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Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform (PI3-kinase subunit gamma) (PI3K-gamma) (PI3Kgamma) (PtdIns-3-kinase subunit gamma) (EC 2.7.1.153) (Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit gamma) (PtdIns-3-kinase subunit p110-gamma) (p110gamma) (Phosphoinositide-3-kinase catalytic gamma polypeptide) (Serine/threonine protein kinase PIK3CG) (EC 2.7.11.1) (p120-PI3K)

 PK3CG_HUMAN             Reviewed;        1102 AA.
P48736; A4D0Q6; Q8IV23; Q9BZC8;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
04-APR-2006, sequence version 3.
22-NOV-2017, entry version 184.
RecName: Full=Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform;
Short=PI3-kinase subunit gamma;
Short=PI3K-gamma;
Short=PI3Kgamma;
Short=PtdIns-3-kinase subunit gamma;
EC=2.7.1.153;
AltName: Full=Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit gamma;
Short=PtdIns-3-kinase subunit p110-gamma;
Short=p110gamma;
AltName: Full=Phosphoinositide-3-kinase catalytic gamma polypeptide;
AltName: Full=Serine/threonine protein kinase PIK3CG;
EC=2.7.11.1;
AltName: Full=p120-PI3K;
Name=PIK3CG;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, AND TISSUE
SPECIFICITY.
PubMed=7624799; DOI=10.1126/science.7624799;
Stoyanov B., Volinia S., Hanck T., Rubio I., Loubtchenkov M.,
Malek D., Stoyanova S., Vanhaesebroeck B., Dhand R., Nuernberg B.,
Gierschik P., Seedorf K., Hsuan J.J., Waterfield M.D., Wetzker R.;
"Cloning and characterization of a G protein-activated human
phosphoinositide-3 kinase.";
Science 269:690-693(1995).
[2]
SEQUENCE REVISION.
Waterfield M.D.;
Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Michalke M., Schaefer M., Stoyanov B., Wetzker R., Nuernberg B.;
"Regulation of a G-protein-activated phosphoinositide-3-kinase.";
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreas;
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).
[8]
INTERACTION WITH EPHA8.
PubMed=11416136; DOI=10.1128/MCB.21.14.4579-4597.2001;
Gu C., Park S.;
"The EphA8 receptor regulates integrin activity through p110gamma
phosphatidylinositol-3 kinase in a tyrosine kinase activity-
independent manner.";
Mol. Cell. Biol. 21:4579-4597(2001).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH GRK2.
PubMed=12163475; DOI=10.1083/jcb.200202113;
Naga Prasad S.V., Laporte S.A., Chamberlain D., Caron M.G., Barak L.,
Rockman H.A.;
"Phosphoinositide 3-kinase regulates beta2-adrenergic receptor
endocytosis by AP-2 recruitment to the receptor/beta-arrestin
complex.";
J. Cell Biol. 158:563-575(2002).
[10]
PHOSPHORYLATION AT SER-1101.
PubMed=12502714; DOI=10.1074/jbc.M210351200;
Czupalla C., Culo M., Muller E.C., Brock C., Reusch H.P., Spicher K.,
Krause E., Nurnberg B.;
"Identification and characterization of the autophosphorylation sites
of phosphoinositide 3-kinase isoforms beta and gamma.";
J. Biol. Chem. 278:11536-11545(2003).
[11]
FUNCTION IN CARDIAC CONTRACTILITY, AND MUTAGENESIS OF LYS-833.
PubMed=15294162; DOI=10.1016/j.cell.2004.07.017;
Patrucco E., Notte A., Barberis L., Selvetella G., Maffei A.,
Brancaccio M., Marengo S., Russo G., Azzolino O., Rybalkin S.D.,
Silengo L., Altruda F., Wetzker R., Wymann M.P., Lembo G., Hirsch E.;
"PI3Kgamma modulates the cardiac response to chronic pressure overload
by distinct kinase-dependent and -independent effects.";
Cell 118:375-387(2004).
[12]
INTERACTION WITH PIK3R5.
PubMed=15797027; DOI=10.1016/j.cub.2005.02.020;
Suire S., Coadwell J., Ferguson G.J., Davidson K., Hawkins P.,
Stephens L.;
"p84, a new Gbetagamma-activated regulatory subunit of the type IB
phosphoinositide 3-kinase p110gamma.";
Curr. Biol. 15:566-570(2005).
[13]
FUNCTION AS A PROTEIN KINASE, INTERACTION WITH GRK2 AND TPM2, AND
MUTAGENESIS OF ARG-947.
PubMed=16094730; DOI=10.1038/ncb1278;
Naga Prasad S.V., Jayatilleke A., Madamanchi A., Rockman H.A.;
"Protein kinase activity of phosphoinositide 3-kinase regulates beta-
adrenergic receptor endocytosis.";
Nat. Cell Biol. 7:785-796(2005).
[14]
REVIEW ON FUNCTION.
PubMed=17290298; DOI=10.1038/nri2036;
Rommel C., Camps M., Ji H.;
"PI3K delta and PI3K gamma: partners in crime in inflammation in
rheumatoid arthritis and beyond?";
Nat. Rev. Immunol. 7:191-201(2007).
[15]
REVIEW ON FUNCTION IN LEUKOCYTES AND ENDOTHELIAL CELLS, AND REVIEW ON
ANTINFLAMMATORY THERAPY TARGET.
PubMed=18278175; DOI=10.1160/TH07-10-0632;
Barberis L., Hirsch E.;
"Targeting phosphoinositide 3-kinase gamma to fight inflammation and
more.";
Thromb. Haemost. 99:279-285(2008).
