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Database: UniProt
Entry: P48736
LinkDB: P48736
Original site: P48736 
ID   PK3CG_HUMAN             Reviewed;        1102 AA.
AC   P48736; A4D0Q6; Q8IV23; Q9BZC8;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 3.
DT   11-DEC-2019, entry version 202.
DE   RecName: Full=Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform;
DE            Short=PI3-kinase subunit gamma;
DE            Short=PI3K-gamma;
DE            Short=PI3Kgamma;
DE            Short=PtdIns-3-kinase subunit gamma;
DE            EC=2.7.1.153;
DE   AltName: Full=Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit gamma;
DE            Short=PtdIns-3-kinase subunit p110-gamma;
DE            Short=p110gamma;
DE   AltName: Full=Phosphoinositide-3-kinase catalytic gamma polypeptide;
DE   AltName: Full=Serine/threonine protein kinase PIK3CG;
DE            EC=2.7.11.1;
DE   AltName: Full=p120-PI3K;
GN   Name=PIK3CG;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ACTIVITY REGULATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=7624799; DOI=10.1126/science.7624799;
RA   Stoyanov B., Volinia S., Hanck T., Rubio I., Loubtchenkov M., Malek D.,
RA   Stoyanova S., Vanhaesebroeck B., Dhand R., Nuernberg B., Gierschik P.,
RA   Seedorf K., Hsuan J.J., Waterfield M.D., Wetzker R.;
RT   "Cloning and characterization of a G protein-activated human
RT   phosphoinositide-3 kinase.";
RL   Science 269:690-693(1995).
RN   [2]
RP   SEQUENCE REVISION.
RA   Waterfield M.D.;
RL   Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Michalke M., Schaefer M., Stoyanov B., Wetzker R., Nuernberg B.;
RT   "Regulation of a G-protein-activated phosphoinositide-3-kinase.";
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12690205; DOI=10.1126/science.1083423;
RA   Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA   Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA   Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA   Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA   Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA   Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA   Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA   Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA   Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA   Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA   Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA   Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA   Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA   Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA   Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA   Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA   Adams M.D., Tsui L.-C.;
RT   "Human chromosome 7: DNA sequence and biology.";
RL   Science 300:767-772(2003).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pancreas;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   INTERACTION WITH EPHA8.
RX   PubMed=11416136; DOI=10.1128/mcb.21.14.4579-4597.2001;
RA   Gu C., Park S.;
RT   "The EphA8 receptor regulates integrin activity through p110gamma
RT   phosphatidylinositol-3 kinase in a tyrosine kinase activity-independent
RT   manner.";
RL   Mol. Cell. Biol. 21:4579-4597(2001).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH GRK2.
RX   PubMed=12163475; DOI=10.1083/jcb.200202113;
RA   Naga Prasad S.V., Laporte S.A., Chamberlain D., Caron M.G., Barak L.,
RA   Rockman H.A.;
RT   "Phosphoinositide 3-kinase regulates beta2-adrenergic receptor endocytosis
RT   by AP-2 recruitment to the receptor/beta-arrestin complex.";
RL   J. Cell Biol. 158:563-575(2002).
RN   [10]
RP   PHOSPHORYLATION AT SER-1101.
RX   PubMed=12502714; DOI=10.1074/jbc.m210351200;
RA   Czupalla C., Culo M., Muller E.C., Brock C., Reusch H.P., Spicher K.,
RA   Krause E., Nurnberg B.;
RT   "Identification and characterization of the autophosphorylation sites of
RT   phosphoinositide 3-kinase isoforms beta and gamma.";
RL   J. Biol. Chem. 278:11536-11545(2003).
RN   [11]
RP   FUNCTION IN CARDIAC CONTRACTILITY, AND MUTAGENESIS OF LYS-833.
RX   PubMed=15294162; DOI=10.1016/j.cell.2004.07.017;
RA   Patrucco E., Notte A., Barberis L., Selvetella G., Maffei A.,
RA   Brancaccio M., Marengo S., Russo G., Azzolino O., Rybalkin S.D.,
RA   Silengo L., Altruda F., Wetzker R., Wymann M.P., Lembo G., Hirsch E.;
RT   "PI3Kgamma modulates the cardiac response to chronic pressure overload by
RT   distinct kinase-dependent and -independent effects.";
RL   Cell 118:375-387(2004).
