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Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform (PI3-kinase subunit alpha) (PI3K-alpha) (PI3Kalpha) (PtdIns-3-kinase subunit alpha) (EC 2.7.1.153) (Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit alpha) (PtdIns-3-kinase subunit p110-alpha) (p110alpha) (Phosphoinositide-3-kinase catalytic alpha polypeptide) (Serine/threonine protein kinase PIK3CA) (EC 2.7.11.1)

 PK3CA_HUMAN             Reviewed;        1068 AA.
P42336; Q14CW1; Q99762;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
20-FEB-2007, sequence version 2.
22-NOV-2017, entry version 192.
RecName: Full=Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform;
Short=PI3-kinase subunit alpha;
Short=PI3K-alpha;
Short=PI3Kalpha;
Short=PtdIns-3-kinase subunit alpha;
EC=2.7.1.153 {ECO:0000250|UniProtKB:P32871};
AltName: Full=Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit alpha;
Short=PtdIns-3-kinase subunit p110-alpha;
Short=p110alpha;
AltName: Full=Phosphoinositide-3-kinase catalytic alpha polypeptide;
AltName: Full=Serine/threonine protein kinase PIK3CA;
EC=2.7.11.1 {ECO:0000250|UniProtKB:P32871};
Name=PIK3CA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS VAL-43 AND ARG-332.
PubMed=7713498; DOI=10.1006/geno.1994.1655;
Volinia S., Hiles I., Ormondroyd E., Nizetic D., Antonacci R.,
Rocchi M., Waterfield M.;
"Molecular cloning, cDNA sequence, and chromosomal localization of the
human phosphatidylinositol 3-kinase p110 alpha (PIK3CA) gene.";
Genomics 24:472-477(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9043658; DOI=10.1016/S0968-0896(96)00196-4;
Stirdivant S.M., Ahern J., Conroy R.R., Barnett S.F., Ledder L.M.,
Oliff A., Heimbrook D.C.;
"Cloning and mutagenesis of the p110 alpha subunit of human
phosphoinositide 3'-hydroxykinase.";
Bioorg. Med. Chem. 5:65-74(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INTERACTION WITH APPL1.
PubMed=10490823; DOI=10.1038/sj.onc.1203080;
Mitsuuchi Y., Johnson S.W., Sonoda G., Tanno S., Golemis E.A.,
Testa J.R.;
"Identification of a chromosome 3p14.3-21.1 gene, APPL, encoding an
adaptor molecule that interacts with the oncoprotein-serine/threonine
kinase AKT2.";
Oncogene 18:4891-4898(1999).
[5]
FUNCTION IN INVADOPODIA FORMATION, AND CHARACTERIZATION OF VARIANTS
LYS-545 AND ARG-1047.
PubMed=21708979; DOI=10.1083/jcb.201009126;
Yamaguchi H., Yoshida S., Muroi E., Yoshida N., Kawamura M.,
Kouchi Z., Nakamura Y., Sakai R., Fukami K.;
"Phosphoinositide 3-kinase signaling pathway mediated by p110{alpha}
regulates invadopodia formation.";
J. Cell Biol. 193:1275-1288(2011).
[6]
INTERACTION WITH FAM83B.
PubMed=23676467;
Cipriano R., Miskimen K.L., Bryson B.L., Foy C.R., Bartel C.A.,
Jackson M.W.;
"FAM83B-mediated activation of PI3K/AKT and MAPK signaling cooperates
to promote epithelial cell transformation and resistance to targeted
therapies.";
Oncotarget 4:729-738(2013).
[7]
REVIEW ON CANCER.
PubMed=18418043; DOI=10.4161/cc.7.9.5817;
Huang C.-H., Mandelker D., Gabelli S.B., Amzel L.M.;
"Insights into the oncogenic effects of PIK3CA mutations from the
structure of p110alpha/p85alpha.";
Cell Cycle 7:1151-1156(2008).
[8]
REVIEW ON FUNCTION, AND REVIEW ON CANCER.
PubMed=18794883; DOI=10.1038/onc.2008.244;
Zhao L., Vogt P.K.;
"Class I PI3K in oncogenic cellular transformation.";
Oncogene 27:5486-5496(2008).
[9]
REVIEW ON FUNCTION.
PubMed=19200708; DOI=10.1016/j.ceb.2008.12.007;
Jia S., Roberts T.M., Zhao J.J.;
"Should individual PI3 kinase isoforms be targeted in cancer?";
Curr. Opin. Cell Biol. 21:199-208(2009).
[10]
X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS) IN A COMPLEX WITH PIK3R1, AND
DOMAINS.
PubMed=18079394; DOI=10.1126/science.1150799;
Huang C.-H., Mandelker D., Schmidt-Kittler O., Samuels Y.,
Velculescu V.E., Kinzler K.W., Vogelstein B., Gabelli S.B.,
Amzel L.M.;
"The structure of a human p110alpha/p85alpha complex elucidates the
effects of oncogenic PI3Kalpha mutations.";
Science 318:1744-1748(2007).
[11]
STRUCTURE BY NMR OF 331-481.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the C2 domain from human PI3-kinase p110
subunit alpha.";
Submitted (APR-2008) to the PDB data bank.
[12]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF MUTANT HIS-1047 IN COMPLEX
WITH WORTMANNIN AND PIK3R1, INTERACTION WITH PIK3R1, CHARACTERIZATION
OF VARIANT ARG-1047, AND DOMAINS.
PubMed=19805105; DOI=10.1073/pnas.0908444106;
Mandelker D., Gabelli S.B., Schmidt-Kittler O., Zhu J., Cheong I.,
Huang C.H., Kinzler K.W., Vogelstein B., Amzel L.M.;
"A frequent kinase domain mutation that changes the interaction
between PI3Kalpha and the membrane.";
Proc. Natl. Acad. Sci. U.S.A. 106:16996-17001(2009).
[13]
VARIANTS CANCER LYS-542; LYS-545; PRO-546; ASN-1021; ARG-1047;
LEU-1047 AND TYR-1065.
PubMed=15289301; DOI=10.1158/0008-5472.CAN-04-1170;
Broderick D.K., Di C., Parrett T.J., Samuels Y.R., Cummins J.M.,
McLendon R.E., Fults D.W., Velculescu V.E., Bigner D.D., Yan H.;
"Mutations of PIK3CA in anaplastic oligodendrogliomas, high-grade
astrocytomas, and medulloblastomas.";
Cancer Res. 64:5048-5050(2004).
[14]
INVOLVEMENT IN OC, AND VARIANTS CANCER GLY-545; LYS-545; LYS-546;
GLU-546; ARG-1047 AND LEU-1047.
PubMed=15520168; DOI=10.1158/0008-5472.CAN-04-2933;
Campbell I.G., Russell S.E., Choong D.Y.H., Montgomery K.G.,
Ciavarella M.L., Hooi C.S.F., Cristiano B.E., Pearson R.B.,
Phillips W.A.;
"Mutation of the PIK3CA gene in ovarian and breast cancer.";
Cancer Res. 64:7678-7681(2004).
[15]
VARIANT CANCER ARG-1047.
PubMed=15016963; DOI=10.1126/science.1096502;
Samuels Y., Wang Z., Bardelli A., Silliman N., Ptak J., Szabo S.,
Yan H., Gazdar A., Powell S.M., Riggins G.J., Willson J.K.V.,
Markowitz S., Kinzler K.W., Vogelstein B., Velculescu V.E.;
"High frequency of mutations of the PIK3CA gene in human cancers.";
Science 304:554-554(2004).
[16]
VARIANTS CANCER GLN-88; LYS-542; ALA-545 AND ASN-1025.