[16]
REVIEW ON FUNCTION IN CARDIAC CONTRACTILITY.
PubMed=19147653; DOI=10.1093/cvr/cvp014;
Oudit G.Y., Penninger J.M.;
"Cardiac regulation by phosphoinositide 3-kinases and PTEN.";
Cardiovasc. Res. 82:250-260(2009).
[17]
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).
[18]
FUNCTION.
PubMed=21393242; DOI=10.1074/jbc.M110.217026;
Wilson L.S., Baillie G.S., Pritchard L.M., Umana B., Terrin A.,
Zaccolo M., Houslay M.D., Maurice D.H.;
"A phosphodiesterase 3B-based signaling complex integrates exchange
protein activated by cAMP 1 and phosphatidylinositol 3-kinase signals
in human arterial endothelial cells.";
J. Biol. Chem. 286:16285-16296(2011).
[19]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 144-1102.
PubMed=10580505; DOI=10.1038/46319;
Walker E.H., Perisic O., Ried C., Stephens L., Williams R.L.;
"Structural insights into phosphoinositide 3-kinase catalysis and
signalling.";
Nature 402:313-320(1999).
[20]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 144-1101 IN A COMPLEX WITH
AS-604850 AND AS-605240, AND ENZYME REGULATION.
PubMed=16127437; DOI=10.1038/nm1284;
Camps M., Rueckle T., Ji H., Ardissone V., Rintelen F., Shaw J.,
Ferrandi C., Chabert C., Gillieron C., Francon B., Martin T.,
Gretener D., Perrin D., Leroy D., Vitte P.-A., Hirsch E., Wymann M.P.,
Cirillo R., Schwarz M.K., Rommel C.;
"Blockade of PI3Kgamma suppresses joint inflammation and damage in
mouse models of rheumatoid arthritis.";
Nat. Med. 11:936-943(2005).
-!- FUNCTION: Phosphoinositide-3-kinase (PI3K) that phosphorylates
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.
Links G-protein coupled receptor activation to PIP3 production.
Involved in immune, inflammatory and allergic responses. Modulates
leukocyte chemotaxis to inflammatory sites and in response to
chemoattractant agents. May control leukocyte polarization and
migration by regulating the spatial accumulation of PIP3 and by
regulating the organization of F-actin formation and integrin-
based adhesion at the leading edge. Controls motility of dendritic
cells. Together with PIK3CD is involved in natural killer (NK)
cell development and migration towards the sites of inflammation.
Participates in T-lymphocyte migration. Regulates T-lymphocyte
proliferation and cytokine production. Together with PIK3CD
participates in T-lymphocyte development. Required for B-
lymphocyte development and signaling. Together with PIK3CD
participates in neutrophil respiratory burst. Together with PIK3CD
is involved in neutrophil chemotaxis and extravasation. Together
with PIK3CB promotes platelet aggregation and thrombosis.
Regulates alpha-IIb/beta-3 integrins (ITGA2B/ ITGB3) adhesive
function in platelets downstream of P2Y12 through a lipid kinase
activity-independent mechanism. May have also a lipid kinase
activity-dependent function in platelet aggregation. Involved in
endothelial progenitor cell migration. Negative regulator of
cardiac contractility. Modulates cardiac contractility by
anchoring protein kinase A (PKA) and PDE3B activation, reducing
cAMP levels. Regulates cardiac contractility also by promoting
beta-adrenergic receptor internalization by binding to GRK2 and by
non-muscle tropomyosin phosphorylation. Also has serine/threonine
protein kinase activity: both lipid and protein kinase activities
are required for beta-adrenergic receptor endocytosis. May also
have a scaffolding role in modulating cardiac contractility.
Contributes to cardiac hypertrophy under pathological stress.
Through simultaneous binding of PDE3B to RAPGEF3 and PIK3R6 is
assembled in a signaling complex in which the PI3K gamma complex
is activated by RAPGEF3 and which is involved in angiogenesis.
{ECO:0000269|PubMed:12163475, ECO:0000269|PubMed:15294162,
ECO:0000269|PubMed:16094730, ECO:0000269|PubMed:21393242,
ECO:0000269|PubMed:7624799}.
-!- CATALYTIC ACTIVITY: ATP + 1-phosphatidyl-1D-myo-inositol 4,5-
bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-
trisphosphate.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Activated by both the alpha and the beta-gamma
G proteins following stimulation of G protein-coupled receptors
(GPCRs). Activation by GPCRs is assisted by the regulatory
subunits (PIK3R5 or PIK3R6) leading to the translocation from the
cytosol to the plasma membrane and to kinase activation. Inhibited
by AS-604850 and AS-605240. {ECO:0000269|PubMed:16127437,
ECO:0000269|PubMed:7624799}.
-!- PATHWAY: Phospholipid metabolism; phosphatidylinositol phosphate
biosynthesis.
-!- SUBUNIT: Heterodimer of a catalytic subunit PIK3CG and a PIK3R5 or
PIK3R6 regulatory subunit. Interacts with GRK2 through the PIK
helical domain. Interaction with GRK2 is required for targeting to
agonist-occupied receptor. Interacts with PDE3B (By similarity).
