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P42337

- PK3CA_MOUSE

UniProt

P42337 - PK3CA_MOUSE

Protein

Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform

Gene

Pik3ca

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Phosphoinositide-3-kinase (PI3K) that phosphorylates PtdIns (Phosphatidylinositol), PtdIns4P (Phosphatidylinositol 4-phosphate) and PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Participates in cellular signaling in response to various growth factors. Involved in the activation of AKT1 upon stimulation by receptor tyrosine kinases ligands such as EGF, insulin, IGF1, VEGFA and PDGF. Involved in signaling via insulin-receptor substrate (IRS) proteins. Essential in endothelial cell migration during vascular development through VEGFA signaling, possibly by regulating RhoA activity. Required for lymphatic vasculature development, possibly by binding to RAS and by activation by EGF and FGF2, but not by PDGF. Regulates invadopodia formation in breast cancer cells through the PDPK1-AKT1 pathway. Participates in cardiomyogenesis in embryonic stem cells through a AKT1 pathway. Participates in vasculogenesis in embryonic stem cells through PDK1 and protein kinase C pathway. Has also serine-protein kinase activity: phosphorylates PIK3R1 (p85alpha regulatory subunit), EIF4EBP1 and HRAS.6 Publications

    Catalytic activityi

    ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate.
    ATP + a protein = ADP + a phosphoprotein.

    GO - Molecular functioni

    1. 1-phosphatidylinositol-3-kinase activity Source: MGI
    2. 1-phosphatidylinositol-4-phosphate 3-kinase activity Source: RefGenome
    3. ATP binding Source: UniProtKB-KW
    4. insulin receptor substrate binding Source: MGI
    5. phosphatidylinositol-4,5-bisphosphate 3-kinase activity Source: RefGenome
    6. protein binding Source: IntAct
    7. protein kinase activator activity Source: BHF-UCL
    8. protein serine/threonine kinase activity Source: UniProtKB-KW

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. glucose metabolic process Source: MGI
    3. hypomethylation of CpG island Source: BHF-UCL
    4. negative regulation of anoikis Source: Ensembl
    5. negative regulation of fibroblast apoptotic process Source: MGI
    6. negative regulation of neuron apoptotic process Source: MGI
    7. phosphatidylinositol-3-phosphate biosynthetic process Source: GOC
    8. phosphatidylinositol-mediated signaling Source: InterPro
    9. positive regulation of peptidyl-serine phosphorylation Source: BHF-UCL
    10. positive regulation of protein kinase activity Source: GOC
    11. protein kinase B signaling Source: MGI
    12. protein phosphorylation Source: MGI
    13. regulation of genetic imprinting Source: BHF-UCL
    14. regulation of multicellular organism growth Source: MGI

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Angiogenesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.1.137. 3474.
    ReactomeiREACT_188185. DAP12 signaling.
    REACT_188578. Signaling by SCF-KIT.
    REACT_196455. Signaling by FGFR mutants.
    REACT_196460. Signaling by FGFR1 fusion mutants.
    REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_198634. Regulation of signaling by CBL.
    REACT_198973. Synthesis of PIPs at the plasma membrane.
    REACT_199123. Signaling by constitutively active EGFR.
    REACT_203296. PI3K events in ERBB4 signaling.
    REACT_204733. G alpha (12/13) signalling events.
    REACT_205300. PI3K/AKT activation.
    REACT_206286. GAB1 signalosome.
    REACT_207651. G alpha (q) signalling events.
    REACT_210240. Role of phospholipids in phagocytosis.
    REACT_210793. Interleukin receptor SHC signaling.
    REACT_211860. Tie2 Signaling.
    REACT_213364. Role of LAT2/NTAL/LAB on calcium mobilization.
    REACT_215348. PI3K events in ERBB2 signaling.
    REACT_220092. GPVI-mediated activation cascade.
    REACT_223993. PI-3K cascade.
    REACT_225145. Downstream TCR signaling.
    REACT_225477. Costimulation by the CD28 family.
    REACT_225836. Interleukin-3, 5 and GM-CSF signaling.
    REACT_226151. CD28 dependent PI3K/Akt signaling.
    REACT_226341. PIP3 activates AKT signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform (EC:2.7.1.153)
    Short name:
    PI3-kinase subunit alpha
    Short name:
    PI3K-alpha
    Short name:
    PI3Kalpha
    Short name:
    PtdIns-3-kinase subunit alpha
    Alternative name(s):
    Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit alpha
    Short name:
    PtdIns-3-kinase subunit p110-alpha
    Short name:
    p110alpha
    Phosphoinositide-3-kinase catalytic alpha polypeptide
    Serine/threonine protein kinase PIK3CA (EC:2.7.11.1)
    Gene namesi
    Name:Pik3ca
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:1206581. Pik3ca.