PubMed=15924253; DOI=10.1007/s00401-005-1000-1;
Hartmann C., Bartels G., Gehlhaar C., Holtkamp N., von Deimling A.;
"PIK3CA mutations in glioblastoma multiforme.";
Acta Neuropathol. 109:639-642(2005).
[17]
VARIANTS CANCER LYS-542; LYS-545 AND ARG-1047.
PubMed=15784156; DOI=10.1186/1471-2407-5-29;
Li V.S.W., Wong C.W., Chan T.L., Chan A.S.W., Zhao W., Chu K.-M.,
So S., Chen X., Yuen S.T., Leung S.Y.;
"Mutations of PIK3CA in gastric adenocarcinoma.";
BMC Cancer 5:29-29(2005).
[18]
INVOLVEMENT IN CRC, AND CHARACTERIZATION OF VARIANTS CRC HIS-38;
VAL-106; ARG-420; GLN-453; LYS-542; LYS-545; ILE-1043 AND ARG-1047.
PubMed=15930273; DOI=10.1158/0008-5472.CAN-04-4114;
Ikenoue T., Kanai F., Hikiba Y., Obata T., Tanaka Y., Imamura J.,
Ohta M., Jazag A., Guleng B., Tateishi K., Asaoka Y., Matsumura M.,
Kawabe T., Omata M.;
"Functional analysis of PIK3CA gene mutations in human colorectal
cancer.";
Cancer Res. 65:4562-4567(2005).
[19]
VARIANTS CANCER GLN-542; LYS-542; GLY-545; LYS-545; ARG-1007;
HIS-1021; CYS-1021; VAL-1035; ILE-1043; TYR-1047; ARG-1047; ASP-1050;
LYS-1052 AND LEU-1065.
PubMed=16322209; DOI=10.1158/0008-5472.CAN-05-2620;
Oda K., Stokoe D., Taketani Y., McCormick F.;
"High frequency of coexistent mutations of PIK3CA and PTEN genes in
endometrial carcinoma.";
Cancer Res. 65:10669-10673(2005).
[20]
INVOLVEMENT IN CRC, AND VARIANTS CANCER LYS-542; GLY-545; LYS-545;
GLN-1023; ARG-1047 AND LEU-1047.
PubMed=15994075; DOI=10.1016/j.ejca.2005.04.022;
Velho S., Oliveira C., Ferreira A., Ferreira A.C., Suriano G.,
Schwartz S. Jr., Duval A., Carneiro F., Machado J.C., Hamelin R.,
Seruca R.;
"The prevalence of PIK3CA mutations in gastric and colon cancer.";
Eur. J. Cancer 41:1649-1654(2005).
[21]
VARIANTS CANCER LYS-545 AND ARG-1047.
PubMed=15712344; DOI=10.1002/humu.9316;
Wang Y., Helland A., Holm R., Kristensen G.B., Boerresen-Dale A.-L.;
"PIK3CA mutations in advanced ovarian carcinomas.";
Hum. Mutat. 25:322-322(2005).
[22]
VARIANT HCC ALA-545.
PubMed=15608678; DOI=10.1038/sj.onc.1208304;
Lee J.W., Soung Y.H., Kim S.Y., Lee H.W., Park W.S., Nam S.W.,
Kim S.H., Lee J.Y., Yoo N.J., Lee S.H.;
"PIK3CA gene is frequently mutated in breast carcinomas and
hepatocellular carcinomas.";
Oncogene 24:1477-1480(2005).
[23]
VARIANTS CANCER CYS-343; LYS-542; LYS-545 AND ARG-1047, AND VARIANT
MET-391.
PubMed=16533766; DOI=10.1158/1078-0432.CCR-05-2173;
Qiu W., Schoenleben F., Li X., Ho D.J., Close L.G., Manolidis S.,
Bennett B.P., Su G.H.;
"PIK3CA mutations in head and neck squamous cell carcinoma.";
Clin. Cancer Res. 12:1441-1446(2006).
[24]
VARIANT CANCER ARG-1047.
PubMed=16114017; DOI=10.1002/ijc.21444;
Or Y.Y.-Y., Hui A.B.-Y., To K.-F., Lam C.N.-Y., Lo K.-W.;
"PIK3CA mutations in nasopharyngeal carcinoma.";
Int. J. Cancer 118:1065-1067(2006).
[25]
VARIANTS BC LYS-542; VAL-542; LYS-545; ARG-546; ARG-1047 AND LEU-1047.
PubMed=16353168; DOI=10.1002/path.1908;
Buttitta F., Felicioni L., Barassi F., Martella C., Paolizzi D.,
Fresu G., Salvatore S., Cuccurullo F., Mezzetti A., Campani D.,
Marchetti A.;
"PIK3CA mutation and histological type in breast carcinoma: high
frequency of mutations in lobular carcinoma.";
J. Pathol. 208:350-355(2006).
[26]
CHARACTERIZATION OF VARIANTS CANCER LYS-542; LYS-545 AND ARG-1047.
PubMed=16432179; DOI=10.1073/pnas.0510857103;
Bader A.G., Kang S., Vogt P.K.;
"Cancer-specific mutations in PIK3CA are oncogenic in vivo.";
Proc. Natl. Acad. Sci. U.S.A. 103:1475-1479(2006).
[27]
VARIANTS KERSEB LYS-542; LYS-545; GLY-545 AND ARG-1047.
PubMed=17673550; DOI=10.1073/pnas.0705218104;
Hafner C., Lopez-Knowles E., Luis N.M., Toll A., Baselga E.,
Fernandez-Casado A., Hernandez S., Ribe A., Mentzel T., Stoehr R.,
Hofstaedter F., Landthaler M., Vogt T., Pujol R.M., Hartmann A.,
Real F.X.;
"Oncogenic PIK3CA mutations occur in epidermal nevi and seborrheic
keratoses with a characteristic mutation pattern.";
Proc. Natl. Acad. Sci. U.S.A. 104:13450-13454(2007).
[28]
VARIANTS CLOVE ARG-420; LYS-542 AND ARG-1047.
PubMed=22658544; DOI=10.1016/j.ajhg.2012.05.006;
Kurek K.C., Luks V.L., Ayturk U.M., Alomari A.I., Fishman S.J.,
Spencer S.A., Mulliken J.B., Bowen M.E., Yamamoto G.L.,
Kozakewich H.P., Warman M.L.;
"Somatic mosaic activating mutations in PIK3CA cause CLOVES
syndrome.";
Am. J. Hum. Genet. 90:1108-1115(2012).
[29]
VARIANTS MCAP LYS-81; GLN-88; ARG-364; LYS-365; TYR-378; GLU-453 DEL;
LYS-545; LYS-726; ARG-914; CYS-1021; ALA-1025; VAL-1035; ILE-1043;
TYR-1047 AND SER-1049.
PubMed=22729224; DOI=10.1038/ng.2331;
Riviere J.B., Mirzaa G.M., O'Roak B.J., Beddaoui M., Alcantara D.,
Conway R.L., St-Onge J., Schwartzentruber J.A., Gripp K.W.,
Nikkel S.M., Worthylake T., Sullivan C.T., Ward T.R., Butler H.E.,
Kramer N.A., Albrecht B., Armour C.M., Armstrong L., Caluseriu O.,
Cytrynbaum C., Drolet B.A., Innes A.M., Lauzon J.L., Lin A.E.,
Mancini G.M., Meschino W.S., Reggin J.D., Saggar A.K.,
Lerman-Sagie T., Uyanik G., Weksberg R., Zirn B., Beaulieu C.L.,
Majewski J., Bulman D.E., O'Driscoll M., Shendure J., Graham J.M. Jr.,
Boycott K.M., Dobyns W.B.;
"De novo germline and postzygotic mutations in AKT3, PIK3R2 and PIK3CA
cause a spectrum of related megalencephaly syndromes.";
Nat. Genet. 44:934-940(2012).
