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P42336

- PK3CA_HUMAN

UniProt

P42336 - PK3CA_HUMAN

Protein

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

Gene

PIK3CA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 2 (20 Feb 2007)
      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.1 Publication

    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: UniProtKB
    2. 1-phosphatidylinositol-4-phosphate 3-kinase activity Source: RefGenome
    3. ATP binding Source: UniProtKB-KW
    4. kinase activity Source: Reactome
    5. phosphatidylinositol 3-kinase activity Source: UniProtKB
    6. phosphatidylinositol-4,5-bisphosphate 3-kinase activity Source: Reactome
    7. protein binding Source: UniProtKB
    8. protein kinase activator activity Source: Ensembl
    9. protein serine/threonine kinase activity Source: UniProtKB-KW

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. blood coagulation Source: Reactome
    3. cardiac muscle contraction Source: UniProtKB
    4. endothelial cell migration Source: UniProtKB
    5. epidermal growth factor receptor signaling pathway Source: Reactome
    6. Fc-epsilon receptor signaling pathway Source: Reactome
    7. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
    8. fibroblast growth factor receptor signaling pathway Source: Reactome
    9. glucose metabolic process Source: Ensembl
    10. hypomethylation of CpG island Source: Ensembl
    11. innate immune response Source: Reactome
    12. insulin receptor signaling pathway Source: Reactome
    13. insulin receptor signaling pathway via phosphatidylinositol 3-kinase Source: UniProtKB
    14. leukocyte migration Source: Reactome
    15. negative regulation of anoikis Source: UniProtKB
    16. negative regulation of fibroblast apoptotic process Source: Ensembl
    17. negative regulation of neuron apoptotic process Source: Ensembl
    18. neurotrophin TRK receptor signaling pathway Source: Reactome
    19. phosphatidylinositol-3-phosphate biosynthetic process Source: GOC
    20. phosphatidylinositol biosynthetic process Source: Reactome
    21. phosphatidylinositol-mediated signaling Source: Reactome
    22. phosphatidylinositol phosphorylation Source: BHF-UCL
    23. phospholipid metabolic process Source: Reactome
    24. platelet activation Source: UniProtKB
    25. positive regulation of peptidyl-serine phosphorylation Source: Ensembl
    26. protein kinase B signaling Source: Ensembl
    27. regulation of genetic imprinting Source: Ensembl
    28. regulation of multicellular organism growth Source: Ensembl
    29. small molecule metabolic process Source: Reactome
    30. T cell costimulation Source: Reactome
    31. T cell receptor signaling pathway Source: Reactome
    32. vasculature development Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Angiogenesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS04527-MONOMER.
    BRENDAi2.7.1.137. 2681.
    ReactomeiREACT_111040. Signaling by SCF-KIT.
    REACT_115852. Signaling by constitutively active EGFR.
    REACT_115961. PI3K events in ERBB4 signaling.
    REACT_116008. PI3K events in ERBB2 signaling.
    REACT_121025. Synthesis of PIPs at the plasma membrane.
    REACT_121141. Signaling by FGFR1 fusion mutants.
    REACT_121398. Signaling by FGFR mutants.
    REACT_12464. PI3K/AKT activation.
    REACT_12555. Downstream TCR signaling.
    REACT_12578. GAB1 signalosome.
    REACT_12621. Tie2 Signaling.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_147814. DAP12 signaling.
    REACT_160158. Role of phospholipids in phagocytosis.
    REACT_163769. Role of LAT2/NTAL/LAB on calcium mobilization.
    REACT_1695. GPVI-mediated activation cascade.
    REACT_17025. Downstream signal transduction.
    REACT_18283. G alpha (q) signalling events.
    REACT_18407. G alpha (12/13) signalling events.
    REACT_19344. Costimulation by the CD28 family.
    REACT_19358. CD28 dependent PI3K/Akt signaling.
    REACT_21270. PI-3K cascade.
    REACT_23787. Regulation of signaling by CBL.
    REACT_23832. Nephrin interactions.
    REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
    REACT_23891. Interleukin receptor SHC signaling.
    REACT_75829. PIP3 activates AKT signaling.
    REACT_976. PI3K Cascade.
    SignaLinkiP42336.

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:8975. PIK3CA.

    Subcellular locationi

    GO - Cellular componenti

    1. 1-phosphatidylinositol-4-phosphate 3-kinase, class IA complex Source: UniProtKB
    2. cytosol Source: Reactome
    3. lamellipodium Source: Ensembl
    4. phosphatidylinositol 3-kinase complex Source: BHF-UCL
    5. plasma membrane Source: RefGenome

