PIK3CA (phosphoinositide-3-kinase, catalytic, alpha polypeptide)

2018-06-01   Julia Phillips , Enric Domingo 

Department of Oncology, University of Oxford, Oxford, United Kingdom \\\/ enric.domingo@oncology.ox.ac.uk




Review on PIK3CA, with data on DNA, on the protein encoded, and where the gene is implicated.


Atlas Image
Relative size of the 21 exons of PIK3CA. The entire exon 1 is UTR (untranslated region). Exon numeration corresponds to the prevalent transcript (NM-006218).


The PIK3CA gene spans a total genomic size of 86,190 bases and is composed of 21 exons, 20 of them coding exons of varying lengths. Putative pseudogenes of PIK3CA have been described on chromosomes 16 (gi 28913054) and 22q11.2 (gi 5931525), the later one in the Cat Eye Syndrome region. These regions are highly homolog to the sequences of exons 9 and 11-13 of the PIK3CA gene.


The human PIK3CA transcript has an open reading frame of 3,207-bp, predicting a protein of 1,068 amino acid residues.


A pseudogene has been identified in chromosome 20 (LOC100422375) spanning exons 9 to 13 with 95% homology in both exons and introns. A non-specific amplification of PIK3CA could result in a E545A false positive mutation which is the amino-acid most commonly mutated in PIK3CA.


Atlas Image
p110alpha conserved domains. Through its adaptor binding domain p110alpha interacts with the regulatory subunit. C2 domain, protein-kinase-C-homology-2 domain.


The PIK3CA gene encodes the p110alpha protein which is a catalytic subunit of the class I PI 3-kinases (PI3K). Class I PI3K are heterodimeric molecules composed of a catalytic subunit, a p110, and a regulatory subunit. There are three possible calatytic subunits p110alpha, beta or delta.


Widely expressed.


The p110alpha localizes in the cytoplasm.


Class I PI 3-kinases (PI3K) are one of the most prevalently dysregulated pathways in human cancer and it is linked to many cellular functions, including cell growth, proliferation, differentiation, motility, survival and intracellular trafficking. PI3K convert PI(4,5)P2 to PI(3,4,5)P3 on the inner leaflet of the plasma membrane. The PI(3,4,)P3 provokes the recruitment to cellular membranes of a variety of signalling proteins, containing PX domain, pleckstrin homology domains (PH domains), FYVE domains and other phosphoinositide-binding domains. One of these is the protein kinase B (PKB/AKT) a very well known protein that is activated as a result of its translocation to the cell membrane where it is then phosphorylated and activated by another kinase, called phosphoinositide dependent kinase 1 (PDK1). The phosphorylation of AKT leads to the activation of the TSC/mTOR pathway. Accordingly, PIK3CA and PTEN genetic alterations are usually alternative events.