RN   [12]
RP   INTERACTION WITH PIK3R5.
RX   PubMed=15797027; DOI=10.1016/j.cub.2005.02.020;
RA   Suire S., Coadwell J., Ferguson G.J., Davidson K., Hawkins P., Stephens L.;
RT   "p84, a new Gbetagamma-activated regulatory subunit of the type IB
RT   phosphoinositide 3-kinase p110gamma.";
RL   Curr. Biol. 15:566-570(2005).
RN   [13]
RP   FUNCTION AS A PROTEIN KINASE, INTERACTION WITH GRK2 AND TPM2, AND
RP   MUTAGENESIS OF ARG-947.
RX   PubMed=16094730; DOI=10.1038/ncb1278;
RA   Naga Prasad S.V., Jayatilleke A., Madamanchi A., Rockman H.A.;
RT   "Protein kinase activity of phosphoinositide 3-kinase regulates beta-
RT   adrenergic receptor endocytosis.";
RL   Nat. Cell Biol. 7:785-796(2005).
RN   [14]
RP   REVIEW ON FUNCTION.
RX   PubMed=17290298; DOI=10.1038/nri2036;
RA   Rommel C., Camps M., Ji H.;
RT   "PI3K delta and PI3K gamma: partners in crime in inflammation in rheumatoid
RT   arthritis and beyond?";
RL   Nat. Rev. Immunol. 7:191-201(2007).
RN   [15]
RP   REVIEW ON FUNCTION IN LEUKOCYTES AND ENDOTHELIAL CELLS, AND REVIEW ON
RP   ANTINFLAMMATORY THERAPY TARGET.
RX   PubMed=18278175; DOI=10.1160/th07-10-0632;
RA   Barberis L., Hirsch E.;
RT   "Targeting phosphoinositide 3-kinase gamma to fight inflammation and
RT   more.";
RL   Thromb. Haemost. 99:279-285(2008).
RN   [16]
RP   REVIEW ON FUNCTION IN CARDIAC CONTRACTILITY.
RX   PubMed=19147653; DOI=10.1093/cvr/cvp014;
RA   Oudit G.Y., Penninger J.M.;
RT   "Cardiac regulation by phosphoinositide 3-kinases and PTEN.";
RL   Cardiovasc. Res. 82:250-260(2009).
RN   [17]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [18]
RP   FUNCTION.
RX   PubMed=21393242; DOI=10.1074/jbc.m110.217026;
RA   Wilson L.S., Baillie G.S., Pritchard L.M., Umana B., Terrin A., Zaccolo M.,
RA   Houslay M.D., Maurice D.H.;
RT   "A phosphodiesterase 3B-based signaling complex integrates exchange protein
RT   activated by cAMP 1 and phosphatidylinositol 3-kinase signals in human
RT   arterial endothelial cells.";
RL   J. Biol. Chem. 286:16285-16296(2011).
RN   [19]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 144-1102.
RX   PubMed=10580505; DOI=10.1038/46319;
RA   Walker E.H., Perisic O., Ried C., Stephens L., Williams R.L.;
RT   "Structural insights into phosphoinositide 3-kinase catalysis and
RT   signalling.";
RL   Nature 402:313-320(1999).
RN   [20]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 144-1101 IN A COMPLEX WITH
RP   AS-604850 AND AS-605240, AND ACTIVITY REGULATION.
RX   PubMed=16127437; DOI=10.1038/nm1284;
RA   Camps M., Rueckle T., Ji H., Ardissone V., Rintelen F., Shaw J.,
RA   Ferrandi C., Chabert C., Gillieron C., Francon B., Martin T., Gretener D.,
RA   Perrin D., Leroy D., Vitte P.-A., Hirsch E., Wymann M.P., Cirillo R.,
RA   Schwarz M.K., Rommel C.;
RT   "Blockade of PI3Kgamma suppresses joint inflammation and damage in mouse
RT   models of rheumatoid arthritis.";
RL   Nat. Med. 11:936-943(2005).