    Pathology & Biotechi

    Involvement in diseasei

    PIK3CA mutations are involved in various type of cancer. Most of the cancer-associated mutations are missense mutations and map to one of the three hotspots: Glu-542; Glu-545 and His-1047. Mutated isoforms participate in cellular transformation and tumorigenesis induced by oncogenic receptor tyrosine kinases (RTKs) and HRAS/KRAS. Interaction with HRAS/KRAS is required for Ras-driven tumor formation. Mutations increasing the lipid kinase activity are required for oncogenic signaling. The protein kinase activity may not be required for tumorigenesis.
    Colorectal cancer (CRC) [MIM:114500]: A complex disease characterized by malignant lesions arising from the inner wall of the large intestine (the colon) and the rectum. Genetic alterations are often associated with progression from premalignant lesion (adenoma) to invasive adenocarcinoma. Risk factors for cancer of the colon and rectum include colon polyps, long-standing ulcerative colitis, and genetic family history.
    Note: The gene represented in this entry may be involved in disease pathogenesis.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti38 – 381R → H in CRC; likely involved in disease pathogenesis; shows an increase in lipid kinase activity; may disrupt the interaction between the PI3K-ABD domain and the N-terminal lobe of PI3K/PI4K kinase domain possibly affecting the conformation of the kinase domain.
    VAR_026166
    Natural varianti106 – 1061G → V in CRC; likely involved in disease pathogenesis; shows an increase in lipid kinase activity.
    VAR_026168
    Natural varianti420 – 4201C → R in CLOVE and CRC; shows an increase in lipid kinase activity; may increase the affinity for lipid membranes. 1 Publication
    VAR_026171
    Natural varianti453 – 4531E → Q in CRC; likely involved in disease pathogenesis; shows an increase in lipid kinase activity; may disrupt the interaction of the C2 PI3K-type domain with the iSH2 region of the p85 regulatory subunit.
    VAR_026172
    Natural varianti542 – 5421E → K in CLOVE, KERSEB, CRC and BC; also found in glioblastoma multiforme and endometrial carcinoma; shows an increase in lipid kinase activity; oncogenic in vivo; occurs in the interface between the PI3K helical domain and the nSH2 (N-terminal SH2) region of the p85 regulatory subunit and may reduce the inhibitory effect of p85; requires interaction with RAS to induce cellular transformation. 9 Publications
    VAR_026173
    Natural varianti545 – 5451E → K in MCAP, KERSEB, CRC and BC; shows an increase in lipid kinase activity; oncogenic in vivo; occurs in the interface between the PI3K helical domain and the nSH2 (N-terminal SH2) region of the p85 regulatory subunit and may reduce the inhibitory effect of p85; requires interaction with RAS to induce cellular transformation; enhances invadopodia-mediated extracellular matrix degradation and invasion in breast cancer cells. 10 Publications
    VAR_026178
    Natural varianti1023 – 10231R → Q in CRC; unknown pathological significance. 1 Publication
    VAR_026187
    Natural varianti1043 – 10431M → I in MCAP and CRC; also found in an endometrial carcinoma sample; shows an increase in lipid kinase activity. 2 Publications
    VAR_026190
    Natural varianti1047 – 10471H → R in CLOVE, KERSEB, CRC, BC and OC; also found in an endometrial carcinoma sample; shows an increase in lipid kinase activity; oncogenic in vivo; requires binding to p85 regulatory subunit to induce cellular transformation but not interaction with RAS; may mimic the conformatitonal change triggered by the interaction with RAS; enhances invadopodia-mediated extracellular matrix degradation and invasion in breast cancer cells; increases lipid kinase activity; may alter the interaction of the PI3K/PI4K kinase domain with the cell membrane. 12 Publications
    VAR_026192
    Breast cancer (BC) [MIM:114480]: A common malignancy originating from breast epithelial tissue. Breast neoplasms can be distinguished by their histologic pattern. Invasive ductal carcinoma is by far the most common type. Breast cancer is etiologically and genetically heterogeneous. Important genetic factors have been indicated by familial occurrence and bilateral involvement. Mutations at more than one locus can be involved in different families or even in the same case.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti542 – 5421E → K in CLOVE, KERSEB, CRC and BC; also found in glioblastoma multiforme and endometrial carcinoma; shows an increase in lipid kinase activity; oncogenic in vivo; occurs in the interface between the PI3K helical domain and the nSH2 (N-terminal SH2) region of the p85 regulatory subunit and may reduce the inhibitory effect of p85; requires interaction with RAS to induce cellular transformation. 9 Publications
    VAR_026173
    Natural varianti542 – 5421E → V in BC; unknown pathological significance. 1 Publication
    VAR_026175
    Natural varianti545 – 5451E → K in MCAP, KERSEB, CRC and BC; shows an increase in lipid kinase activity; oncogenic in vivo; occurs in the interface between the PI3K helical domain and the nSH2 (N-terminal SH2) region of the p85 regulatory subunit and may reduce the inhibitory effect of p85; requires interaction with RAS to induce cellular transformation; enhances invadopodia-mediated extracellular matrix degradation and invasion in breast cancer cells. 10 Publications
