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Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha (PI3K-C2-alpha) (PtdIns-3-kinase C2 subunit alpha) (EC 2.7.1.154) (Phosphoinositide 3-kinase-C2-alpha)

 P3C2A_HUMAN             Reviewed;        1686 AA.
O00443; B0LPH2; B4E2G4; Q14CQ9;
30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
10-JUL-2007, sequence version 2.
31-JAN-2018, entry version 167.
RecName: Full=Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha;
Short=PI3K-C2-alpha;
Short=PtdIns-3-kinase C2 subunit alpha;
EC=2.7.1.154;
AltName: Full=Phosphoinositide 3-kinase-C2-alpha;
Name=PIK3C2A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, COFACTOR, ENZYME
REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
PubMed=9337861; DOI=10.1042/bj3260139;
Domin J., Pages F., Volinia S., Rittenhouse S.E., Zvelebil M.J.,
Stein R.C., Waterfield M.D.;
"Cloning of a human phosphoinositide 3-kinase with a C2 domain which
displays reduced sensitivity to the inhibitor wortmannin.";
Biochem. J. 326:139-147(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[7]
FUNCTION, ENZYME REGULATION, AND SUBCELLULAR LOCATION.
PubMed=10766823; DOI=10.1074/jbc.275.16.11943;
Domin J., Gaidarov I., Smith M.E.K., Keen J.H., Waterfield M.D.;
"The class II phosphoinositide 3-kinase PI3K-C2alpha is concentrated
in the trans-Golgi network and present in clathrin-coated vesicles.";
J. Biol. Chem. 275:11943-11950(2000).
[8]
FUNCTION, COFACTOR, AND IDENTIFICATION IN A COMPLEX WITH ERBB2 AND
EGFR.
PubMed=10805725; DOI=10.1128/MCB.20.11.3817-3830.2000;
Arcaro A., Zvelebil M.J., Wallasch C., Ullrich A., Waterfield M.D.,
Domin J.;
"Class II phosphoinositide 3-kinases are downstream targets of
activated polypeptide growth factor receptors.";
Mol. Cell. Biol. 20:3817-3830(2000).
[9]
SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, PHOSPHORYLATION,
AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=11606566; DOI=10.1074/jbc.M104610200;
Didichenko S.A., Thelen M.;
"Phosphatidylinositol 3-kinase c2alpha contains a nuclear localization
sequence and associates with nuclear speckles.";
J. Biol. Chem. 276:48135-48142(2001).
[10]
FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, INTERACTION WITH
CLATHRIN, AND MUTAGENESIS OF 103-LEU--ASP-107.
PubMed=11239472; DOI=10.1016/S1097-2765(01)00191-5;
Gaidarov I., Smith M.E.K., Domin J., Keen J.H.;
"The class II phosphoinositide 3-kinase C2alpha is activated by
clathrin and regulates clathrin-mediated membrane trafficking.";
Mol. Cell 7:443-449(2001).
[11]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=14563213; DOI=10.1186/1472-6890-3-4;
El Sheikh S.S., Domin J., Tomtitchong P., Abel P., Stamp G.,
Lalani E.-N.;
"Topographical expression of class IA and class II phosphoinositide 3-
kinase enzymes in normal human tissues is consistent with a role in
differentiation.";
BMC Clin. Pathol. 3:4-4(2003).
[12]
FUNCTION, PHOSPHORYLATION AT SER-259, MUTAGENESIS OF SER-254; SER-259;
SER-262 AND SER-266, LACK OF PHOSPHORYLATION AT SER-244; SER-249;
SER-251; SER-254; SER-262 AND SER-266, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=12719431; DOI=10.1074/jbc.M301657200;
Didichenko S.A., Fragoso C.M., Thelen M.;
"Mitotic and stress-induced phosphorylation of HsPI3K-C2alpha targets
the protein for degradation.";
J. Biol. Chem. 278:26055-26064(2003).
[13]
FUNCTION IN ASSEMBLY AND CELLULAR DISTRIBUTION OF CLATHRIN,
INTERACTION WITH CLATHRIN, MUTAGENESIS OF ASP-1250, AND REGION.