[30]
VARIANTS CWS5 ASP-118; LYS-135; LYS-218; ILE-356; LYS-382 AND ALA-545.
PubMed=23246288; DOI=10.1016/j.ajhg.2012.10.021;
Orloff M.S., He X., Peterson C., Chen F., Chen J.L., Mester J.L.,
Eng C.;
"Germline PIK3CA and AKT1 mutations in Cowden and Cowden-like
syndromes.";
Am. J. Hum. Genet. 92:76-80(2013).
[31]
VARIANT MCAP ASN-112, CHARACTERIZATION OF VARIANT MCAP ASN-112,
FUNCTION, AND SUBUNIT.
PubMed=26593112; DOI=10.1002/humu.22933;
Donato N.D., Rump A., Mirzaa G.M., Alcantara D., Oliver A.,
Schrock E., Dobyns W.B., O'Driscoll M.;
"Identification and characterisation of a novel constitutional PIK3CA
mutation in a child lacking the typical segmental overgrowth of
'PIK3CA-related overgrowth spectrum' (PROS).";
Hum. Mutat. 37:242-245(2016).
-!- FUNCTION: 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 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. Also has serine-protein
kinase activity: phosphorylates PIK3R1 (p85alpha regulatory
subunit), EIF4EBP1 and HRAS. Plays a role in the positive
regulation of phagocytosis and pinocytosis (By similarity).
{ECO:0000250|UniProtKB:P42337, ECO:0000269|PubMed:21708979,
ECO:0000269|PubMed:26593112}.
-!- CATALYTIC ACTIVITY: ATP + 1-phosphatidyl-1D-myo-inositol 4,5-
bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-
trisphosphate. {ECO:0000250|UniProtKB:P32871}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000250|UniProtKB:P32871}.
-!- SUBUNIT: Heterodimer of a catalytic subunit PIK3CA and a p85
regulatory subunit (PIK3R1, PIK3R2 or PIK3R3) (PubMed:26593112).
Interacts with IRS1 in nuclear extracts (By similarity). 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). Interacts with FAM83B; activates the
PI3K/AKT signaling cascade (PubMed:23676467).
{ECO:0000250|UniProtKB:P42337, ECO:0000269|PubMed:23676467,
ECO:0000269|PubMed:26593112}.
-!- INTERACTION:
P21860:ERBB3; NbExp=3; IntAct=EBI-2116585, EBI-720706;
P35568:IRS1; NbExp=20; IntAct=EBI-2116585, EBI-517592;
P27986:PIK3R1; NbExp=22; IntAct=EBI-2116585, EBI-79464;
Q92569:PIK3R3; NbExp=4; IntAct=EBI-2116585, EBI-79893;
-!- DOMAIN: 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. {ECO:0000269|PubMed:18079394,
ECO:0000269|PubMed:19805105}.
-!- DISEASE: Note=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.
{ECO:0000269|PubMed:15016963, ECO:0000269|PubMed:15289301,
ECO:0000269|PubMed:15520168, ECO:0000269|PubMed:15712344,
ECO:0000269|PubMed:15784156, ECO:0000269|PubMed:15924253,
ECO:0000269|PubMed:15930273, ECO:0000269|PubMed:15994075,
ECO:0000269|PubMed:16114017, ECO:0000269|PubMed:16322209,
ECO:0000269|PubMed:16353168, ECO:0000269|PubMed:16432179,
ECO:0000269|PubMed:16533766, ECO:0000269|PubMed:17673550,
ECO:0000269|PubMed:19805105, ECO:0000269|PubMed:21708979,
ECO:0000269|PubMed:22658544, ECO:0000269|PubMed:22729224}.
-!- DISEASE: 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.
{ECO:0000269|PubMed:15930273, ECO:0000269|PubMed:15994075}.
Note=The gene represented in this entry may be involved in disease
pathogenesis.
-!- DISEASE: 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.
{ECO:0000269|PubMed:16353168}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- DISEASE: 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.
{ECO:0000269|PubMed:15520168}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- DISEASE: 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. {ECO:0000269|PubMed:15608678}. Note=The gene
represented in this entry may be involved in disease pathogenesis.
-!- DISEASE: 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. {ECO:0000269|PubMed:17673550}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: 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.
{ECO:0000269|PubMed:22729224, ECO:0000269|PubMed:26593112}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: 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.
{ECO:0000269|PubMed:22658544}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: 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.
{ECO:0000269|PubMed:23246288}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: The avian sarcoma virus 16 genome encodes an
oncogene derived from PIK3CA. {ECO:0000305|PubMed:18418043}.
-!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
{ECO:0000255|PROSITE-ProRule:PRU00877, ECO:0000255|PROSITE-
ProRule:PRU00879, ECO:0000255|PROSITE-ProRule:PRU00880}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PIK3CAID415ch3q26.html";
-----------------------------------------------------------------------
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EMBL; Z29090; CAA82333.1; -; mRNA.
EMBL; U79143; AAB39753.1; -; mRNA.
EMBL; BC113601; AAI13602.1; -; mRNA.
EMBL; BC113603; AAI13604.1; -; mRNA.
CCDS; CCDS43171.1; -.
PIR; I38110; I38110.
RefSeq; NP_006209.2; NM_006218.3.
RefSeq; XP_006713721.1; XM_006713658.3.
RefSeq; XP_011511196.1; XM_011512894.2.
UniGene; Hs.553498; -.
UniGene; Hs.715194; -.
UniGene; Hs.732394; -.
PDB; 2ENQ; NMR; -; A=331-481.
PDB; 2RD0; X-ray; 3.05 A; A=1-1068.
PDB; 3HHM; X-ray; 2.80 A; A=1-1068.
PDB; 3HIZ; X-ray; 3.30 A; A=1-1068.
PDB; 3ZIM; X-ray; 2.85 A; A=107-1046.
PDB; 4JPS; X-ray; 2.20 A; A=1-1068.
PDB; 4L1B; X-ray; 2.59 A; A=1-1068.
PDB; 4L23; X-ray; 2.50 A; A=1-1068.
PDB; 4L2Y; X-ray; 2.80 A; A=1-1068.
PDB; 4OVU; X-ray; 2.96 A; A=1-1068.
PDB; 4OVV; X-ray; 3.50 A; A=1-1068.
PDB; 4TUU; X-ray; 2.64 A; A=105-1048.
PDB; 4TV3; X-ray; 2.85 A; A=105-1048.
PDB; 4WAF; X-ray; 2.39 A; A=2-1068.
PDB; 4YKN; X-ray; 2.90 A; A=2-1068.
PDB; 4ZOP; X-ray; 2.62 A; A=1-1068.
PDB; 5DXH; X-ray; 3.00 A; A/D=2-1068.
PDB; 5DXT; X-ray; 2.25 A; A=107-1068.
PDB; 5FI4; X-ray; 2.50 A; A=1-1068.
PDB; 5ITD; X-ray; 3.02 A; A=1-1068.
PDB; 5SW8; X-ray; 3.30 A; A=1-1068.
PDB; 5SWG; X-ray; 3.11 A; A=1-1068.
PDB; 5SWO; X-ray; 3.50 A; A=1-1068.
PDB; 5SWP; X-ray; 3.41 A; A=1-1068.
PDB; 5SWR; X-ray; 3.31 A; A=1-1068.
PDB; 5SWT; X-ray; 3.49 A; A=1-1068.