    VAR_026178
    Natural varianti546 – 5461Q → E in BC; unknown pathological significance. 1 Publication
    VAR_026179
    Natural varianti546 – 5461Q → R in BC; unknown pathological significance. 1 Publication
    VAR_026182
    Natural varianti1047 – 10471H → L in BC; unknown pathological significance. 4 Publications
    VAR_026191
    Natural varianti1047 – 10471H → R in CLOVE, KERSEB, CRC, BC and OC; also found in an endometrial carcinoma sample; shows an increase in lipid kinase activity; oncogenic in vivo; requires binding to p85 regulatory subunit to induce cellular transformation but not interaction with RAS; may mimic the conformatitonal change triggered by the interaction with RAS; enhances invadopodia-mediated extracellular matrix degradation and invasion in breast cancer cells; increases lipid kinase activity; may alter the interaction of the PI3K/PI4K kinase domain with the cell membrane. 12 Publications
    VAR_026192
    Ovarian cancer (OC) [MIM:167000]: The term ovarian cancer defines malignancies originating from ovarian tissue. Although many histologic types of ovarian tumors have been described, epithelial ovarian carcinoma is the most common form. Ovarian cancers are often asymptomatic and the recognized signs and symptoms, even of late-stage disease, are vague. Consequently, most patients are diagnosed with advanced disease.
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti546 – 5461Q → K in OC; unknown pathological significance. 1 Publication
    VAR_026180
    Natural varianti1047 – 10471H → R in CLOVE, KERSEB, CRC, BC and OC; also found in an endometrial carcinoma sample; shows an increase in lipid kinase activity; oncogenic in vivo; requires binding to p85 regulatory subunit to induce cellular transformation but not interaction with RAS; may mimic the conformatitonal change triggered by the interaction with RAS; enhances invadopodia-mediated extracellular matrix degradation and invasion in breast cancer cells; increases lipid kinase activity; may alter the interaction of the PI3K/PI4K kinase domain with the cell membrane. 12 Publications
    VAR_026192
    Hepatocellular carcinoma (HCC) [MIM:114550]: A primary malignant neoplasm of epithelial liver cells. The major risk factors for HCC are chronic hepatitis B virus (HBV) infection, chronic hepatitis C virus (HCV) infection, prolonged dietary aflatoxin exposure, alcoholic cirrhosis, and cirrhosis due to other causes.1 Publication
    Note: The gene represented in this entry may be involved in disease pathogenesis.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti545 – 5451E → A in CWS5 and HCC; also found in a glioblastoma multiforme sample. 3 Publications
    VAR_026176
    Keratosis, seborrheic (KERSEB) [MIM:182000]: A common benign skin tumor. Seborrheic keratoses usually begin with the appearance of one or more sharply defined, light brown, flat macules. The lesions may be sparse or numerous. As they initially grow, they develop a velvety to finely verrucous surface, followed by an uneven warty surface with multiple plugged follicles and a dull or lackluster appearance.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti542 – 5421E → K in CLOVE, KERSEB, CRC and BC; also found in glioblastoma multiforme and endometrial carcinoma; shows an increase in lipid kinase activity; oncogenic in vivo; occurs in the interface between the PI3K helical domain and the nSH2 (N-terminal SH2) region of the p85 regulatory subunit and may reduce the inhibitory effect of p85; requires interaction with RAS to induce cellular transformation. 9 Publications
    VAR_026173
    Natural varianti545 – 5451E → G in KERSEB; also found in an endometrial carcinoma sample. 4 Publications
    VAR_026177
    Natural varianti545 – 5451E → K in MCAP, KERSEB, CRC and BC; shows an increase in lipid kinase activity; oncogenic in vivo; occurs in the interface between the PI3K helical domain and the nSH2 (N-terminal SH2) region of the p85 regulatory subunit and may reduce the inhibitory effect of p85; requires interaction with RAS to induce cellular transformation; enhances invadopodia-mediated extracellular matrix degradation and invasion in breast cancer cells. 10 Publications
    VAR_026178
    Natural varianti1047 – 10471H → R in CLOVE, KERSEB, CRC, BC and OC; also found in an endometrial carcinoma sample; shows an increase in lipid kinase activity; oncogenic in vivo; requires binding to p85 regulatory subunit to induce cellular transformation but not interaction with RAS; may mimic the conformatitonal change triggered by the interaction with RAS; enhances invadopodia-mediated extracellular matrix degradation and invasion in breast cancer cells; increases lipid kinase activity; may alter the interaction of the PI3K/PI4K kinase domain with the cell membrane. 12 Publications
    VAR_026192
    Megalencephaly-capillary malformation-polymicrogyria syndrome (MCAP) [MIM:602501]: A syndrome characterized by a spectrum of anomalies including primary megalencephaly, prenatal overgrowth, brain and body asymmetry, cutaneous vascular malformations, digital anomalies consisting of syndactyly with or without postaxial polydactyly, connective tissue dysplasia involving the skin, subcutaneous tissue, and joints, and cortical brain malformations, most distinctively polymicrogyria.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti81 – 811E → K in MCAP. 1 Publication
    VAR_069251