    Subcellular locationi

    GO - Cellular componenti

    1. 1-phosphatidylinositol-4-phosphate 3-kinase, class IA complex Source: Ensembl
    2. lamellipodium Source: MGI
    3. phosphatidylinositol 3-kinase complex Source: MGI
    4. plasma membrane Source: RefGenome

    Pathology & Biotechi

    Disruption phenotypei

    Lethal. Embryonic fibroblasts cells are resistant to oncogenic transformation induced by oncogenic receptor tyrosine kinases (RTKs), are unable to differentiate into adipocytes and deficient in cellular signaling in response to various growth factors. Defective responsiveness to insulin led to reduced somatic growth, hyperinsulinemia, glucose intolerance, hyperphagia and increased adiposity.4 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi208 – 2081T → D: Abolishes binding to HRAS and KRAS; does not affect kinase activity; displays defective development of the lymphatic vasculature, resulting in perinatal appearance of chylous ascites and is highly resistant to endogenous Ras oncogene-induced tumorigenesis; when associated with A-227. 1 Publication
    Mutagenesisi227 – 2271K → A: Abolishes binding to HRAS and KRAS; does not affect kinase activity; displays defective development of the lymphatic vasculature, resulting in perinatal appearance of chylous ascites and is highly resistant to endogenous Ras oncogene-induced tumorigenesis; when associated with D-208. 1 Publication
    Mutagenesisi933 – 9331D → A: Loss of kinase activity; displays early embryonic lethality at E10-11 and severe defects in angiogenic sprouting and vascular remodeling. Heterozygous mice yield adult mice with markedly impaired insulin signaling and reduced activation of effector pathways such as Akt/PKB. 1 Publication

    Keywords - Diseasei

    Proto-oncogene

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10681068Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoformPRO_0000088786Add
    BLAST

    Proteomic databases

    MaxQBiP42337.
    PaxDbiP42337.
    PRIDEiP42337.

    PTM databases

    PhosphoSiteiP42337.

    Expressioni

    Gene expression databases

    ArrayExpressiP42337.
    BgeeiP42337.
    GenevestigatoriP42337.

    Interactioni

    Subunit structurei

    Heterodimer of a catalytic subunit PIK3CA and a p85 regulatory subunit (PIK3R1, PIK3R2 or PIK3R3). Interacts with IRS1 in nuclear extracts. Interacts with RUFY3. Interacts with RASD2. Interacts with APPL1. Interacts with HRAS and KRAS. Interaction with HRAS/KRAS is required for PI3K pathway signaling and cell proliferation stimulated by EGF and FGF2.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HRASP011122EBI-641748,EBI-350145From a different organism.
    Pik3r1P264506EBI-641748,EBI-641764

    Protein-protein interaction databases

    BioGridi202160. 5 interactions.
    DIPiDIP-32095N.
    IntActiP42337. 10 interactions.
    MINTiMINT-219865.
    STRINGi10090.ENSMUSP00000103878.