PDB; 5SX8; X-ray; 3.47 A; A=1-1068.
PDB; 5SX9; X-ray; 3.52 A; A=1-1068.
PDB; 5SXA; X-ray; 3.35 A; A=1-1068.
PDB; 5SXB; X-ray; 3.30 A; A=1-1068.
PDB; 5SXC; X-ray; 3.55 A; A=1-1068.
PDB; 5SXD; X-ray; 3.50 A; A=1-1068.
PDB; 5SXE; X-ray; 3.51 A; A=1-1068.
PDB; 5SXF; X-ray; 3.46 A; A=1-1068.
PDB; 5SXI; X-ray; 3.40 A; A=1-1068.
PDB; 5SXJ; X-ray; 3.42 A; A=1-1068.
PDB; 5SXK; X-ray; 3.55 A; A=1-1068.
PDB; 5UBR; X-ray; 2.40 A; A=107-1050.
PDB; 5UK8; X-ray; 2.50 A; A=1-1068.
PDB; 5UKJ; X-ray; 2.80 A; A=1-1068.
PDB; 5UL1; X-ray; 3.00 A; A=1-1068.
PDBsum; 2ENQ; -.
PDBsum; 2RD0; -.
PDBsum; 3HHM; -.
PDBsum; 3HIZ; -.
PDBsum; 3ZIM; -.
PDBsum; 4JPS; -.
PDBsum; 4L1B; -.
PDBsum; 4L23; -.
PDBsum; 4L2Y; -.
PDBsum; 4OVU; -.
PDBsum; 4OVV; -.
PDBsum; 4TUU; -.
PDBsum; 4TV3; -.
PDBsum; 4WAF; -.
PDBsum; 4YKN; -.
PDBsum; 4ZOP; -.
PDBsum; 5DXH; -.
PDBsum; 5DXT; -.
PDBsum; 5FI4; -.
PDBsum; 5ITD; -.
PDBsum; 5SW8; -.
PDBsum; 5SWG; -.
PDBsum; 5SWO; -.
PDBsum; 5SWP; -.
PDBsum; 5SWR; -.
PDBsum; 5SWT; -.
PDBsum; 5SX8; -.
PDBsum; 5SX9; -.
PDBsum; 5SXA; -.
PDBsum; 5SXB; -.
PDBsum; 5SXC; -.
PDBsum; 5SXD; -.
PDBsum; 5SXE; -.
PDBsum; 5SXF; -.
PDBsum; 5SXI; -.
PDBsum; 5SXJ; -.
PDBsum; 5SXK; -.
PDBsum; 5UBR; -.
PDBsum; 5UK8; -.
PDBsum; 5UKJ; -.
PDBsum; 5UL1; -.
ProteinModelPortal; P42336; -.
SMR; P42336; -.
BioGrid; 111308; 85.
CORUM; P42336; -.
DIP; DIP-42728N; -.
IntAct; P42336; 53.
MINT; MINT-1367228; -.
STRING; 9606.ENSP00000263967; -.
BindingDB; P42336; -.
ChEMBL; CHEMBL4005; -.
DrugBank; DB00201; Caffeine.
DrugBank; DB05240; XL147.
DrugBank; DB05241; XL765.
GuidetoPHARMACOLOGY; 2153; -.
iPTMnet; P42336; -.
PhosphoSitePlus; P42336; -.
BioMuta; PI3KCA; -.
DMDM; 126302584; -.
EPD; P42336; -.
MaxQB; P42336; -.
PaxDb; P42336; -.
PeptideAtlas; P42336; -.
PRIDE; P42336; -.
DNASU; 5290; -.
Ensembl; ENST00000263967; ENSP00000263967; ENSG00000121879.
GeneID; 5290; -.
KEGG; hsa:5290; -.
UCSC; uc003fjk.4; human.
CTD; 5290; -.
DisGeNET; 5290; -.
EuPathDB; HostDB:ENSG00000121879.3; -.
GeneCards; PIK3CA; -.
GeneReviews; PIK3CA; -.
HGNC; HGNC:8975; PIK3CA.
HPA; CAB017804; -.
HPA; HPA009985; -.
MalaCards; PIK3CA; -.
MIM; 114480; phenotype.
MIM; 114500; phenotype.
MIM; 114550; phenotype.
MIM; 167000; phenotype.
MIM; 171834; gene.
MIM; 182000; phenotype.
MIM; 602501; phenotype.
MIM; 612918; phenotype.
MIM; 615108; phenotype.
neXtProt; NX_P42336; -.
OpenTargets; ENSG00000121879; -.
Orphanet; 140944; CLOVE syndrome.
Orphanet; 201; Cowden syndrome.
Orphanet; 276280; Hemihyperplasia-multiple lipomatosis syndrome.
Orphanet; 99802; Hemimegalencephaly.
Orphanet; 144; Hereditary nonpolyposis colon cancer.
Orphanet; 295239; Macrodactyly of fingers, unilateral.
Orphanet; 295243; Macrodactyly of toes, unilateral.
Orphanet; 60040; Megalencephaly-capillary malformation-polymicrogyria syndrome.
Orphanet; 314662; Segmental progressive overgrowth syndrome with fibroadipose hyperplasia.
PharmGKB; PA33308; -.
eggNOG; KOG0904; Eukaryota.
eggNOG; COG5032; LUCA.
GeneTree; ENSGT00760000119110; -.
HOVERGEN; HBG052721; -.
InParanoid; P42336; -.
KO; K00922; -.
OMA; PMVRAFA; -.
OrthoDB; EOG091G027R; -.
PhylomeDB; P42336; -.
TreeFam; TF102031; -.
BioCyc; MetaCyc:HS04527-MONOMER; -.
BRENDA; 2.7.1.137; 2681.
BRENDA; 2.7.1.153; 2681.
Reactome; R-HSA-109704; PI3K Cascade.
Reactome; R-HSA-114604; GPVI-mediated activation cascade.
Reactome; R-HSA-1236382; Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants.
Reactome; R-HSA-1250342; PI3K events in ERBB4 signaling.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-1266695; Interleukin-7 signaling.
Reactome; R-HSA-1433557; Signaling by SCF-KIT.
Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
Reactome; R-HSA-180292; GAB1 signalosome.
Reactome; R-HSA-1839117; Signaling by cytosolic FGFR1 fusion mutants.
Reactome; R-HSA-186763; Downstream signal transduction.
Reactome; R-HSA-1963642; PI3K events in ERBB2 signaling.
Reactome; R-HSA-198203; PI3K/AKT activation.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-2029485; Role of phospholipids in phagocytosis.
Reactome; R-HSA-210993; Tie2 Signaling.
Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
Reactome; R-HSA-2424491; DAP12 signaling.
Reactome; R-HSA-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
Reactome; R-HSA-373753; Nephrin family interactions.
Reactome; R-HSA-388841; Costimulation by the CD28 family.
Reactome; R-HSA-389357; CD28 dependent PI3K/Akt signaling.
Reactome; R-HSA-392451; G beta:gamma signalling through PI3Kgamma.
Reactome; R-HSA-416476; G alpha (q) signalling events.
Reactome; R-HSA-416482; G alpha (12/13) signalling events.
Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-HSA-512988; Interleukin-3, 5 and GM-CSF signaling.
Reactome; R-HSA-5637810; Constitutive Signaling by EGFRvIII.
Reactome; R-HSA-5654689; PI-3K cascade:FGFR1.
Reactome; R-HSA-5654695; PI-3K cascade:FGFR2.
Reactome; R-HSA-5654710; PI-3K cascade:FGFR3.
Reactome; R-HSA-5654720; PI-3K cascade:FGFR4.