CC   -!- FUNCTION: Phosphoinositide-3-kinase (PI3K) that phosphorylates
CC       PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate
CC       phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role
CC       by recruiting PH domain-containing proteins to the membrane, including
CC       AKT1 and PDPK1, activating signaling cascades involved in cell growth,
CC       survival, proliferation, motility and morphology. Links G-protein
CC       coupled receptor activation to PIP3 production. Involved in immune,
CC       inflammatory and allergic responses. Modulates leukocyte chemotaxis to
CC       inflammatory sites and in response to chemoattractant agents. May
CC       control leukocyte polarization and migration by regulating the spatial
CC       accumulation of PIP3 and by regulating the organization of F-actin
CC       formation and integrin-based adhesion at the leading edge. Controls
CC       motility of dendritic cells. Together with PIK3CD is involved in
CC       natural killer (NK) cell development and migration towards the sites of
CC       inflammation. Participates in T-lymphocyte migration. Regulates T-
CC       lymphocyte proliferation and cytokine production. Together with PIK3CD
CC       participates in T-lymphocyte development. Required for B-lymphocyte
CC       development and signaling. Together with PIK3CD participates in
CC       neutrophil respiratory burst. Together with PIK3CD is involved in
CC       neutrophil chemotaxis and extravasation. Together with PIK3CB promotes
CC       platelet aggregation and thrombosis. Regulates alpha-IIb/beta-3
CC       integrins (ITGA2B/ ITGB3) adhesive function in platelets downstream of
CC       P2Y12 through a lipid kinase activity-independent mechanism. May have
CC       also a lipid kinase activity-dependent function in platelet
CC       aggregation. Involved in endothelial progenitor cell migration.
CC       Negative regulator of cardiac contractility. Modulates cardiac
CC       contractility by anchoring protein kinase A (PKA) and PDE3B activation,
CC       reducing cAMP levels. Regulates cardiac contractility also by promoting
CC       beta-adrenergic receptor internalization by binding to GRK2 and by non-
CC       muscle tropomyosin phosphorylation. Also has serine/threonine protein
CC       kinase activity: both lipid and protein kinase activities are required
CC       for beta-adrenergic receptor endocytosis. May also have a scaffolding
CC       role in modulating cardiac contractility. Contributes to cardiac
CC       hypertrophy under pathological stress. Through simultaneous binding of
CC       PDE3B to RAPGEF3 and PIK3R6 is assembled in a signaling complex in
CC       which the PI3K gamma complex is activated by RAPGEF3 and which is
CC       involved in angiogenesis. {ECO:0000269|PubMed:12163475,
CC       ECO:0000269|PubMed:15294162, ECO:0000269|PubMed:16094730,
CC       ECO:0000269|PubMed:21393242, ECO:0000269|PubMed:7624799}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC         bisphosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC         inositol-3,4,5-trisphosphate) + ADP + H(+); Xref=Rhea:RHEA:21292,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57836,
CC         ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.153;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1;
CC   -!- ACTIVITY REGULATION: Activated by both the alpha and the beta-gamma G
CC       proteins following stimulation of G protein-coupled receptors (GPCRs).
CC       Activation by GPCRs is assisted by the regulatory subunits (PIK3R5 or
CC       PIK3R6) leading to the translocation from the cytosol to the plasma
CC       membrane and to kinase activation. Inhibited by AS-604850 and AS-
CC       605240. {ECO:0000269|PubMed:16127437, ECO:0000269|PubMed:7624799}.
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylinositol phosphate
CC       biosynthesis.
CC   -!- SUBUNIT: Heterodimer of a catalytic subunit PIK3CG and a PIK3R5 or
CC       PIK3R6 regulatory subunit. Interacts with GRK2 through the PIK helical
CC       domain. Interaction with GRK2 is required for targeting to agonist-
CC       occupied receptor. Interacts with PDE3B (By similarity). Interacts with
CC       TPM2. Interacts with EPHA8; regulates integrin-mediated cell adhesion
CC       to substrate. Interacts with HRAS; the interaction is required for
CC       membrane recruitment and beta-gamma G protein dimer-dependent
CC       activation of the PI3K gamma complex PIK3CG:PIK3R6 (By similarity).
CC       {ECO:0000250}.