    Natural varianti88 – 881R → Q in MCAP; also found in a glioblastoma multiforme sample; may disrupt the interaction between the PI3K-ABD domain and the N-terminal lobe of PI3K/PI4K kinase domain possibly affecting the conformation of the kinase domain. 2 Publications
    VAR_026167
    Natural varianti364 – 3641G → R in MCAP. 1 Publication
    VAR_069252
    Natural varianti365 – 3651E → K in MCAP. 1 Publication
    VAR_069253
    Natural varianti378 – 3781C → Y in MCAP. 1 Publication
    VAR_069254
    Natural varianti453 – 4531Missing in MCAP and MPPH. 1 Publication
    VAR_069255
    Natural varianti545 – 5451E → K in MCAP, KERSEB, CRC and BC; shows an increase in lipid kinase activity; oncogenic in vivo; occurs in the interface between the PI3K helical domain and the nSH2 (N-terminal SH2) region of the p85 regulatory subunit and may reduce the inhibitory effect of p85; requires interaction with RAS to induce cellular transformation; enhances invadopodia-mediated extracellular matrix degradation and invasion in breast cancer cells. 10 Publications
    VAR_026178
    Natural varianti726 – 7261E → K in MCAP. 1 Publication
    VAR_069256
    Natural varianti914 – 9141G → R in MCAP. 1 Publication
    VAR_069257
    Natural varianti1021 – 10211Y → C in MCAP; also found in an endometrial carcinoma sample. 2 Publications
    VAR_026184
    Natural varianti1025 – 10251T → A in MCAP. 1 Publication
    VAR_069258
    Natural varianti1035 – 10351A → V in MCAP; also found in an endometrial carcinoma sample. 2 Publications
    VAR_026189
    Natural varianti1043 – 10431M → I in MCAP and CRC; also found in an endometrial carcinoma sample; shows an increase in lipid kinase activity. 2 Publications
    VAR_026190
    Natural varianti1047 – 10471H → Y in MCAP; also found in an endometrial carcinoma sample. 2 Publications
    VAR_026193
    Natural varianti1049 – 10491G → S in MCAP. 1 Publication
    VAR_069259
    Megalencephaly-polymicrogyria-polydactyly-hydrocephalus syndrome (MPPH) [MIM:603387]: A syndrome characterized by megalencephaly, hydrocephalus, and polymicrogyria; polydactyly may also be seen. There is considerable phenotypic similarity between this disorder and the megalencephaly-capillary malformation syndrome.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti453 – 4531Missing in MCAP and MPPH. 1 Publication
    VAR_069255
    Congenital lipomatous overgrowth, vascular malformations, and epidermal nevi (CLOVE) [MIM:612918]: A sporadically occurring, non-hereditary disorder characterized by asymmetric somatic hypertrophy and anomalies in multiple organs. It is defined by four main clinical findings: congenital lipomatous overgrowth, vascular malformations, epidermal nevi, and skeletal/spinal abnormalities. The presence of truncal overgrowth and characteristic patterned macrodactyly at birth differentiates CLOVE from other syndromic forms of overgrowth.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti420 – 4201C → R in CLOVE and CRC; shows an increase in lipid kinase activity; may increase the affinity for lipid membranes. 1 Publication
    VAR_026171
    Natural varianti542 – 5421E → K in CLOVE, KERSEB, CRC and BC; also found in glioblastoma multiforme and endometrial carcinoma; shows an increase in lipid kinase activity; oncogenic in vivo; occurs in the interface between the PI3K helical domain and the nSH2 (N-terminal SH2) region of the p85 regulatory subunit and may reduce the inhibitory effect of p85; requires interaction with RAS to induce cellular transformation. 9 Publications
    VAR_026173
    Natural varianti1047 – 10471H → R in CLOVE, KERSEB, CRC, BC and OC; also found in an endometrial carcinoma sample; shows an increase in lipid kinase activity; oncogenic in vivo; requires binding to p85 regulatory subunit to induce cellular transformation but not interaction with RAS; may mimic the conformatitonal change triggered by the interaction with RAS; enhances invadopodia-mediated extracellular matrix degradation and invasion in breast cancer cells; increases lipid kinase activity; may alter the interaction of the PI3K/PI4K kinase domain with the cell membrane. 12 Publications
    VAR_026192
    Cowden syndrome 5 (CWS5) [MIM:615108]: A form of Cowden syndrome, a hamartomatous polyposis syndrome with age-related penetrance. Cowden syndrome is characterized by hamartomatous lesions affecting derivatives of ectodermal, mesodermal and endodermal layers, macrocephaly, facial trichilemmomas (benign tumors of the hair follicle infundibulum), acral keratoses, papillomatous papules, and elevated risk for development of several types of malignancy, particularly breast carcinoma in women and thyroid carcinoma in both men and women. Colon cancer and renal cell carcinoma have also been reported. Hamartomas can be found in virtually every organ, but most commonly in the skin, gastrointestinal tract, breast and thyroid.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti118 – 1181G → D in CWS5. 1 Publication
    VAR_069786
    Natural varianti135 – 1351E → K in CWS5. 1 Publication
    VAR_069787
    Natural varianti218 – 2181E → K in CWS5. 1 Publication
    VAR_069788
    Natural varianti356 – 3561V → I in CWS5. 1 Publication
    VAR_069789
    Natural varianti382 – 3821R → K in CWS5. 1 Publication
    VAR_069790
    Natural varianti545 – 5451E → A in CWS5 and HCC; also found in a glioblastoma multiforme sample. 3 Publications
    VAR_026176