Reactome; R-HSA-5655253; Signaling by FGFR2 in disease.
Reactome; R-HSA-5655291; Signaling by FGFR4 in disease.
Reactome; R-HSA-5655302; Signaling by FGFR1 in disease.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-HSA-8851907; MET activates PI3K/AKT signaling.
Reactome; R-HSA-8853334; Signaling by FGFR3 fusions in cancer.
Reactome; R-HSA-8853338; Signaling by FGFR3 point mutants in cancer.
Reactome; R-HSA-8853659; RET signaling.
Reactome; R-HSA-912526; Interleukin receptor SHC signaling.
Reactome; R-HSA-912631; Regulation of signaling by CBL.
SignaLink; P42336; -.
SIGNOR; P42336; -.
ChiTaRS; PIK3CA; human.
EvolutionaryTrace; P42336; -.
GeneWiki; P110%CE%B1; -.
GenomeRNAi; 5290; -.
PRO; PR:P42336; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000121879; -.
CleanEx; HS_PIK3CA; -.
ExpressionAtlas; P42336; baseline and differential.
Genevisible; P42336; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; ISS:BHF-UCL.
GO; GO:0005943; C:phosphatidylinositol 3-kinase complex, class IA; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IDA:UniProtKB.
GO; GO:0035005; F:1-phosphatidylinositol-4-phosphate 3-kinase activity; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0043560; F:insulin receptor substrate binding; IEA:Ensembl.
GO; GO:0016301; F:kinase activity; IDA:MGI.
GO; GO:0035004; F:phosphatidylinositol 3-kinase activity; ISS:BHF-UCL.
GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; IBA:GO_Central.
GO; GO:0030295; F:protein kinase activator activity; IEA:Ensembl.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0002250; P:adaptive immune response; IBA:GO_Central.
GO; GO:0060612; P:adipose tissue development; IEA:Ensembl.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0043276; P:anoikis; NAS:ParkinsonsUK-UCL.
GO; GO:0007411; P:axon guidance; TAS:Reactome.
GO; GO:0060048; P:cardiac muscle contraction; TAS:UniProtKB.
GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central.
GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
GO; GO:0043542; P:endothelial cell migration; TAS:UniProtKB.
GO; GO:0097009; P:energy homeostasis; IEA:Ensembl.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0038128; P:ERBB2 signaling pathway; TAS:Reactome.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
GO; GO:0006006; P:glucose metabolic process; IEA:Ensembl.
GO; GO:0044029; P:hypomethylation of CpG island; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0038028; P:insulin receptor signaling pathway via phosphatidylinositol 3-kinase; TAS:UniProtKB.
GO; GO:0038111; P:interleukin-7-mediated signaling pathway; TAS:Reactome.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0001889; P:liver development; IEA:Ensembl.
GO; GO:2000811; P:negative regulation of anoikis; IMP:UniProtKB.
GO; GO:2000270; P:negative regulation of fibroblast apoptotic process; IEA:Ensembl.
GO; GO:0016242; P:negative regulation of macroautophagy; NAS:ParkinsonsUK-UCL.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IBA:GO_Central.
GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
GO; GO:0046854; P:phosphatidylinositol phosphorylation; ISS:BHF-UCL.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome.
GO; GO:0016310; P:phosphorylation; IDA:MGI.
GO; GO:0030168; P:platelet activation; TAS:UniProtKB.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:0032008; P:positive regulation of TOR signaling; NAS:ParkinsonsUK-UCL.
GO; GO:0043491; P:protein kinase B signaling; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
GO; GO:0043457; P:regulation of cellular respiration; IEA:Ensembl.
GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
GO; GO:2000653; P:regulation of genetic imprinting; IEA:Ensembl.
GO; GO:0040014; P:regulation of multicellular organism growth; IEA:Ensembl.
GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; TAS:Reactome.
GO; GO:0031295; P:T cell costimulation; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0001944; P:vasculature development; TAS:UniProtKB.
Gene3D; 1.10.1070.11; -; 1.
Gene3D; 2.60.40.150; -; 1.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000403; PI3/4_kinase_cat_dom.
InterPro; IPR036940; PI3/4_kinase_cat_sf.
InterPro; IPR018936; PI3/4_kinase_CS.
InterPro; IPR003113; PI3K_adapt-bd_dom.
InterPro; IPR002420; PI3K_C2_dom.
InterPro; IPR000341; PI3K_Ras-bd_dom.
InterPro; IPR008290; PI3K_Vps34.
InterPro; IPR015433; PI_Kinase.
InterPro; IPR001263; PInositide-3_kin_accessory_dom.
InterPro; IPR029071; Ubiquitin-like_domsf.
PANTHER; PTHR10048; PTHR10048; 1.
Pfam; PF00454; PI3_PI4_kinase; 1.
Pfam; PF00792; PI3K_C2; 1.
Pfam; PF02192; PI3K_p85B; 1.
Pfam; PF00794; PI3K_rbd; 1.
Pfam; PF00613; PI3Ka; 1.
PIRSF; PIRSF000587; PI3K_Vps34; 1.
SMART; SM00142; PI3K_C2; 1.
SMART; SM00143; PI3K_p85B; 1.
SMART; SM00144; PI3K_rbd; 1.
SMART; SM00145; PI3Ka; 1.
SMART; SM00146; PI3Kc; 1.
SUPFAM; SSF48371; SSF48371; 1.
SUPFAM; SSF49562; SSF49562; 1.
SUPFAM; SSF54236; SSF54236; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00915; PI3_4_KINASE_1; 1.
PROSITE; PS00916; PI3_4_KINASE_2; 1.
PROSITE; PS50290; PI3_4_KINASE_3; 1.
PROSITE; PS51544; PI3K_ABD; 1.
PROSITE; PS51547; PI3K_C2; 1.
PROSITE; PS51546; PI3K_RBD; 1.
PROSITE; PS51545; PIK_HELICAL; 1.
1: Evidence at protein level;
3D-structure; Angiogenesis; ATP-binding; Complete proteome;
Disease mutation; Kinase; Nucleotide-binding; Phagocytosis;
Polymorphism; Proto-oncogene; Reference proteome;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 1068 Phosphatidylinositol 4,5-bisphosphate 3-
kinase catalytic subunit alpha isoform.
/FTId=PRO_0000088785.
DOMAIN 16 105 PI3K-ABD. {ECO:0000255|PROSITE-
ProRule:PRU00877}.
DOMAIN 187 289 PI3K-RBD. {ECO:0000255|PROSITE-
ProRule:PRU00879}.
DOMAIN 330 487 C2 PI3K-type. {ECO:0000255|PROSITE-
ProRule:PRU00880}.
DOMAIN 517 694 PIK helical. {ECO:0000255|PROSITE-
ProRule:PRU00878}.
DOMAIN 797 1068 PI3K/PI4K. {ECO:0000255|PROSITE-
ProRule:PRU00269}.
VARIANT 38 38 R -> 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;
dbSNP:rs772110575).
{ECO:0000269|PubMed:15930273}.
/FTId=VAR_026166.
VARIANT 43 43 I -> V (in dbSNP:rs1051399).
{ECO:0000269|PubMed:7713498}.
/FTId=VAR_042942.
VARIANT 81 81 E -> K (in MCAP).
{ECO:0000269|PubMed:22729224}.
/FTId=VAR_069251.
VARIANT 88 88 R -> Q (in MCAP; also found in a
glioblastoma multiforme sample;
dbSNP:rs121913287).
{ECO:0000269|PubMed:15924253,
ECO:0000269|PubMed:22729224}.
/FTId=VAR_026167.
VARIANT 106 106 G -> V (in CRC; likely involved in
disease pathogenesis; shows an increase
in lipid kinase activity).