    Structurei

    Secondary structure

    1
    1068
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 125
    Beta strandi18 – 258
    Beta strandi31 – 377
    Helixi42 – 5211
    Helixi53 – 553
    Turni57 – 604
    Helixi65 – 673
    Beta strandi69 – 746
    Beta strandi77 – 815
    Helixi90 – 923
    Beta strandi94 – 1029
    Helixi109 – 1124
    Helixi117 – 1215
    Helixi125 – 1295
    Helixi134 – 1429
    Helixi144 – 15310
    Turni154 – 1574
    Helixi158 – 1658
    Helixi179 – 1824
    Beta strandi189 – 1968
    Turni199 – 2024
    Beta strandi205 – 2128
    Helixi217 – 23014
    Helixi236 – 24611
    Helixi247 – 2493
    Beta strandi250 – 2545
    Helixi267 – 2693
    Helixi271 – 2799
    Beta strandi284 – 2896
    Helixi290 – 2956
    Beta strandi324 – 3274
    Beta strandi332 – 3409
    Beta strandi348 – 3503
    Beta strandi354 – 36411
    Beta strandi378 – 3803
    Beta strandi382 – 39211
    Turni393 – 3953
    Beta strandi401 – 4088
    Beta strandi423 – 4308
    Beta strandi434 – 4363
    Beta strandi439 – 4446
    Beta strandi454 – 4563
    Beta strandi458 – 4603
    Beta strandi468 – 4703
    Beta strandi472 – 4776
    Beta strandi481 – 4855
    Helixi489 – 49911
    Turni529 – 5357
    Helixi545 – 5539
    Helixi555 – 5584
    Helixi562 – 5643
    Helixi565 – 5695
    Helixi578 – 58811
    Helixi595 – 5984
    Turni599 – 6024
    Helixi609 – 62113
    Helixi625 – 6306
    Helixi632 – 6365
    Helixi639 – 6413
    Beta strandi643 – 6464
    Helixi648 – 65912
    Helixi661 – 67313
    Helixi678 – 69417
    Turni695 – 6973
    Helixi698 – 72023
    Helixi728 – 73811
    Helixi742 – 7476
    Beta strandi749 – 7524
    Beta strandi759 – 7613
    Beta strandi779 – 7846
    Helixi790 – 7923
    Beta strandi795 – 80511
    Helixi808 – 82720
    Beta strandi838 – 8425
    Beta strandi845 – 8495
    Beta strandi854 – 8563
    Helixi857 – 8604
    Helixi876 – 8849
    Helixi887 – 8893
    Helixi890 – 91122
    Turni918 – 9203
    Beta strandi921 – 9244
    Beta strandi929 – 9313
    Helixi941 – 9455
    Helixi957 – 9648
    Beta strandi965 – 9673
    Helixi975 – 99319
    Helixi995 – 100410
    Beta strandi1013 – 10153
    Helixi1016 – 102510
    Helixi1032 – 104312
    Turni1046 – 10494
    Turni1057 – 10593

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4A55X-ray3.50A1-1068[»]
    ProteinModelPortaliP42337.
    SMRiP42337. Positions 16-105, 107-1046.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini16 – 10590PI3K-ABDPROSITE-ProRule annotationAdd
    BLAST
    Domaini187 – 289103PI3K-RBDPROSITE-ProRule annotationAdd
    BLAST
    Domaini330 – 487158C2 PI3K-typePROSITE-ProRule annotationAdd
    BLAST
    Domaini517 – 694178PIK helicalPROSITE-ProRule annotationAdd
    BLAST
    Domaini797 – 1068272PI3K/PI4KPROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The PI3K-ABD domain and the PI3K-RBD domain interact with the PI3K/PI4K kinase domain. The C2 PI3K-type domain may facilitate the recruitment to the plasma membrane. The inhibitory interactions with PIK3R1 are mediated by the PI3K-ABD domain and the C2 PI3K-type domain with the iSH2 (inter-SH2) region of PIK3R1, and the C2 PI3K-type domain, the PI3K helical domain, and the PI3K/PI4K kinase domain with the nSH2 (N-terminal SH2) region of PIK3R1.By similarity

    Sequence similaritiesi

    Belongs to the PI3/PI4-kinase family.PROSITE-ProRule annotation
    Contains 1 C2 PI3K-type domain.PROSITE-ProRule annotation
    Contains 1 PI3K-ABD domain.PROSITE-ProRule annotation
    Contains 1 PI3K-RBD domain.PROSITE-ProRule annotation
    Contains 1 PI3K/PI4K domain.PROSITE-ProRule annotation
    Contains 1 PIK helical domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5032.
    GeneTreeiENSGT00620000087742.
    HOGENOMiHOG000252911.
    HOVERGENiHBG052721.
    InParanoidiQ0VGQ5.
    KOiK00922.
    OMAiAFAVRCL.
    OrthoDBiEOG70CR65.
    TreeFamiTF102031.