Somatic mutations at the PIK3CA gene have been found in tumors and thus, it is a bona fide oncogene (Samuels et al., 2004). Sequencing analyses of pancancer genomes suggests that PIK3CA has at least 19 mutational hotspots (Chang et al, 2016). Most mutations occur in two of the five domains of p110alpha, the helical and kinase domains. However, while there are no frequent hotspot mutations within the Ras-binding domain (RBD), hotspot mutations within the adaptor-binding domain (ABD) and the C2 domain are also frequently found. Hotspots Arg38 and Arg88 are located within the ABD at the interface with the kinase domain. These mutations disrupt hydrogen bonds between the domains which may alter the conformation of the kinase domain and therefore its enzymatic activity. Similarly, hotspots Asn345 and Glu453 within the C2 domain occur at the interface with the iSH2 domain of p85 and are expected to alter the interaction between these domains. Within the helical domain, the most common hotspots Glu542 and Glu545 are usually mutated into lysine and are located at the interface with the nSH2 domain of p85. A structural model of the p110/niSH2 complex suggests that the contacts between these amino acids and the nSH2 domain occur within a region of the nSH2 domain which is also in contact with the kinase domain of p110. These contacts may serve as the mechanism by which the helical domain mutations alter the activity of the enzyme. In the kinase domain, His1047 is frequently mutated to arginine within a helix at the end of the activation loop. Another less frequent kinase mutation of Met1043 occurs within the same helix and likely has similar effects on enzymatic activity. Thr1025 mutations are located near the N-terminus of the catalytic loop which may directly alter the conformation of the catalytic loop as the mechanism by which the mutation alters enzymatic activity (Huang, 2008). Two other hotspot positions, Lys111 and Gly118, are located outside of the five domains in the 81 residue linker between ABD and RBD (Chang, 2016).
The distribution of PIK3CA hotspot mutations can be significantly variable across tumour types in the kinase and helical domain. For example, cervical and bladder cancers share similar distributions of hotspots but they have far fewer H1047R kinase mutations than breast cancer. Similarly, endometrial and colorectal cancers share distribution patterns but display more R88Q mutations than other tumor types, maybe because this change is a target mutation of POLE genomic instability. However, colorectal cancers differ from endometrial cancers in their clonality. In endometrial tumors, both E545 helical domain mutations and H1047 kinase domain mutations are early clonal mutations whereas in colorectal cancer several E545 mutations are subclonal and H1047 mutations clonal (Chang, 2016). The variation in hotspot distributions suggests different functions need to be targeted in different tumour types.
Different domain mutations in PIK3CA have been associated with differential signaling. Kinase domain mutations have higher activation of PI3K complexes and increased G-alpha signaling events. However, some components of the G-alpha signaling pathway such as RHO GTPase complexes have lower activity in the kinase domain mutants relative to other PIK3CA mutants. Additionally, helical domain mutations are associated with lower activation of pathways related to proliferation, such as FOXM1, MYC, and PLK1, in comparison to other PIK3CA mutants. The different patterns of pathway activation associated with mutations of specific PIK3CA domains suggest that kinase domain mutations are more strongly associated with proliferation activity, whereas helical domain mutations are more strongly associated with motility activities. These differences in function across domain specific mutations may drive the varying distribution of mutations seen across cancer types (Yau, 2014).


PIK3CA has a small CpG island in the gene promoter but no methylation has been described.

Implicated in

Entity name
A wide variety of human cancers
PIK3CA mutations lead to constitutive activation of p110alpha enzymatic activity, stimulate AKT signaling, and allow growth factor-independent growth (Bader et al., 2005). In addition, when expressed in normal cells, these mutations allow anchorage-independent growth, further attesting to their important role in cancer development (Kang et al., 2005). PIK3CA somatic mutations are frequent in a variety of human primary tumors and cancer cell lines such as, among others, those of the colon, breast, and stomach (Samuels et al., 2004). However, in other tumors, i.e. those of the lung, head and neck, brain, endometrium, ovary, prostate, osteosarcoma and pancreas, hematopoietic malignancies, PIK3CA mutations are not as common (Angulo et al., 2008; Qiu et al., 2006; Muller et al., 2007; Samuels et al., 2004; Schonleben et al., 2006). PIK3CA gene amplification has also been proposed as a mechanism for oncogene activation in some tumors (Angulo et al., 2008).
Entity name
Cowden syndrome
Syndrome characterized by multiple noncancerous hamartomas and high predisposition to breast, thyroid and other tumour types. Germline PIK3CA mutations may account for around 10% of cases. Most of these mutations are in different positions to main hotspot somatic PIK3CA mutations. Mutations in the genes from the same pathway PTEN and AKT1 may account for about 25% and 2% of cases respectively.


Pubmed IDLast YearTitleAuthors
164321792006Cancer-specific mutations in PIK3CA are oncogenic in vivo.Bader AG et al
178774602008Effects of oncogenic p110alpha subunit mutations on the lipid kinase activity of phosphoinositide 3-kinase.Carson JD et al
266190112016Identifying recurrent mutations in cancer reveals widespread lineage diversity and mutational specificity.Chang MT et al
184180432008Insights into the oncogenic effects of PIK3CA mutations from the structure of p110alpha/p85alpha.Huang CH et al
212169292011PIK3CA mutations in patients with advanced cancers treated with PI3K/AKT/mTOR axis inhibitors.Janku F et al
295088572018Targeting the PI3K pathway in cancer: are we making headway?Janku F et al
294010022018Phosphatidylinositol 3-Kinase α-Selective Inhibition With Alpelisib (BYL719) in PIK3CA-Altered Solid Tumors: Results From the First-in-Human Study.Juric D et al
167649262007Rare mutations of the PIK3CA gene in malignancies of the hematopoietic system as well as endometrium, ovary, prostate and osteosarcomas, and discovery of a PIK3CA pseudogene.Müller CI et al
232462882013Germline PIK3CA and AKT1 mutations in Cowden and Cowden-like syndromes.Orloff MS et al
267120862016PIK3CA Mutation, Aspirin Use after Diagnosis and Survival of Colorectal Cancer. A Systematic Review and Meta-analysis of Epidemiological Studies.Paleari L et al
196213912010Cyclooxygenase-2 inhibition inhibits PI3K/AKT kinase activity in epithelial ovarian cancer.Uddin S et al