Interacts with TPM2. Interacts with EPHA8; regulates integrin-
mediated cell adhesion to substrate. Interacts with HRAS; the
interaction is required for membrane recruitment and beta-gamma G
protein dimer-dependent activation of the PI3K gamma complex
PIK3CG:PIK3R6 (By similarity). {ECO:0000250}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-1030384, EBI-1030384;
Q13370:PDE3B; NbExp=3; IntAct=EBI-1030384, EBI-6172856;
O02696:PIK3R5 (xeno); NbExp=6; IntAct=EBI-1030384, EBI-6172343;
Q3U6Q4:Pik3r6 (xeno); NbExp=6; IntAct=EBI-1030384, EBI-4303950;
P68404-2:Prkcb (xeno); NbExp=2; IntAct=EBI-1030384, EBI-16063464;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12163475}.
Cell membrane {ECO:0000269|PubMed:12163475}.
-!- TISSUE SPECIFICITY: Pancreas, skeletal muscle, liver and heart.
{ECO:0000269|PubMed:7624799}.
-!- MISCELLANEOUS: Candidate target in therapy for inflammatory
diseases. Selective inhibitors and protein ablation are anti-
inflammatory in multiple disease models such as asthma, rheumatoid
arthritis, allergy, systemic lupus erythematosus, airway
inflammation, lung injury and pancreatitis (PubMed:18278175).
{ECO:0000305|PubMed:18278175}.
-!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
{ECO:0000255|PROSITE-ProRule:PRU00877, ECO:0000255|PROSITE-
ProRule:PRU00879, ECO:0000255|PROSITE-ProRule:PRU00880}.
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EMBL; X83368; CAA58284.1; -; mRNA.
EMBL; AF327656; AAG61115.1; -; mRNA.
EMBL; AC005018; AAQ96873.1; -; Genomic_DNA.
EMBL; CH236947; EAL24396.1; -; Genomic_DNA.
EMBL; CH471070; EAW83387.1; -; Genomic_DNA.
EMBL; BC035683; AAH35683.1; -; mRNA.
CCDS; CCDS5739.1; -.
RefSeq; NP_001269355.1; NM_001282426.1.
RefSeq; NP_001269356.1; NM_001282427.1.
RefSeq; NP_002640.2; NM_002649.3.
RefSeq; XP_005250500.1; XM_005250443.3.
UniGene; Hs.32942; -.
UniGene; Hs.561747; -.
PDB; 1E8Y; X-ray; 2.00 A; A=144-1102.
PDB; 1E8Z; X-ray; 2.40 A; A=144-1102.
PDB; 1HE8; X-ray; 3.00 A; A=144-1102.
PDB; 2A4Z; X-ray; 2.90 A; A=144-1102.
PDB; 2A5U; X-ray; 2.70 A; A=144-1102.
PDB; 2CHW; X-ray; 2.60 A; A=144-1102.
PDB; 2CHX; X-ray; 2.50 A; A=144-1102.
PDB; 2CHZ; X-ray; 2.60 A; A=144-1102.
PDB; 2V4L; X-ray; 2.50 A; A=144-1102.
PDB; 3APC; X-ray; 2.54 A; A=144-1102.
PDB; 3APD; X-ray; 2.55 A; A=144-1102.
PDB; 3APF; X-ray; 2.82 A; A=144-1102.
PDB; 3CSF; X-ray; 2.80 A; A=144-1102.
PDB; 3CST; X-ray; 3.20 A; A=144-1102.
PDB; 3DBS; X-ray; 2.80 A; A=144-1102.
PDB; 3DPD; X-ray; 2.85 A; A=144-1102.
PDB; 3ENE; X-ray; 2.40 A; A=144-1102.
PDB; 3IBE; X-ray; 2.80 A; A=144-1102.
PDB; 3L08; X-ray; 2.70 A; A=144-1102.
PDB; 3L13; X-ray; 3.00 A; A=144-1102.
PDB; 3L16; X-ray; 2.90 A; A=144-1102.
PDB; 3L17; X-ray; 3.00 A; A=144-1102.
PDB; 3L54; X-ray; 2.30 A; A=144-1102.
PDB; 3LJ3; X-ray; 2.43 A; A=144-1102.
PDB; 3MJW; X-ray; 2.87 A; A=144-1102.
PDB; 3ML8; X-ray; 2.70 A; A=144-1102.
PDB; 3ML9; X-ray; 2.55 A; A=144-1102.
PDB; 3NZS; X-ray; 2.75 A; A=147-1094.
PDB; 3NZU; X-ray; 2.60 A; A=147-1094.
PDB; 3OAW; X-ray; 2.75 A; A=144-1102.
PDB; 3P2B; X-ray; 3.20 A; A=144-1102.
PDB; 3PRE; X-ray; 2.91 A; A=144-1102.
PDB; 3PRZ; X-ray; 2.60 A; A=144-1102.
PDB; 3PS6; X-ray; 2.60 A; A=144-1102.
PDB; 3QAQ; X-ray; 2.90 A; A=144-1102.
PDB; 3QAR; X-ray; 2.65 A; A=144-1102.
PDB; 3QJZ; X-ray; 2.90 A; A=144-1102.
PDB; 3QK0; X-ray; 2.85 A; A=144-1102.
PDB; 3R7Q; X-ray; 2.50 A; A=144-1102.
PDB; 3R7R; X-ray; 2.90 A; A=144-1102.
PDB; 3S2A; X-ray; 2.55 A; A=144-1102.
PDB; 3SD5; X-ray; 3.20 A; A=144-1102.
PDB; 3T8M; X-ray; 2.50 A; A=144-1102.
PDB; 3TJP; X-ray; 2.70 A; A=144-1102.
PDB; 3TL5; X-ray; 2.79 A; A=144-1102.
PDB; 3ZVV; X-ray; 2.50 A; A=144-1102.
PDB; 3ZW3; X-ray; 2.80 A; A=144-1102.