PubMed=16215232; DOI=10.1074/jbc.M507731200;
Gaidarov I., Zhao Y., Keen J.H.;
"Individual phosphoinositide 3-kinase C2alpha domain activities
independently regulate clathrin function.";
J. Biol. Chem. 280:40766-40772(2005).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108 AND SER-259, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60; SER-108; SER-259 AND
SER-338, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[19]
FUNCTION IN DYNAMIN-INDEPENDENT ENDOCYTOSIS.
PubMed=21081650; DOI=10.1242/jcs.071712;
Krag C., Malmberg E.K., Salcini A.E.;
"PI3KC2alpha, a class II PI3K, is required for dynamin-independent
internalization pathways.";
J. Cell Sci. 123:4240-4250(2010).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108 AND SER-259, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[22]
TISSUE SPECIFICITY.
PubMed=21127054; DOI=10.1074/jbc.M110.200295;
Dominguez V., Raimondi C., Somanath S., Bugliani M., Loder M.K.,
Edling C.E., Divecha N., da Silva-Xavier G., Marselli L.,
Persaud S.J., Turner M.D., Rutter G.A., Marchetti P., Falasca M.,
Maffucci T.;
"Class II phosphoinositide 3-kinase regulates exocytosis of insulin
granules in pancreatic beta cells.";
J. Biol. Chem. 286:4216-4225(2011).
[23]
REVIEW ON FUNCTION.
PubMed=17371240; DOI=10.1042/BST0350229;
Falasca M., Maffucci T.;
"Role of class II phosphoinositide 3-kinase in cell signalling.";
Biochem. Soc. Trans. 35:211-214(2007).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259 AND SER-327, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108; SER-259; SER-327;
SER-630; SER-1281 AND SER-1553, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[27]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1405-1544, PHOSPHOINOSITIDE
BINDING, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-1488; VAL-1490;
LEU-1491; ARG-1493 AND ARG-1503.
PubMed=17038310; DOI=10.1074/jbc.M607079200;
Stahelin R.V., Karathanassis D., Bruzik K.S., Waterfield M.D.,
Bravo J., Williams R.L., Cho W.;
"Structural and membrane binding analysis of the Phox homology domain
of phosphoinositide 3-kinase-C2alpha.";
J. Biol. Chem. 281:39396-39406(2006).
[28]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1421-1532.
Parkinson G.N., Vines D., Driscoll P.C., Djordjevic S.;
"Ligand-binding specificity of PI3kinase C2alpha PX domain.";
Submitted (OCT-2006) to the PDB data bank.
-!- FUNCTION: Generates phosphatidylinositol 3-phosphate (PtdIns3P)
and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) that act
as second messengers. Has a role in several intracellular
trafficking events. Functions in insulin signaling and secretion.
Required for translocation of the glucose transporter SLC2A4/GLUT4
to the plasma membrane and glucose uptake in response to insulin-
mediated RHOQ activation. Regulates insulin secretion through two
different mechanisms: involved in glucose-induced insulin
secretion downstream of insulin receptor in a pathway that
involves AKT1 activation and TBC1D4/AS160 phosphorylation, and
participates in the late step of insulin granule exocytosis
probably in insulin granule fusion. Synthesizes PtdIns3P in
response to insulin signaling. Functions in clathrin-coated
endocytic vesicle formation and distribution. Regulates dynamin-
independent endocytosis, probably by recruiting EEA1 to
internalizing vesicles. In neurosecretory cells synthesizes
PtdIns3P on large dense core vesicles. Participates in calcium
induced contraction of vascular smooth muscle by regulating myosin
light chain (MLC) phosphorylation through a mechanism involving
Rho kinase-dependent phosphorylation of the MLCP-regulatory
subunit MYPT1. May play a role in the EGF signaling cascade. May
be involved in mitosis and UV-induced damage response. Required
for maintenance of normal renal structure and function by
supporting normal podocyte function. {ECO:0000269|PubMed:10766823,
ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:11239472,
ECO:0000269|PubMed:12719431, ECO:0000269|PubMed:16215232,
ECO:0000269|PubMed:21081650, ECO:0000269|PubMed:9337861}.
-!- CATALYTIC ACTIVITY: ATP + 1-phosphatidyl-1D-myo-inositol 4-
phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:10805725,
ECO:0000269|PubMed:9337861};
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:10805725,
ECO:0000269|PubMed:9337861};
Note=Ca(2+) or Mg(2+). Mn(2+) cannot be used.
{ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:9337861};
-!- ENZYME REGULATION: Activated by insulin (By similarity). Only
slightly inhibited by wortmannin and LY294002. Activated by
clathrin. {ECO:0000250, ECO:0000269|PubMed:10766823,
ECO:0000269|PubMed:11239472, ECO:0000269|PubMed:9337861}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=122 uM for PtdIns (in the absence of phosphatidylserine)
{ECO:0000269|PubMed:9337861};
KM=64 uM for PtdIns (in the presence of phosphatidylserine)
{ECO:0000269|PubMed:9337861};
KM=25 uM for PtdIns4P (in the presence of phosphatidylserine)
{ECO:0000269|PubMed:9337861};
KM=15 uM for ATP (with PtdIns as substrate) (in the absence of
phosphatidylserine) {ECO:0000269|PubMed:9337861};
KM=32 uM for ATP (with PtdIns as substrate) (in the presence of
phosphatidylserine) {ECO:0000269|PubMed:9337861};
KM=54 uM for ATP (with PtdIns4P as substrate) (in the presence
of phosphatidylserine) {ECO:0000269|PubMed:9337861};
Vmax=990 pmol/min/mg enzyme with PtdIns as substrate (in the
absence of phosphatidylserine) {ECO:0000269|PubMed:9337861};
Vmax=200 pmol/min/mg enzyme with PtdIns as substrate (in the
presence of phosphatidylserine) {ECO:0000269|PubMed:9337861};
Vmax=240 pmol/min/mg enzyme with PtdIns4P as substrate (in the
presence of phosphatidylserine) {ECO:0000269|PubMed:9337861};
Vmax=6800 pmol/min/mg enzyme toward ATP with PtdIns as substrate
(in the absence of phosphatidylserine)
{ECO:0000269|PubMed:9337861};
Vmax=805 pmol/min/mg enzyme toward ATP with PtdIns as substrate
(in the presence of phosphatidylserine)
{ECO:0000269|PubMed:9337861};
Vmax=880 pmol/min/mg enzyme toward ATP with PtdIns4P as
substrate (in the presence of phosphatidylserine)
{ECO:0000269|PubMed:9337861};
Note=In the absence of the carrier phosphatidylserine, enzymatic
kinetics toward PtdIns4P are non-linear.;
-!- SUBUNIT: Part of a complex with ERBB2 and EGFR. Interacts with
clathrin trimers. {ECO:0000269|PubMed:10805725,
ECO:0000269|PubMed:11239472, ECO:0000269|PubMed:16215232}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10766823,
ECO:0000269|PubMed:11239472, ECO:0000269|PubMed:17038310}. Golgi
apparatus {ECO:0000269|PubMed:10766823,
ECO:0000269|PubMed:11239472}. Cytoplasmic vesicle, clathrin-coated
vesicle {ECO:0000269|PubMed:10766823,
ECO:0000269|PubMed:11239472}. Nucleus
{ECO:0000269|PubMed:11606566}. Cytoplasm
{ECO:0000269|PubMed:11606566, ECO:0000269|PubMed:14563213}.
Note=Inserts preferentially into membranes containing
PtdIns(4,5)P2 (PubMed:17038310). Associated with RNA-containing
structures (PubMed:11606566). {ECO:0000269|PubMed:11606566,
ECO:0000269|PubMed:17038310}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O00443-1; Sequence=Displayed;
Name=2;
IsoId=O00443-2; Sequence=VSP_056158;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in columnar and transitional
epithelia, mononuclear cells, smooth muscle cells, and endothelial
cells lining capillaries and small venules (at protein level).
Ubiquitously expressed, with highest levels in heart, placenta and
ovary, and lowest levels in the kidney. Detected at low levels in
islets of Langerhans from type 2 diabetes mellitus individuals.
{ECO:0000269|PubMed:14563213, ECO:0000269|PubMed:21127054,
ECO:0000269|PubMed:9337861}.
-!- PTM: Phosphorylated upon insulin stimulation; which may lead to
enzyme activation (By similarity). Phosphorylated on Ser-259
during mitosis and upon UV irradiation; which does not change
enzymatic activity but leads to proteasomal degradation. Ser-259
phosphorylation may be mediated by CDK1 or JNK, depending on the
physiological state of the cell. {ECO:0000250,
ECO:0000269|PubMed:11606566, ECO:0000269|PubMed:12719431}.
-!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
{ECO:0000255|PROSITE-ProRule:PRU00879, ECO:0000255|PROSITE-
ProRule:PRU00880}.
