PI51B_MOUSE
ID PI51B_MOUSE Reviewed; 539 AA.
AC P70181; O70335; Q8JZY6;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Phosphatidylinositol 4-phosphate 5-kinase type-1 beta {ECO:0000305|PubMed:18772378};
DE Short=PIP5KI-beta {ECO:0000305|PubMed:18772378};
DE Short=PtdIns(4)P-5-kinase 1 beta {ECO:0000305|PubMed:18772378};
DE EC=2.7.1.68 {ECO:0000269|PubMed:22942276, ECO:0000269|PubMed:8798574, ECO:0000269|PubMed:9367159, ECO:0000269|PubMed:9535851};
DE AltName: Full=68 kDa type I phosphatidylinositol 4-phosphate 5-kinase beta {ECO:0000303|PubMed:8798574};
DE AltName: Full=Phosphatidylinositol 4-phosphate 5-kinase type I alpha {ECO:0000312|EMBL:BAA13030.1};
DE Short=PIP5KIalpha;
DE AltName: Full=Phosphatidylinositol 4-phosphate 5-kinase type I beta {ECO:0000305|PubMed:18772378};
DE Short=PIP5KIbeta {ECO:0000305|PubMed:18772378};
GN Name=Pip5k1b {ECO:0000312|MGI:MGI:107930};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND TISSUE SPECIFICITY.
RC TISSUE=Insulinoma;
RX PubMed=8798574; DOI=10.1074/jbc.271.39.23611;
RA Ishihara H., Shibasaki Y., Kizuki N., Katagiri H., Yazaki Y., Asano T.,
RA Oka Y.;
RT "Cloning of cDNAs encoding two isoforms of 68-kDa type I
RT phosphatidylinositol 4-phosphate 5-kinase.";
RL J. Biol. Chem. 271:23611-23614(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Machesky L.M.;
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Amnion, Heart, and Retina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9367159; DOI=10.1038/36621;
RA Rameh L.E., Tolias K.F., Duckworth B.C., Cantley L.C.;
RT "A new pathway for synthesis of phosphatidylinositol-4,5-bisphosphate.";
RL Nature 390:192-196(1997).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF LYS-138.
RX PubMed=9535851; DOI=10.1074/jbc.273.15.8741;
RA Ishihara H., Shibasaki Y., Kizuki N., Wada T., Yazaki Y., Asano T., Oka Y.;
RT "Type I phosphatidylinositol-4-phosphate 5-kinases. Cloning of the third
RT isoform and deletion/substitution analysis of members of this novel lipid
RT kinase family.";
RL J. Biol. Chem. 273:8741-8748(1998).
RN [7]
RP FUNCTION, INTERACTION WITH RAC1, AND MUTAGENESIS OF ASP-227.
RX PubMed=10679324; DOI=10.1016/s0960-9822(00)00315-8;
RA Tolias K.F., Hartwig J.H., Ishihara H., Shibasaki Y., Cantley L.C.,
RA Carpenter C.L.;
RT "Type Ialpha phosphatidylinositol-4-phosphate 5-kinase mediates Rac-
RT dependent actin assembly.";
RL Curr. Biol. 10:153-156(2000).
RN [8]
RP FUNCTION, INTERACTION WITH PLD1 AND PLD2, AND SUBCELLULAR LOCATION.
RX PubMed=11032811; DOI=10.1093/emboj/19.20.5440;
RA Divecha N., Roefs M., Halstead J.R., D'Andrea S., Fernandez-Borga M.,
RA Oomen L., Saqib K.M., Wakelam M.J.O., D'Santos C.;
RT "Interaction of the type Ialpha PIPkinase with phospholipase D: a role for
RT the local generation of phosphatidylinositol 4, 5-bisphosphate in the
RT regulation of PLD2 activity.";
RL EMBO J. 19:5440-5449(2000).
RN [9]
RP INTERACTION WITH ARF1.
RX PubMed=10747863; DOI=10.1074/jbc.c901019199;
RA Jones D.H., Morris J.B., Morgan C.P., Kondo H., Irvine R.F., Cockcroft S.;
RT "Type I phosphatidylinositol 4-phosphate 5-kinase directly interacts with
RT ADP-ribosylation factor 1 and is responsible for phosphatidylinositol 4,5-
RT bisphosphate synthesis in the Golgi compartment.";
RL J. Biol. Chem. 275:13962-13966(2000).
RN [10]
RP INTERACTION WITH AJUBA.