    Keywords - Diseasei

    Disease mutation, Proto-oncogene

    Organism-specific databases

    MIMi114480. phenotype.
    114500. phenotype.
    114550. phenotype.
    167000. phenotype.
    182000. phenotype.
    602501. phenotype.
    603387. phenotype.
    612918. phenotype.
    615108. phenotype.
    Orphaneti140944. CLOVE syndrome.
    201. Cowden syndrome.
    99802. Hemimegalencephaly.
    144. Hereditary nonpolyposis colon cancer.
    295239. Macrodactyly of fingers, unilateral.
    60040. Megalencephaly-capillary malformation-polymicrogyria syndrome.
    314662. Segmental progressive overgrowth syndrome with fibroadipose hyperplasia.
    PharmGKBiPA33308.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10681068Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoformPRO_0000088785Add
    BLAST

    Proteomic databases

    MaxQBiP42336.
    PaxDbiP42336.
    PRIDEiP42336.

    PTM databases

    PhosphoSiteiP42336.

    Expressioni

    Gene expression databases

    ArrayExpressiP42336.
    BgeeiP42336.
    CleanExiHS_PIK3CA.
    GenevestigatoriP42336.

    Organism-specific databases

    HPAiCAB017804.
    HPA009985.

    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 By similarity. Interacts with RASD2 By similarity. Interacts with APPL1. Interacts with HRAS and KRAS By similarity. Interaction with HRAS/KRAS is required for PI3K pathway signaling and cell proliferation stimulated by EGF and FGF2 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ERBB3P218603EBI-2116585,EBI-720706
    IRS1P3556820EBI-2116585,EBI-517592
    PIK3R1P2798613EBI-2116585,EBI-79464

    Protein-protein interaction databases

    BioGridi111308. 50 interactions.
    DIPiDIP-42728N.
    IntActiP42336. 26 interactions.
    MINTiMINT-1367228.
    STRINGi9606.ENSP00000263967.

    Structurei

    Secondary structure

    1
    1068
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 106
    Beta strandi13 – 153
    Beta strandi18 – 258
    Beta strandi31 – 377
    Helixi42 – 5211
    Helixi53 – 553
    Beta strandi56 – 583
    Helixi59 – 613
    Helixi65 – 673
    Beta strandi69 – 746
    Turni75 – 773
    Beta strandi79 – 824
    Helixi89 – 913
    Beta strandi94 – 1029
    Helixi108 – 12114
    Helixi126 – 1305
    Helixi134 – 1429
    Helixi144 – 15512
    Turni156 – 1594
    Helixi160 – 1667
    Helixi179 – 1824
    Beta strandi185 – 19814
    Turni199 – 2024
    Beta strandi203 – 21210
    Helixi217 – 22610
    Turni230 – 2323
    Turni236 – 2394
    Helixi240 – 2456
    Helixi246 – 2483
    Beta strandi249 – 2546
    Turni255 – 2584
    Helixi267 – 2693
    Helixi271 – 2799
    Beta strandi284 – 2896
    Helixi290 – 2945
    Helixi306 – 3094
    Beta strandi324 – 3263
    Helixi327 – 3293
    Beta strandi332 – 34211
    Turni348 – 3503
    Beta strandi353 – 36210
    Beta strandi365 – 3684
    Beta strandi377 – 3804
    Beta strandi382 – 39211
    Helixi393 – 3953
    Beta strandi401 – 41313
    Beta strandi416 – 43015
    Beta strandi434 – 4363
    Beta strandi439 – 4446
    Beta strandi454 – 4563
    Beta strandi458 – 4603
    Beta strandi468 – 4703
    Beta strandi472 – 4776
    Beta strandi481 – 4855
    Helixi489 – 4924
    Helixi495 – 4984
    Beta strandi511 – 5133
    Helixi517 – 5204
    Helixi526 – 53611
    Helixi539 – 5413
    Helixi545 – 5539
    Turni554 – 5574
    Helixi558 – 5603
    Helixi562 – 5643
    Helixi565 – 5717
    Helixi577 – 58913
    Helixi595 – 5984
    Helixi599 – 6024
    Helixi609 – 62214
    Helixi625 – 63814
    Helixi639 – 6413
    Beta strandi643 – 6464
    Helixi648 – 65710
    Helixi661 – 67212
    Turni673 – 6764
    Turni678 – 6803
    Helixi681 – 69414
    Helixi698 – 72023
    Turni721 – 7255
    Helixi728 – 73912
    Helixi742 – 7487
    Beta strandi749 – 7535
    Beta strandi756 – 7616
    Helixi766 – 7683
    Beta strandi774 – 7763
    Beta strandi779 – 7846
    Helixi790 – 7923
    Beta strandi795 – 80511
    Helixi808 – 82518
    Turni826 – 8283
    Beta strandi838 – 8425
    Beta strandi845 – 8495
    Beta strandi852 – 8565
    Helixi857 – 8615
    Turni865 – 8673
    Helixi871 – 8733
    Helixi876 – 8849
    Helixi887 – 8893
    Helixi890 – 91122
    Beta strandi920 – 9245
    Beta strandi929 – 9313
    Helixi942 – 9454
    Helixi958 – 9647
    Turni965 – 9673
    Beta strandi969 – 9713
    Beta strandi972 – 9743
    Helixi975 – 99319
    Helixi995 – 10039
    Turni1004 – 10074
    Helixi1016 – 102510
    Turni1026 – 10294
    Helixi1032 – 104716
    Beta strandi1053 – 10553
    Beta strandi1056 – 10583

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ENQNMR-A331-481[»]
    2RD0X-ray3.05A1-1068[»]
    3HHMX-ray2.80A1-1068[»]
    3HIZX-ray3.30A1-1068[»]
    3ZIMX-ray2.85A107-1046[»]
    4JPSX-ray2.20A1-1068[»]
    4L1BX-ray2.59A1-1068[»]
    4L23X-ray2.50A1-1068[»]
    4L2YX-ray2.80A1-1068[»]
    ProteinModelPortaliP42336.
    SMRiP42336. Positions 16-105, 107-1046.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP42336.

    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 PIK3R1.2 Publications

    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.
    HOVERGENiHBG052721.
    InParanoidiP42336.
    KOiK00922.
    OMAiAFAVRCL.
    OrthoDBiEOG70CR65.
    PhylomeDBiP42336.
    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.