CC   -!- INTERACTION:
CC       Self; NbExp=2; IntAct=EBI-1030384, EBI-1030384;
CC       Q13370:PDE3B; NbExp=3; IntAct=EBI-1030384, EBI-6172856;
CC       O02696:PIK3R5 (xeno); NbExp=6; IntAct=EBI-1030384, EBI-6172343;
CC       Q3U6Q4:Pik3r6 (xeno); NbExp=6; IntAct=EBI-1030384, EBI-4303950;
CC       P68404-2:Prkcb (xeno); NbExp=2; IntAct=EBI-1030384, EBI-16063464;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12163475}. Cell
CC       membrane {ECO:0000269|PubMed:12163475}.
CC   -!- TISSUE SPECIFICITY: Pancreas, skeletal muscle, liver and heart.
CC       {ECO:0000269|PubMed:7624799}.
CC   -!- MISCELLANEOUS: Candidate target in therapy for inflammatory diseases.
CC       Selective inhibitors and protein ablation are anti-inflammatory in
CC       multiple disease models such as asthma, rheumatoid arthritis, allergy,
CC       systemic lupus erythematosus, airway inflammation, lung injury and
CC       pancreatitis (PubMed:18278175). {ECO:0000305|PubMed:18278175}.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00877, ECO:0000255|PROSITE-ProRule:PRU00879,
CC       ECO:0000255|PROSITE-ProRule:PRU00880}.
DR   EMBL; X83368; CAA58284.1; -; mRNA.
DR   EMBL; AF327656; AAG61115.1; -; mRNA.
DR   EMBL; AC005018; AAQ96873.1; -; Genomic_DNA.
DR   EMBL; CH236947; EAL24396.1; -; Genomic_DNA.
DR   EMBL; CH471070; EAW83387.1; -; Genomic_DNA.
DR   EMBL; BC035683; AAH35683.1; -; mRNA.
DR   CCDS; CCDS5739.1; -.
DR   RefSeq; NP_001269355.1; NM_001282426.1.
DR   RefSeq; NP_001269356.1; NM_001282427.1.
DR   RefSeq; NP_002640.2; NM_002649.3.
DR   RefSeq; XP_005250500.1; XM_005250443.3.
DR   PDB; 1E8Y; X-ray; 2.00 A; A=144-1102.
DR   PDB; 1E8Z; X-ray; 2.40 A; A=144-1102.
DR   PDB; 1HE8; X-ray; 3.00 A; A=144-1102.
DR   PDB; 2A4Z; X-ray; 2.90 A; A=144-1102.
DR   PDB; 2A5U; X-ray; 2.70 A; A=144-1102.
DR   PDB; 2CHW; X-ray; 2.60 A; A=144-1102.
DR   PDB; 2CHX; X-ray; 2.50 A; A=144-1102.
DR   PDB; 2CHZ; X-ray; 2.60 A; A=144-1102.
DR   PDB; 2V4L; X-ray; 2.50 A; A=144-1102.
DR   PDB; 3APC; X-ray; 2.54 A; A=144-1102.
DR   PDB; 3APD; X-ray; 2.55 A; A=144-1102.
DR   PDB; 3APF; X-ray; 2.82 A; A=144-1102.
DR   PDB; 3CSF; X-ray; 2.80 A; A=144-1102.
DR   PDB; 3CST; X-ray; 3.20 A; A=144-1102.
DR   PDB; 3DBS; X-ray; 2.80 A; A=144-1102.
DR   PDB; 3DPD; X-ray; 2.85 A; A=144-1102.
DR   PDB; 3ENE; X-ray; 2.40 A; A=144-1102.
DR   PDB; 3IBE; X-ray; 2.80 A; A=144-1102.
DR   PDB; 3L08; X-ray; 2.70 A; A=144-1102.
DR   PDB; 3L13; X-ray; 3.00 A; A=144-1102.
DR   PDB; 3L16; X-ray; 2.90 A; A=144-1102.
DR   PDB; 3L17; X-ray; 3.00 A; A=144-1102.
DR   PDB; 3L54; X-ray; 2.30 A; A=144-1102.
DR   PDB; 3LJ3; X-ray; 2.43 A; A=144-1102.
DR   PDB; 3MJW; X-ray; 2.87 A; A=144-1102.