RX PubMed=15870270; DOI=10.1128/mcb.25.10.3956-3966.2005;
RA Kisseleva M., Feng Y., Ward M., Song C., Anderson R.A., Longmore G.D.;
RT "The LIM protein Ajuba regulates phosphatidylinositol 4,5-bisphosphate
RT levels in migrating cells through an interaction with and activation of
RT PIPKI alpha.";
RL Mol. Cell. Biol. 25:3956-3966(2005).
RN [11]
RP FUNCTION IN PLATELETS.
RX PubMed=18772378; DOI=10.1073/pnas.0804139105;
RA Wang Y., Chen X., Lian L., Tang T., Stalker T.J., Sasaki T., Kanaho Y.,
RA Brass L.F., Choi J.K., Hartwig J.H., Abrams C.S.;
RT "Loss of PIP5KIbeta demonstrates that PIP5KI isoform-specific PIP2
RT synthesis is required for IP3 formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:14064-14069(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445; SER-447 AND SER-448, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=22942276; DOI=10.1074/jbc.m112.370155;
RA Shulga Y.V., Anderson R.A., Topham M.K., Epand R.M.;
RT "Phosphatidylinositol-4-phosphate 5-kinase isoforms exhibit acyl chain
RT selectivity for both substrate and lipid activator.";
RL J. Biol. Chem. 287:35953-35963(2012).
CC -!- FUNCTION: Catalyzes the phosphorylation of phosphatidylinositol 4-
CC phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5-
CC bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that
CC regulates several cellular processes such as signal transduction,
CC vesicle trafficking, actin cytoskeleton dynamics, cell adhesion, and
CC cell motility (PubMed:8798574, PubMed:9367159, PubMed:9535851,
CC PubMed:22942276). PtdIns(4,5)P2 can directly act as a second messenger
CC or can be utilized as a precursor to generate other second messengers:
CC inositol 1,4,5-trisphosphate (IP3), diacylglycerol (DAG) or
CC phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3/PIP3) (By
CC similarity). Mediates RAC1-dependent reorganization of actin filaments
CC (PubMed:10679324). Contributes to the activation of phospholipase PLD2
CC (PubMed:11032811). Together with PIP5K1A, is required, after
CC stimulation by G-protein coupled receptors, for the synthesis of IP3
CC that will induce stable platelet adhesion (PubMed:18772378).
CC {ECO:0000250|UniProtKB:Q99755, ECO:0000269|PubMed:10679324,
CC ECO:0000269|PubMed:11032811, ECO:0000269|PubMed:18772378,
CC ECO:0000269|PubMed:22942276, ECO:0000269|PubMed:8798574,
CC ECO:0000269|PubMed:9367159, ECO:0000269|PubMed:9535851}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-
CC phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:14425,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58178,
CC ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.68;
CC Evidence={ECO:0000269|PubMed:22942276, ECO:0000269|PubMed:8798574,
CC ECO:0000269|PubMed:9367159, ECO:0000269|PubMed:9535851};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14426;
CC Evidence={ECO:0000305|PubMed:22942276, ECO:0000305|PubMed:8798574,
CC ECO:0000305|PubMed:9367159, ECO:0000305|PubMed:9535851};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-
CC 3-phospho-1D-myo-inositol 4-phosphate + ATP = 1-octadecanoyl-2-
CC (5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phospho-1D-myo-inositol
CC 4,5-bisphosphate + ADP + H(+); Xref=Rhea:RHEA:40363,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77136,
CC ChEBI:CHEBI:77137, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:22942276};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40364;
CC Evidence={ECO:0000305|PubMed:22942276};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phospho-1D-
CC myo-inositol 4-phosphate + ATP = 1-octadecanoyl-2-(9Z)-octadecenoyl-
CC sn-glycero-3-phospho-1D-myo-inositol 4,5-bisphosphate + ADP + H(+);
CC Xref=Rhea:RHEA:40367, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:77139, ChEBI:CHEBI:77140, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:22942276};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40368;
CC Evidence={ECO:0000305|PubMed:22942276};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phospho-1D-
CC myo-inositol + ATP = 1-octadecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-
CC phospho-1D-myo-inositol 5-phosphate + ADP + H(+);
CC Xref=Rhea:RHEA:40379, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:77163, ChEBI:CHEBI:77164, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:22942276};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40380;
CC Evidence={ECO:0000305|PubMed:22942276};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-
CC phospho-1D-myo-inositol + ATP = 1-octadecanoyl-2-(9Z,12Z)-
CC octadecadienoyl-sn-glycero-3-phospho-1D-myo-inositol 5-phosphate +
CC ADP + H(+); Xref=Rhea:RHEA:40383, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:77158, ChEBI:CHEBI:77159,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:22942276};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40384;
CC Evidence={ECO:0000305|PubMed:22942276};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phospho-(1D-myo-inositol) + ATP = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-sn-glycero-3-phospho-1D-myo-inositol 5-phosphate +
CC ADP + H(+); Xref=Rhea:RHEA:40375, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:77160, ChEBI:CHEBI:133606,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:22942276};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40376;
CC Evidence={ECO:0000305|PubMed:22942276};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phospho-1D-myo-
CC inositol + ATP = 1,2-di(9Z,12Z)-octadecadienoyl-sn-glycero-3-phospho-
CC 1D-myo-inositol 5-phosphate + ADP + H(+); Xref=Rhea:RHEA:40387,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77165,
CC ChEBI:CHEBI:77167, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:22942276};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40388;
CC Evidence={ECO:0000305|PubMed:22942276};
CC -!- ACTIVITY REGULATION: Activated by phosphatidic acid.
