5)P2ArrowR-HSA-1675910 (Reactome)
PI(3,5)P2ArrowR-HSA-1675921 (Reactome)
PI(3,5)P2ArrowR-HSA-1676041 (Reactome)
PI(3,5)P2ArrowR-HSA-1676134 (Reactome)
PI(3,5)P2ArrowR-HSA-1676161 (Reactome)
PI(3,5)P2ArrowR-HSA-1676168 (Reactome)
PI(3,5)P2R-HSA-1675836 (Reactome)
PI(3,5)P2R-HSA-1675896 (Reactome)
PI(3,5)P2R-HSA-1676005 (Reactome)
PI(3,5)P2R-HSA-1676020 (Reactome)
PI(3,5)P2R-HSA-1676041 (Reactome)
PI(3,5)P2R-HSA-1676065 (Reactome)
PI(3,5)P2R-HSA-1676105 (Reactome)
PI(3,5)P2R-HSA-1676161 (Reactome)
PI(3,5)P2R-HSA-1676174 (Reactome)
PI(3,5)P2R-HSA-1676203 (Reactome)
PI(4,5)P2ArrowR-HSA-1675776 (Reactome)
PI(4,5)P2ArrowR-HSA-1676082 (Reactome)
PI(4,5)P2ArrowR-HSA-1676191 (Reactome)
PI(4,5)P2R-HSA-1675824 (Reactome)
PI(4,5)P2R-HSA-1676048 (Reactome)
PI(4,5)P2R-HSA-1676177 (Reactome)
PI3PArrowR-HSA-1675836 (Reactome)
PI3PArrowR-HSA-1675939 (Reactome)
PI3PArrowR-HSA-1675961 (Reactome)
PI3PArrowR-HSA-1676005 (Reactome)
PI3PArrowR-HSA-1676020 (Reactome)
PI3PArrowR-HSA-1676024 (Reactome)
PI3PArrowR-HSA-1676162 (Reactome)
PI3PArrowR-HSA-1676164 (Reactome)
PI3PArrowR-HSA-1676174 (Reactome)
PI3PR-HSA-1675795 (Reactome)
PI3PR-HSA-1675910 (Reactome)
PI3PR-HSA-1675921 (Reactome)
PI3PR-HSA-1675994 (Reactome)
PI3PR-HSA-1676114 (Reactome)
PI3PR-HSA-1676134 (Reactome)
PI3PR-HSA-1676141 (Reactome)
PI3PR-HSA-1676145 (Reactome)
PI3PR-HSA-1676168 (Reactome)
PI4K2A/2Bmim-catalysisR-HSA-1675780 (Reactome)
PI4K2A/2Bmim-catalysisR-HSA-1675974 (Reactome)
PI4KA/2A/2Bmim-catalysisR-HSA-1676185 (Reactome)
PI4KA/2Bmim-catalysisR-HSA-1675813 (Reactome)
PI4KBR-HSA-1676152 (Reactome)
PI4PArrowR-HSA-1675780 (Reactome)
PI4PArrowR-HSA-1675813 (Reactome)
PI4PArrowR-HSA-1675815 (Reactome)
PI4PArrowR-HSA-1675824 (Reactome)
PI4PArrowR-HSA-1675883 (Reactome)
PI4PArrowR-HSA-1675974 (Reactome)
PI4PArrowR-HSA-1676149 (Reactome)
PI4PArrowR-HSA-1676177 (Reactome)
PI4PArrowR-HSA-1676185 (Reactome)
PI4PArrowR-HSA-1676204 (Reactome)
PI4PR-HSA-1675815 (Reactome)
PI4PR-HSA-1675928 (Reactome)
PI4PR-HSA-1675988 (Reactome)
PI4PR-HSA-1676082 (Reactome)
PI4PR-HSA-1676109 (Reactome)
PI4PR-HSA-1676124 (Reactome)
PI4PR-HSA-1676133 (Reactome)
PI4PR-HSA-1676206 (Reactome)
PI5PArrowR-HSA-1675810 (Reactome)
PI5PArrowR-HSA-1675866 (Reactome)
PI5PArrowR-HSA-1676065 (Reactome)
PI5PArrowR-HSA-1676105 (Reactome)
PI5PArrowR-HSA-1676203 (Reactome)
PI5PR-HSA-1675776 (Reactome)
PI:PITPNBArrowR-HSA-1483219 (Reactome)
PI:PITPNBArrowR-HSA-1483229 (Reactome)
PI:PITPNBR-HSA-1483087 (Reactome)
PI:PITPNBR-HSA-1483229 (Reactome)
PIArrowR-HSA-1483087 (Reactome)
PIArrowR-HSA-1675795 (Reactome)
PIArrowR-HSA-1675988 (Reactome)
PIArrowR-HSA-1675994 (Reactome)
PIArrowR-HSA-1676114 (Reactome)
PIArrowR-HSA-1676124 (Reactome)
PIArrowR-HSA-1676133 (Reactome)
PIArrowR-HSA-1676141 (Reactome)
PIK3(2)mim-catalysisR-HSA-1676109 (Reactome)
PIK3C(1)mim-catalysisR-HSA-1676048 (Reactome)
PIK3C2A/3mim-catalysisR-HSA-1675939 (Reactome)
PIK3C2A/3mim-catalysisR-HSA-1675961 (Reactome)
PIK3C2A/3mim-catalysisR-HSA-1676024 (Reactome)
PIK3C2A/Gmim-catalysisR-HSA-1675928 (Reactome)
PIK3C2A:Ca2+/Mg2+mim-catalysisR-HSA-1676206 (Reactome)
PIKFYVE:VAC14:FIG4mim-catalysisR-HSA-1675866 (Reactome)
PIKFYVE:VAC14:FIG4mim-catalysisR-HSA-1675910 (Reactome)