    Family and domain databases

    Gene3Di1.10.1070.11. 1 hit.
    1.25.40.70. 1 hit.
    2.60.40.150. 1 hit.
    InterProiIPR016024. ARM-type_fold.
    IPR000008. C2_dom.
    IPR011009. Kinase-like_dom.
    IPR000403. PI3/4_kinase_cat_dom.
    IPR018936. PI3/4_kinase_CS.
    IPR003113. PI3K_adapt-bd_dom.
    IPR002420. PI3K_C2_dom.
    IPR000341. PI3K_Ras-bd_dom.
    IPR015433. PI_Kinase.
    IPR001263. PInositide-3_kin_accessory_dom.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view]
    PANTHERiPTHR10048. PTHR10048. 1 hit.
    PfamiPF00454. PI3_PI4_kinase. 1 hit.
    PF00792. PI3K_C2. 1 hit.
    PF02192. PI3K_p85B. 1 hit.
    PF00794. PI3K_rbd. 1 hit.
    PF00613. PI3Ka. 1 hit.
    [Graphical view]
    SMARTiSM00239. C2. 1 hit.
    SM00142. PI3K_C2. 1 hit.
    SM00143. PI3K_p85B. 1 hit.
    SM00144. PI3K_rbd. 1 hit.
    SM00145. PI3Ka. 1 hit.
    SM00146. PI3Kc. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 1 hit.
    SSF49562. SSF49562. 1 hit.
    SSF54236. SSF54236. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS00915. PI3_4_KINASE_1. 1 hit.
    PS00916. PI3_4_KINASE_2. 1 hit.
    PS50290. PI3_4_KINASE_3. 1 hit.
    PS51544. PI3K_ABD. 1 hit.
    PS51547. PI3K_C2. 1 hit.
    PS51546. PI3K_RBD. 1 hit.
    PS51545. PIK_HELICAL. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P42337-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPPRPSSGEL WGIHLMPPRI LVECLLPNGM IVTLECLREA TLVTIKHELF     50
    REARKYPLHQ LLQDETSYIF VSVTQEAERE EFFDETRRLC DLRLFQPFLK 100
    VIEPVGNREE KILNREIGFV IGMPVCEFDM VKDPEVQDFR RNILNVCKEA 150
    VDLRDLNSPH SRAMYVYPPN VESSPELPKH IYNKLDKGQI IVVIWVIVSP 200
    NNDKQKYTLK INHDCVPEQV IAEAIRKKTR SMLLSSEQLK LCVLEYQGKY 250
    ILKVCGCDEY FLEKYPLSQY KYIRSCIMLG RMPNLMLMAK ESLYSQLPID 300
    SFTMPSYSRR ISTATPYMNG ETSTKSLWVI NSALRIKILC ATYVNVNIRD 350
    IDKIYVRTGI YHGGEPLCDN VNTQRVPCSN PRWNEWLNYD IYIPDLPRAA 400
    RLCLSICSVK GRKGAKEEHC PLAWGNINLF DYTDTLVSGK MALNLWPVPH 450
    GLEDLLNPIG VTGSNPNKET PCLELEFDWF SSVVKFPDMS VIEEHANWSV 500
    SREAGFSYSH TGLSNRLARD NELRENDKEQ LRALCTRDPL SEITEQEKDF 550
    LWSHRHYCVT IPEILPKLLL SVKWNSRDEV AQMYCLVKDW PPIKPEQAME 600
    LLDCNYPDPM VRSFAVRCLE KYLTDDKLSQ YLIQLVQVLK YEQYLDNLLV 650
    RFLLKKALTN QRIGHFFFWH LKSEMHNKTV SQRFGLLLES YCRACGMYLK 700
    HLNRQVEAME KLINLTDILK QEKKDETQKV QMKFLVEQMR QPDFMDALQG 750
    FLSPLNPAHQ LGNLRLEECR IMSSAKRPLW LNWENPDIMS ELLFQNNEII 800
    FKNGDDLRQD MLTLQIIRIM ENIWQNQGLD LRMLPYGCLS IGDCVGLIEV 850
    VRNSHTIMQI QCKGGLKGAL QFNSHTLHQW LKDKNKGEIY DAAIDLFTRS 900
    CAGYCVATFI LGIGDRHNSN IMVKDDGQLF HIDFGHFLDH KKKKFGYKRE 950
    RVPFVLTQDF LIVISKGAQE YTKTREFERF QEMCYKAYLA IRQHANLFIN 1000
    LFSMMLGSGM PELQSFDDIA YIRKTLALDK TEQEALEYFT KQMNDAHHGG 1050
    WTTKMDWIFH TIKQHALN 1068
    Length:1,068
    Mass (Da):124,412
    Last modified:July 27, 2011 - v2
    Checksum:iD593283B416ABFD0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti399 – 3991A → L in AAA18334. (PubMed:8139567)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U03279 mRNA. Translation: AAA18334.1.
    CH466530 Genomic DNA. Translation: EDL34990.1.
    BC089038 mRNA. Translation: AAH89038.1.
    BC130228 mRNA. Translation: AAI30229.1.
    CCDSiCCDS38409.1.
    RefSeqiNP_032865.2. NM_008839.2.
    XP_006535472.1. XM_006535409.1.
    XP_006535473.1. XM_006535410.1.
    UniGeneiMm.260521.