PDB; 4ANU; X-ray; 2.81 A; A=144-1102.
PDB; 4ANV; X-ray; 2.13 A; A=144-1102.
PDB; 4ANW; X-ray; 2.31 A; A=144-1102.
PDB; 4ANX; X-ray; 2.73 A; A=144-1102.
PDB; 4AOF; X-ray; 3.30 A; A=144-1102.
PDB; 4DK5; X-ray; 2.95 A; A=144-1102.
PDB; 4EZJ; X-ray; 2.67 A; A=144-1102.
PDB; 4EZK; X-ray; 2.80 A; A=144-1102.
PDB; 4EZL; X-ray; 2.94 A; A=144-1102.
PDB; 4F1S; X-ray; 3.00 A; A=144-1102.
PDB; 4FA6; X-ray; 2.70 A; A=144-1102.
PDB; 4FAD; X-ray; 2.70 A; A=144-1102.
PDB; 4FHJ; X-ray; 2.60 A; A=144-1102.
PDB; 4FHK; X-ray; 3.00 A; A=144-1102.
PDB; 4FJY; X-ray; 2.90 A; A=144-1102.
PDB; 4FJZ; X-ray; 3.00 A; A=144-1102.
PDB; 4FLH; X-ray; 2.60 A; A=144-1102.
PDB; 4FUL; X-ray; 2.47 A; A=144-1102.
PDB; 4G11; X-ray; 3.40 A; A=144-1102.
PDB; 4GB9; X-ray; 2.44 A; A=144-1102.
PDB; 4HLE; X-ray; 2.78 A; A=144-1102.
PDB; 4HVB; X-ray; 2.35 A; A=144-1102.
PDB; 4J6I; X-ray; 2.90 A; A=144-1102.
PDB; 4KZ0; X-ray; 2.87 A; A=144-1102.
PDB; 4KZC; X-ray; 3.25 A; A=144-1102.
PDB; 4PS3; X-ray; 2.90 A; A=144-1102.
PDB; 4PS7; X-ray; 2.69 A; A=144-1102.
PDB; 4PS8; X-ray; 2.99 A; A=144-1102.
PDB; 4URK; X-ray; 2.90 A; A=144-1102.
PDB; 4WWN; X-ray; 2.70 A; A=144-1102.
PDB; 4WWO; X-ray; 2.30 A; A=144-1102.
PDB; 4WWP; X-ray; 2.40 A; A=144-1102.
PDB; 4XX5; X-ray; 2.76 A; A=144-1102.
PDB; 4XZ4; X-ray; 2.60 A; A=144-1102.
PDB; 5EDS; X-ray; 2.80 A; A=144-1102.
PDB; 5G2N; X-ray; 2.68 A; A=144-1102.
PDB; 5G55; X-ray; 2.45 A; A=144-1102.
PDB; 5JHA; X-ray; 2.51 A; A=144-1102.
PDB; 5JHB; X-ray; 2.48 A; A=144-1102.
PDB; 5KAE; X-ray; 2.65 A; A=144-1102.
PDB; 5OQ4; X-ray; 2.70 A; A=144-1102.
PDB; 5T23; X-ray; 2.78 A; A=144-1102.
PDBsum; 1E8Y; -.
PDBsum; 1E8Z; -.
PDBsum; 1HE8; -.
PDBsum; 2A4Z; -.
PDBsum; 2A5U; -.
PDBsum; 2CHW; -.
PDBsum; 2CHX; -.
PDBsum; 2CHZ; -.
PDBsum; 2V4L; -.
PDBsum; 3APC; -.
PDBsum; 3APD; -.
PDBsum; 3APF; -.
PDBsum; 3CSF; -.
PDBsum; 3CST; -.
PDBsum; 3DBS; -.
PDBsum; 3DPD; -.
PDBsum; 3ENE; -.
PDBsum; 3IBE; -.
PDBsum; 3L08; -.
PDBsum; 3L13; -.
PDBsum; 3L16; -.
PDBsum; 3L17; -.
PDBsum; 3L54; -.
PDBsum; 3LJ3; -.
PDBsum; 3MJW; -.
PDBsum; 3ML8; -.
PDBsum; 3ML9; -.
PDBsum; 3NZS; -.
PDBsum; 3NZU; -.
PDBsum; 3OAW; -.
PDBsum; 3P2B; -.
PDBsum; 3PRE; -.
PDBsum; 3PRZ; -.
PDBsum; 3PS6; -.
PDBsum; 3QAQ; -.
PDBsum; 3QAR; -.
PDBsum; 3QJZ; -.
PDBsum; 3QK0; -.
PDBsum; 3R7Q; -.
PDBsum; 3R7R; -.
PDBsum; 3S2A; -.
PDBsum; 3SD5; -.
PDBsum; 3T8M; -.
PDBsum; 3TJP; -.
PDBsum; 3TL5; -.
PDBsum; 3ZVV; -.
PDBsum; 3ZW3; -.
PDBsum; 4ANU; -.
PDBsum; 4ANV; -.
PDBsum; 4ANW; -.
PDBsum; 4ANX; -.
PDBsum; 4AOF; -.
PDBsum; 4DK5; -.
PDBsum; 4EZJ; -.
PDBsum; 4EZK; -.
PDBsum; 4EZL; -.
PDBsum; 4F1S; -.
PDBsum; 4FA6; -.
PDBsum; 4FAD; -.
PDBsum; 4FHJ; -.
PDBsum; 4FHK; -.
PDBsum; 4FJY; -.
PDBsum; 4FJZ; -.
PDBsum; 4FLH; -.