{ECO:0000269|PubMed:15930273}.
/FTId=VAR_026168.
VARIANT 112 112 I -> N (in MCAP; increased
phosphatidylinositol 3-kinase signaling;
decreased interaction with p85 regulatory
subunit; no effect on protein abundance;
dbSNP:rs863225460).
{ECO:0000269|PubMed:26593112}.
/FTId=VAR_075634.
VARIANT 118 118 G -> D (in CWS5; dbSNP:rs587777790).
{ECO:0000269|PubMed:23246288}.
/FTId=VAR_069786.
VARIANT 135 135 E -> K (in CWS5; dbSNP:rs587777791).
{ECO:0000269|PubMed:23246288}.
/FTId=VAR_069787.
VARIANT 218 218 E -> K (in CWS5; dbSNP:rs587777792).
{ECO:0000269|PubMed:23246288}.
/FTId=VAR_069788.
VARIANT 332 332 S -> R (in dbSNP:rs1051407).
{ECO:0000269|PubMed:7713498}.
/FTId=VAR_042943.
VARIANT 343 343 Y -> C (found in a cancer sample; unknown
pathological significance).
{ECO:0000269|PubMed:16533766}.
/FTId=VAR_026169.
VARIANT 356 356 V -> I (in CWS5; dbSNP:rs587777793).
{ECO:0000269|PubMed:23246288}.
/FTId=VAR_069789.
VARIANT 364 364 G -> R (in MCAP).
{ECO:0000269|PubMed:22729224}.
/FTId=VAR_069252.
VARIANT 365 365 E -> K (in MCAP).
{ECO:0000269|PubMed:22729224}.
/FTId=VAR_069253.
VARIANT 378 378 C -> Y (in MCAP; dbSNP:rs397514565).
{ECO:0000269|PubMed:22729224}.
/FTId=VAR_069254.
VARIANT 382 382 R -> K (in CWS5; dbSNP:rs587777794).
{ECO:0000269|PubMed:23246288}.
/FTId=VAR_069790.
VARIANT 391 391 I -> M (in dbSNP:rs2230461).
{ECO:0000269|PubMed:16533766}.
/FTId=VAR_026170.
VARIANT 420 420 C -> R (in CLOVE and CRC; shows an
increase in lipid kinase activity; may
increase the affinity for lipid
membranes; dbSNP:rs121913272).
{ECO:0000269|PubMed:15930273,
ECO:0000269|PubMed:22658544}.
/FTId=VAR_026171.
VARIANT 453 453 E -> 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).
{ECO:0000269|PubMed:15930273}.
/FTId=VAR_026172.
VARIANT 453 453 Missing (in MCAP).
{ECO:0000269|PubMed:22729224}.
/FTId=VAR_069255.
VARIANT 542 542 E -> 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; dbSNP:rs121913273).
{ECO:0000269|PubMed:15289301,
ECO:0000269|PubMed:15784156,
ECO:0000269|PubMed:15924253,
ECO:0000269|PubMed:15930273,
ECO:0000269|PubMed:15994075,
ECO:0000269|PubMed:16322209,
ECO:0000269|PubMed:16353168,
ECO:0000269|PubMed:16432179,
ECO:0000269|PubMed:16533766,
ECO:0000269|PubMed:17673550,
ECO:0000269|PubMed:22658544}.
/FTId=VAR_026173.
VARIANT 542 542 E -> Q (found in an endometrial carcinoma
sample; unknown pathological
significance).
{ECO:0000269|PubMed:16322209}.
/FTId=VAR_026174.
VARIANT 542 542 E -> V (in BC; unknown pathological
significance).
{ECO:0000269|PubMed:16353168}.
/FTId=VAR_026175.
VARIANT 545 545 E -> A (in CWS5 and HCC; also found in a
glioblastoma multiforme sample;
dbSNP:rs121913274).
{ECO:0000269|PubMed:15608678,
ECO:0000269|PubMed:15924253,
ECO:0000269|PubMed:23246288}.
/FTId=VAR_026176.
VARIANT 545 545 E -> G (in KERSEB; also found in an
endometrial carcinoma sample;
dbSNP:rs121913274).
{ECO:0000269|PubMed:15520168,
ECO:0000269|PubMed:15994075,
ECO:0000269|PubMed:16322209,
ECO:0000269|PubMed:17673550}.
/FTId=VAR_026177.
VARIANT 545 545 E -> 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; dbSNP:rs104886003).
{ECO:0000269|PubMed:15289301,
ECO:0000269|PubMed:15520168,
ECO:0000269|PubMed:15712344,
ECO:0000269|PubMed:15784156,
ECO:0000269|PubMed:15930273,
ECO:0000269|PubMed:15994075,
ECO:0000269|PubMed:16322209,
ECO:0000269|PubMed:16353168,
ECO:0000269|PubMed:16432179,
ECO:0000269|PubMed:16533766,
ECO:0000269|PubMed:17673550,
ECO:0000269|PubMed:21708979,
ECO:0000269|PubMed:22729224}.
/FTId=VAR_026178.
VARIANT 546 546 Q -> E (in BC; unknown pathological
significance; dbSNP:rs121913286).
{ECO:0000269|PubMed:15520168}.
/FTId=VAR_026179.
VARIANT 546 546 Q -> K (in OC; unknown pathological
significance; dbSNP:rs121913286).
{ECO:0000269|PubMed:15520168}.
/FTId=VAR_026180.
VARIANT 546 546 Q -> P (found in an anaplastic
astrocytoma sample; unknown pathological
significance).
{ECO:0000269|PubMed:15289301}.
/FTId=VAR_026181.
VARIANT 546 546 Q -> R (in BC; unknown pathological
significance; dbSNP:rs397517201).
{ECO:0000269|PubMed:16353168}.
/FTId=VAR_026182.
VARIANT 726 726 E -> K (in MCAP; dbSNP:rs867262025).
{ECO:0000269|PubMed:22729224}.
/FTId=VAR_069256.
VARIANT 914 914 G -> R (in MCAP; dbSNP:rs587776932).
{ECO:0000269|PubMed:22729224}.
/FTId=VAR_069257.
VARIANT 1007 1007 G -> R (found in an endometrial carcinoma
sample; unknown pathological
significance).
{ECO:0000269|PubMed:16322209}.
/FTId=VAR_026183.
VARIANT 1021 1021 Y -> C (in MCAP; also found in an
endometrial carcinoma sample;
dbSNP:rs121913288).
{ECO:0000269|PubMed:16322209,
ECO:0000269|PubMed:22729224}.
/FTId=VAR_026184.
VARIANT 1021 1021 Y -> H (found in an endometrial carcinoma
sample; unknown pathological
significance).
{ECO:0000269|PubMed:16322209}.
/FTId=VAR_026185.
VARIANT 1021 1021 Y -> N (found in a glioblastoma
multiforme sample; unknown pathological
significance).
{ECO:0000269|PubMed:15289301}.
/FTId=VAR_026186.
VARIANT 1023 1023 R -> Q (in CRC; unknown pathological
significance).
{ECO:0000269|PubMed:15994075}.
/FTId=VAR_026187.
VARIANT 1025 1025 T -> A (in MCAP; dbSNP:rs397517202).
{ECO:0000269|PubMed:22729224}.
/FTId=VAR_069258.
VARIANT 1025 1025 T -> N (found in a glioblastoma
multiforme sample; unknown pathological
significance).
{ECO:0000269|PubMed:15924253}.
/FTId=VAR_026188.
VARIANT 1035 1035 A -> V (in MCAP; also found in an
endometrial carcinoma sample).