    Genome annotation databases

    EnsembliENSMUST00000029201; ENSMUSP00000029201; ENSMUSG00000027665.
    ENSMUST00000108243; ENSMUSP00000103878; ENSMUSG00000027665.
    GeneIDi18706.
    KEGGimmu:18706.
    UCSCiuc008owd.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U03279 mRNA. Translation: AAA18334.1 .
    CH466530 Genomic DNA. Translation: EDL34990.1 .
    BC089038 mRNA. Translation: AAH89038.1 .
    BC130228 mRNA. Translation: AAI30229.1 .
    CCDSi CCDS38409.1.
    RefSeqi NP_032865.2. NM_008839.2.
    XP_006535472.1. XM_006535409.1.
    XP_006535473.1. XM_006535410.1.
    UniGenei Mm.260521.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4A55 X-ray 3.50 A 1-1068 [» ]
    ProteinModelPortali P42337.
    SMRi P42337. Positions 16-105, 107-1046.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202160. 5 interactions.
    DIPi DIP-32095N.
    IntActi P42337. 10 interactions.
    MINTi MINT-219865.
    STRINGi 10090.ENSMUSP00000103878.

    Chemistry

    BindingDBi P42337.
    ChEMBLi CHEMBL2499.

    PTM databases

    PhosphoSitei P42337.

    Proteomic databases

    MaxQBi P42337.
    PaxDbi P42337.
    PRIDEi P42337.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000029201 ; ENSMUSP00000029201 ; ENSMUSG00000027665 .
    ENSMUST00000108243 ; ENSMUSP00000103878 ; ENSMUSG00000027665 .
    GeneIDi 18706.
    KEGGi mmu:18706.
    UCSCi uc008owd.2. mouse.

    Organism-specific databases

    CTDi 5290.
    MGIi MGI:1206581. Pik3ca.

    Phylogenomic databases

    eggNOGi COG5032.
    GeneTreei ENSGT00620000087742.
    HOGENOMi HOG000252911.
    HOVERGENi HBG052721.
    InParanoidi Q0VGQ5.
    KOi K00922.
    OMAi AFAVRCL.
    OrthoDBi EOG70CR65.
    TreeFami TF102031.

    Enzyme and pathway databases

    BRENDAi 2.7.1.137. 3474.
    Reactomei REACT_188185. DAP12 signaling.
    REACT_188578. Signaling by SCF-KIT.
    REACT_196455. Signaling by FGFR mutants.
    REACT_196460. Signaling by FGFR1 fusion mutants.
    REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_198634. Regulation of signaling by CBL.
    REACT_198973. Synthesis of PIPs at the plasma membrane.
    REACT_199123. Signaling by constitutively active EGFR.
    REACT_203296. PI3K events in ERBB4 signaling.
    REACT_204733. G alpha (12/13) signalling events.
    REACT_205300. PI3K/AKT activation.
    REACT_206286. GAB1 signalosome.
    REACT_207651. G alpha (q) signalling events.
    REACT_210240. Role of phospholipids in phagocytosis.
    REACT_210793. Interleukin receptor SHC signaling.
    REACT_211860. Tie2 Signaling.
    REACT_213364. Role of LAT2/NTAL/LAB on calcium mobilization.
    REACT_215348. PI3K events in ERBB2 signaling.
    REACT_220092. GPVI-mediated activation cascade.
    REACT_223993. PI-3K cascade.
    REACT_225145. Downstream TCR signaling.
    REACT_225477. Costimulation by the CD28 family.
    REACT_225836. Interleukin-3, 5 and GM-CSF signaling.
    REACT_226151. CD28 dependent PI3K/Akt signaling.
    REACT_226341. PIP3 activates AKT signaling.

    Miscellaneous databases

    ChiTaRSi PIK3CA. mouse.
    NextBioi 294769.
    PROi P42337.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P42337.
    Bgeei P42337.
    Genevestigatori P42337.