Other Information

Locus ID:

NCBI: 5290
MIM: 171834
HGNC: 8975
Ensembl: ENSG00000121879


dbSNP: 5290
ClinVar: 5290
TCGA: ENSG00000121879


Gene IDTranscript IDUniprot

Expression (GTEx)



PathwaySourceExternal ID
Inositol phosphate metabolismKEGGko00562
ErbB signaling pathwayKEGGko04012
Phosphatidylinositol signaling systemKEGGko04070
Autophagy - animalKEGGko04140
mTOR signaling pathwayKEGGko04150
Axon guidanceKEGGko04360
VEGF signaling pathwayKEGGko04370
Focal adhesionKEGGko04510
Toll-like receptor signaling pathwayKEGGko04620
Jak-STAT signaling pathwayKEGGko04630
Natural killer cell mediated cytotoxicityKEGGko04650
T cell receptor signaling pathwayKEGGko04660
B cell receptor signaling pathwayKEGGko04662
Fc epsilon RI signaling pathwayKEGGko04664
Leukocyte transendothelial migrationKEGGko04670
Regulation of actin cytoskeletonKEGGko04810
Insulin signaling pathwayKEGGko04910
Progesterone-mediated oocyte maturationKEGGko04914
Type II diabetes mellitusKEGGko04930
Colorectal cancerKEGGko05210
Renal cell carcinomaKEGGko05211
Pancreatic cancerKEGGko05212
Endometrial cancerKEGGko05213
Prostate cancerKEGGko05215
Chronic myeloid leukemiaKEGGko05220
Acute myeloid leukemiaKEGGko05221
Small cell lung cancerKEGGko05222
Non-small cell lung cancerKEGGko05223
Inositol phosphate metabolismKEGGhsa00562
ErbB signaling pathwayKEGGhsa04012
Phosphatidylinositol signaling systemKEGGhsa04070
Autophagy - animalKEGGhsa04140
mTOR signaling pathwayKEGGhsa04150
Axon guidanceKEGGhsa04360
VEGF signaling pathwayKEGGhsa04370
Focal adhesionKEGGhsa04510
Toll-like receptor signaling pathwayKEGGhsa04620
Jak-STAT signaling pathwayKEGGhsa04630
Natural killer cell mediated cytotoxicityKEGGhsa04650
T cell receptor signaling pathwayKEGGhsa04660
B cell receptor signaling pathwayKEGGhsa04662
Fc epsilon RI signaling pathwayKEGGhsa04664
Leukocyte transendothelial migrationKEGGhsa04670
Regulation of actin cytoskeletonKEGGhsa04810
Insulin signaling pathwayKEGGhsa04910
Type II diabetes mellitusKEGGhsa04930
Pathways in cancerKEGGhsa05200
Colorectal cancerKEGGhsa05210
Renal cell carcinomaKEGGhsa05211
Pancreatic cancerKEGGhsa05212
Endometrial cancerKEGGhsa05213
Prostate cancerKEGGhsa05215
Chronic myeloid leukemiaKEGGhsa05220
Acute myeloid leukemiaKEGGhsa05221
Small cell lung cancerKEGGhsa05222
Non-small cell lung cancerKEGGhsa05223
Chemokine signaling pathwayKEGGko04062
Chemokine signaling pathwayKEGGhsa04062
Neurotrophin signaling pathwayKEGGko04722
Neurotrophin signaling pathwayKEGGhsa04722
Fc gamma R-mediated phagocytosisKEGGko04666
Fc gamma R-mediated phagocytosisKEGGhsa04666
Progesterone-mediated oocyte maturationKEGGhsa04914
Aldosterone-regulated sodium reabsorptionKEGGko04960
Aldosterone-regulated sodium reabsorptionKEGGhsa04960
Chagas disease (American trypanosomiasis)KEGGko05142
Chagas disease (American trypanosomiasis)KEGGhsa05142
Bacterial invasion of epithelial cellsKEGGko05100
Bacterial invasion of epithelial cellsKEGGhsa05100
Carbohydrate digestion and absorptionKEGGko04973
Carbohydrate digestion and absorptionKEGGhsa04973
Hepatitis CKEGGko05160
Hepatitis CKEGGhsa05160
Osteoclast differentiationKEGGko04380
Osteoclast differentiationKEGGhsa04380
Influenza AKEGGko05164
Influenza AKEGGhsa05164
Cholinergic synapseKEGGhsa04725
HTLV-I infectionKEGGko05166
HTLV-I infectionKEGGhsa05166
Epstein-Barr virus infectionKEGGhsa05169
Epstein-Barr virus infectionKEGGko05169
Viral carcinogenesisKEGGhsa05203
Viral carcinogenesisKEGGko05203
PI3K-Akt signaling pathwayKEGGhsa04151
PI3K-Akt signaling pathwayKEGGko04151
Hepatitis BKEGGhsa05161
HIF-1 signaling pathwayKEGGhsa04066