DR   PDB; 3ML8; X-ray; 2.70 A; A=144-1102.
DR   PDB; 3ML9; X-ray; 2.55 A; A=144-1102.
DR   PDB; 3NZS; X-ray; 2.75 A; A=147-1094.
DR   PDB; 3NZU; X-ray; 2.60 A; A=147-1094.
DR   PDB; 3OAW; X-ray; 2.75 A; A=144-1102.
DR   PDB; 3P2B; X-ray; 3.20 A; A=144-1102.
DR   PDB; 3PRE; X-ray; 2.91 A; A=144-1102.
DR   PDB; 3PRZ; X-ray; 2.60 A; A=144-1102.
DR   PDB; 3PS6; X-ray; 2.60 A; A=144-1102.
DR   PDB; 3QAQ; X-ray; 2.90 A; A=144-1102.
DR   PDB; 3QAR; X-ray; 2.65 A; A=144-1102.
DR   PDB; 3QJZ; X-ray; 2.90 A; A=144-1102.
DR   PDB; 3QK0; X-ray; 2.85 A; A=144-1102.
DR   PDB; 3R7Q; X-ray; 2.50 A; A=144-1102.
DR   PDB; 3R7R; X-ray; 2.90 A; A=144-1102.
DR   PDB; 3S2A; X-ray; 2.55 A; A=144-1102.
DR   PDB; 3SD5; X-ray; 3.20 A; A=144-1102.
DR   PDB; 3T8M; X-ray; 2.50 A; A=144-1102.
DR   PDB; 3TJP; X-ray; 2.70 A; A=144-1102.
DR   PDB; 3TL5; X-ray; 2.79 A; A=144-1102.
DR   PDB; 3ZVV; X-ray; 2.50 A; A=144-1102.
DR   PDB; 3ZW3; X-ray; 2.80 A; A=144-1102.
DR   PDB; 4ANU; X-ray; 2.81 A; A=144-1102.
DR   PDB; 4ANV; X-ray; 2.13 A; A=144-1102.
DR   PDB; 4ANW; X-ray; 2.31 A; A=144-1102.
DR   PDB; 4ANX; X-ray; 2.73 A; A=144-1102.
DR   PDB; 4AOF; X-ray; 3.30 A; A=144-1102.
DR   PDB; 4DK5; X-ray; 2.95 A; A=144-1102.
DR   PDB; 4EZJ; X-ray; 2.67 A; A=144-1102.
DR   PDB; 4EZK; X-ray; 2.80 A; A=144-1102.
DR   PDB; 4EZL; X-ray; 2.94 A; A=144-1102.
DR   PDB; 4F1S; X-ray; 3.00 A; A=144-1102.
DR   PDB; 4FA6; X-ray; 2.70 A; A=144-1102.
DR   PDB; 4FAD; X-ray; 2.70 A; A=144-1102.
DR   PDB; 4FHJ; X-ray; 2.60 A; A=144-1102.
DR   PDB; 4FHK; X-ray; 3.00 A; A=144-1102.
DR   PDB; 4FJY; X-ray; 2.90 A; A=144-1102.
DR   PDB; 4FJZ; X-ray; 3.00 A; A=144-1102.
DR   PDB; 4FLH; X-ray; 2.60 A; A=144-1102.
DR   PDB; 4FUL; X-ray; 2.47 A; A=144-1102.
DR   PDB; 4G11; X-ray; 3.40 A; A=144-1102.
DR   PDB; 4GB9; X-ray; 2.44 A; A=144-1102.
DR   PDB; 4HLE; X-ray; 2.78 A; A=144-1102.
DR   PDB; 4HVB; X-ray; 2.35 A; A=144-1102.
DR   PDB; 4J6I; X-ray; 2.90 A; A=144-1102.
DR   PDB; 4KZ0; X-ray; 2.87 A; A=144-1102.
DR   PDB; 4KZC; X-ray; 3.25 A; A=144-1102.
DR   PDB; 4PS3; X-ray; 2.90 A; A=144-1102.
DR   PDB; 4PS7; X-ray; 2.69 A; A=144-1102.
DR   PDB; 4PS8; X-ray; 2.99 A; A=144-1102.