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EMBL; Y13367; CAA73797.1; -; mRNA.
EMBL; AK304262; BAG65126.1; -; mRNA.
EMBL; EU332862; ABY87551.1; -; Genomic_DNA.
EMBL; AC107956; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC116533; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC126389; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471064; EAW68447.1; -; Genomic_DNA.
EMBL; BC113658; AAI13659.1; -; mRNA.
CCDS; CCDS7824.1; -. [O00443-1]
PIR; PC4345; PC4345.
RefSeq; NP_001308307.1; NM_001321378.1. [O00443-1]
RefSeq; NP_002636.2; NM_002645.3. [O00443-1]
RefSeq; XP_016873413.1; XM_017017924.1. [O00443-1]
UniGene; Hs.175343; -.
UniGene; Hs.736397; -.
PDB; 2AR5; X-ray; 1.80 A; A=1421-1532.
PDB; 2IWL; X-ray; 2.60 A; X=1405-1544.
PDB; 2REA; X-ray; 2.50 A; A=1421-1532.
PDB; 2RED; X-ray; 2.10 A; A=1421-1532.
PDBsum; 2AR5; -.
PDBsum; 2IWL; -.
PDBsum; 2REA; -.
PDBsum; 2RED; -.
ProteinModelPortal; O00443; -.
SMR; O00443; -.
BioGrid; 111304; 70.
CORUM; O00443; -.
DIP; DIP-33727N; -.
ELM; O00443; -.
IntAct; O00443; 46.
MINT; MINT-2794824; -.
STRING; 9606.ENSP00000265970; -.
BindingDB; O00443; -.
ChEMBL; CHEMBL1075102; -.
GuidetoPHARMACOLOGY; 2150; -.
SwissLipids; SLP:000000892; -.
iPTMnet; O00443; -.
PhosphoSitePlus; O00443; -.
BioMuta; PIK3C2A; -.
EPD; O00443; -.
MaxQB; O00443; -.
PaxDb; O00443; -.
PeptideAtlas; O00443; -.
PRIDE; O00443; -.
DNASU; 5286; -.
Ensembl; ENST00000265970; ENSP00000265970; ENSG00000011405. [O00443-1]
GeneID; 5286; -.
KEGG; hsa:5286; -.
UCSC; uc001mmq.6; human. [O00443-1]
CTD; 5286; -.
DisGeNET; 5286; -.
EuPathDB; HostDB:ENSG00000011405.13; -.
GeneCards; PIK3C2A; -.
HGNC; HGNC:8971; PIK3C2A.
HPA; HPA037641; -.
HPA; HPA037642; -.
MIM; 603601; gene.
neXtProt; NX_O00443; -.
OpenTargets; ENSG00000011405; -.
PharmGKB; PA33304; -.
eggNOG; KOG0905; Eukaryota.
eggNOG; COG5032; LUCA.
GeneTree; ENSGT00760000119110; -.
HOGENOM; HOG000006920; -.
HOVERGEN; HBG082099; -.
InParanoid; O00443; -.
KO; K00923; -.
OMA; TIQRGQW; -.
OrthoDB; EOG091G00FC; -.
PhylomeDB; O00443; -.
TreeFam; TF102031; -.
BioCyc; MetaCyc:HS00315-MONOMER; -.
BRENDA; 2.7.1.154; 2681.
Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
Reactome; R-HSA-1660514; Synthesis of PIPs at the Golgi membrane.
Reactome; R-HSA-1660516; Synthesis of PIPs at the early endosome membrane.
Reactome; R-HSA-1660517; Synthesis of PIPs at the late endosome membrane.
Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
SABIO-RK; O00443; -.
SIGNOR; O00443; -.
ChiTaRS; PIK3C2A; human.
EvolutionaryTrace; O00443; -.
GeneWiki; PIK3C2A; -.
GenomeRNAi; 5286; -.
PRO; PR:O00443; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000011405; -.
CleanEx; HS_PIK3C2A; -.
ExpressionAtlas; O00443; baseline and differential.
Genevisible; O00443; HS.
GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0031982; C:vesicle; IDA:UniProtKB.
GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; TAS:ProtInc.
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:0035004; F:phosphatidylinositol 3-kinase activity; TAS:UniProtKB.
GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
GO; GO:0016477; P:cell migration; IBA:GO_Central.