PDBsum; 4FUL; -.
PDBsum; 4G11; -.
PDBsum; 4GB9; -.
PDBsum; 4HLE; -.
PDBsum; 4HVB; -.
PDBsum; 4J6I; -.
PDBsum; 4KZ0; -.
PDBsum; 4KZC; -.
PDBsum; 4PS3; -.
PDBsum; 4PS7; -.
PDBsum; 4PS8; -.
PDBsum; 4URK; -.
PDBsum; 4WWN; -.
PDBsum; 4WWO; -.
PDBsum; 4WWP; -.
PDBsum; 4XX5; -.
PDBsum; 4XZ4; -.
PDBsum; 5EDS; -.
PDBsum; 5G2N; -.
PDBsum; 5G55; -.
PDBsum; 5JHA; -.
PDBsum; 5JHB; -.
PDBsum; 5KAE; -.
PDBsum; 5OQ4; -.
PDBsum; 5T23; -.
ProteinModelPortal; P48736; -.
SMR; P48736; -.
BioGrid; 111312; 22.
DIP; DIP-37781N; -.
IntAct; P48736; 19.
MINT; MINT-155782; -.
STRING; 9606.ENSP00000352121; -.
BindingDB; P48736; -.
ChEMBL; CHEMBL3267; -.
DrugBank; DB06831; 2-((9H-PURIN-6-YLTHIO)METHYL)-5-CHLORO-3-(2-METHOXYPHENYL)QUINAZOLIN-4(3H)-ONE.
DrugBank; DB02656; 2-(4-Morpholinyl)-8-Phenyl-4h-1-Benzopyran-4-One.
DrugBank; DB02375; Myricetin.
DrugBank; DB06836; N-(5-(4-CHLORO-3-(2-HYDROXY-ETHYLSULFAMOYL)- PHENYLTHIAZOLE-2-YL)-ACETAMIDE.
DrugBank; DB04216; Quercetin.
DrugBank; DB02010; Staurosporine.
DrugBank; DB05241; XL765.
GuidetoPHARMACOLOGY; 2156; -.
SwissLipids; SLP:000000909; -.
iPTMnet; P48736; -.
PhosphoSitePlus; P48736; -.
BioMuta; PIK3CG; -.
DMDM; 92090623; -.
EPD; P48736; -.
MaxQB; P48736; -.
PaxDb; P48736; -.
PeptideAtlas; P48736; -.
PRIDE; P48736; -.
DNASU; 5294; -.
Ensembl; ENST00000359195; ENSP00000352121; ENSG00000105851.
Ensembl; ENST00000440650; ENSP00000392258; ENSG00000105851.
Ensembl; ENST00000496166; ENSP00000419260; ENSG00000105851.
GeneID; 5294; -.
KEGG; hsa:5294; -.
UCSC; uc003vdu.5; human.
CTD; 5294; -.
DisGeNET; 5294; -.
EuPathDB; HostDB:ENSG00000105851.10; -.
GeneCards; PIK3CG; -.
HGNC; HGNC:8978; PIK3CG.
HPA; HPA069976; -.
MIM; 601232; gene.
neXtProt; NX_P48736; -.
OpenTargets; ENSG00000105851; -.
PharmGKB; PA33311; -.
eggNOG; KOG0904; Eukaryota.
eggNOG; COG5032; LUCA.
GeneTree; ENSGT00760000119110; -.
HOGENOM; HOG000252912; -.
HOVERGEN; HBG101026; -.
InParanoid; P48736; -.
KO; K21289; -.
OMA; FTEEVLW; -.
OrthoDB; EOG091G027R; -.
PhylomeDB; P48736; -.
TreeFam; TF102031; -.
BioCyc; MetaCyc:HS02818-MONOMER; -.
BRENDA; 2.7.1.137; 2681.
BRENDA; 2.7.1.153; 2681.
Reactome; R-HSA-114604; GPVI-mediated activation cascade.
Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
Reactome; R-HSA-392451; G beta:gamma signalling through PI3Kgamma.
SignaLink; P48736; -.
SIGNOR; P48736; -.
UniPathway; UPA00220; -.
EvolutionaryTrace; P48736; -.
GeneWiki; PIK3CG; -.
GenomeRNAi; 5294; -.
PRO; PR:P48736; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000105851; -.
CleanEx; HS_PIK3CG; -.
ExpressionAtlas; P48736; baseline and differential.
Genevisible; P48736; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0042629; C:mast cell granule; IEA:GOC.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005944; C:phosphatidylinositol 3-kinase complex, class IB; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IBA:GO_Central.
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:0046875; F:ephrin receptor binding; IPI:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0016301; F:kinase activity; IDA:MGI.
GO; GO:0035004; F:phosphatidylinositol 3-kinase activity; TAS:UniProtKB.
GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; IBA:GO_Central.
GO; GO:0004672; F:protein kinase activity; TAS:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0002250; P:adaptive immune response; TAS:UniProtKB.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
GO; GO:0001816; P:cytokine production; TAS:UniProtKB.
GO; GO:0002407; P:dendritic cell chemotaxis; TAS:UniProtKB.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IDA:UniProtKB.
GO; GO:0097284; P:hepatocyte apoptotic process; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; TAS:UniProtKB.
GO; GO:0045087; P:innate immune response; TAS:UniProtKB.
GO; GO:0043303; P:mast cell degranulation; TAS:UniProtKB.
GO; GO:0035747; P:natural killer cell chemotaxis; TAS:UniProtKB.
GO; GO:0055118; P:negative regulation of cardiac muscle contraction; TAS:UniProtKB.