CC {ECO:0000269|PubMed:8798574, ECO:0000269|PubMed:9535851}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=34 uM for phosphatidylinositol-4-phosphate/PtdIns(4)P
CC {ECO:0000269|PubMed:9535851};
CC KM=27 uM for ATP {ECO:0000269|PubMed:9535851};
CC KM=3.7 uM for 1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-
CC glycero-3-phospho-1D-myo-inositol 4-phosphate
CC {ECO:0000269|PubMed:22942276};
CC KM=4.9 uM for 1-octadecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-
CC phospho-1D-myo-inositol 4-phosphate {ECO:0000269|PubMed:22942276};
CC -!- SUBUNIT: Interacts with RAC1, AJUBA, PLD1, PLD2 and ARF1.
CC {ECO:0000269|PubMed:10679324, ECO:0000269|PubMed:10747863,
CC ECO:0000269|PubMed:11032811, ECO:0000269|PubMed:15870270}.
CC -!- INTERACTION:
CC P70181; Q9QYB1: Clic4; NbExp=4; IntAct=EBI-645167, EBI-645175;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:11032811}.
CC Cell membrane {ECO:0000269|PubMed:11032811}. Endomembrane system
CC {ECO:0000250}. Note=Associated with membranes. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P70181-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P70181-2; Sequence=VSP_016012;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain and testis. Barely
CC detectable in liver and skeletal muscle. {ECO:0000269|PubMed:8798574}.
CC -!- CAUTION: There is confusion in the literature with phosphatidylinositol
CC 4-phosphate 5-kinase type I nomenclature due to the fact that
CC frequently mouse PIP5K1B is named Phosphatidylinositol 4-phosphate 5-
CC kinase type I alpha. {ECO:0000305}.
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DR EMBL; D86176; BAA13030.1; -; mRNA.
DR EMBL; AF048695; AAC05374.1; -; mRNA.
DR EMBL; AK149354; BAE28830.1; -; mRNA.
DR EMBL; AK164552; BAE37836.1; -; mRNA.
DR EMBL; AK146100; BAE26901.1; -; mRNA.
DR EMBL; BC034864; AAH34864.1; -; mRNA.
DR CCDS; CCDS37940.1; -. [P70181-1]
DR RefSeq; NP_032872.1; NM_008846.3. [P70181-1]
DR RefSeq; XP_006526826.1; XM_006526763.3. [P70181-1]
DR AlphaFoldDB; P70181; -.
DR SMR; P70181; -.
DR BioGRID; 202171; 2.
DR IntAct; P70181; 3.
DR STRING; 10090.ENSMUSP00000025800; -.
DR BindingDB; P70181; -.
DR SwissLipids; SLP:000000549; -.
DR iPTMnet; P70181; -.
DR PhosphoSitePlus; P70181; -.
DR MaxQB; P70181; -.
DR PaxDb; P70181; -.
DR PeptideAtlas; P70181; -.
DR PRIDE; P70181; -.
DR ProteomicsDB; 301819; -. [P70181-1]
DR ProteomicsDB; 301820; -. [P70181-2]
DR Antibodypedia; 2767; 157 antibodies from 28 providers.
DR DNASU; 18719; -.
DR Ensembl; ENSMUST00000025800; ENSMUSP00000025800; ENSMUSG00000024867. [P70181-1]
DR Ensembl; ENSMUST00000112673; ENSMUSP00000108292; ENSMUSG00000024867. [P70181-2]
DR GeneID; 18719; -.
DR KEGG; mmu:18719; -.
