ID A0JNZ1_MOUSE Unreviewed; 1046 AA. AC A0JNZ1; DT 12-DEC-2006, integrated into UniProtKB/TrEMBL. DT 12-DEC-2006, sequence version 1. DT 27-MAR-2024, entry version 132. DE RecName: Full=phosphatidylinositol-4,5-bisphosphate 3-kinase {ECO:0000256|ARBA:ARBA00012010}; DE EC=2.7.1.153 {ECO:0000256|ARBA:ARBA00012010}; GN Name=Pik3cb {ECO:0000313|EMBL:AAI27074.1, GN ECO:0000313|MGI:MGI:1922019}; 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|EMBL:AAI27074.1}; RN [1] {ECO:0000313|EMBL:AAI27074.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=PCR rescued clones {ECO:0000313|EMBL:AAI27074.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M., RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.; 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). CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5- CC bisphosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- CC inositol-3,4,5-trisphosphate) + ADP + H(+); Xref=Rhea:RHEA:21292, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57836, CC ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.153; CC Evidence={ECO:0000256|ARBA:ARBA00023981}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21293; CC Evidence={ECO:0000256|ARBA:ARBA00023981}; CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}. CC -!- PATHWAY: Phospholipid metabolism; phosphatidylinositol phosphate CC biosynthesis. {ECO:0000256|ARBA:ARBA00004805}. CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K CC subfamily. {ECO:0000256|ARBA:ARBA00006209}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC127073; AAI27074.1; -; mRNA. DR AlphaFoldDB; A0JNZ1; -. DR EPD; A0JNZ1; -. DR PeptideAtlas; A0JNZ1; -. DR UCSC; uc012gyy.1; mouse. DR AGR; MGI:1922019; -. DR MGI; MGI:1922019; Pik3cb. DR UniPathway; UPA00220; -. DR ChiTaRS; Pik3cb; mouse. DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IEA:InterPro. DR GO; GO:0046934; F:1-phosphatidylinositol-4,5-bisphosphate 3-kinase activity; IEA:UniProtKB-EC. DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:InterPro. DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:UniProtKB-UniRule. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd08693; C2_PI3K_class_I_beta_delta; 1. DR CDD; cd00872; PI3Ka_I; 1. DR CDD; cd05173; PI3Kc_IA_beta; 1. DR Gene3D; 3.10.20.770; -; 1. DR Gene3D; 2.60.40.150; C2 domain; 1. 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 InterPro; IPR016024; ARM-type_fold. 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; IPR003113; PI3K_ABD. DR InterPro; IPR001263; PI3K_accessory_dom. DR InterPro; IPR042236; PI3K_accessory_sf. DR InterPro; IPR000341; PI3K_Ras-bd_dom. DR InterPro; IPR037702; PI3Kbeta_dom. DR InterPro; IPR015433; PI_Kinase. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR PANTHER; PTHR10048:SF33; PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE 3-KINASE CATALYTIC SUBUNIT BETA ISOFORM; 1. DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1. DR Pfam; PF00454; PI3_PI4_kinase; 1. DR Pfam; PF00792; PI3K_C2; 1. DR Pfam; PF02192; PI3K_p85B; 1. DR Pfam; PF00794; PI3K_rbd; 1. DR Pfam; PF00613; PI3Ka; 1. DR SMART; SM00142; PI3K_C2; 1. DR SMART; SM00143; PI3K_p85B; 1. DR SMART; SM00144; PI3K_rbd; 1. DR SMART; SM00145; PI3Ka; 1. DR SMART; SM00146; PI3Kc; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF54236; Ubiquitin-like; 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; PS51544; PI3K_ABD; 1. DR PROSITE; PS51546; PI3K_RBD; 1. DR PROSITE; PS51545; PIK_HELICAL; 1. PE 2: Evidence at transcript level; KW Kinase {ECO:0000256|ARBA:ARBA00022777}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 20..109 FT /note="PI3K-ABD" FT /evidence="ECO:0000259|PROSITE:PS51544" FT DOMAIN 188..281 FT /note="PI3K-RBD" FT /evidence="ECO:0000259|PROSITE:PS51546" FT DOMAIN 305..472 FT /note="C2 PI3K-type" FT /evidence="ECO:0000259|PROSITE:PS51547" FT DOMAIN 500..677 FT /note="PIK helical" FT /evidence="ECO:0000259|PROSITE:PS51545" FT DOMAIN 748..1029 FT /note="PI3K/PI4K catalytic" FT /evidence="ECO:0000259|PROSITE:PS50290" SQ SEQUENCE 1046 AA; 119637 MW; 09AED8DD8E1C4356 CRC64; MPPAMADNLD IWAVDSQIAS DGAISVDFLL PTGIYIQLEV PREATISYIK QMLWKQVHNY PMFNLLMDID SYMFACVNQT AVYEELEDET RRLCDVRPFL PVLKLVTRSC DPAEKLDSKI GVLIGKGLHE FDALKDPEVN EFRRKMRKFS EAKIQSLVGL SWIDWLKHTY PPEHEPSVLE NLEDKLYGGK LVVAVHFENS QDVFSFQVSP NLNPIKINEL AIQKRLTIRG KEDEASPCDY VLQYIRNCVM NRTLPHFILV ECCKIKKMYE QEMIAIEAAI NRNSSNLPLP LPPKKTRVIS HIWDNNNPFQ ITLVKGNKLN TEETVKVHVR AGLFHGTELL CKTVVSSEIS GKNDHIWNEQ LEFDINICDL PRMARLCFAV YAVLDKVKTK KSTKTINPSK YQTIRKAGKV HYPVAWVNTM VFDFKGQLRS GDVILHSWSS FPDELEEMLN PMGTVQTNPY AENATALHIT FPENKKQPCY YPPFDKIIEK AAELASGDSA NVSSRGGKKF LAVLKEILDR DPLSQLCENE MDLIWTLRQD CRENFPQSLP KLLLSIKWNK LEDVAQLQAL LQIWPKLPPR EALELLDFNY PDQYVREYAV GCLRQMSDEE LSQYLLQLVQ VLKYEPFLDC ALSRFLLERA LDNRRIGQFL FWHLRSEVHT PAVSVQFGVI LEAYCRGSVG HMKVLSKQVE ALNKLKTLNS LIKLNAVKLS RAKGKEAMHT CLKQSAYREA LSDLQSPLNP CVILSELYVE KCKYMDSKMK PLWLVYSSRA FGEDSVGVIF KNGDDLRQDM LTLQMLRLMD LLWKEAGLDL RMLPYGCLAT GDRSGLIEVV STSETIADIQ LNSSNVAATA AFNKDALLNW LKEYNSGDDL DRAIEEFTLS CAGYCVASYV LGIGDRHSDN IMVKKTGQLF HIDFGHILGN FKSKFGIKRE RVPFILTYDF IHVIQQGKTG NTEKFGRFRQ CCEDAYLILR RHGNLFITLF ALMLTAGLPE LTSVKDIQYL KDSLALGKSE EEALKQFKQK FDEALRESWT TKVNWMAHTV RKDYRS //