ID A0A6Q8PGN9_HUMAN Unreviewed; 483 AA.
AC A0A6Q8PGN9;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 18-JUN-2025, entry version 23.
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=PIK3CA {ECO:0000313|Ensembl:ENSP00000502323.1};
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|Ensembl:ENSP00000502323.1, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000502323.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11237011; DOI=10.1038/35057062;
RG International Human Genome Sequencing Consortium;
RA Lander E.S., Linton L.M., Birren B., Nusbaum C., Zody M.C., Baldwin J.,
RA Devon K., Dewar K., Doyle M., FitzHugh W., Funke R., Gage D., Harris K.,
RA Heaford A., Howland J., Kann L., Lehoczky J., LeVine R., McEwan P.,
RA McKernan K., Meldrim J., Mesirov J.P., Miranda C., Morris W., Naylor J.,
RA Raymond C., Rosetti M., Santos R., Sheridan A., Sougnez C.,
RA Stange-Thomann N., Stojanovic N., Subramanian A., Wyman D., Rogers J.,
RA Sulston J., Ainscough R., Beck S., Bentley D., Burton J., Clee C.,
RA Carter N., Coulson A., Deadman R., Deloukas P., Dunham A., Dunham I.,
RA Durbin R., French L., Grafham D., Gregory S., Hubbard T., Humphray S.,
RA Hunt A., Jones M., Lloyd C., McMurray A., Matthews L., Mercer S., Milne S.,
RA Mullikin J.C., Mungall A., Plumb R., Ross M., Shownkeen R., Sims S.,
RA Waterston R.H., Wilson R.K., Hillier L.W., McPherson J.D., Marra M.A.,
RA Mardis E.R., Fulton L.A., Chinwalla A.T., Pepin K.H., Gish W.R.,
RA Chissoe S.L., Wendl M.C., Delehaunty K.D., Miner T.L., Delehaunty A.,
RA Kramer J.B., Cook L.L., Fulton R.S., Johnson D.L., Minx P.J., Clifton S.W.,
RA Hawkins T., Branscomb E., Predki P., Richardson P., Wenning S., Slezak T.,
RA Doggett N., Cheng J.F., Olsen A., Lucas S., Elkin C., Uberbacher E.,
RA Frazier M., Gibbs R.A., Muzny D.M., Scherer S.E., Bouck J.B.,
RA Sodergren E.J., Worley K.C., Rives C.M., Gorrell J.H., Metzker M.L.,
RA Naylor S.L., Kucherlapati R.S., Nelson D.L., Weinstock G.M., Sakaki Y.,
RA Fujiyama A., Hattori M., Yada T., Toyoda A., Itoh T., Kawagoe C.,
RA Watanabe H., Totoki Y., Taylor T., Weissenbach J., Heilig R., Saurin W.,
RA Artiguenave F., Brottier P., Bruls T., Pelletier E., Robert C., Wincker P.,
RA Smith D.R., Doucette-Stamm L., Rubenfield M., Weinstock K., Lee H.M.,
RA Dubois J., Rosenthal A., Platzer M., Nyakatura G., Taudien S., Rump A.,
RA Yang H., Yu J., Wang J., Huang G., Gu J., Hood L., Rowen L., Madan A.,
RA Qin S., Davis R.W., Federspiel N.A., Abola A.P., Proctor M.J., Myers R.M.,
RA Schmutz J., Dickson M., Grimwood J., Cox D.R., Olson M.V., Kaul R.,
RA Raymond C., Shimizu N., Kawasaki K., Minoshima S., Evans G.A.,
RA Athanasiou M., Schultz R., Roe B.A., Chen F., Pan H., Ramser J.,
RA Lehrach H., Reinhardt R., McCombie W.R., de la Bastide M., Dedhia N.,
RA Blocker H., Hornischer K., Nordsiek G., Agarwala R., Aravind L.,
RA Bailey J.A., Bateman A., Batzoglou S., Birney E., Bork P., Brown D.G.,
RA Burge C.B., Cerutti L., Chen H.C., Church D., Clamp M., Copley R.R.,
RA Doerks T., Eddy S.R., Eichler E.E., Furey T.S., Galagan J., Gilbert J.G.,
RA Harmon C., Hayashizaki Y., Haussler D., Hermjakob H., Hokamp K., Jang W.,
RA Johnson L.S., Jones T.A., Kasif S., Kaspryzk A., Kennedy S., Kent W.J.,
RA Kitts P., Koonin E.V., Korf I., Kulp D., Lancet D., Lowe T.M.,
RA McLysaght A., Mikkelsen T., Moran J.V., Mulder N., Pollara V.J.,
RA Ponting C.P., Schuler G., Schultz J., Slater G., Smit A.F., Stupka E.,
RA Szustakowski J., Thierry-Mieg D., Thierry-Mieg J., Wagner L., Wallis J.,
RA Wheeler R., Williams A., Wolf Y.I., Wolfe K.H., Yang S.P., Yeh R.F.,
RA Collins F., Guyer M.S., Peterson J., Felsenfeld A., Wetterstrand K.A.,
RA Patrinos A., Morgan M.J., de Jong P., Catanese J.J., Osoegawa K.,
RA Shizuya H., Choi S., Chen Y.J.;
RT "Initial sequencing and analysis of the human genome.";
RL Nature 409:860-921(2001).