    P42336-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPPRPSSGEL WGIHLMPPRI LVECLLPNGM IVTLECLREA TLITIKHELF     50
    KEARKYPLHQ LLQDESSYIF VSVTQEAERE EFFDETRRLC DLRLFQPFLK 100
    VIEPVGNREE KILNREIGFA IGMPVCEFDM VKDPEVQDFR RNILNVCKEA 150
    VDLRDLNSPH SRAMYVYPPN VESSPELPKH IYNKLDKGQI IVVIWVIVSP 200
    NNDKQKYTLK INHDCVPEQV IAEAIRKKTR SMLLSSEQLK LCVLEYQGKY 250
    ILKVCGCDEY FLEKYPLSQY KYIRSCIMLG RMPNLMLMAK ESLYSQLPMD 300
    CFTMPSYSRR ISTATPYMNG ETSTKSLWVI NSALRIKILC ATYVNVNIRD 350
    IDKIYVRTGI YHGGEPLCDN VNTQRVPCSN PRWNEWLNYD IYIPDLPRAA 400
    RLCLSICSVK GRKGAKEEHC PLAWGNINLF DYTDTLVSGK MALNLWPVPH 450
    GLEDLLNPIG VTGSNPNKET PCLELEFDWF SSVVKFPDMS VIEEHANWSV 500
    SREAGFSYSH AGLSNRLARD NELRENDKEQ LKAISTRDPL SEITEQEKDF 550
    LWSHRHYCVT IPEILPKLLL SVKWNSRDEV AQMYCLVKDW PPIKPEQAME 600
    LLDCNYPDPM VRGFAVRCLE KYLTDDKLSQ YLIQLVQVLK YEQYLDNLLV 650
    RFLLKKALTN QRIGHFFFWH LKSEMHNKTV SQRFGLLLES YCRACGMYLK 700
    HLNRQVEAME KLINLTDILK QEKKDETQKV QMKFLVEQMR RPDFMDALQG 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 CTKTREFERF QEMCYKAYLA IRQHANLFIN 1000
    LFSMMLGSGM PELQSFDDIA YIRKTLALDK TEQEALEYFM KQMNDAHHGG 1050
    WTTKMDWIFH TIKQHALN 1068
    Length:1,068
    Mass (Da):124,284
    Last modified:February 20, 2007 - v2
    Checksum:i041487231A9A1207
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti170 – 1701N → H in CAA82333. (PubMed:7713498)Curated
    Sequence conflicti187 – 1871K → R in CAA82333. (PubMed:7713498)Curated
    Sequence conflicti286 – 2872ML → KM in CAA82333. (PubMed:7713498)Curated
    Sequence conflicti346 – 3461V → L in CAA82333. (PubMed:7713498)Curated
    Sequence conflicti723 – 7231K → R in CAA82333. (PubMed:7713498)Curated
    Sequence conflicti751 – 7511F → L in CAA82333. (PubMed:7713498)Curated
    Sequence conflicti767 – 7671E → K in CAA82333. (PubMed:7713498)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti38 – 381R → H in CRC; likely involved in disease pathogenesis; shows an increase in lipid kinase activity; may disrupt the interaction between the PI3K-ABD domain and the N-terminal lobe of PI3K/PI4K kinase domain possibly affecting the conformation of the kinase domain.
    VAR_026166
    Natural varianti43 – 431I → V.1 Publication
    Corresponds to variant rs1051399 [ dbSNP | Ensembl ].
    VAR_042942
    Natural varianti81 – 811E → K in MCAP. 1 Publication
    VAR_069251
    Natural varianti88 – 881R → Q in MCAP; also found in a glioblastoma multiforme sample; may disrupt the interaction between the PI3K-ABD domain and the N-terminal lobe of PI3K/PI4K kinase domain possibly affecting the conformation of the kinase domain. 2 Publications
    VAR_026167
    Natural varianti106 – 1061G → V in CRC; likely involved in disease pathogenesis; shows an increase in lipid kinase activity.
    VAR_026168
    Natural varianti118 – 1181G → D in CWS5. 1 Publication
    VAR_069786
    Natural varianti135 – 1351E → K in CWS5. 1 Publication
    VAR_069787
    Natural varianti218 – 2181E → K in CWS5. 1 Publication
    VAR_069788
    Natural varianti332 – 3321S → R.1 Publication
    Corresponds to variant rs1051407 [ dbSNP | Ensembl ].
    VAR_042943
    Natural varianti343 – 3431Y → C Found in a cancer sample; unknown pathological significance. 1 Publication
    VAR_026169
    Natural varianti356 – 3561V → I in CWS5. 1 Publication
    VAR_069789
    Natural varianti364 – 3641G → R in MCAP. 1 Publication
    VAR_069252
    Natural varianti365 – 3651E → K in MCAP. 1 Publication
    VAR_069253
    Natural varianti378 – 3781C → Y in MCAP. 1 Publication
    VAR_069254
    Natural varianti382 – 3821R → K in CWS5. 1 Publication
    VAR_069790
    Natural varianti391 – 3911I → M.1 Publication
    Corresponds to variant rs3729680 [ dbSNP | Ensembl ].
    VAR_026170
    Natural varianti420 – 4201C → R in CLOVE and CRC; shows an increase in lipid kinase activity; may increase the affinity for lipid membranes. 1 Publication
    VAR_026171
    Natural varianti453 – 4531E → Q in CRC; likely involved in disease pathogenesis; shows an increase in lipid kinase activity; may disrupt the interaction of the C2 PI3K-type domain with the iSH2 region of the p85 regulatory subunit.
    VAR_026172
    Natural varianti453 – 4531Missing in MCAP and MPPH. 1 Publication
    VAR_069255