GO; GO:0048268; P:clathrin coat assembly; TAS:UniProtKB.
GO; GO:0006897; P:endocytosis; IMP:UniProtKB.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:UniProtKB.
GO; GO:0006887; P:exocytosis; TAS:UniProtKB.
GO; GO:0008286; P:insulin receptor signaling pathway; TAS:UniProtKB.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IBA:GO_Central.
GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; TAS:UniProtKB.
GO; GO:0014829; P:vascular smooth muscle contraction; TAS:UniProtKB.
Gene3D; 1.10.1070.11; -; 1.
Gene3D; 2.60.40.150; -; 2.
Gene3D; 3.30.1520.10; -; 1.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR000008; C2_dom.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR001683; Phox.
InterPro; IPR000403; PI3/4_kinase_cat_dom.
InterPro; IPR036940; PI3/4_kinase_cat_sf.
InterPro; IPR018936; PI3/4_kinase_CS.
InterPro; IPR002420; PI3K_C2_dom.
InterPro; IPR000341; PI3K_Ras-bd_dom.
InterPro; IPR015433; PI_Kinase.
InterPro; IPR001263; PInositide-3_kin_accessory_dom.
InterPro; IPR036871; PX_dom_sf.
InterPro; IPR029071; Ubiquitin-like_domsf.
PANTHER; PTHR10048; PTHR10048; 1.
Pfam; PF00168; C2; 1.
Pfam; PF00454; PI3_PI4_kinase; 1.
Pfam; PF00792; PI3K_C2; 1.
Pfam; PF00794; PI3K_rbd; 1.
Pfam; PF00613; PI3Ka; 1.
Pfam; PF00787; PX; 1.
SMART; SM00239; C2; 2.
SMART; SM00142; PI3K_C2; 1.
SMART; SM00144; PI3K_rbd; 1.
SMART; SM00145; PI3Ka; 1.
SMART; SM00146; PI3Kc; 1.
SMART; SM00312; PX; 1.
SUPFAM; SSF48371; SSF48371; 1.
SUPFAM; SSF49562; SSF49562; 2.
SUPFAM; SSF54236; SSF54236; 1.
SUPFAM; SSF56112; SSF56112; 1.
SUPFAM; SSF64268; SSF64268; 1.
PROSITE; PS50004; C2; 1.
PROSITE; PS00915; PI3_4_KINASE_1; 1.
PROSITE; PS00916; PI3_4_KINASE_2; 1.
PROSITE; PS50290; PI3_4_KINASE_3; 1.
PROSITE; PS51547; PI3K_C2; 1.
PROSITE; PS51546; PI3K_RBD; 1.
PROSITE; PS51545; PIK_HELICAL; 1.
PROSITE; PS50195; PX; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; ATP-binding;
Cell membrane; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
Endocytosis; Exocytosis; Golgi apparatus; Kinase; Membrane;
Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Transferase.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}.
CHAIN 2 1686 Phosphatidylinositol 4-phosphate 3-kinase
C2 domain-containing subunit alpha.
/FTId=PRO_0000088795.
DOMAIN 421 509 PI3K-RBD. {ECO:0000255|PROSITE-
ProRule:PRU00879}.
DOMAIN 682 841 C2 PI3K-type. {ECO:0000255|PROSITE-
ProRule:PRU00041, ECO:0000255|PROSITE-
ProRule:PRU00880}.
DOMAIN 861 1037 PIK helical. {ECO:0000255|PROSITE-
ProRule:PRU00878}.
DOMAIN 1133 1397 PI3K/PI4K. {ECO:0000255|PROSITE-
ProRule:PRU00269}.
DOMAIN 1422 1538 PX. {ECO:0000255|PROSITE-
ProRule:PRU00147}.
DOMAIN 1559 1662 C2. {ECO:0000255|PROSITE-
ProRule:PRU00041}.
REGION 2 142 Interaction with clathrin; sufficient to
induce clathrin assembly.
REGION 1488 1493 Interaction with PtdIns(4,5)P2-containing
membranes.
MOTIF 1608 1619 Nuclear localization signal.
{ECO:0000269|PubMed:11606566}.
SITE 244 244 Not phosphorylated.
{ECO:0000269|PubMed:12719431}.
SITE 249 249 Not phosphorylated.
{ECO:0000269|PubMed:12719431}.
SITE 251 251 Not phosphorylated.
