P4K2B_MOUSE
ID P4K2B_MOUSE Reviewed; 469 AA.
AC Q8CBQ5; Q91Z30; Q9D072; Q9D471;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Phosphatidylinositol 4-kinase type 2-beta;
DE EC=2.7.1.67 {ECO:0000250|UniProtKB:Q8TCG2};
DE AltName: Full=Phosphatidylinositol 4-kinase type II-beta;
GN Name=Pi4k2b;
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).
RC STRAIN=C57BL/6J;
RA Hong W.;
RT "Beta isoform of mouse type II phosphatidylinositol 4-kinase
RT (PI4KIIbeta).";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=Kunmingbai;
RA Li W., Lu G.;
RT "A gene from our subtracted mouse compacted embryo cDNA library.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Testis, and Urinary bladder;
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 1).
RC STRAIN=FVB/N; TISSUE=Embryo, and Mammary tumor;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas, and Testis;
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).
CC -!- FUNCTION: Together with PI4K2A and the type III PI4Ks (PIK4CA and
CC PIK4CB) it contributes to the overall PI4-kinase activity of the cell.
CC This contribution may be especially significant in plasma membrane,
CC endosomal and Golgi compartments. The phosphorylation of
CC phosphatidylinositol (PI) to PI4P is the first committed step in the
CC generation of phosphatidylinositol 4,5-bisphosphate (PIP2), a precursor
CC of the second messenger inositol 1,4,5-trisphosphate (InsP3).
CC Contributes to the production of InsP3 in stimulated cells and is
CC likely to be involved in the regulation of vesicular trafficking.
CC {ECO:0000250|UniProtKB:Q8TCG2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a
CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP +
CC H(+); Xref=Rhea:RHEA:19877, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216;
CC EC=2.7.1.67; Evidence={ECO:0000250|UniProtKB:Q8TCG2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19878;
CC Evidence={ECO:0000250|UniProtKB:Q8TCG2};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q8TCG2}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q8TCG2}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q8TCG2}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8TCG2}. Cell membrane
CC {ECO:0000250|UniProtKB:Q8TCG2}. Early endosome membrane
CC {ECO:0000250|UniProtKB:Q8TCG2}. Note=Mainly cytosolic, association with
CC membranes of the Golgi, endoplasmic and plasma membrane is stimulated
CC by active RAC1. Association with early endosomes has not been
CC confirmed. {ECO:0000250|UniProtKB:Q8TCG2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CBQ5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CBQ5-2; Sequence=VSP_024828;
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type II PI4K
CC subfamily. {ECO:0000305}.
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DR EMBL; AF411321; AAL04155.1; -; mRNA.
DR EMBL; AY148879; AAN37399.1; -; mRNA.
DR EMBL; AK011751; BAB27819.1; -; mRNA.
DR EMBL; AK016754; BAB30411.1; -; mRNA.
DR EMBL; AK035523; BAC29091.1; -; mRNA.
DR EMBL; AK170730; BAE41986.1; -; mRNA.
DR EMBL; BC010257; AAH10257.1; -; mRNA.
DR EMBL; BC062144; AAH62144.1; -; mRNA.
DR CCDS; CCDS19287.1; -. [Q8CBQ5-1]
DR CCDS; CCDS39086.1; -. [Q8CBQ5-2]
DR RefSeq; NP_080227.2; NM_025951.3. [Q8CBQ5-1]
DR RefSeq; NP_083020.2; NM_028744.3. [Q8CBQ5-2]
DR AlphaFoldDB; Q8CBQ5; -.
DR SMR; Q8CBQ5; -.
DR STRING; 10090.ENSMUSP00000031081; -.
DR iPTMnet; Q8CBQ5; -.
DR PhosphoSitePlus; Q8CBQ5; -.
DR SwissPalm; Q8CBQ5; -.
DR EPD; Q8CBQ5; -.
DR MaxQB; Q8CBQ5; -.
DR PaxDb; Q8CBQ5; -.
DR PeptideAtlas; Q8CBQ5; -.
DR PRIDE; Q8CBQ5; -.
DR ProteomicsDB; 294095; -. [Q8CBQ5-1]
DR ProteomicsDB; 294096; -. [Q8CBQ5-2]
DR Antibodypedia; 1318; 188 antibodies from 26 providers.
DR DNASU; 67073; -.
DR Ensembl; ENSMUST00000031081; ENSMUSP00000031081; ENSMUSG00000029186. [Q8CBQ5-1]
DR Ensembl; ENSMUST00000031082; ENSMUSP00000031082; ENSMUSG00000029186. [Q8CBQ5-2]
DR GeneID; 67073; -.