Proteoglycans in cancerKEGGhsa05205
Proteoglycans in cancerKEGGko05205
Estrogen signaling pathwayKEGGhsa04915
Estrogen signaling pathwayKEGGko04915
TNF signaling pathwayKEGGhsa04668
TNF signaling pathwayKEGGko04668
Prolactin signaling pathwayKEGGhsa04917
Prolactin signaling pathwayKEGGko04917
MicroRNAs in cancerKEGGhsa05206
MicroRNAs in cancerKEGGko05206
Non-alcoholic fatty liver disease (NAFLD)KEGGhsa04932
Non-alcoholic fatty liver disease (NAFLD)KEGGko04932
Ras signaling pathwayKEGGhsa04014
Rap1 signaling pathwayKEGGhsa04015
Rap1 signaling pathwayKEGGko04015
FoxO signaling pathwayKEGGhsa04068
Thyroid hormone signaling pathwayKEGGhsa04919
Inflammatory mediator regulation of TRP channelsKEGGhsa04750
Inflammatory mediator regulation of TRP channelsKEGGko04750
Platelet activationKEGGhsa04611
AMPK signaling pathwayKEGGhsa04152
AMPK signaling pathwayKEGGko04152
cAMP signaling pathwayKEGGhsa04024
cAMP signaling pathwayKEGGko04024
Signaling pathways regulating pluripotency of stem cellsKEGGhsa04550
Signaling pathways regulating pluripotency of stem cellsKEGGko04550
Central carbon metabolism in cancerKEGGhsa05230
Choline metabolism in cancerKEGGhsa05231
Central carbon metabolism in cancerKEGGko05230
Choline metabolism in cancerKEGGko05231
PI3K-Akt signalingKEGGhsa_M00676
PI3K-Akt signalingKEGGM00676
Sphingolipid signaling pathwayKEGGhsa04071
Sphingolipid signaling pathwayKEGGko04071
Regulation of lipolysis in adipocytesKEGGhsa04923
Diseases of signal transductionREACTOMER-HSA-5663202
Signaling by EGFR in CancerREACTOMER-HSA-1643713
Signaling by Ligand-Responsive EGFR Variants in CancerREACTOMER-HSA-5637815
Constitutive Signaling by Ligand-Responsive EGFR Cancer VariantsREACTOMER-HSA-1236382
Signaling by EGFRvIII in CancerREACTOMER-HSA-5637812
Constitutive Signaling by EGFRvIIIREACTOMER-HSA-5637810
Signaling by FGFR in diseaseREACTOMER-HSA-1226099
Signaling by FGFR1 in diseaseREACTOMER-HSA-5655302
FGFR1 mutant receptor activationREACTOMER-HSA-1839124
Signaling by cytosolic FGFR1 fusion mutantsREACTOMER-HSA-1839117
Signaling by FGFR2 in diseaseREACTOMER-HSA-5655253
Signaling by FGFR3 in diseaseREACTOMER-HSA-5655332
Signaling by FGFR4 in diseaseREACTOMER-HSA-5655291
PI3K/AKT Signaling in CancerREACTOMER-HSA-2219528
Constitutive Signaling by Aberrant PI3K in CancerREACTOMER-HSA-2219530
Immune SystemREACTOMER-HSA-168256
Adaptive Immune SystemREACTOMER-HSA-1280218
TCR signalingREACTOMER-HSA-202403
Downstream TCR signalingREACTOMER-HSA-202424
Costimulation by the CD28 familyREACTOMER-HSA-388841
CD28 co-stimulationREACTOMER-HSA-389356
CD28 dependent PI3K/Akt signalingREACTOMER-HSA-389357
Signaling by the B Cell Receptor (BCR)REACTOMER-HSA-983705
Downstream signaling events of B Cell Receptor (BCR)REACTOMER-HSA-1168372
PIP3 activates AKT signalingREACTOMER-HSA-1257604
Negative regulation of the PI3K/AKT networkREACTOMER-HSA-199418
Innate Immune SystemREACTOMER-HSA-168249
Fcgamma receptor (FCGR) dependent phagocytosisREACTOMER-HSA-2029480
Role of phospholipids in phagocytosisREACTOMER-HSA-2029485
DAP12 interactionsREACTOMER-HSA-2172127
DAP12 signalingREACTOMER-HSA-2424491
Fc epsilon receptor (FCERI) signalingREACTOMER-HSA-2454202
Role of LAT2/NTAL/LAB on calcium mobilizationREACTOMER-HSA-2730905
Cytokine Signaling in Immune systemREACTOMER-HSA-1280215
Signaling by InterleukinsREACTOMER-HSA-449147
Interleukin-2 signalingREACTOMER-HSA-451927
Interleukin receptor SHC signalingREACTOMER-HSA-912526
Interleukin-3, 5 and GM-CSF signalingREACTOMER-HSA-512988
Regulation of signaling by CBLREACTOMER-HSA-912631
Platelet activation, signaling and aggregationREACTOMER-HSA-76002