{ECO:0000269|PubMed:12719431}.
SITE 254 254 Not phosphorylated.
{ECO:0000269|PubMed:12719431}.
SITE 262 262 Not phosphorylated.
{ECO:0000269|PubMed:12719431}.
SITE 266 266 Not phosphorylated.
{ECO:0000269|PubMed:12719431}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 60 60 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 108 108 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 259 259 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:12719431}.
MOD_RES 327 327 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 338 338 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 630 630 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1281 1281 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1553 1553 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 484 1686 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056158.
VARIANT 1415 1415 T -> A (in dbSNP:rs11604561).
/FTId=VAR_023333.
MUTAGEN 103 107 LLLDD->AAAAA: Reduces clathrin binding.
{ECO:0000269|PubMed:11239472}.
MUTAGEN 254 254 S->A: No effect on phosphorylation in
vitro. {ECO:0000269|PubMed:12719431}.
MUTAGEN 259 259 S->A,D,E: Abolishes phosphorylation, no
change in activity.
{ECO:0000269|PubMed:12719431}.
MUTAGEN 259 259 S->A: Protects from proteolysis.
{ECO:0000269|PubMed:12719431}.
MUTAGEN 262 262 S->A: No effect on phosphorylation in
vitro. {ECO:0000269|PubMed:12719431}.
MUTAGEN 266 266 S->A: No effect on phosphorylation in
vitro. {ECO:0000269|PubMed:12719431}.
MUTAGEN 1250 1250 D->A: Abolishes lipid kinase activity.
Affects clathrin distribution when
combined with a truncation encompassing
the region of clathrin interaction.
{ECO:0000269|PubMed:16215232}.
MUTAGEN 1488 1488 R->A: Reduces affinity for PtdIns(4,5)P2-
containing membranes 7-fold.
{ECO:0000269|PubMed:17038310}.
MUTAGEN 1490 1490 V->A: Reduces affinity for PtdIns(4,5)P2-
containing membranes 7-fold.
{ECO:0000269|PubMed:17038310}.
MUTAGEN 1491 1491 L->A: Reduces affinity for PtdIns(4,5)P2-
containing membranes 5-fold.
{ECO:0000269|PubMed:17038310}.
MUTAGEN 1493 1493 R->A: Reduces affinity for PtdIns(4,5)P2-
containing membranes 23-fold.
{ECO:0000269|PubMed:17038310}.
MUTAGEN 1503 1503 R->A: Abolishes interaction with
PtdIns(4,5)P2-containing membranes.
{ECO:0000269|PubMed:17038310}.
CONFLICT 5 5 S -> F (in Ref. 1; CAA73797).
{ECO:0000305}.
CONFLICT 15 15 S -> F (in Ref. 1; CAA73797).
{ECO:0000305}.
CONFLICT 483 483 N -> K (in Ref. 2; BAG65126).
{ECO:0000305}.
CONFLICT 796 796 F -> C (in Ref. 1; CAA73797).
{ECO:0000305}.
CONFLICT 799 799 K -> R (in Ref. 1; CAA73797).
{ECO:0000305}.
CONFLICT 922 922 V -> G (in Ref. 1; CAA73797).
{ECO:0000305}.
CONFLICT 1129 1129 M -> L (in Ref. 1; CAA73797).
{ECO:0000305}.
CONFLICT 1450 1450 R -> W (in Ref. 1; CAA73797).
{ECO:0000305}.
CONFLICT 1464 1464 D -> V (in Ref. 1; CAA73797).
{ECO:0000305}.
HELIX 1418 1421 {ECO:0000244|PDB:2IWL}.
STRAND 1422 1433 {ECO:0000244|PDB:2AR5}.
STRAND 1437 1440 {ECO:0000244|PDB:2AR5}.
STRAND 1443 1450 {ECO:0000244|PDB:2AR5}.
STRAND 1457 1462 {ECO:0000244|PDB:2AR5}.
HELIX 1463 1476 {ECO:0000244|PDB:2AR5}.
HELIX 1479 1481 {ECO:0000244|PDB:2AR5}.
STRAND 1491 1495 {ECO:0000244|PDB:2AR5}.
HELIX 1498 1515 {ECO:0000244|PDB:2AR5}.
HELIX 1519 1522 {ECO:0000244|PDB:2AR5}.
HELIX 1525 1530 {ECO:0000244|PDB:2AR5}.