{ECO:0000269|PubMed:16322209,
ECO:0000269|PubMed:22729224}.
/FTId=VAR_026189.
VARIANT 1043 1043 M -> I (in MCAP and CRC; also found in an
endometrial carcinoma sample; shows an
increase in lipid kinase activity;
dbSNP:rs121913283).
{ECO:0000269|PubMed:15930273,
ECO:0000269|PubMed:16322209,
ECO:0000269|PubMed:22729224}.
/FTId=VAR_026190.
VARIANT 1047 1047 H -> L (in BC; unknown pathological
significance; dbSNP:rs121913279).
{ECO:0000269|PubMed:15289301,
ECO:0000269|PubMed:15520168,
ECO:0000269|PubMed:15994075,
ECO:0000269|PubMed:16353168}.
/FTId=VAR_026191.
VARIANT 1047 1047 H -> 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; dbSNP:rs121913279).
{ECO:0000269|PubMed:15016963,
ECO:0000269|PubMed:15289301,
ECO:0000269|PubMed:15520168,
ECO:0000269|PubMed:15712344,
ECO:0000269|PubMed:15784156,
ECO:0000269|PubMed:15930273,
ECO:0000269|PubMed:15994075,
ECO:0000269|PubMed:16114017,
ECO:0000269|PubMed:16322209,
ECO:0000269|PubMed:16353168,
ECO:0000269|PubMed:16432179,
ECO:0000269|PubMed:16533766,
ECO:0000269|PubMed:17673550,
ECO:0000269|PubMed:19805105,
ECO:0000269|PubMed:21708979,
ECO:0000269|PubMed:22658544}.
/FTId=VAR_026192.
VARIANT 1047 1047 H -> Y (in MCAP; also found in an
endometrial carcinoma sample;
dbSNP:rs121913281).
{ECO:0000269|PubMed:16322209,
ECO:0000269|PubMed:22729224}.
/FTId=VAR_026193.
VARIANT 1049 1049 G -> S (in MCAP; dbSNP:rs121913277).
{ECO:0000269|PubMed:22729224}.
/FTId=VAR_069259.
VARIANT 1050 1050 G -> D (found in an endometrial carcinoma
sample; unknown pathological
significance).
{ECO:0000269|PubMed:16322209}.
/FTId=VAR_026194.
VARIANT 1052 1052 T -> K (found in an endometrial carcinoma
sample; unknown pathological
significance).
{ECO:0000269|PubMed:16322209}.
/FTId=VAR_026195.
VARIANT 1065 1065 H -> L (found in an endometrial carcinoma
sample; unknown pathological
significance).
{ECO:0000269|PubMed:16322209}.
/FTId=VAR_026196.
VARIANT 1065 1065 H -> Y (found in brain tumors; unknown
pathological significance).
{ECO:0000269|PubMed:15289301}.
/FTId=VAR_026197.
CONFLICT 170 170 N -> H (in Ref. 1; CAA82333).
{ECO:0000305}.
CONFLICT 187 187 K -> R (in Ref. 1; CAA82333).
{ECO:0000305}.
CONFLICT 286 287 ML -> KM (in Ref. 1; CAA82333).
{ECO:0000305}.
CONFLICT 346 346 V -> L (in Ref. 1; CAA82333).
{ECO:0000305}.
CONFLICT 723 723 K -> R (in Ref. 1; CAA82333).
{ECO:0000305}.
CONFLICT 751 751 F -> L (in Ref. 1; CAA82333).
{ECO:0000305}.
CONFLICT 767 767 E -> K (in Ref. 1; CAA82333).
{ECO:0000305}.
STRAND 5 10 {ECO:0000244|PDB:4JPS}.
STRAND 13 15 {ECO:0000244|PDB:4JPS}.
STRAND 18 25 {ECO:0000244|PDB:4JPS}.
STRAND 27 29 {ECO:0000244|PDB:5SW8}.
STRAND 31 37 {ECO:0000244|PDB:4JPS}.
HELIX 42 52 {ECO:0000244|PDB:4JPS}.
HELIX 53 55 {ECO:0000244|PDB:4JPS}.
STRAND 56 58 {ECO:0000244|PDB:2RD0}.
HELIX 59 61 {ECO:0000244|PDB:4JPS}.
HELIX 65 67 {ECO:0000244|PDB:4JPS}.
STRAND 69 74 {ECO:0000244|PDB:4JPS}.
STRAND 75 77 {ECO:0000244|PDB:4OVU}.
STRAND 79 82 {ECO:0000244|PDB:4JPS}.
STRAND 86 88 {ECO:0000244|PDB:5SW8}.
HELIX 89 91 {ECO:0000244|PDB:4JPS}.
STRAND 94 102 {ECO:0000244|PDB:4JPS}.
STRAND 105 107 {ECO:0000244|PDB:5SXA}.
HELIX 108 121 {ECO:0000244|PDB:4JPS}.
HELIX 126 130 {ECO:0000244|PDB:4JPS}.
HELIX 134 142 {ECO:0000244|PDB:4JPS}.
HELIX 144 155 {ECO:0000244|PDB:4JPS}.
TURN 156 159 {ECO:0000244|PDB:4JPS}.
HELIX 160 166 {ECO:0000244|PDB:4JPS}.
HELIX 179 182 {ECO:0000244|PDB:4JPS}.
STRAND 185 198 {ECO:0000244|PDB:4JPS}.
TURN 199 202 {ECO:0000244|PDB:4JPS}.
STRAND 203 212 {ECO:0000244|PDB:4JPS}.
HELIX 217 226 {ECO:0000244|PDB:4JPS}.
TURN 228 230 {ECO:0000244|PDB:5FI4}.
STRAND 232 234 {ECO:0000244|PDB:4OVU}.
HELIX 237 242 {ECO:0000244|PDB:4WAF}.
TURN 243 245 {ECO:0000244|PDB:4L1B}.
HELIX 246 248 {ECO:0000244|PDB:4JPS}.
STRAND 249 254 {ECO:0000244|PDB:4JPS}.
TURN 255 258 {ECO:0000244|PDB:3HIZ}.
STRAND 263 265 {ECO:0000244|PDB:5DXH}.
HELIX 267 269 {ECO:0000244|PDB:4JPS}.
HELIX 271 279 {ECO:0000244|PDB:4JPS}.
STRAND 284 289 {ECO:0000244|PDB:4JPS}.
HELIX 290 294 {ECO:0000244|PDB:4JPS}.
HELIX 306 309 {ECO:0000244|PDB:4JPS}.
STRAND 319 321 {ECO:0000244|PDB:5SXA}.
STRAND 323 326 {ECO:0000244|PDB:5DXT}.
HELIX 327 329 {ECO:0000244|PDB:4JPS}.
STRAND 332 342 {ECO:0000244|PDB:4JPS}.
TURN 348 350 {ECO:0000244|PDB:4JPS}.
STRAND 353 362 {ECO:0000244|PDB:4JPS}.
STRAND 365 368 {ECO:0000244|PDB:4JPS}.
STRAND 376 379 {ECO:0000244|PDB:4TUU}.
STRAND 382 392 {ECO:0000244|PDB:4JPS}.
HELIX 393 395 {ECO:0000244|PDB:4JPS}.
STRAND 401 413 {ECO:0000244|PDB:4JPS}.
STRAND 416 430 {ECO:0000244|PDB:4JPS}.
STRAND 434 436 {ECO:0000244|PDB:4JPS}.
STRAND 439 444 {ECO:0000244|PDB:4JPS}.
STRAND 454 456 {ECO:0000244|PDB:3ZIM}.
STRAND 458 460 {ECO:0000244|PDB:2RD0}.