GPVI-mediated activation cascadeREACTOMER-HSA-114604
Cell surface interactions at the vascular wallREACTOMER-HSA-202733
Tie2 SignalingREACTOMER-HSA-210993
Signal TransductionREACTOMER-HSA-162582
Signaling by EGFRREACTOMER-HSA-177929
GAB1 signalosomeREACTOMER-HSA-180292
Signaling by FGFRREACTOMER-HSA-190236
Signaling by FGFR1REACTOMER-HSA-5654736
Downstream signaling of activated FGFR1REACTOMER-HSA-5654687
PI-3K cascade:FGFR1REACTOMER-HSA-5654689
Signaling by FGFR2REACTOMER-HSA-5654738
Downstream signaling of activated FGFR2REACTOMER-HSA-5654696
PI-3K cascade:FGFR2REACTOMER-HSA-5654695
Signaling by FGFR3REACTOMER-HSA-5654741
Downstream signaling of activated FGFR3REACTOMER-HSA-5654708
PI-3K cascade:FGFR3REACTOMER-HSA-5654710
Signaling by FGFR4REACTOMER-HSA-5654743
Downstream signaling of activated FGFR4REACTOMER-HSA-5654716
PI-3K cascade:FGFR4REACTOMER-HSA-5654720
Signaling by Insulin receptorREACTOMER-HSA-74752
Insulin receptor signalling cascadeREACTOMER-HSA-74751
IRS-mediated signallingREACTOMER-HSA-112399
PI3K CascadeREACTOMER-HSA-109704
Signalling by NGFREACTOMER-HSA-166520
NGF signalling via TRKA from the plasma membraneREACTOMER-HSA-187037
PI3K/AKT activationREACTOMER-HSA-198203
Signaling by PDGFREACTOMER-HSA-186797
Downstream signal transductionREACTOMER-HSA-186763
Signaling by VEGFREACTOMER-HSA-194138
Signaling by SCF-KITREACTOMER-HSA-1433557
Signaling by ERBB2REACTOMER-HSA-1227986
PI3K events in ERBB2 signalingREACTOMER-HSA-1963642
Signaling by ERBB4REACTOMER-HSA-1236394
PI3K events in ERBB4 signalingREACTOMER-HSA-1250342
Signaling by GPCRREACTOMER-HSA-372790
GPCR downstream signalingREACTOMER-HSA-388396
G alpha (q) signalling eventsREACTOMER-HSA-416476
G alpha (12/13) signalling eventsREACTOMER-HSA-416482
G-protein beta:gamma signallingREACTOMER-HSA-397795
G beta:gamma signalling through PI3KgammaREACTOMER-HSA-392451
Gastrin-CREB signalling pathway via PKC and MAPKREACTOMER-HSA-881907
Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R)REACTOMER-HSA-2404192
IGF1R signaling cascadeREACTOMER-HSA-2428924
IRS-related events triggered by IGF1RREACTOMER-HSA-2428928
Metabolism of lipids and lipoproteinsREACTOMER-HSA-556833
Phospholipid metabolismREACTOMER-HSA-1483257
PI MetabolismREACTOMER-HSA-1483255
Synthesis of PIPs at the plasma membraneREACTOMER-HSA-1660499
Cell-Cell communicationREACTOMER-HSA-1500931
Nephrin interactionsREACTOMER-HSA-373753
Developmental BiologyREACTOMER-HSA-1266738
Axon guidanceREACTOMER-HSA-422475
Insulin resistanceKEGGhsa04931
Phospholipase D signaling pathwayKEGGko04072
Phospholipase D signaling pathwayKEGGhsa04072
AGE-RAGE signaling pathway in diabetic complicationsKEGGko04933
AGE-RAGE signaling pathway in diabetic complicationsKEGGhsa04933
Longevity regulating pathwayKEGGhsa04211
Longevity regulating pathway - multiple speciesKEGGko04213
Longevity regulating pathway - multiple speciesKEGGhsa04213
PI5P, PP2A and IER3 Regulate PI3K/AKT SignalingREACTOMER-HSA-6811558
Signaling by FGFR3 point mutants in cancerREACTOMER-HSA-8853338
Signaling by FGFR3 fusions in cancerREACTOMER-HSA-8853334
EGFR tyrosine kinase inhibitor resistanceKEGGko01521
Platinum drug resistanceKEGGko01524
Endocrine resistanceKEGGko01522
Platinum drug resistanceKEGGhsa01524
EGFR tyrosine kinase inhibitor resistanceKEGGhsa01521
Endocrine resistanceKEGGhsa01522
RET signalingREACTOMER-HSA-8853659
Breast cancerKEGGko05224
Breast cancerKEGGhsa05224
Signaling by METREACTOMER-HSA-6806834
MET activates PI3K/AKT signalingREACTOMER-HSA-8851907
Fluid shear stress and atherosclerosisKEGGko05418
Fluid shear stress and atherosclerosisKEGGhsa05418