PIKFYVE:VAC14:FIG4mim-catalysisR-HSA-1675921 (Reactome)
PIKFYVE:VAC14:FIG4mim-catalysisR-HSA-1676005 (Reactome)
PIKFYVE:VAC14:FIG4mim-catalysisR-HSA-1676020 (Reactome)
PIKFYVE:VAC14:FIG4mim-catalysisR-HSA-1676168 (Reactome)
PIKFYVE:VAC14:FIG4mim-catalysisR-HSA-1676174 (Reactome)
PIP4K2/5K1mim-catalysisR-HSA-1676145 (Reactome)
PIP4K2A/Bmim-catalysisR-HSA-1675776 (Reactome)
PIP5K1A-Cmim-catalysisR-HSA-1675773 (Reactome)
PIP5K1A-Cmim-catalysisR-HSA-1676082 (Reactome)
PIP5K1A/Bmim-catalysisR-HSA-1675810 (Reactome)
PIP5K1A/Bmim-catalysisR-HSA-1676134 (Reactome)
PIR-HSA-1483219 (Reactome)
PIR-HSA-1675780 (Reactome)
PIR-HSA-1675810 (Reactome)
PIR-HSA-1675813 (Reactome)
PIR-HSA-1675866 (Reactome)
PIR-HSA-1675883 (Reactome)
PIR-HSA-1675939 (Reactome)
PIR-HSA-1675961 (Reactome)
PIR-HSA-1675974 (Reactome)
PIR-HSA-1676024 (Reactome)
PIR-HSA-1676185 (Reactome)
PTEN:Mg2+mim-catalysisR-HSA-1676149 (Reactome)
PTEN:Mg2+mim-catalysisR-HSA-1676191 (Reactome)
PiArrowR-HSA-1675795 (Reactome)
PiArrowR-HSA-1675824 (Reactome)
PiArrowR-HSA-1675836 (Reactome)
PiArrowR-HSA-1675949 (Reactome)
PiArrowR-HSA-1675988 (Reactome)
PiArrowR-HSA-1675994 (Reactome)
PiArrowR-HSA-1676005 (Reactome)
PiArrowR-HSA-1676020 (Reactome)
PiArrowR-HSA-1676065 (Reactome)
PiArrowR-HSA-1676105 (Reactome)
PiArrowR-HSA-1676114 (Reactome)
PiArrowR-HSA-1676124 (Reactome)
PiArrowR-HSA-1676133 (Reactome)
PiArrowR-HSA-1676141 (Reactome)
PiArrowR-HSA-1676149 (Reactome)
PiArrowR-HSA-1676162 (Reactome)
PiArrowR-HSA-1676164 (Reactome)
PiArrowR-HSA-1676174 (Reactome)
PiArrowR-HSA-1676177 (Reactome)
PiArrowR-HSA-1676191 (Reactome)
PiArrowR-HSA-1676203 (Reactome)
PiArrowR-HSA-1676204 (Reactome)
R-HSA-1483087 (Reactome) At the Golgi membrane, phosphatidylinositol (PI) is exchanged for phosphatidylcholine (PC) within the phosphatidylinositol transfer protein beta isoform (PITPNB) complex (Tilley et al. 2004, Yolder et al. 2001, Carvou et al. 2010, Schouten et al. 2002, Vordtriede et al. 2005, Shadan et al. 2008).
R-HSA-1483211 (Reactome) The complex between phosphatidylcholine (PC) and phosphatidylinositol transfer protein beta isoform (PITPNB) transports from the Golgi membrane to the ER membrane (Carvou et al. 2010, Shadan et al. 2008).
R-HSA-1483219 (Reactome) At the ER membrane, phosphatidylcholine (PC) is exchanged for phosphatidylinositol (PI) within the phosphatidylinositol transfer protein beta isoform (PITPNB) complex (Tilley et al. 2004, Yolder et al. 2001, Carvou et al. 2010, Schouten et al. 2002, Vordtriede et al. 2005, Shadan et al. 2008).
R-HSA-1483229 (Reactome) The phosphatidylinositol transfer protein beta isoform (PITPNB) bound to phosphatidylinositol (PI) complex transports from the endoplasmic reticulum (ER) membrane to the Golgi membrane (Carvou et al. 2010, Shadan et al. 2008).
R-HSA-1675773 (Reactome) At the plasma membrane, phosphatidylinositol-4-phosphate 5-kinase type-1 alpha (PIP5K1A), beta (PIP5K1B), and gamma (PIP5K1C) phosphorylate phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2) to produce phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3). This is a minor reaction, however, and its physiological role is uncertain.