DR   PDB; 4URK; X-ray; 2.90 A; A=144-1102.
DR   PDB; 4WWN; X-ray; 2.70 A; A=144-1102.
DR   PDB; 4WWO; X-ray; 2.30 A; A=144-1102.
DR   PDB; 4WWP; X-ray; 2.40 A; A=144-1102.
DR   PDB; 4XX5; X-ray; 2.76 A; A=144-1102.
DR   PDB; 4XZ4; X-ray; 2.60 A; A=144-1102.
DR   PDB; 5EDS; X-ray; 2.80 A; A=144-1102.
DR   PDB; 5G2N; X-ray; 2.68 A; A=144-1102.
DR   PDB; 5G55; X-ray; 2.45 A; A=144-1102.
DR   PDB; 5JHA; X-ray; 2.51 A; A=144-1102.
DR   PDB; 5JHB; X-ray; 2.48 A; A=144-1102.
DR   PDB; 5KAE; X-ray; 2.65 A; A=144-1102.
DR   PDB; 5OQ4; X-ray; 2.70 A; A=144-1102.
DR   PDB; 5T23; X-ray; 2.78 A; A=144-1102.
DR   PDB; 6AUD; X-ray; 2.02 A; A=144-1102.
DR   PDB; 6C1S; X-ray; 2.31 A; A=144-1102.
DR   PDB; 6FH5; X-ray; 2.84 A; A=144-1102.
DR   PDB; 6GQ7; X-ray; 2.84 A; A=144-1102.
DR   PDBsum; 1E8Y; -.
DR   PDBsum; 1E8Z; -.
DR   PDBsum; 1HE8; -.
DR   PDBsum; 2A4Z; -.
DR   PDBsum; 2A5U; -.
DR   PDBsum; 2CHW; -.
DR   PDBsum; 2CHX; -.
DR   PDBsum; 2CHZ; -.
DR   PDBsum; 2V4L; -.
DR   PDBsum; 3APC; -.
DR   PDBsum; 3APD; -.
DR   PDBsum; 3APF; -.
DR   PDBsum; 3CSF; -.
DR   PDBsum; 3CST; -.
DR   PDBsum; 3DBS; -.
DR   PDBsum; 3DPD; -.
DR   PDBsum; 3ENE; -.
DR   PDBsum; 3IBE; -.
DR   PDBsum; 3L08; -.
DR   PDBsum; 3L13; -.
DR   PDBsum; 3L16; -.
DR   PDBsum; 3L17; -.
DR   PDBsum; 3L54; -.
DR   PDBsum; 3LJ3; -.
DR   PDBsum; 3MJW; -.
DR   PDBsum; 3ML8; -.
DR   PDBsum; 3ML9; -.
DR   PDBsum; 3NZS; -.
DR   PDBsum; 3NZU; -.
DR   PDBsum; 3OAW; -.
DR   PDBsum; 3P2B; -.
DR   PDBsum; 3PRE; -.
DR   PDBsum; 3PRZ; -.
DR   PDBsum; 3PS6; -.
DR   PDBsum; 3QAQ; -.
DR   PDBsum; 3QAR; -.
DR   PDBsum; 3QJZ; -.
DR   PDBsum; 3QK0; -.
DR   PDBsum; 3R7Q; -.
DR   PDBsum; 3R7R; -.
DR   PDBsum; 3S2A; -.
DR   PDBsum; 3SD5; -.
DR   PDBsum; 3T8M; -.
DR   PDBsum; 3TJP; -.
DR   PDBsum; 3TL5; -.
DR   PDBsum; 3ZVV; -.
DR   PDBsum; 3ZW3; -.
DR   PDBsum; 4ANU; -.
DR   PDBsum; 4ANV; -.
DR   PDBsum; 4ANW; -.
DR   PDBsum; 4ANX; -.
DR   PDBsum; 4AOF; -.
DR   PDBsum; 4DK5; -.
DR   PDBsum; 4EZJ; -.
DR   PDBsum; 4EZK; -.
DR   PDBsum; 4EZL; -.
DR   PDBsum; 4F1S; -.
DR   PDBsum; 4FA6; -.
DR   PDBsum; 4FAD; -.
DR   PDBsum; 4FHJ; -.