STRAND 468 470 {ECO:0000244|PDB:4JPS}.
STRAND 472 477 {ECO:0000244|PDB:4JPS}.
STRAND 481 485 {ECO:0000244|PDB:5DXT}.
HELIX 489 492 {ECO:0000244|PDB:4JPS}.
HELIX 495 498 {ECO:0000244|PDB:2RD0}.
STRAND 504 506 {ECO:0000244|PDB:5SWP}.
HELIX 508 512 {ECO:0000244|PDB:5DXT}.
HELIX 513 515 {ECO:0000244|PDB:5SXB}.
HELIX 517 520 {ECO:0000244|PDB:4L23}.
HELIX 526 536 {ECO:0000244|PDB:4JPS}.
STRAND 539 541 {ECO:0000244|PDB:4TUU}.
HELIX 545 553 {ECO:0000244|PDB:4JPS}.
TURN 554 557 {ECO:0000244|PDB:4JPS}.
HELIX 558 560 {ECO:0000244|PDB:4JPS}.
HELIX 562 564 {ECO:0000244|PDB:4JPS}.
HELIX 565 571 {ECO:0000244|PDB:4JPS}.
HELIX 577 589 {ECO:0000244|PDB:4JPS}.
HELIX 595 598 {ECO:0000244|PDB:4JPS}.
HELIX 599 602 {ECO:0000244|PDB:4JPS}.
HELIX 609 622 {ECO:0000244|PDB:4JPS}.
HELIX 625 638 {ECO:0000244|PDB:4JPS}.
HELIX 639 641 {ECO:0000244|PDB:4JPS}.
STRAND 643 646 {ECO:0000244|PDB:4JPS}.
HELIX 648 657 {ECO:0000244|PDB:4JPS}.
HELIX 661 672 {ECO:0000244|PDB:4JPS}.
TURN 673 676 {ECO:0000244|PDB:4JPS}.
TURN 678 680 {ECO:0000244|PDB:4JPS}.
HELIX 681 694 {ECO:0000244|PDB:4JPS}.
HELIX 698 720 {ECO:0000244|PDB:4JPS}.
TURN 721 725 {ECO:0000244|PDB:4JPS}.
HELIX 728 739 {ECO:0000244|PDB:4JPS}.
HELIX 742 748 {ECO:0000244|PDB:4JPS}.
STRAND 749 753 {ECO:0000244|PDB:4JPS}.
STRAND 756 761 {ECO:0000244|PDB:4JPS}.
HELIX 766 768 {ECO:0000244|PDB:4JPS}.
STRAND 774 776 {ECO:0000244|PDB:3HHM}.
STRAND 779 784 {ECO:0000244|PDB:4JPS}.
HELIX 790 792 {ECO:0000244|PDB:4JPS}.
STRAND 795 805 {ECO:0000244|PDB:4JPS}.
HELIX 808 825 {ECO:0000244|PDB:4JPS}.
TURN 826 828 {ECO:0000244|PDB:4JPS}.
STRAND 838 842 {ECO:0000244|PDB:4JPS}.
STRAND 845 849 {ECO:0000244|PDB:4JPS}.
STRAND 852 856 {ECO:0000244|PDB:4JPS}.
HELIX 857 861 {ECO:0000244|PDB:4JPS}.
STRAND 862 864 {ECO:0000244|PDB:5SWG}.
TURN 865 867 {ECO:0000244|PDB:3HHM}.
HELIX 871 873 {ECO:0000244|PDB:2RD0}.
HELIX 876 884 {ECO:0000244|PDB:4JPS}.
HELIX 887 889 {ECO:0000244|PDB:4JPS}.
HELIX 890 911 {ECO:0000244|PDB:4JPS}.
STRAND 920 924 {ECO:0000244|PDB:4JPS}.
STRAND 929 931 {ECO:0000244|PDB:4JPS}.
TURN 938 941 {ECO:0000244|PDB:4YKN}.
HELIX 942 945 {ECO:0000244|PDB:4JPS}.
HELIX 958 964 {ECO:0000244|PDB:4JPS}.
TURN 965 967 {ECO:0000244|PDB:4JPS}.
STRAND 969 971 {ECO:0000244|PDB:4JPS}.
STRAND 972 974 {ECO:0000244|PDB:5DXT}.
HELIX 975 993 {ECO:0000244|PDB:4JPS}.
HELIX 995 1003 {ECO:0000244|PDB:4JPS}.
TURN 1004 1007 {ECO:0000244|PDB:4JPS}.
STRAND 1013 1015 {ECO:0000244|PDB:5UK8}.
HELIX 1016 1025 {ECO:0000244|PDB:4JPS}.
TURN 1026 1029 {ECO:0000244|PDB:4JPS}.
HELIX 1032 1047 {ECO:0000244|PDB:4JPS}.
STRAND 1048 1050 {ECO:0000244|PDB:5SW8}.
STRAND 1053 1055 {ECO:0000244|PDB:3HHM}.
STRAND 1056 1058 {ECO:0000244|PDB:4JPS}.
SEQUENCE 1068 AA; 124284 MW; 041487231A9A1207 CRC64;
MPPRPSSGEL WGIHLMPPRI LVECLLPNGM IVTLECLREA TLITIKHELF KEARKYPLHQ
LLQDESSYIF VSVTQEAERE EFFDETRRLC DLRLFQPFLK VIEPVGNREE KILNREIGFA
IGMPVCEFDM VKDPEVQDFR RNILNVCKEA VDLRDLNSPH SRAMYVYPPN VESSPELPKH
IYNKLDKGQI IVVIWVIVSP NNDKQKYTLK INHDCVPEQV IAEAIRKKTR SMLLSSEQLK
LCVLEYQGKY ILKVCGCDEY FLEKYPLSQY KYIRSCIMLG RMPNLMLMAK ESLYSQLPMD
CFTMPSYSRR ISTATPYMNG ETSTKSLWVI NSALRIKILC ATYVNVNIRD IDKIYVRTGI
YHGGEPLCDN VNTQRVPCSN PRWNEWLNYD IYIPDLPRAA RLCLSICSVK GRKGAKEEHC
PLAWGNINLF DYTDTLVSGK MALNLWPVPH GLEDLLNPIG VTGSNPNKET PCLELEFDWF
SSVVKFPDMS VIEEHANWSV SREAGFSYSH AGLSNRLARD NELRENDKEQ LKAISTRDPL
SEITEQEKDF LWSHRHYCVT IPEILPKLLL SVKWNSRDEV AQMYCLVKDW PPIKPEQAME
LLDCNYPDPM VRGFAVRCLE KYLTDDKLSQ YLIQLVQVLK YEQYLDNLLV RFLLKKALTN
QRIGHFFFWH LKSEMHNKTV SQRFGLLLES YCRACGMYLK HLNRQVEAME KLINLTDILK
QEKKDETQKV QMKFLVEQMR RPDFMDALQG FLSPLNPAHQ LGNLRLEECR IMSSAKRPLW
LNWENPDIMS ELLFQNNEII FKNGDDLRQD MLTLQIIRIM ENIWQNQGLD LRMLPYGCLS
IGDCVGLIEV VRNSHTIMQI QCKGGLKGAL QFNSHTLHQW LKDKNKGEIY DAAIDLFTRS
CAGYCVATFI LGIGDRHNSN IMVKDDGQLF HIDFGHFLDH KKKKFGYKRE RVPFVLTQDF
LIVISKGAQE CTKTREFERF QEMCYKAYLA IRQHANLFIN LFSMMLGSGM PELQSFDDIA
YIRKTLALDK TEQEALEYFM KQMNDAHHGG WTTKMDWIFH TIKQHALN


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