The following lists the above proteins with their corresponding literature references: PIP5K1A (Zhang et al. 1997, Tolias et al. 1998), PIP5K1B (Zhang et al. 1997, Tolias et al. 1998), and PIP5K1C (Wenk et al. 2001, Di Paolo et al. 2002, Krauss et al. 2003).
R-HSA-1675776 (Reactome) At the plasma membrane, phosphatidylinositol-5-phosphate 4-kinase type-2 alpha (PIP4K2A) and beta (PIP4K2B) homodimers and heterodimers (Clarke et al. 2010) phosphorylate phosphatidylinositol 5-phosphate (PI5P) to phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2).

The following lists the above proteins with their corresponding literature references: PIP4K2A (Rameh et al. 1997, Clarke et al. 2008) and PIP4K2B (Rameh et al. 1997).
R-HSA-1675780 (Reactome) At the plasma membrane, phosphatidylinositol 4-kinase type 2-alpha (PI4K2A) (Balla et al. 2002, Minogue et al. 2001) and beta (PI4K2B) (Balla et al. 2002, Wei et al. 2002) phosphorylate phosphatidylinositol (PI) to phosphatidylinositol 4-phosphate (PI4P).
R-HSA-1675795 (Reactome) At the late endosome membrane, myotubularin (MTM1), myotubularin-related protein 2 (MTMR2), myotubularin-related protein 4 (MTMR4), and myotubularin-related protein 7 (MTMR7) dephosphorylate phosphatidylinositol 3-phosphate (PI3P) to phosphatidylinositol (PI).

