ID E9QAN8_MOUSE Unreviewed; 1632 AA.
AC E9QAN8;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=Phosphatidylinositol-4-phosphate 3-kinase catalytic subunit type 2 beta {ECO:0000313|Ensembl:ENSMUSP00000076911.6};
GN Name=Pik3c2b {ECO:0000313|Ensembl:ENSMUSP00000076911.6,
GN ECO:0000313|MGI:MGI:2685045};
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 {ECO:0000313|Ensembl:ENSMUSP00000076911.6, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0000313|Ensembl:ENSMUSP00000076911.6, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000076911.6,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [3] {ECO:0000313|Ensembl:ENSMUSP00000076911.6}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000076911.6};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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-3,4-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:18373,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57658,
CC ChEBI:CHEBI:58178, ChEBI:CHEBI:456216; EC=2.7.1.154;
CC Evidence={ECO:0000256|ARBA:ARBA00029297};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18374;
CC Evidence={ECO:0000256|ARBA:ARBA00029297};
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-3-phosphate) + ADP +
CC H(+); Xref=Rhea:RHEA:12709, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216;
CC EC=2.7.1.137; Evidence={ECO:0000256|ARBA:ARBA00023985};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12710;
CC Evidence={ECO:0000256|ARBA:ARBA00023985};
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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DR RefSeq; NP_001092746.2; NM_001099276.2.
DR RefSeq; XP_006529594.1; XM_006529531.3.
DR RefSeq; XP_006529595.1; XM_006529532.2.
DR AlphaFoldDB; E9QAN8; -.
DR SMR; E9QAN8; -.
DR STRING; 10090.ENSMUSP00000076911; -.
DR iPTMnet; E9QAN8; -.
DR PhosphoSitePlus; E9QAN8; -.
DR EPD; E9QAN8; -.
DR MaxQB; E9QAN8; -.
DR PaxDb; 10090-ENSMUSP00000076911; -.
DR ProteomicsDB; 324507; -.
DR Antibodypedia; 34558; 250 antibodies from 30 providers.
DR DNASU; 240752; -.
DR Ensembl; ENSMUST00000077730.7; ENSMUSP00000076911.6; ENSMUSG00000026447.18.
DR GeneID; 240752; -.
DR KEGG; mmu:240752; -.
DR UCSC; uc011wry.1; mouse.
DR AGR; MGI:2685045; -.
DR CTD; 5287; -.
DR MGI; MGI:2685045; Pik3c2b.
DR VEuPathDB; HostDB:ENSMUSG00000026447; -.
DR eggNOG; KOG0905; Eukaryota.
DR GeneTree; ENSGT00940000158263; -.
DR HOGENOM; CLU_002191_0_0_1; -.
DR InParanoid; E9QAN8; -.
DR OMA; QMAAGFR; -.
DR OrthoDB; 10350at2759; -.
DR PhylomeDB; E9QAN8; -.
DR TreeFam; TF102031; -.
DR BRENDA; 2.7.1.154; 3474.
DR Reactome; R-MMU-1660499; Synthesis of PIPs at the plasma membrane.
DR BioGRID-ORCS; 240752; 2 hits in 79 CRISPR screens.
DR ChiTaRS; Pik3c2b; mouse.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; E9QAN8; Protein.
DR Bgee; ENSMUSG00000026447; Expressed in animal zygote and 79 other cell types or tissues.
DR ExpressionAtlas; E9QAN8; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030139; C:endocytic vesicle; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; ISO:MGI.
DR GO; GO:0035005; F:1-phosphatidylinositol-4-phosphate 3-kinase activity; ISO:MGI.
DR GO; GO:0001727; F:lipid kinase activity; IDA:MGI.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:1905037; P:autophagosome organization; IGI:MGI.
DR GO; GO:0009267; P:cellular response to starvation; IGI:MGI.
DR GO; GO:0016236; P:macroautophagy; IGI:MGI.
DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IDA:MGI.
DR GO; GO:0036092; P:phosphatidylinositol-3-phosphate biosynthetic process; IGI:MGI.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04012; C2A_PI3K_class_II; 1.
DR CDD; cd08381; C2B_PI3K_class_II; 1.
DR CDD; cd00869; PI3Ka_II; 1.
DR CDD; cd00895; PI3Kc_C2_beta; 1.
DR CDD; cd07290; PX_PI3K_C2_beta; 1.
DR Gene3D; 2.60.40.150; C2 domain; 2.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR Gene3D; 1.25.40.70; Phosphatidylinositol 3-kinase, accessory domain (PIK); 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR002420; PI3K-type_C2_dom.
DR InterPro; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR042236; PI3K_accessory_sf.
DR InterPro; IPR000341; PI3K_Ras-bd_dom.