    Natural varianti542 – 5421E → K in CLOVE, KERSEB, CRC and BC; also found in glioblastoma multiforme and endometrial carcinoma; shows an increase in lipid kinase activity; oncogenic in vivo; occurs in the interface between the PI3K helical domain and the nSH2 (N-terminal SH2) region of the p85 regulatory subunit and may reduce the inhibitory effect of p85; requires interaction with RAS to induce cellular transformation. 9 Publications
    VAR_026173
    Natural varianti542 – 5421E → Q Found in an endometrial carcinoma sample; unknown pathological significance. 1 Publication
    VAR_026174
    Natural varianti542 – 5421E → V in BC; unknown pathological significance. 1 Publication
    VAR_026175
    Natural varianti545 – 5451E → A in CWS5 and HCC; also found in a glioblastoma multiforme sample. 3 Publications
    VAR_026176
    Natural varianti545 – 5451E → G in KERSEB; also found in an endometrial carcinoma sample. 4 Publications
    VAR_026177
    Natural varianti545 – 5451E → K in MCAP, KERSEB, CRC and BC; shows an increase in lipid kinase activity; oncogenic in vivo; occurs in the interface between the PI3K helical domain and the nSH2 (N-terminal SH2) region of the p85 regulatory subunit and may reduce the inhibitory effect of p85; requires interaction with RAS to induce cellular transformation; enhances invadopodia-mediated extracellular matrix degradation and invasion in breast cancer cells. 10 Publications
    VAR_026178
    Natural varianti546 – 5461Q → E in BC; unknown pathological significance. 1 Publication
    VAR_026179
    Natural varianti546 – 5461Q → K in OC; unknown pathological significance. 1 Publication
    VAR_026180
    Natural varianti546 – 5461Q → P Found in an anaplastic astrocytoma sample; unknown pathological significance. 1 Publication
    VAR_026181
    Natural varianti546 – 5461Q → R in BC; unknown pathological significance. 1 Publication
    VAR_026182
    Natural varianti726 – 7261E → K in MCAP. 1 Publication
    VAR_069256
    Natural varianti914 – 9141G → R in MCAP. 1 Publication
    VAR_069257
    Natural varianti1007 – 10071G → R Found in an endometrial carcinoma sample; unknown pathological significance. 1 Publication
    VAR_026183
    Natural varianti1021 – 10211Y → C in MCAP; also found in an endometrial carcinoma sample. 2 Publications
    VAR_026184
    Natural varianti1021 – 10211Y → H Found in an endometrial carcinoma sample; unknown pathological significance. 1 Publication
    VAR_026185
    Natural varianti1021 – 10211Y → N Found in a glioblastoma multiforme sample; unknown pathological significance. 1 Publication
    VAR_026186
    Natural varianti1023 – 10231R → Q in CRC; unknown pathological significance. 1 Publication
    VAR_026187
    Natural varianti1025 – 10251T → A in MCAP. 1 Publication
    VAR_069258
    Natural varianti1025 – 10251T → N Found in a glioblastoma multiforme sample; unknown pathological significance. 1 Publication
    VAR_026188
    Natural varianti1035 – 10351A → V in MCAP; also found in an endometrial carcinoma sample. 2 Publications
    VAR_026189
    Natural varianti1043 – 10431M → I in MCAP and CRC; also found in an endometrial carcinoma sample; shows an increase in lipid kinase activity. 2 Publications
    VAR_026190
    Natural varianti1047 – 10471H → L in BC; unknown pathological significance. 4 Publications
    VAR_026191
    Natural varianti1047 – 10471H → R in CLOVE, KERSEB, CRC, BC and OC; also found in an endometrial carcinoma sample; shows an increase in lipid kinase activity; oncogenic in vivo; requires binding to p85 regulatory subunit to induce cellular transformation but not interaction with RAS; may mimic the conformatitonal change triggered by the interaction with RAS; enhances invadopodia-mediated extracellular matrix degradation and invasion in breast cancer cells; increases lipid kinase activity; may alter the interaction of the PI3K/PI4K kinase domain with the cell membrane. 12 Publications
    VAR_026192
    Natural varianti1047 – 10471H → Y in MCAP; also found in an endometrial carcinoma sample. 2 Publications
    VAR_026193
    Natural varianti1049 – 10491G → S in MCAP. 1 Publication
    VAR_069259
    Natural varianti1050 – 10501G → D Found in an endometrial carcinoma sample; unknown pathological significance. 1 Publication
    VAR_026194
    Natural varianti1052 – 10521T → K Found in an endometrial carcinoma sample; unknown pathological significance. 1 Publication
    VAR_026195
    Natural varianti1065 – 10651H → L Found in an endometrial carcinoma sample; unknown pathological significance. 1 Publication
    VAR_026196
    Natural varianti1065 – 10651H → Y Found in brain tumors; unknown pathological significance. 1 Publication
    VAR_026197