RN [2] {ECO:0000313|Ensembl:ENSP00000502323.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496913; DOI=10.1038/nature03001;
RG International Human Genome Sequencing Consortium;
RT "Finishing the euchromatic sequence of the human genome.";
RL Nature 431:931-945(2004).
RN [3] {ECO:0000313|Ensembl:ENSP00000502323.1, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4] {ECO:0000313|Ensembl:ENSP00000502323.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2025) to UniProtKB.
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. {ECO:0000256|PROSITE-
CC ProRule:PRU00880}.
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DR EMBL; AC076966; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A6Q8PGN9; -.
DR SMR; A0A6Q8PGN9; -.
DR MassIVE; A0A6Q8PGN9; -.
DR Ensembl; ENST00000675786.1; ENSP00000502323.1; ENSG00000121879.6.
DR HGNC; HGNC:8975; PIK3CA.
DR GeneTree; ENSGT00940000155531; -.
DR OrthoDB; 67688at2759; -.
DR UniPathway; UPA00220; -.
DR Proteomes; UP000005640; Chromosome 3.
DR Bgee; ENSG00000121879; Expressed in calcaneal tendon and 201 other cell types or tissues.
DR ExpressionAtlas; A0A6Q8PGN9; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-ARBA.
DR GO; GO:0046934; F:1-phosphatidylinositol-4,5-bisphosphate 3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR CDD; cd08398; C2_PI3K_class_I_alpha; 1.
DR FunFam; 2.60.40.150:FF:000041; Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit; 1.
DR FunFam; 3.10.20.770:FF:000005; Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit; 1.
DR FunFam; 3.10.20.90:FF:000055; Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit; 1.
DR FunFam; 3.10.20.90:FF:000074; Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 3.10.20.90; Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 1; 2.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR002420; PI3K-type_C2_dom.
DR InterPro; IPR003113; PI3K_ABD.
DR InterPro; IPR000341; PI3K_Ras-bd_dom.
DR InterPro; IPR015433; PI_Kinase.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10048:SF107; PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE 3-KINASE CATALYTIC SUBUNIT ALPHA ISOFORM; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00792; PI3K_C2; 1.
DR Pfam; PF02192; PI3K_p85B; 1.
DR Pfam; PF00794; PI3K_rbd; 1.
DR SMART; SM00142; PI3K_C2; 1.
DR SMART; SM00143; PI3K_p85B; 1.
DR SMART; SM00144; PI3K_rbd; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS51547; C2_PI3K; 1.
DR PROSITE; PS51544; PI3K_ABD; 1.
DR PROSITE; PS51546; PI3K_RBD; 1.
PE 1: Evidence at protein level;
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A6Q8PGN9,
KW ECO:0007829|ProteomicsDB:A0A6Q8PGN9};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640}.
FT DOMAIN 16..105
FT /note="PI3K-ABD"
FT /evidence="ECO:0000259|PROSITE:PS51544"
FT DOMAIN 187..289
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 330..481
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
SQ SEQUENCE 483 AA; 55586 MW; 54B994E5D5264089 CRC64;
MPPRPSSGEL WGIHLMPPRI LVECLLPNGM IVTLECLREA TLITIKHELF KEARKYPLHQ
LLQDESSYIF VSVTQEAERE EFFDETRRLC DLRLFQPFLK VIEPVGNREE KILNREIGFA
IGMPVCEFDM VKDPEVQDFR RNILNVCKEA VDLRDLNSPH SRAMYVYPPN VESSPELPKH
IYNKLDKGQI IVVIWVIVSP NNDKQKYTLK INHDCVPEQV IAEAIRKKTR SMLLSSEQLK
LCVLEYQGKY ILKVCGCDEY FLEKYPLSQY KYIRSCIMLG RMPNLMLMAK ESLYSQLPMD
CFTMPSYSRR ISTATPYMNG ETSTKSLWVI NSALRIKILC ATYVNVNIRD IDKIYVRTGI
YHGGEPLCDN VNTQRVPCSN PRWNEWLNYD IYIPDLPRAA RLCLSICSVK GRKGAKEEHC
PLAWGNINLF DYTDTLVSGK MALNLWPVPH GLEDLLNPIG VTGSNPNKLF FHLLGNSMLR
VGV
//