GO; GO:2000270; P:negative regulation of fibroblast apoptotic process; IEA:Ensembl.
GO; GO:0010897; P:negative regulation of triglyceride catabolic process; IEA:Ensembl.
GO; GO:0030593; P:neutrophil chemotaxis; TAS:UniProtKB.
GO; GO:0072672; P:neutrophil extravasation; TAS:UniProtKB.
GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IDA:UniProtKB.
GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
GO; GO:0016310; P:phosphorylation; IDA:MGI.
GO; GO:0030168; P:platelet activation; TAS:Reactome.
GO; GO:0070527; P:platelet aggregation; TAS:UniProtKB.
GO; GO:0002675; P:positive regulation of acute inflammatory response; IEA:Ensembl.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:UniProtKB.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:UniProtKB.
GO; GO:1903169; P:regulation of calcium ion transmembrane transport; IEA:Ensembl.
GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; TAS:UniProtKB.
GO; GO:0002679; P:respiratory burst involved in defense response; TAS:UniProtKB.
GO; GO:0032252; P:secretory granule localization; IEA:Ensembl.
GO; GO:0042110; P:T cell activation; TAS:UniProtKB.
GO; GO:0010818; P:T cell chemotaxis; TAS:UniProtKB.
GO; GO:0042098; P:T cell proliferation; 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; PF00794; PI3K_rbd; 1.
Pfam; PF00613; PI3Ka; 1.
PIRSF; PIRSF000587; PI3K_Vps34; 1.
SMART; SM00142; PI3K_C2; 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; Cell membrane; Chemotaxis;
Complete proteome; Cytoplasm; Endocytosis; Immunity;
Inflammatory response; Kinase; Membrane; Nucleotide-binding;
Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
Transferase.
CHAIN 1 1102 Phosphatidylinositol 4,5-bisphosphate 3-
kinase catalytic subunit gamma isoform.
/FTId=PRO_0000088792.
DOMAIN 34 141 PI3K-ABD. {ECO:0000255|PROSITE-
ProRule:PRU00877}.
DOMAIN 217 309 PI3K-RBD. {ECO:0000255|PROSITE-
ProRule:PRU00879}.
DOMAIN 357 521 C2 PI3K-type. {ECO:0000255|PROSITE-
ProRule:PRU00880}.
DOMAIN 541 723 PIK helical. {ECO:0000255|PROSITE-
ProRule:PRU00878}.
DOMAIN 828 1073 PI3K/PI4K. {ECO:0000255|PROSITE-
ProRule:PRU00269}.
NP_BIND 829 838 ATP. {ECO:0000250}.
NP_BIND 864 872 ATP. {ECO:0000250}.
NP_BIND 961 969 ATP. {ECO:0000250}.
COMPBIAS 19 23 Poly-Arg.
MOD_RES 1024 1024 Phosphothreonine; by PKA.
{ECO:0000250|UniProtKB:Q9JHG7}.
MOD_RES 1101 1101 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:12502714}.
MUTAGEN 833 833 K->R: Reduced inflammatory reactions but
no alterations in cardiac contractility.
{ECO:0000269|PubMed:15294162}.
MUTAGEN 947 947 R->P: Abolishes protein and lipid kinase
activity. Does not abolishes interaction
with GRK2. {ECO:0000269|PubMed:16094730}.
CONFLICT 30 30 Missing (in Ref. 1; CAA58284).
{ECO:0000305}.
CONFLICT 459 459 Q -> R (in Ref. 1; CAA58284 and 3;
AAG61115). {ECO:0000305}.
HELIX 145 158 {ECO:0000244|PDB:1E8Y}.
HELIX 165 167 {ECO:0000244|PDB:3APC}.
STRAND 169 171 {ECO:0000244|PDB:1E8Y}.
HELIX 172 179 {ECO:0000244|PDB:1E8Y}.
HELIX 181 190 {ECO:0000244|PDB:1E8Y}.
HELIX 193 198 {ECO:0000244|PDB:1E8Y}.
HELIX 209 212 {ECO:0000244|PDB:1E8Y}.
HELIX 213 215 {ECO:0000244|PDB:5G2N}.
STRAND 216 218 {ECO:0000244|PDB:1E8Y}.
STRAND 220 226 {ECO:0000244|PDB:1E8Y}.
STRAND 229 235 {ECO:0000244|PDB:4ANV}.
HELIX 241 243 {ECO:0000244|PDB:1E8Y}.
HELIX 246 252 {ECO:0000244|PDB:1E8Y}.
HELIX 256 259 {ECO:0000244|PDB:1HE8}.
STRAND 263 265 {ECO:0000244|PDB:1HE8}.
STRAND 271 274 {ECO:0000244|PDB:1E8Y}.
STRAND 283 285 {ECO:0000244|PDB:4ANV}.
HELIX 287 289 {ECO:0000244|PDB:1E8Y}.
HELIX 291 298 {ECO:0000244|PDB:1E8Y}.
STRAND 303 308 {ECO:0000244|PDB:1E8Y}.
HELIX 313 316 {ECO:0000244|PDB:1E8Y}.
HELIX 354 356 {ECO:0000244|PDB:4ANV}.
STRAND 359 369 {ECO:0000244|PDB:1E8Y}.
STRAND 375 377 {ECO:0000244|PDB:4ANW}.
STRAND 380 391 {ECO:0000244|PDB:1E8Y}.
STRAND 393 398 {ECO:0000244|PDB:1E8Y}.
STRAND 406 419 {ECO:0000244|PDB:1E8Y}.
HELIX 420 422 {ECO:0000244|PDB:1E8Y}.