Protein levels (Protein atlas)

Not detected


Entity IDNameTypeEvidenceAssociationPKPDPMIDs
PA164722345MIR10AGeneLiterature, MultilinkAnnotationassociated24522205
PA443622Carcinoma, Non-Small-Cell LungDiseaseClinicalAnnotationassociatedPKPD20157331


Pubmed IDYearTitleCitations
150169632004High frequency of mutations of the PIK3CA gene in human cancers.1136
206197392010Effects of KRAS, BRAF, NRAS, and PIK3CA mutations on the efficacy of cetuximab plus chemotherapy in chemotherapy-refractory metastatic colorectal cancer: a retrospective consortium analysis.666
166187172006KRAS mutation status is predictive of response to cetuximab therapy in colorectal cancer.634
190299812008Effective use of PI3K and MEK inhibitors to treat mutant Kras G12D and PIK3CA H1047R murine lung cancers.573
179365632007A functional genetic approach identifies the PI3K pathway as a major determinant of trastuzumab resistance in breast cancer.516
179365632007A functional genetic approach identifies the PI3K pathway as a major determinant of trastuzumab resistance in breast cancer.516
212523152011DAXX/ATRX, MEN1, and mTOR pathway genes are frequently altered in pancreatic neuroendocrine tumors.498
186768302008An integrative genomic and proteomic analysis of PIK3CA, PTEN, and AKT mutations in breast cancer.396
159509052005Mutant PIK3CA promotes cell growth and invasion of human cancer cells.331
158052482005PIK3CA mutations correlate with hormone receptors, node metastasis, and ERBB2, and are mutually exclusive with PTEN loss in human breast carcinoma.302


Julia Phillips ; Enric Domingo

PIK3CA (phosphoinositide-3-kinase, catalytic, alpha polypeptide)

Atlas Genet Cytogenet Oncol Haematol. 2018-06-01

Online version: http://atlasgeneticsoncology.org/gene/415/pik3ca-(phosphoinositide-3-kinase-catalytic-alpha-polypeptide)

Historical Card

2009-04-01 PIK3CA (phosphoinositide-3-kinase, catalytic, alpha polypeptide) by  Montserrat Sanchez-Cespedes 

Programa dEpigenetica i Biologia del Cancer-PEBC, Institut dInvestigacions Biomediques Bellvitge (IDIBELL), Hospital Durant i Reynals, Avinguda Gran Via de lHospitalet, 199-203 08907-LHospitalet de Llobregat-Barcelona, Spain