DR KEGG; mmu:67073; -.
DR UCSC; uc008xkq.2; mouse. [Q8CBQ5-1]
DR UCSC; uc008xkr.2; mouse. [Q8CBQ5-2]
DR CTD; 55300; -.
DR MGI; MGI:1914323; Pi4k2b.
DR VEuPathDB; HostDB:ENSMUSG00000029186; -.
DR eggNOG; KOG2381; Eukaryota.
DR GeneTree; ENSGT00390000010434; -.
DR HOGENOM; CLU_032516_1_0_1; -.
DR InParanoid; Q8CBQ5; -.
DR OMA; FHWAWLS; -.
DR OrthoDB; 1273723at2759; -.
DR PhylomeDB; Q8CBQ5; -.
DR TreeFam; TF314740; -.
DR Reactome; R-MMU-1483248; Synthesis of PIPs at the ER membrane.
DR Reactome; R-MMU-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-MMU-1660514; Synthesis of PIPs at the Golgi membrane.
DR Reactome; R-MMU-1660516; Synthesis of PIPs at the early endosome membrane.
DR BioGRID-ORCS; 67073; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Pi4k2b; mouse.
DR PRO; PR:Q8CBQ5; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8CBQ5; protein.
DR Bgee; ENSMUSG00000029186; Expressed in left lung lobe and 237 other tissues.
DR ExpressionAtlas; Q8CBQ5; baseline and differential.
DR Genevisible; Q8CBQ5; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0007032; P:endosome organization; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; ISS:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR039756; Lsb6/PI4K2.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR PANTHER; PTHR12865; PTHR12865; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Cytoplasm;
KW Endoplasmic reticulum; Endosome; Golgi apparatus; Kinase; Lipid metabolism;
KW Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..469
FT /note="Phosphatidylinositol 4-kinase type 2-beta"
FT /id="PRO_0000285165"
FT DOMAIN 108..439
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..120
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 141..143
FT /note="Important for substrate binding"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT REGION 149..162
FT /note="Important for interaction with membranes"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT REGION 252..260
FT /note="Important for interaction with membranes"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT REGION 289..297
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 330..350
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 345..354
FT /note="Important for interaction with membranes"
FT /evidence="ECO:0000250|UniProtKB:Q9BTU6"
FT COMPBIAS 65..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8TCG2"
FT BINDING 136
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8TCG2"
FT BINDING 245..248
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8TCG2"
FT BINDING 259..260
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8TCG2"
FT BINDING 332
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8TCG2"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TCG2"
FT VAR_SEQ 84..129
FT /note="ETNTFLEDPEFADIVLKAEQAIEIGVFPERISQGSSGSYFVKDSKR -> GP
FT ELCPFYSRSLCYKTTTALGYY (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072, ECO:0000303|Ref.2"
FT /id="VSP_024828"
FT CONFLICT 199
FT /note="W -> L (in Ref. 1; AAL04155 and 3; BAB27819)"
FT /evidence="ECO:0000305"
FT CONFLICT 229..236
FT /note="GRKFHRIG -> AESPSDR (in Ref. 2; AAN37399)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="F -> S (in Ref. 2; AAN37399 and 3; BAB30411)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="F -> Y (in Ref. 2; AAN37399 and 3; BAB30411)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="R -> K (in Ref. 4; AAH10257)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 469 AA; 53478 MW; B5CE80948E5B8954 CRC64;
MAEACEPTRP SEDEDEEREP LLPRVAWAQP RRVAPGSAVR MQADEGADVL REPATDEPPA
VSGEGSISAS LSTELDRTRT TSSETNTFLE DPEFADIVLK AEQAIEIGVF PERISQGSSG
SYFVKDSKRN IIGVFKPKSE EPYGQLNPKW TKYVHKVCCP CCFGRGCLLP NQGYLSEAGA
YLVDVKLNLG IVPKTKVVWL VSETFNYSAI DRAKSRGKKY ALEKVPKVGR KFHRIGLPPK
VGSFQLFVKD YKEAEYWLRR FEAEPLPENI RKQFQSQFEK LVILDYIIRN TDRGNDNWLV
KYDEMKYAKK IESEESNWID NKQLLIKIAA IDNGLAFPFK HPDEWRAYPF HWAWLPQAKV
PFSEETRNLI LPYISDMNFV QDLCEDLYEL FKTDKGFDRA AFENQMSVMR GQILNLTQAL
RDGKSPMQLA QMPCVIVECS KSGSQGRVVH LGSSFTQTVH CRKPFFSSW