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z29090 mRNA. Translation: CAA82333.1.
    U79143 mRNA. Translation: AAB39753.1.
    BC113601 mRNA. Translation: AAI13602.1.
    BC113603 mRNA. Translation: AAI13604.1.
    CCDSiCCDS43171.1.
    PIRiI38110.
    RefSeqiNP_006209.2. NM_006218.2.
    XP_006713721.1. XM_006713658.1.
    UniGeneiHs.553498.
    Hs.715194.

    Genome annotation databases

    EnsembliENST00000263967; ENSP00000263967; ENSG00000121879.
    GeneIDi5290.
    KEGGihsa:5290.
    UCSCiuc003fjk.3. human.

    Polymorphism databases

    DMDMi126302584.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z29090 mRNA. Translation: CAA82333.1 .
    U79143 mRNA. Translation: AAB39753.1 .
    BC113601 mRNA. Translation: AAI13602.1 .
    BC113603 mRNA. Translation: AAI13604.1 .
    CCDSi CCDS43171.1.
    PIRi I38110.
    RefSeqi NP_006209.2. NM_006218.2.
    XP_006713721.1. XM_006713658.1.
    UniGenei Hs.553498.
    Hs.715194.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2ENQ NMR - A 331-481 [» ]
    2RD0 X-ray 3.05 A 1-1068 [» ]
    3HHM X-ray 2.80 A 1-1068 [» ]
    3HIZ X-ray 3.30 A 1-1068 [» ]
    3ZIM X-ray 2.85 A 107-1046 [» ]
    4JPS X-ray 2.20 A 1-1068 [» ]
    4L1B X-ray 2.59 A 1-1068 [» ]
    4L23 X-ray 2.50 A 1-1068 [» ]
    4L2Y X-ray 2.80 A 1-1068 [» ]
    ProteinModelPortali P42336.
    SMRi P42336. Positions 16-105, 107-1046.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111308. 50 interactions.
    DIPi DIP-42728N.
    IntActi P42336. 26 interactions.
    MINTi MINT-1367228.
    STRINGi 9606.ENSP00000263967.

    Chemistry

    BindingDBi P42336.
    ChEMBLi CHEMBL4005.
    GuidetoPHARMACOLOGYi 2153.

    PTM databases

    PhosphoSitei P42336.

    Polymorphism databases

    DMDMi 126302584.

    Proteomic databases

    MaxQBi P42336.
    PaxDbi P42336.
    PRIDEi P42336.

    Protocols and materials databases

    DNASUi 5290.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263967 ; ENSP00000263967 ; ENSG00000121879 .
    GeneIDi 5290.
    KEGGi hsa:5290.
    UCSCi uc003fjk.3. human.

    Organism-specific databases

    CTDi 5290.
    GeneCardsi GC03P178865.
    GeneReviewsi PIK3CA.
    HGNCi HGNC:8975. PIK3CA.
    HPAi CAB017804.
    HPA009985.
    MIMi 114480. phenotype.
    114500. phenotype.
    114550. phenotype.
    167000. phenotype.
    171834. gene.
    182000. phenotype.
    602501. phenotype.
    603387. phenotype.
    612918. phenotype.
    615108. phenotype.
    neXtProti NX_P42336.
    Orphaneti 140944. CLOVE syndrome.
    201. Cowden syndrome.
    99802. Hemimegalencephaly.
    144. Hereditary nonpolyposis colon cancer.
    295239. Macrodactyly of fingers, unilateral.
    60040. Megalencephaly-capillary malformation-polymicrogyria syndrome.
    314662. Segmental progressive overgrowth syndrome with fibroadipose hyperplasia.
    PharmGKBi PA33308.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5032.
    HOVERGENi HBG052721.
    InParanoidi P42336.
    KOi K00922.
    OMAi AFAVRCL.
    OrthoDBi EOG70CR65.
    PhylomeDBi P42336.
    TreeFami TF102031.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS04527-MONOMER.
    BRENDAi 2.7.1.137. 2681.
    Reactomei REACT_111040. Signaling by SCF-KIT.
    REACT_115852. Signaling by constitutively active EGFR.
    REACT_115961. PI3K events in ERBB4 signaling.
    REACT_116008. PI3K events in ERBB2 signaling.
    REACT_121025. Synthesis of PIPs at the plasma membrane.
    REACT_121141. Signaling by FGFR1 fusion mutants.
    REACT_121398. Signaling by FGFR mutants.
    REACT_12464. PI3K/AKT activation.
    REACT_12555. Downstream TCR signaling.
    REACT_12578. GAB1 signalosome.
    REACT_12621. Tie2 Signaling.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_147814. DAP12 signaling.
    REACT_160158. Role of phospholipids in phagocytosis.
    REACT_163769. Role of LAT2/NTAL/LAB on calcium mobilization.
    REACT_1695. GPVI-mediated activation cascade.
    REACT_17025. Downstream signal transduction.
    REACT_18283. G alpha (q) signalling events.
    REACT_18407. G alpha (12/13) signalling events.
    REACT_19344. Costimulation by the CD28 family.
    REACT_19358. CD28 dependent PI3K/Akt signaling.
    REACT_21270. PI-3K cascade.
    REACT_23787. Regulation of signaling by CBL.
    REACT_23832. Nephrin interactions.
    REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
    REACT_23891. Interleukin receptor SHC signaling.
    REACT_75829. PIP3 activates AKT signaling.
    REACT_976. PI3K Cascade.
    SignaLinki P42336.

    Miscellaneous databases

    ChiTaRSi PIK3CA. human.
    EvolutionaryTr