DR   PDBsum; 4FHK; -.
DR   PDBsum; 4FJY; -.
DR   PDBsum; 4FJZ; -.
DR   PDBsum; 4FLH; -.
DR   PDBsum; 4FUL; -.
DR   PDBsum; 4G11; -.
DR   PDBsum; 4GB9; -.
DR   PDBsum; 4HLE; -.
DR   PDBsum; 4HVB; -.
DR   PDBsum; 4J6I; -.
DR   PDBsum; 4KZ0; -.
DR   PDBsum; 4KZC; -.
DR   PDBsum; 4PS3; -.
DR   PDBsum; 4PS7; -.
DR   PDBsum; 4PS8; -.
DR   PDBsum; 4URK; -.
DR   PDBsum; 4WWN; -.
DR   PDBsum; 4WWO; -.
DR   PDBsum; 4WWP; -.
DR   PDBsum; 4XX5; -.
DR   PDBsum; 4XZ4; -.
DR   PDBsum; 5EDS; -.
DR   PDBsum; 5G2N; -.
DR   PDBsum; 5G55; -.
DR   PDBsum; 5JHA; -.
DR   PDBsum; 5JHB; -.
DR   PDBsum; 5KAE; -.
DR   PDBsum; 5OQ4; -.
DR   PDBsum; 5T23; -.
DR   PDBsum; 6AUD; -.
DR   PDBsum; 6C1S; -.
DR   PDBsum; 6FH5; -.
DR   PDBsum; 6GQ7; -.
DR   SMR; P48736; -.
DR   BioGrid; 111312; 44.
DR   DIP; DIP-37781N; -.
DR   IntAct; P48736; 19.
DR   MINT; P48736; -.
DR   STRING; 9606.ENSP00000352121; -.
DR   BindingDB; P48736; -.
DR   ChEMBL; CHEMBL3267; -.
DR   DrugBank; DB07503; (5E)-5-[(2,2-DIFLUORO-1,3-BENZODIOXOL-5-YL)METHYLENE]-1,3-THIAZOLIDINE-2,4-DIONE.
DR   DrugBank; DB08300; 1-methyl-3-naphthalen-2-yl-1H-pyrazolo[3,4-d]pyrimidin-4-amine.
DR   DrugBank; DB06831; 2-((9H-PURIN-6-YLTHIO)METHYL)-5-CHLORO-3-(2-METHOXYPHENYL)QUINAZOLIN-4(3H)-ONE.
DR   DrugBank; DB07335; 3-[4-AMINO-1-(1-METHYLETHYL)-1H-PYRAZOLO[3,4-D]PYRIMIDIN-3-YL]PHENOL.
DR   DrugBank; DB07073; 5,5-dimethyl-2-morpholin-4-yl-5,6-dihydro-1,3-benzothiazol-7(4H)-one.
DR   DrugBank; DB04769; 5-QUINOXALIN-6-YLMETHYLENE-THIAZOLIDINE-2,4-DIONE.
DR   DrugBank; DB11952; Duvelisib.
DR   DrugBank; DB12010; Fostamatinib.
DR   DrugBank; DB02656; LY-294002.
DR   DrugBank; DB02375; Myricetin.
DR   DrugBank; DB06836; N-(5-{4-Chloro-3-[(2-hydroxyethyl)sulfamoyl]phenyl}-4-methyl-1,3-thiazol-2-yl)acetamide.
DR   DrugBank; DB04216; Quercetin.
DR   DrugBank; DB02010; Staurosporine.
DR   DrugBank; DB05552; TG100-115.
DR   DrugBank; DB08059; Wortmannin.
DR   DrugBank; DB05241; XL765.
DR   DrugCentral; P48736; -.
DR   GuidetoPHARMACOLOGY; 2156; -.
DR   SwissLipids; SLP:000000909; -.
DR   iPTMnet; P48736; -.
DR   PhosphoSitePlus; P48736; -.
DR   BioMuta; PIK3CG; -.
DR   DMDM; 92090623; -.
DR   EPD; P48736; -.
DR   jPOST; P48736; -.
DR   MassIVE; P48736; -.
DR   MaxQB; P48736; -.
DR   PaxDb; P48736; -.