STRAND 428 434 {ECO:0000244|PDB:1E8Y}.
STRAND 462 469 {ECO:0000244|PDB:1E8Y}.
STRAND 473 475 {ECO:0000244|PDB:4ANV}.
STRAND 478 483 {ECO:0000244|PDB:1E8Y}.
STRAND 484 486 {ECO:0000244|PDB:5T23}.
HELIX 499 502 {ECO:0000244|PDB:1E8Y}.
STRAND 511 513 {ECO:0000244|PDB:1E8Y}.
STRAND 515 520 {ECO:0000244|PDB:1E8Y}.
HELIX 549 560 {ECO:0000244|PDB:1E8Y}.
STRAND 563 565 {ECO:0000244|PDB:4XX5}.
HELIX 569 577 {ECO:0000244|PDB:1E8Y}.
HELIX 579 582 {ECO:0000244|PDB:1E8Y}.
HELIX 586 588 {ECO:0000244|PDB:1E8Y}.
HELIX 589 593 {ECO:0000244|PDB:1E8Y}.
HELIX 601 612 {ECO:0000244|PDB:1E8Y}.
HELIX 615 618 {ECO:0000244|PDB:1E8Y}.
HELIX 624 630 {ECO:0000244|PDB:1E8Y}.
STRAND 632 634 {ECO:0000244|PDB:1HE8}.
HELIX 638 648 {ECO:0000244|PDB:1E8Y}.
HELIX 653 666 {ECO:0000244|PDB:1E8Y}.
HELIX 667 669 {ECO:0000244|PDB:1E8Y}.
STRAND 671 674 {ECO:0000244|PDB:1E8Y}.
HELIX 676 687 {ECO:0000244|PDB:1E8Y}.
HELIX 689 705 {ECO:0000244|PDB:1E8Y}.
TURN 707 709 {ECO:0000244|PDB:1E8Y}.
HELIX 710 721 {ECO:0000244|PDB:1E8Y}.
TURN 722 724 {ECO:0000244|PDB:3ML8}.
HELIX 726 751 {ECO:0000244|PDB:1E8Y}.
STRAND 755 757 {ECO:0000244|PDB:1E8Y}.
HELIX 761 774 {ECO:0000244|PDB:1E8Y}.
TURN 775 778 {ECO:0000244|PDB:1E8Y}.
STRAND 783 785 {ECO:0000244|PDB:1E8Y}.
STRAND 788 796 {ECO:0000244|PDB:1E8Y}.
HELIX 798 800 {ECO:0000244|PDB:1E8Y}.
STRAND 806 808 {ECO:0000244|PDB:1E8Y}.
STRAND 811 818 {ECO:0000244|PDB:1E8Y}.
STRAND 828 836 {ECO:0000244|PDB:1E8Y}.
HELIX 838 856 {ECO:0000244|PDB:1E8Y}.
TURN 857 859 {ECO:0000244|PDB:1E8Y}.
STRAND 869 873 {ECO:0000244|PDB:1E8Y}.
STRAND 876 880 {ECO:0000244|PDB:1E8Y}.
STRAND 885 887 {ECO:0000244|PDB:1E8Y}.
HELIX 888 895 {ECO:0000244|PDB:1E8Y}.
STRAND 898 900 {ECO:0000244|PDB:3LJ3}.
HELIX 906 914 {ECO:0000244|PDB:1E8Y}.
STRAND 915 917 {ECO:0000244|PDB:2A4Z}.
HELIX 918 941 {ECO:0000244|PDB:1E8Y}.
HELIX 949 951 {ECO:0000244|PDB:1E8Y}.
STRAND 952 955 {ECO:0000244|PDB:1E8Y}.
TURN 956 958 {ECO:0000244|PDB:1HE8}.
STRAND 960 962 {ECO:0000244|PDB:1E8Y}.
HELIX 965 970 {ECO:0000244|PDB:3L54}.
HELIX 989 994 {ECO:0000244|PDB:1E8Y}.
TURN 998 1000 {ECO:0000244|PDB:4ANV}.
HELIX 1004 1021 {ECO:0000244|PDB:1E8Y}.
HELIX 1024 1038 {ECO:0000244|PDB:1E8Y}.
STRAND 1039 1041 {ECO:0000244|PDB:1E8Y}.
TURN 1042 1045 {ECO:0000244|PDB:3PRE}.
HELIX 1046 1054 {ECO:0000244|PDB:1E8Y}.
TURN 1055 1058 {ECO:0000244|PDB:1E8Y}.
HELIX 1061 1078 {ECO:0000244|PDB:1E8Y}.
HELIX 1081 1085 {ECO:0000244|PDB:1E8Y}.
TURN 1090 1092 {ECO:0000244|PDB:5G55}.