DR UCSC; uc008hap.1; mouse. [P70181-1]
DR UCSC; uc012bjs.1; mouse. [P70181-2]
DR CTD; 8395; -.
DR MGI; MGI:107930; Pip5k1b.
DR VEuPathDB; HostDB:ENSMUSG00000024867; -.
DR eggNOG; KOG0229; Eukaryota.
DR GeneTree; ENSGT00940000156639; -.
DR HOGENOM; CLU_004312_5_1_1; -.
DR InParanoid; P70181; -.
DR OMA; NSNMKER; -.
DR OrthoDB; 1562683at2759; -.
DR PhylomeDB; P70181; -.
DR TreeFam; TF319618; -.
DR BRENDA; 2.7.1.68; 3474.
DR Reactome; R-MMU-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-MMU-201688; WNT mediated activation of DVL.
DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR SABIO-RK; P70181; -.
DR BioGRID-ORCS; 18719; 2 hits in 59 CRISPR screens.
DR ChiTaRS; Pip5k1b; mouse.
DR PRO; PR:P70181; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; P70181; protein.
DR Bgee; ENSMUSG00000024867; Expressed in choroid plexus of fourth ventricle and 206 other tissues.
DR Genevisible; P70181; MM.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001931; C:uropod; ISO:MGI.
DR GO; GO:0016308; F:1-phosphatidylinositol-4-phosphate 5-kinase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; IGI:MGI.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IDA:MGI.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.800.10; -; 1.
DR InterPro; IPR023610; PInositol-4-P-5-kinase.
DR InterPro; IPR002498; PInositol-4-P-5-kinase_core.
DR InterPro; IPR027484; PInositol-4-P-5-kinase_N.
DR PANTHER; PTHR23086; PTHR23086; 1.
DR Pfam; PF01504; PIP5K; 1.
DR SMART; SM00330; PIPKc; 1.
DR PROSITE; PS51455; PIPK; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Cytoplasm; Kinase;
KW Lipid metabolism; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..539
FT /note="Phosphatidylinositol 4-phosphate 5-kinase type-1
FT beta"
FT /id="PRO_0000185459"
FT DOMAIN 25..395
FT /note="PIPK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00781"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 401..452
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016012"
FT MUTAGEN 138
FT /note="K->A: Almost complete loss of 1-
FT phosphatidylinositol-4-phosphate 5-kinase activity."
FT /evidence="ECO:0000269|PubMed:9535851"
FT MUTAGEN 227
FT /note="D->A: Reduced 1-phosphatidylinositol-4-phosphate 5-
FT kinase activity by 98%. Loss of actin-remodeling activity."
FT /evidence="ECO:0000269|PubMed:10679324"
FT CONFLICT 291
FT /note="V -> A (in Ref. 2; AAC05374)"
FT /evidence="ECO:0000305"
FT CONFLICT 425
FT /note="V -> L (in Ref. 2; AAC05374)"
FT /evidence="ECO:0000305"
FT CONFLICT 437
FT /note="R -> Q (in Ref. 2; AAC05374)"
FT /evidence="ECO:0000305"
FT CONFLICT 525..528
FT /note="TLDL -> ALET (in Ref. 2; AAC05374)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 539 AA; 60803 MW; A8478C9E21546AC3 CRC64;
MSSTAENGDA VPGKQNEEKT YKKTASSAIK GAIQLGIGYT VGNLTSKPER DVLMQDFYVV
ESVFLPSEGS NLTPAHHYPD FRFKTYAPLA FRYFRELFGI KPDDYLYSIC SEPLIELSNP
GASGSLFFLT SDDEFIIKTV QHKEAEFLQK LLPGYYMNLN QNPRTLLPKF YGLYCMQSGG
INIRIVVMNN VLPRAMRMHL TYDLKGSTYK RRASRKEREK PNPTFKDLDF LQDMHEGLYF
DTETYNALMK TLQRDCRVLE SFKIMDYSLL LGIHILDHSL KDKEEEPLQN VPDAKRPGMQ
KVLYSTAMES IQGPGKSADG IIAENPDTMG GIPAKSHKGE KLLLFMGIID ILQSYRLMKK
LEHSWKALVY DGDTVSVHRP SFYADRFLKF MNSRVFKKIQ ALKASPSKKR CNSIAALKAT
SQEIVSSISQ EWKDEKRDLL TEGQSFSSLD EEALGSRHRP DLVPSTPSLF EAASLATTIS
SSSLYVGEHY PHDRTTLYSN SKGLPSSSTF TLEEGTIYLT AEPNTLDLQD DASVLDVYL