The following lists the above proteins with their corresponding literature references: MTM1 (Cao et al. 2007, Cao et al. 2008, Tsujita et al. 2004, Tronchere et al. 2004, Kim et al. 2002); MTMR2 (Cao et al. 2008, Kim et al. 2002); MTMR4 (Lorenzo et al. 2006); and MTMR7 (Mochizuki & Majerus 2003, Lorenzo et al. 2006).
R-HSA-1675810 (Reactome) At the plasma membrane, phosphatidylinositol-4-phosphate 5-kinase type-1 alpha (PIP5K1A) and beta (PIP5K1B) phosphorylate phosphatidylinositol (PI) to produce phosphatidylinositol 5-phosphate (PI5P) (Tolias et al. 1998).
R-HSA-1675813 (Reactome) At the endoplasmic reticulum (ER) membrane, phosphatidylinositol 4-kinase alpha (PI4KA) (Wong et al. 1997, Gehrmann et al. 1999) or phosphatidylinositol 4-kinase type 2-beta (PI4K2B) (Wei et al. 2002) phosphorylate phosphatidylinositol (PI) to produce phosphatidylinositol 4-phosphate (PI4P).
R-HSA-1675815 (Reactome) Phosphatidylinositol 4-phosphate (PI4P) translocates from the Golgi membrane to the plasma membrane via a secretory vesicle mechanism (Szentpetery et al. 2010, Godi et al. 2004, Hammond et al. 2009).
R-HSA-1675824 (Reactome) At the Golgi membrane, phosphatidylinositol 4-phosphate (PI4P) inositol polyphosphate 5-phosphatase OCRL-1 (OCRL) (Choudhury et al. 2009, Suchy et al. 1995, Zhang et al. 1995) and 72 kDa inositol polyphosphate 5-phosphatase (INPP5E) (Bilas et al. 2009) dephosphorylate phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) to form phosphatidylinositol 4-phosphate (PI4P). INPP5E is located in the Golgi membrane, mediated by its N-terminal proline-rich domain (Kong et al. 2000).
R-HSA-1675834 (Reactome) In mice, phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2) translocates from the plasma membrane to the early endosome membrane (Watt et al. 2004). A similar event has also been detected in cells from Chlorocebus sabaeus (Green Monkey) (Ivetac et al. 2005). In humans this event is inferred from the other two occurrences.
R-HSA-1675836 (Reactome) At the plasma membrane, synaptic inositol-1,4,5-trisphosphate 5-phosphatase 1 aka synaptojanin-1 (SYNJ1) (Guo et al. 1999, Mani et al. 2007) and -2 (SYNJ2) (Malecz et al. 2000) dephosphorylate phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) to phosphatidylinositol 3-phosphate (PI3P).
R-HSA-1675866 (Reactome) At the late endosome membrane, the PAS complex, consisting of FYVE finger-containing phosphoinositide kinase (PIKFYVE), yeast VAC14 homologue (VAC14), and polyphosphoinositide phosphatase aka SAC3 (FIG4), binds to the membrane via PIKFYVE's FYVE finger. The PIKFYVE kinase component phosphorylates phosphatidylinositol (PI) to phosphatidylinositol 5-phosphate (PI5P) (Sbrissa et al. 1999, Sbrissa et al. 2002). The PAS complex is present in the cytosol and is recruited to the membrane.
R-HSA-1675883 (Reactome) At the Golgi membrane, activated phosphatidylinositol 4-kinase beta (PI4KB) complexed to ADP-ribosylation factor 1/3 (ARF1/3) phosphorylates phosphatidylinositol (PI) to phosphatidylinositol 4-phosphate (PI4P) (Suzuki et al. 1997).
R-HSA-1675896 (Reactome) Phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) translocates from the early endosome membrane to the Golgi membrane (Rutherford et al. 2006).
R-HSA-1675910 (Reactome) At the late endosome membrane, the PAS complex, consisting of FYVE finger-containing phosphoinositide kinase (PIKFYVE), yeast VAC14 homologue (VAC14), and polyphosphoinositide phosphatase aka SAC3 (FIG4), binds to the membrane via PIKFYVE's FYVE finger (Sbrissa et al. 2002, Cao et al. 2007). The PIKFYVE kinase component phosphorylates phosphatidylinositol 3-phosphate (PI3P) to phosphatidylinositol 3,5-bisphosphate PI(3,5)P2 (Sbrissa et al. 1999). The PAS complex is present in the cytosol and is recruited to the membrane (Sbrissa et al. 2007).
R-HSA-1675921 (Reactome) At the Golgi membrane, the PAS complex, consisting of FYVE finger-containing phosphoinositide kinase (PIKFYVE), yeast VAC14 homologue (VAC14), and polyphosphoinositide phosphatase aka SAC3 (FIG4), binds to the membrane via PIKFYVE's FYVE finger (Sbrissa et al. 2002). The PIKFYVE kinase component phosphorylates phosphatidylinositol 3-phosphate (PI3P) to phosphatidylinositol 3,5-bisphosphate PI(3,5)P2 (Sbrissa et al. 1999, McEwen et al. 1999). The PAS complex is present in the cytosol and is recruited to the membrane (Sbrissa et al. 2007). VAC14 acts as a scaffolding protein via its C-terminal domain (Sbrissa et al. 2008).
R-HSA-1675928 (Reactome) At the Golgi membrane, phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunit alpha (PIK3C2A) (Domin et al. 2000, Arcaro et al. 2000) and phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunit gamma (PIK3C2G) (Ono et al. 1998, Rozycka et al. 1998, Misawa et al. 1998) phosphorylate phosphatidylinositol 4-phosphate (PI4P) to phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2). PIK3C2G phosphorylates phosphatidylinositol (PI) and PI4P but not phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2).
R-HSA-1675939 (Reactome) At the early endosome membrane, phosphatidylinositol 3-kinase catalytic subunit type 3 (PIK3C3) aka VPS34 binds to phosphoinositide 3-kinase regulatory subunit 4 (PIK3R4). The PIK3C3:PIK3R4 complex and phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunit alpha (PIK3C2A) phosphorylate phosphatidylinositol (PI) to phosphatidylinositol 3-phosphate (PI3P).

The following lists the above proteins with their corresponding literature references: PIK3C3:PIK3R4 complex (Panaretou et al. 1997, Volinia et al. 1995, Cao et al. 2007) and PIK3C2A (Arcaro et al. 2000, Domin et al. 2000).
R-HSA-1675949 (Reactome) At the plasma membrane, phosphatidylinositol 5-phosphatases dephosphorylate phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3) to phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2). The phosphatidylinositol 5-phosphatases involved are: inositol polyphosphate 5-phosphatase K (INPP5K) aka SKIP (Ijuin et al. 2000, Gurung et al. 2003), phosphatidylinositol 4,5-bisphosphate 5-phosphatase A (INPP5J) aka PIPP (Gurung et al. 2003, Mochizuki & Takenawa 1999), phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 1 (INPP5D) aka SHIP1 (Drayer et al. 1995, Kavanaugh et al. 1996, Dunant et al. 2000), and phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2 (INPPL1) aka SHIP2 (Habib et al. 1998, Wisniewski et al. 1999, Pesesse et al. 2001).
R-HSA-1675961 (Reactome) At the Golgi membrane, phosphatidylinositol 3-kinase catalytic subunit type 3 (PIK3C3) aka VPS34 is bound to phosphoinositide 3-kinase regulatory subunit 4 (PIK3R4). This PIK3C3:PIK2R4 complex and phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunit alpha (PIK3C2A) phosphorylate phosphatidylinositol (PI) to phosphatidylinositol 3-phosphate (PI3P).