SEQUENCE 1102 AA; 126454 MW; EF2B1A0E1CBEF406 CRC64;
MELENYKQPV VLREDNCRRR RRMKPRSAAA SLSSMELIPI EFVLPTSQRK CKSPETALLH
VAGHGNVEQM KAQVWLRALE TSVAADFYHR LGPHHFLLLY QKKGQWYEIY DKYQVVQTLD
CLRYWKATHR SPGQIHLVQR HPPSEESQAF QRQLTALIGY DVTDVSNVHD DELEFTRRGL
VTPRMAEVAS RDPKLYAMHP WVTSKPLPEY LWKKIANNCI FIVIHRSTTS QTIKVSPDDT
PGAILQSFFT KMAKKKSLMD IPESQSEQDF VLRVCGRDEY LVGETPIKNF QWVRHCLKNG
EEIHVVLDTP PDPALDEVRK EEWPLVDDCT GVTGYHEQLT IHGKDHESVF TVSLWDCDRK
FRVKIRGIDI PVLPRNTDLT VFVEANIQHG QQVLCQRRTS PKPFTEEVLW NVWLEFSIKI
KDLPKGALLN LQIYCGKAPA LSSKASAESP SSESKGKVQL LYYVNLLLID HRFLLRRGEY
VLHMWQISGK GEDQGSFNAD KLTSATNPDK ENSMSISILL DNYCHPIALP KHQPTPDPEG
DRVRAEMPNQ LRKQLEAIIA TDPLNPLTAE DKELLWHFRY ESLKHPKAYP KLFSSVKWGQ
QEIVAKTYQL LARREVWDQS ALDVGLTMQL LDCNFSDENV RAIAVQKLES LEDDDVLHYL
LQLVQAVKFE PYHDSALARF LLKRGLRNKR IGHFLFWFLR SEIAQSRHYQ QRFAVILEAY
LRGCGTAMLH DFTQQVQVIE MLQKVTLDIK SLSAEKYDVS SQVISQLKQK LENLQNSQLP
ESFRVPYDPG LKAGALAIEK CKVMASKKKP LWLEFKCADP TALSNETIGI IFKHGDDLRQ
DMLILQILRI MESIWETESL DLCLLPYGCI STGDKIGMIE IVKDATTIAK IQQSTVGNTG
AFKDEVLNHW LKEKSPTEEK FQAAVERFVY SCAGYCVATF VLGIGDRHND NIMITETGNL
FHIDFGHILG NYKSFLGINK ERVPFVLTPD FLFVMGTSGK KTSPHFQKFQ DICVKAYLAL
RHHTNLLIIL FSMMLMTGMP QLTSKEDIEY IRDALTVGKN EEDAKKYFLD QIEVCRDKGW
TVQFNWFLHL VLGIKQGEKH SA


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15-288-21071 Phosphatidylinositol-4.5-bisphosphate 3-kinase catalytic subunit beta isoform - EC 2.7.1.153; PI3-kinase p110 subunit beta; PtdIns-3-kinase p110; PI3K; PI3Kbeta Polyclonal 0.05 mg
15-288-21071 Phosphatidylinositol-4.5-bisphosphate 3-kinase catalytic subunit beta isoform - EC 2.7.1.153; PI3-kinase p110 subunit beta; PtdIns-3-kinase p110; PI3K; PI3Kbeta Polyclonal 0.1 mg
EIAAB29565 Homo sapiens,Human,p55PIK,Phosphatidylinositol 3-kinase 55 kDa regulatory subunit gamma,Phosphatidylinositol 3-kinase regulatory subunit gamma,PI3K regulatory subunit gamma,PI3-kinase regulatory subun
CSB-EL018001MO Mouse Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit gamma isoform(PIK3CG) ELISA kit 96T
CSB-EL018001PI Pig Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit gamma isoform(PIK3CG) ELISA kit SpeciesPig 96T
CSB-EL018001HU Human Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit gamma isoform(PIK3CG) ELISA kit 96T
CSB-EL018001MO Mouse Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit gamma isoform(PIK3CG) ELISA kit SpeciesMouse 96T
CSB-EL018001HU Human Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit gamma isoform(PIK3CG) ELISA kit SpeciesHuman 96T
EIAAB29568 Mouse,Mus musculus,p55PIK,Phosphatidylinositol 3-kinase 55 kDa regulatory subunit gamma,Phosphatidylinositol 3-kinase regulatory subunit gamma,PI3K regulatory subunit gamma,PI3-kinase regulatory subun
EIAAB29566 Bos taurus,Bovine,p55PIK,Phosphatidylinositol 3-kinase 85 kDa regulatory subunit gamma,Phosphatidylinositol 3-kinase regulatory subunit gamma,PI3K regulatory subunit gamma,PI3-kinase regulatory subuni
EIAAB26932 I-kappa-B kinase subunit gamma,IkB kinase subunit gamma,IkB kinase-associated protein 1,Ikbkg,IKKAP1,IKKG,IKK-gamma,Inhibitor of nuclear factor kappa-B kinase subunit gamma,mFIP-3,Mouse,Mus musculus,N
PK3CG_MOUSE ELISA Kit FOR Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit gamma isoform; organism: Mouse; gene name: Pik3cg 96T
EIAAB31239 Homo sapiens,Human,p110beta,Phosphatidylinositol-4,5-bisphosphate 3-kinase 110 kDa catalytic subunit beta,Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit beta isoform,PI3Kbeta,PI3K-be
E0704r Pig ELISA Kit FOR Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit gamma isoform 96T
SLFN5_HUMAN Pig ELISA Kit FOR Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit gamma isoform 96T
EIAAB31240 p110beta,Phosphatidylinositol-4,5-bisphosphate 3-kinase 110 kDa catalytic subunit beta,Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit beta isoform,PI3Kbeta,PI3K-beta,PI3-kinase subun
EIAAB31238 Mouse,Mus musculus,p110beta,Phosphatidylinositol-4,5-bisphosphate 3-kinase 110 kDa catalytic subunit beta,Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit beta isoform,PI3Kbeta,PI3K-be
EIAAB26934 FIP3,FIP-3,Homo sapiens,Human,I-kappa-B kinase subunit gamma,IkB kinase subunit gamma,IkB kinase-associated protein 1,IKBKG,IKKAP1,IKKG,IKK-gamma,Inhibitor of nuclear factor kappa-B kinase subunit gam


 

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