    Family and domain databases

    Gene3Di 1.10.1070.11. 1 hit.
    1.25.40.70. 1 hit.
    2.60.40.150. 1 hit.
    InterProi IPR016024. ARM-type_fold.
    IPR000008. C2_dom.
    IPR011009. Kinase-like_dom.
    IPR000403. PI3/4_kinase_cat_dom.
    IPR018936. PI3/4_kinase_CS.
    IPR003113. PI3K_adapt-bd_dom.
    IPR002420. PI3K_C2_dom.
    IPR000341. PI3K_Ras-bd_dom.
    IPR015433. PI_Kinase.
    IPR001263. PInositide-3_kin_accessory_dom.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view ]
    PANTHERi PTHR10048. PTHR10048. 1 hit.
    Pfami PF00454. PI3_PI4_kinase. 1 hit.
    PF00792. PI3K_C2. 1 hit.
    PF02192. PI3K_p85B. 1 hit.
    PF00794. PI3K_rbd. 1 hit.
    PF00613. PI3Ka. 1 hit.
    [Graphical view ]
    SMARTi SM00239. C2. 1 hit.
    SM00142. PI3K_C2. 1 hit.
    SM00143. PI3K_p85B. 1 hit.
    SM00144. PI3K_rbd. 1 hit.
    SM00145. PI3Ka. 1 hit.
    SM00146. PI3Kc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 1 hit.
    SSF49562. SSF49562. 1 hit.
    SSF54236. SSF54236. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS00915. PI3_4_KINASE_1. 1 hit.
    PS00916. PI3_4_KINASE_2. 1 hit.
    PS50290. PI3_4_KINASE_3. 1 hit.
    PS51544. PI3K_ABD. 1 hit.
    PS51547. PI3K_C2. 1 hit.
    PS51546. PI3K_RBD. 1 hit.
    PS51545. PIK_HELICAL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The interaction of small domains between the subunits of phosphatidylinositol 3-kinase determines enzyme activity."
      Klippel A., Escobedo J.A., Hirano M., Williams L.T.
      Mol. Cell. Biol. 14:2675-2685(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
    2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6.
      Tissue: Eye.
    4. "Control of cell size through phosphorylation of upstream binding factor 1 by nuclear phosphatidylinositol 3-kinase."
      Drakas R., Tu X., Baserga R.
      Proc. Natl. Acad. Sci. U.S.A. 101:9272-9276(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IRS1.
    5. "A pharmacological map of the PI3-K family defines a role for p110alpha in insulin signaling."
      Knight Z.A., Gonzalez B., Feldman M.E., Zunder E.R., Goldenberg D.D., Williams O., Loewith R., Stokoe D., Balla A., Toth B., Balla T., Weiss W.A., Williams R.L., Shokat K.M.
      Cell 125:733-747(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Critical role for the p110alpha phosphoinositide-3-OH kinase in growth and metabolic regulation."
      Foukas L.C., Claret M., Pearce W., Okkenhaug K., Meek S., Peskett E., Sancho S., Smith A.J.H., Withers D.J., Vanhaesebroeck B.
      Nature 441:366-370(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ASP-933.
    7. "The p110alpha isoform of PI3K is essential for proper growth factor signaling and oncogenic transformation."
      Zhao J.J., Cheng H., Jia S., Wang L., Gjoerup O.V., Mikami A., Roberts T.M.
      Proc. Natl. Acad. Sci. U.S.A. 103:16296-16300(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    8. "Binding of ras to phosphoinositide 3-kinase p110alpha is required for ras-driven tumorigenesis in mice."
      Gupta S., Ramjaun A.R., Haiko P., Wang Y., Warne P.H., Nicke B., Nye E., Stamp G., Alitalo K., Downward J.
      Cell 129:957-968(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH HRAS AND KRAS, MUTAGENESIS OF THR-208 AND LYS-227.
    9. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    10. "VEGF-mediated PI3K class IA and PKC signaling in cardiomyogenesis and vasculogenesis of mouse embryonic stem cells."
      Bekhite M.M., Finkensieper A., Binas S., Mueller J., Wetzker R., Figulla H.-R., Sauer H., Wartenberg M.
      J. Cell Sci. 124:1819-1830(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION ON CARDIOMYOGENESIS, FUNCTION ON VASCULOGENESIS.

    Entry informationi

    Entry nameiPK3CA_MOUSE
    AccessioniPrimary (citable) accession number: P42337
    Secondary accession number(s): Q0VGQ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 132 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3