The following lists the above proteins with their corresponding literature references: PIK3C3:PIK2R4 (Panaretou et al. 1997, Volinia et al. 1995) and PIK3C2A (Arcaro et al. 2000, Domin et al. 2000).
R-HSA-1675974 (Reactome) At the early endosome membrane, phosphatidylinositol 4-kinase type 2-alpha/beta (PI4K2A/B) (Balla et al. 2002) phosphorylates phosphatidylinositol (PI) to produce phosphatidylinositol 4-phosphate (PI4P).
R-HSA-1675988 (Reactome) At the plasma membrane, synaptic inositol-1,4,5-trisphosphate 5-phosphatase 1 aka Synaptojanin-1 (SYNJ1) (Guo et al. 1999, Mani et al. 2007, Johenning et al. 2004) and -2 (SYNJ2) (Malecz et al. 2000) dephosphorylate phosphatidylinositol 4-phosphate (PI4P) phosphatidylinositol (PI). The SAC1 domains of SYNJ1 and SYNJ2 demonstrate 4-phosphatase activity.
R-HSA-1675994 (Reactome) At the plasma membrane, synaptojanin-1 aka Synaptic inositol-1,4,5-trisphosphate 5-phosphatase 1 (SYNJ1) (Guo et al. 1999), -2 (SYNJ2) and some myotubularins (MTMs) dephosphorylate phosphatidylinositol 3-phosphate (PI3P) to phosphatidylinositol (PI). The MTMs involved are: myotubularin (MTM1) (Cao et al. 2007, Tronchere et al. 2004, Schaletzky et al. 2003, Laporte et al. 2002, Kim et al. 2002) and myotubularin-related proteins 1 (MTMR1) (Kim et al. 2002, Tronchere et al. 2004), 3 (MTMR3) (Kim et al. 2002, Zhao et al. 2001, Walker et al. 2001, Lorenzo et al. 2005), 6 (MTMR6) (Schaletzky et al. 2003, Kim et al. 2002, Choudhury et al. 2006), and 14 (MTMR14) (Tosch et al. 2006).
R-HSA-1676005 (Reactome) At the Golgi membrane, the PAS complex, consisting of FYVE finger-containing phosphoinositide kinase (PIKFYVE), yeast VAC14 homologue (VAC14), and polyphosphoinositide phosphatase aka SAC3 (FIG4), binds to the membrane via PIKFYVE's FYVE finger. The FIG4 phosphatase component dephosphorylates phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) to phosphatidylinositol 3-phosphate (PI3P) (Sbrissa et al. 2007, Sbrissa et al. 2008).
R-HSA-1676020 (Reactome) At the late endosome membrane, the PAS complex, consisting of FYVE finger-containing phosphoinositide kinase (PIKFYVE), yeast VAC14 homologue (VAC14), and polyphosphoinositide phosphatase aka SAC3 (FIG4), binds to the membrane via PIKFYVE's FYVE finger. The FIG4 phosphatase component dephosphorylates phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) to phosphatidylinositol 3-phosphate (PI3P) (Sbrissa et al. 2007, Sbrissa et al. 2008).
R-HSA-1676024 (Reactome) At the late endosome membrane, phosphatidylinositol 3-kinase catalytic subunit type 3 (PIK3C3) aka VPS34 binds to phosphoinositide 3-kinase regulatory subunit 4 (PIK3R4). The PIK3C3:PIK3R4 complex and phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunit alpha (PIK3C2A) phosphorylate phosphatidylinositol (PI) to phosphatidylinositol 3-phosphate (PI3P).

The following lists the above proteins with their corresponding literature references: PIK3C3:PIK3R4 (Panaretou et al. 1997, Volinia et al. 1995, Cao et al. 2007) and PIK3C2A (Arcaro et al. 2000, Domin et al. 2000).
R-HSA-1676041 (Reactome) The presence of phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) in the early endosome membrane stimulates the vesicle maturation into the late endosome (Cabezas et al. 2006, Ikonomov et al. 2006, Ikonomov et al. 2001).
R-HSA-1676048 (Reactome) At the plasma membrane, phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunits form complexes with regulatory subunits. These complexes phosphorylate phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) to phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3) (Stephens et al. 1997). The PI(4,5)P2 3-kinase complexes involved are: PI(4,5)P2 3-kinase catalytic subunit alpha isoform (PIK3CA) bound to PI 3-kinase regulatory subunit alpha/beta/gamma (PIK3R1/2/3); beta (PIK3CB) bound to PIK3R1/2/3; delta (PIK3CD) bound to PIK3R1/2/3; and gamma (PIK3CG) bound to PI 3-kinase regulatory subunit 5 (PIK3R5) or 6 (PIK3R6).