TURN 1535 1537 {ECO:0000244|PDB:2IWL}.
SEQUENCE 1686 AA; 190680 MW; 904AA5470F80DAC6 CRC64;
MAQISSNSGF KECPSSHPEP TRAKDVDKEE ALQMEAEALA KLQKDRQVTD NQRGFELSSS
TRKKAQVYNK QDYDLMVFPE SDSQKRALDI DVEKLTQAEL EKLLLDDSFE TKKTPVLPVT
PILSPSFSAQ LYFRPTIQRG QWPPGLPGPS TYALPSIYPS TYSKQAAFQN GFNPRMPTFP
STEPIYLSLP GQSPYFSYPL TPATPFHPQG SLPIYRPVVS TDMAKLFDKI ASTSEFLKNG
KARTDLEITD SKVSNLQVSP KSEDISKFDW LDLDPLSKPK VDNVEVLDHE EEKNVSSLLA
KDPWDAVLLE ERSTANCHLE RKVNGKSLSV ATVTRSQSLN IRTTQLAKAQ GHISQKDPNG
TSSLPTGSSL LQEVEVQNEE MAAFCRSITK LKTKFPYTNH RTNPGYLLSP VTAQRNICGE
NASVKVSIDI EGFQLPVTFT CDVSSTVEII IMQALCWVHD DLNQVDVGSY VLKVCGQEEV
LQNNHCLGSH EHIQNCRKWD TEIRLQLLTF SAMCQNLART AEDDETPVDL NKHLYQIEKP
CKEAMTRHPV EELLDSYHNQ VELALQIENQ HRAVDQVIKA VRKICSALDG VETLAITESV
KKLKRAVNLP RSKTADVTSL FGGEDTSRSS TRGSLNPENP VQVSINQLTA AIYDLLRLHA
NSGRSPTDCA QSSKSVKEAW TTTEQLQFTI FAAHGISSNW VSNYEKYYLI CSLSHNGKDL
FKPIQSKKVG TYKNFFYLIK WDELIIFPIQ ISQLPLESVL HLTLFGILNQ SSGSSPDSNK
QRKGPEALGK VSLPLFDFKR FLTCGTKLLY LWTSSHTNSV PGTVTKKGYV MERIVLQVDF
PSPAFDIIYT TPQVDRSIIQ QHNLETLEND IKGKLLDILH KDSSLGLSKE DKAFLWEKRY
YCFKHPNCLP KILASAPNWK WVNLAKTYSL LHQWPALYPL IALELLDSKF ADQEVRSLAV
TWIEAISDDE LTDLLPQFVQ ALKYEIYLNS SLVQFLLSRA LGNIQIAHNL YWLLKDALHD
VQFSTRYEHV LGALLSVGGK RLREELLKQT KLVQLLGGVA EKVRQASGSA RQVVLQRSME
RVQSFFQKNK CRLPLKPSLV AKELNIKSCS FFSSNAVPLK VTMVNADPMG EEINVMFKVG
EDLRQDMLAL QMIKIMDKIW LKEGLDLRMV IFKCLSTGRD RGMVELVPAS DTLRKIQVEY
GVTGSFKDKP LAEWLRKYNP SEEEYEKASE NFIYSCAGCC VATYVLGICD RHNDNIMLRS
TGHMFHIDFG KFLGHAQMFG SFKRDRAPFV LTSDMAYVIN GGEKPTIRFQ LFVDLCCQAY
NLIRKQTNLF LNLLSLMIPS GLPELTSIQD LKYVRDALQP QTTDAEATIF FTRLIESSLG
SIATKFNFFI HNLAQLRFSG LPSNDEPILS FSPKTYSFRQ DGRIKEVSVF TYHKKYNPDK
HYIYVVRILR EGQIEPSFVF RTFDEFQELH NKLSIIFPLW KLPGFPNRMV LGRTHIKDVA
AKRKIELNSY LQSLMNASTD VAECDLVCTF FHPLLRDEKA EGIARSADAG SFSPTPGQIG
GAVKLSISYR NGTLFIMVMH IKDLVTEDGA DPNPYVKTYL LPDNHKTSKR KTKISRKTRN
PTFNEMLVYS GYSKETLRQR ELQLSVLSAE SLRENFFLGG VTLPLKDFNL SKETVKWYQL
TAATYL


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