DR InterPro; IPR015433; PI_Kinase.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR042134; PX_PI3K_C2_beta.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10048:SF30; PHOSPHATIDYLINOSITOL 4-PHOSPHATE 3-KINASE C2 DOMAIN-CONTAINING SUBUNIT BETA; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00792; PI3K_C2; 1.
DR Pfam; PF00794; PI3K_rbd; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00142; PI3K_C2; 1.
DR SMART; SM00144; PI3K_rbd; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS51547; C2_PI3K; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR PROSITE; PS51546; PI3K_RBD; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
DR PROSITE; PS50195; PX; 1.
PE 1: Evidence at protein level;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Proteomics identification {ECO:0007829|MaxQB:E9QAN8,
KW ECO:0007829|ProteomicsDB:E9QAN8};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 374..462
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 634..785
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 804..980
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 1049..1327
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 1364..1480
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 1503..1623
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 82..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..178
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1632 AA; 184178 MW; 9E775F4CFA3E7C66 CRC64;
MSSTQGNGEH WKSLESVGIS RKELAMAEAL QMEYDALSRL RHHKEESRAK QNTEPSLISW
DEPALDFYSK PAGRRTDLKL LRGLSGSDPT LNYNSISPPE GLPNSTSQDP QPGPDPWPKG
SLSGDYLYIF DGSEGRCSLS PGSGDTDGSC KKLSPPPLPP RVSIWDAPPL PPRKGSPSPS
KISQPNDINS FSSAEQPPDK LLVAQDPEEG ELPDGRGQGH TLGSVDYDGI NDAITRLNLK
STYDSEISSD ATRGWKEGRG PLDFNKDTSG KPVARSKTMP PQVPPRTYTS RYANRKNATP
GNNRRISAAP VGSRPHTVAN GHELFEVSEE RDEEVAAFCH MLDILRTGSD IQDYSLTGCV
WSTVTPSPEH LGDEVNLKVT VLCDSLREPL TFTCNCSSTV DLLIHQTLCY THDELREVDV
GDFVLKPCGL EEFLQNKHAL GSHEYIQYCR KFDISIRLQL MEQKAIRSDL ARTVNDDQSP
STLNYLIHLQ ERPVKQTISR QALSLLFDTY HNEVDAFLLA DGDFPLKADR VVQSVKAICN
ALAAVETPEI TSALNQLPPC PSRMQPKIQK DPSVLSVREN REKVVEALTA AILDLVELYC
STFNADFQTA VPGSRKHDLV QEACHFPGAL AFTVYGTHRI PIIWATSYED FYLSCSLSHG
GKELCSPLQT RRAHFSKYLF HLIIWDQQIC FPVQVNRLPR ETLLCATLYA LPVPPPGGSS
EANKQKRVPE ALGWVTTPLF NFRQVLTCGR KLLGLWPATQ ENSGARWSAP NFHQPDSVIL
QIDFPSSAFD IKFTSPPGDK FSPRYEFGSL REEDQRKLKD ITQKESLYWL TDADKKQLWE
KRYYCHTEVS SLPLVLASAP SWEWACLPDI YALLQQWTHM NHQDALGLLH ATFPDQEVRR
MAVQWIGSLS DAELLDYLPQ LVQALKYECY LDSPLVRFLL KRAISDLRVT HYFFWLLKDS
LKDSQFSIRY QYLLAALLCC CGKGLREEFN RQCWLVNTLA KLAQQVREAT PSARQGILRV
GLEEVKQFFA LNGSCRLPLS PSLLVKGIVP RDCSYFNSNA VPLKLAFQNV DPLGENIRVI
FKCGDDLRQD MLTLQMIRIM SKIWVQEGLD MRMVIFRCFS TGRGKGMVEM IPNAETLRKI
QVEHGVTGSF KDRPLADWLQ KHNPGEDEYE KAVENFIYSC AGCCVATYIL GICDRHNDNI
MLKTTGHMFH IDFGRFLGHA QMFGNIKRDR APFVFTSDMA YVINGGDKPS SRFHDFVDLC
CQAYNLIRKH THLFLNLLGL MLSCGIPELS DLEDLKYVYD ALRPQDTEAN ATTYFTRLIE
SSLGSVATKL NFFIHNLAQM KFTGSDDRLT LSFAPRTHTL KSSGRIRDVF LCRHEKIFHP
SKGYVYVVKV MRENAHEATY IQRTFEEFQE LHNKLRLLFP SSFLPSFPSR FVIGRSRGEA
VAERRKEELN GYIWHLIHAA PEVAECDLVY TFFHPLPRDE KASGPSPAPK SSDGTWARPV
GKVGGEVKLS ISYKNNKLFI MVMHIRGLQP LQDGNDPDPY VKIYLLPDPQ KTTKRKTKVA
RKTCNPTYNE MLVYDGIPKG DLQQRELQLS VLSEQGFWEN LLLGEVHIRL RELDLAQEKT
GWFGLGSRGH GT
//