The following lists the above proteins with their corresponding literature references: PIK3CA:PIK3R1, PIK3CA:PIK3R2, PIK3CA:PIK3R3 (Dey et al. 1998, Vanhaesebroeck et al. 1997, Meier et al. 2004); PIK3CB:PIK3R1, PIK3CB:PIK3R2, PIK3CB:PIK3R3 (Meier et al. 2004); PIK3CD:PIK3R1, PIK3CD:PIK3R2, PIK3CD:PIK3R3 (Vanhaesebroeck et al. 1997, Meier et al. 2004); and PIK3CG:PIK3R5, PIK3CG:PIK3R6 (Voigt et al. 2006, Suire et al. 2005, Stoyanov et al. 1995).
R-HSA-1676065 (Reactome) At the late endosome membrane, myotubularin (MTM1), myotubularin-related protein 2 (MTMR2), myotubularin-related protein 4 (MTMR4), and myotubularin-related protein 7 (MTMR7) dephosphorylate phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) to phosphatidylinositol 5-phosphate (PI5P).

The following lists the above proteins with their corresponding literature references: MTM1 (Cao et al. 2007, Cao et al. 2008, Tsujita et al. 2004, Tronchere et al. 2004), MTMR2 (Cao et al. 2008), MTMR4 (Lorenzo et al. 2006), and MTMR7 (Mochizuki & Majerus 2003, Lorenzo et al. 2006).
R-HSA-1676082 (Reactome) At the plasma membrane, phosphatidylinositol-4-phosphate 5-kinase type-1 alpha (PIP5K1A), beta (PIP5K1B), and gamma (PIP5K1C) phosphorylate phosphatidylinositol 4-phosphate (PI4P) to produce phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2).

The following lists the above proteins with their corresponding literature references: PIP5K1A (Halstead et al. 2006, Zhang et al. 1997), PIP5K1B (Zhang et al. 1997), and PIP5K1C (Di Paolo et al. 2002).

This reaction is of particular interest because its regulation by small GTPases of the RHO and ARF families, not yet annotated here, ties the process of phosphatidylinositol phosphate biosynthesis to regulation of the actin cytoskeleton and vesicular trafficking, and hence to diverse aspects of cell motility and signalling (Oude Weernink et al., 2004, 2007).
R-HSA-1676105 (Reactome) At the early endosome membrane, myotubularin (MTM1), myotubularin-related protein 2 (MTMR2) and myotubularin-related protein 4 (MTMR4) dephosphorylate phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) to phosphatidylinositol 5-phosphate (PI5P).

The following lists the above proteins with their corresponding literature references: MTM1 (Cao et al. 2007, Cao et al. 2008), MTMR2 (Cao et al. 2008), and MTMR4 (Lorenzo et al. 2006).
R-HSA-1676109 (Reactome) At the plasma membrane, phosphatidylinositol-4,5-bisphosphate (PI(4,5)P2) 3-kinase catalytic subunits form complexes with regulatory subunits. These complexes along with phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunits alpha (PIK3C2A), beta (PIK3C2B), and gamma (PIK3C2G) phosphorylate phosphatidylinositol 4-phosphate (PI4P) to phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2). The PI(4,5)P2 3-kinase complexes involved are: PI(4,5)P2 3-kinase catalytic subunit alpha isoform (PIK3CA) bound to PI 3-kinase regulatory subunit alpha/beta/gamma (PIK3R1/2/3); beta (PIK3CB) bound to PIK3R1/2/3; delta (PIK3CD) bound to PIK3R1/2/3; and gamma (PIK3CG) bound to PI 3-kinase regulatory subunit 5 (PIK3R5) or 6 (PIK3R6).

