ID O00334_HUMAN Unreviewed; 1068 AA. AC O00334; DT 01-JUL-1997, integrated into UniProtKB/TrEMBL. DT 01-JUL-1997, sequence version 1. DT 27-MAR-2024, entry version 156. DE RecName: Full=phosphatidylinositol-4,5-bisphosphate 3-kinase {ECO:0000256|ARBA:ARBA00012010}; DE EC=2.7.1.153 {ECO:0000256|ARBA:ARBA00012010}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:AAB53966.1}; RN [1] {ECO:0000313|EMBL:AAB53966.1} RP NUCLEOTIDE SEQUENCE. RA Mahlum C.E., Becker K.P., Morris A.J.; RT "H. sapiens mRNA for phosphoinositide 3-kinase delta catalytic subunit."; RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases. 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: 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; U57843; AAB53966.1; -; mRNA. DR PIR; PC4348; PC4348. DR AlphaFoldDB; O00334; -. DR PeptideAtlas; O00334; -. DR UniPathway; UPA00220; -. 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; cd05174; PI3Kc_IA_delta; 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; IPR037703; PI3Kdelta_dom. DR InterPro; IPR015433; PI_Kinase. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR PANTHER; PTHR10048:SF35; PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE 3-KINASE CATALYTIC SUBUNIT DELTA 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, ECO:0000313|EMBL:AAB53966.1}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 16..105 FT /note="PI3K-ABD" FT /evidence="ECO:0000259|PROSITE:PS51544" FT DOMAIN 187..278 FT /note="PI3K-RBD" FT /evidence="ECO:0000259|PROSITE:PS51546" FT DOMAIN 284..441 FT /note="C2 PI3K-type" FT /evidence="ECO:0000259|PROSITE:PS51547" FT DOMAIN 521..698 FT /note="PIK helical" FT /evidence="ECO:0000259|PROSITE:PS51545" FT DOMAIN 769..1051 FT /note="PI3K/PI4K catalytic" FT /evidence="ECO:0000259|PROSITE:PS50290" SQ SEQUENCE 1068 AA; 121880 MW; 2B342FDA445C9A31 CRC64; MPPGVDCPME FWTKEENQRV VVDFLLPTGV YLNFPVSRNA NLSTIKQLLW HRAQYEPLFH MLSAPKAYVF TCINQTAEQQ ELEDEQRRLC DVQPFLPVLR LVAREGDRVK KLINSQISLL IGKGLHEFDS LCDPEVNDFR AKMCQFCEEA AARRQQLGWE AWLQYSFPLQ LEPSAQTWGP GTLRLPNRAL LVNVKFEGSE ESFTFQVSTK DVPLALMACA LRKKATVFRQ PLVEQPEDYT LQVNGRHEYL YGSYPLCQFQ VQKPRAKPPP IPAKKPSSVS LWSLEQPFRI ELIQGSKVNA DERMKLVVQA GLFHGNEMLC KTVSSSEVSV CSEPVWKQRL EFDINICDLP RMARLCFALY AVIEKAKKAR STKKKSKKAD CPIAWANLML FDYKDQLKTG ERCLYMWPSV PDEKGELLNP TGTVRSNPNT DSAAALLICL PEVAPHPVYY PALEKLPGGM LLASREWRPE LLWMRLHAED SAPSRMIGVA MPGLGVLPGL VQAPGDAECS RLLQILELGR HSECVHVTEE EQLQLREILE RRGSGELYEH EKDLVWKLRH EVQEHFPEAL ARLLLVTKWN KHEDVAPDAL PAVSWPELPV LSALELLDFS FPDCHVGSFA IKSLRKLTDD ELFQYLLQLV QVLKYESYLD CELTKFLLER ALANRKIGHF LFWHLRSEMH VPSVALRFGL ILEAYCRGST HHMKVLMKQG EALSKLKALN DFVKLSSQKT PKPQTKELMH LCMRQEAYLE ALSHLQSPLD PSTLLAEVCV EQCTFMDSKM KPLWIMYSNE EAGSGGTVGI IFKNGDDLRQ DMLTLQMIQL MDVLWKQEGL DLRMTPYGCL PTGDRTGLIE VVLRSDTIAN IQLNKSNMAA TAAFNKDALL NWLKSKNPGE ALDRAIEEFT LSCAGYCVAT YVLGIGDRHS DNIMIRESGQ LFHIDFGHFL GNFKTKFGIN RERVPFILTY DLVHVIQQGK TNNSEKFERF RGYCERAYTI LRRHGLLFLH LFALMRAAGL PELSCSKDIQ YLKDSLALGK TEEEALKHFR EKFNEALREG WKTKVNWLAH NVSKDNRQ //