The following lists the above proteins with their corresponding literature references: PIK3C2A (Arcaro et al. 2000); PIK3C2B (Arcaro et al. 2000, Arcaro et al. 1998); PIK3C2G (Misawa et al. 1998, Ono et al. 1998); PIK3CA:PIK3R1, PIK3CA:PIK3R2, PIK3CA:PIK3R3 (Vanhaesebroeck et al. 1997); PIK3CB:PIK3R1, PIK3CB:PIK3R2, PIK3CB:PIK3R3 (Meier et al. 2004, Guo et al. 1997); PIK3CD:PIK3R1, PIK3CD:PIK3R2, PIK3CD:PIK3R3 (Vanhaesebroeck et al. 1997); and PIK3CG:PIK3R5, PIK3CG:PIK3R6 (Suire et al. 2005, Stoyanov et al. 1995).
R-HSA-1676114 (Reactome) At the Golgi membrane, phosphatidylinositide phosphatase SAC1 (SACM1L) dephosphorylates phosphatidylinositol 3-phosphate (PI3P) to phosphatidylinositol (PI) but not as efficiently as phosphatidylinositol 4-phosphate (PI4P) dephosphorylation. No significant activity of this enzyme towards phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) was detected (Rohde et al. 2003).
R-HSA-1676124 (Reactome) At the endoplasmic reticulum (ER) membrane, transmembrane protein phosphatidylinositide phosphatase SAC1 (SACM1L) efficiently dephosphorylates phosphatidylinositol 4-phosphate (PI4P), and to a lesser extent phosphatidylinositol 3-phosphate (PI3P), to phosphatidylinositol (PI). No significant activity of this enzyme towards phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) was detected (Rohde et al. 2003).
R-HSA-1676133 (Reactome) At the Golgi membrane, phosphatidylinositide phosphatase SAC1 (SACM1L) efficiently dephosphorylates phosphatidylinositol 4-phosphate (PI4P), and to a lesser extent phosphatidylinositol 3-phosphate (PI3P), to phosphatidylinositol (PI). No significant activity of this enzyme towards phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) was detected (Rohde et al. 2003).
R-HSA-1676134 (Reactome) At the plasma membrane, phosphatidylinositol-4-phosphate 5-kinase type-1 alpha (PIP5K1A) and beta (PIP5K1B) phosphorylate phosphatidylinositol 3-phosphate (PI3P) to phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) (Tolias et al. 1998).
R-HSA-1676141 (Reactome) At the early endosome membrane, myotubularin (MTM1), myotubularin-related protein 2 (MTMR2), and myotubularin-related protein 4 (MTMR4) dephosphorylate phosphatidylinositol 3-phosphate (PI3P) to phosphatidylinositol (PI).

The following lists the above proteins with their corresponding literature references: MTM1 (Cao et al. 2007, Cao et al. 2008, Kim et al. 2002), MTMR2 (Cao et al. 2008, Kim et al. 2002), and MTMR4 (Lorenzo et al. 2006, Zhao et al. 2001).
R-HSA-1676145 (Reactome) At the plasma membrane, phosphatidylinositol-5-phosphate 4-kinase type-2 alpha (PIP4K2A) and beta (PIP4K2B) homodimers and heterodimers (Clarke et al. 2010), along with phosphatidylinositol-4-phosphate 5-kinase type-1 alpha (PIP5K1A), beta (PIP5K1B), and gamma (PIP5K1C) phosphorylate phosphatidylinositol 3-phosphate (PI3P) to phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2).

The following lists the above proteins with their corresponding literature references: PIP4K2A (Zhang et al. 1997, Rameh et al. 1997, Clarke et al. 2008), PIP4K2B (Zhang et al. 1997, Rameh et al. 1997), PIP5K1A (Zhang et al. 1997, Tolias et al. 1998), PIP5K1B (Zhang et al. 1997, Tolias et al. 1998), and PIP5K1C (Wenk et al. 2001, Di Paolo et al. 2002).
R-HSA-1676149 (Reactome) At the plasma membrane, phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase aka phosphatase and tensin homolog (PTEN) dephosphorylates phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2) to phosphatidylinositol 4-phosphate (PI4P) (Myers et al. 1998, Das et al. 2003).
R-HSA-1676152 (Reactome) At the Golgi membrane, ADP-ribosylation factor 1 and 3 (ARF1 and ARF3) complexed to GTP bind to phosphatidylinositol 4-kinase beta (PI4KB) and activate it (Haynes et al. 2007, Wong et al. 1997, Godi et al. 1999).
R-HSA-1676161 (Reactome) Phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) translocates from the late endosome membrane to the Golgi membrane (Rutherford et al. 2006).
R-HSA-1676162 (Reactome) At the early endosome membrane, type I (INPP4A) (Norris et al. 1995, Ivetac et al. 2005) and type II inositol-3,4-bisphosphate 4-phosphatase (INPP4B) (Norris et al. 1997) colocalise with early and recycling endosomes through their C2 domains which bind to the phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2) present in these membranes. It is here that phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2) is dephosphorylated by INPP4A/B to phosphatidylinositol 3-phosphate (PI3P).
R-HSA-1676164 (Reactome) At the plasma membrane, type I and type II inositol-3,4-bisphosphate 4-phosphatase (INPP4A) (Norris et al. 1995, Ivetac et al. 2005) and (INPP4B) (Norris et al. 1997) dephosphorylate phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2) to phosphatidylinositol 3-phosphate (PI3P).
R-HSA-1676168 (Reactome) At the early endosome membrane, the PAS complex, consisting of FYVE finger-containing phosphoinositide kinase (PIKFYVE), yeast VAC14 homologue (VAC14), and polyphosphoinositide phosphatase aka SAC3 (FIG4), binds to the membrane via PIKFYVE's FYVE finger (Sbrissa et al. 2002, Cao et al. 2007). The PIKFYVE kinase component phosphorylates phosphatidylinositol 3-phosphate (PI3P) to phosphatidylinositol 3,5-bisphosphate PI(3,5)P2 (Sbrissa et al. 1999). The PAS complex is present in the cytosol and is recruited to the membrane (Sbrissa et al. 2007).
R-HSA-1676174 (Reactome) At the early endosome membrane, the PAS complex, consisting of FYVE finger-containing phosphoinositide kinase (PIKFYVE), yeast VAC14 homologue (VAC14), and polyphosphoinositide phosphatase aka SAC3 (FIG4), binds to the membrane via PIKFYVE's FYVE finger. The FIG4 phosphatase component dephosphorylates phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) to phosphatidylinositol 3-phosphate (PI3P) (Sbrissa et al. 2007, Sbrissa et al. 2008).
R-HSA-1676177 (Reactome) At the plasma membrane, Synaptojanin-1 (SYNJ1) and -2 (SYNJ2), inositol polyphosphate 5-phosphatase K (INPP5K) aka SKIP, phosphatidylinositol 4,5-bisphosphate 5-phosphatase A (INPP5J) aka PIPP dephosphorylate phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) to form phosphatidylinositol 4-phosphate (PI4P). SYNJ1/2 both have an N-terminal Sac1-like domain, a central 5-phosphatase domain and a C-terminal proline-rich segment, with this latter part being the most divergent part of the protein sequence.

The following lists the above proteins with their corresponding literature references: SYNJ1 (Johenning et al. 2004, Haffner et al. 1997, Guo et al. 1999, Mani et al. 2007), SYNJ2 (Malecz et al. 2000), INPP5K (Injuin et al. 2000, Gurung et al. 2003), and INPP5J (Gurung et al. 2003, Mochizuki & Takenawa 1999).
R-HSA-1676185 (Reactome) At the Golgi membrane, phosphatidylinositol 4-kinase alpha (PI4KA) (Gehrmann et al. 1999, Godi et al. 1999), or phosphatidylinositol 4-kinase type 2-alpha/beta (PI4K2A/B) (Balla et al. 2002, Minogue et al. 2001, Wei et al. 2002) phosphorylate phosphatidylinositol (PI) to produce phosphatidylinositol 4-phosphate (PI4P).
R-HSA-1676191 (Reactome) At the plasma membrane, phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase aka phosphatase and tensin homolog (PTEN) dephosphorylates phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3) to phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) (Maehama & Dixon 1998, Myers et al. 1998, Das et al. 2003).
R-HSA-1676203 (Reactome) At the plasma membrane, synaptojanin-1 aka Synaptic inositol-1,4,5-trisphosphate 5-phosphatase 1 (SYNJ1) (Guo et al. 1999), -2 (SYNJ2) and some myotubularins (MTMs) dephosphorylate phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) to phosphatidylinositol 5-phosphate (PI5P). The MTMs involved are: myotubularin (MTM1) (Cao et al. 2007, Tronchere et al. 2004, Schaletzky et al. 2003, Laporte et al. 2002) and myotubularin-related proteins 1 (MTMR1) (Tronchere et al. 2004), 3 (MTMR3) (Walker et al. 2001, Lorenzo et al. 2005), 6 (MTMR6) (Schaletzky et al. 2003, Choudhury et al. 2006), and 14 (MTMR14) (Tosch et al. 2006).
R-HSA-1676204 (Reactome) At the Golgi membrane, phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase (TPTE2) aka TPIP dephosphorylates phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2) to produce phosphatidylinositol 4-phosphate (PI4P) (Tapparel et al. 2000, Walker et al. 2001). The transmembrane phosphatase TPTE2 gamma isoform colocalises in the Golgi and the endoplasmic reticulum (Tapparel et al. 2000).
R-HSA-1676206 (Reactome) At the early endosome membrane, phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunit alpha (PIK3C2A) (Kraq et al. 2010, Arcaro et al. 2000) phosphorylates phosphatidylinositol 4-phosphate (PI4P) to phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2).
SACM1Lmim-catalysisR-HSA-1676114 (Reactome)
SACM1Lmim-catalysisR-HSA-1676124 (Reactome)
SACM1Lmim-catalysisR-HSA-1676133 (Reactome)
SYNJ/INPP5(1)mim-catalysisR-HSA-1676177 (Reactome)
SYNJ/MTM(1)mim-catalysisR-HSA-1675994 (Reactome)
SYNJ/MTM(1)mim-catalysisR-HSA-1676203 (Reactome)
SYNJmim-catalysisR-HSA-1675836 (Reactome)
SYNJmim-catalysisR-HSA-1675988 (Reactome)
TPTE2-like proteinsmim-catalysisR-HSA-1676204 (Reactome)
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