DR   PeptideAtlas; P48736; -.
DR   PRIDE; P48736; -.
DR   ProteomicsDB; 55933; -.
DR   DNASU; 5294; -.
DR   Ensembl; ENST00000359195; ENSP00000352121; ENSG00000105851.
DR   Ensembl; ENST00000440650; ENSP00000392258; ENSG00000105851.
DR   Ensembl; ENST00000496166; ENSP00000419260; ENSG00000105851.
DR   GeneID; 5294; -.
DR   KEGG; hsa:5294; -.
DR   UCSC; uc003vdu.5; human.
DR   CTD; 5294; -.
DR   DisGeNET; 5294; -.
DR   EuPathDB; HostDB:ENSG00000105851.10; -.
DR   GeneCards; PIK3CG; -.
DR   HGNC; HGNC:8978; PIK3CG.
DR   HPA; HPA069976; -.
DR   MIM; 601232; gene.
DR   neXtProt; NX_P48736; -.
DR   OpenTargets; ENSG00000105851; -.
DR   PharmGKB; PA33311; -.
DR   eggNOG; KOG0904; Eukaryota.
DR   eggNOG; COG5032; LUCA.
DR   GeneTree; ENSGT00940000156858; -.
DR   HOGENOM; HOG000252912; -.
DR   InParanoid; P48736; -.
DR   KO; K21289; -.
DR   OMA; HSFFTKM; -.
DR   OrthoDB; 204282at2759; -.
DR   PhylomeDB; P48736; -.
DR   TreeFam; TF102031; -.
DR   BioCyc; MetaCyc:HS02818-MONOMER; -.
DR   BRENDA; 2.7.1.137; 2681.
DR   BRENDA; 2.7.1.153; 2681.
DR   Reactome; R-HSA-114604; GPVI-mediated activation cascade.
DR   Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
DR   Reactome; R-HSA-392451; G beta:gamma signalling through PI3Kgamma.
DR   Reactome; R-HSA-9027276; Erythropoietin activates Phosphoinositide-3-kinase (PI3K).
DR   SignaLink; P48736; -.
DR   SIGNOR; P48736; -.
DR   UniPathway; UPA00220; -.
DR   ChiTaRS; PIK3CG; human.
DR   EvolutionaryTrace; P48736; -.
DR   GeneWiki; PIK3CG; -.
DR   GenomeRNAi; 5294; -.
DR   Pharos; P48736; Tchem.
DR   PRO; PR:P48736; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; P48736; protein.
DR   Bgee; ENSG00000105851; Expressed in 144 organ(s), highest expression level in bone marrow.
DR   ExpressionAtlas; P48736; baseline and differential.
DR   Genevisible; P48736; HS.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0042629; C:mast cell granule; IEA:GOC.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IBA:GO_Central.
DR   GO; GO:0005944; C:phosphatidylinositol 3-kinase complex, class IB; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IBA:GO_Central.
DR   GO; GO:0035005; F:1-phosphatidylinositol-4-phosphate 3-kinase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046875; F:ephrin receptor binding; IPI:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0016301; F:kinase activity; IDA:MGI.
DR   GO; GO:0035004; F:phosphatidylinositol 3-kinase activity; TAS:UniProtKB.
DR   GO; GO:0052812; F:phosphatidylinositol-3,4-bisphosphate 5-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004672; F:protein kinase activity; TAS:UniProtKB.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0002250; P:adaptive immune response; TAS:UniProtKB.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
DR   GO; GO:0001816; P:cytokine production; TAS:UniProtKB.
DR   GO; GO:0002407; P:dendritic cell chemotaxis; TAS:UniProtKB.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0097284; P:hepatocyte apoptotic process; IEA:Ensembl.
DR   GO; GO:0006954; P:inflammatory response; TAS:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; TAS:UniProtKB.
DR   GO; GO:0043303; P:mast cell degranulation; TAS:UniProtKB.
DR   GO; GO:0035747; P:natural killer cell chemotaxis; TAS:UniProtKB.
DR   GO; GO:0055118; P:negative regulation of cardiac muscle contraction; TAS:UniProtKB.
DR   GO; GO:2000270; P:negative regulation of fibroblast apoptotic process; IEA:Ensembl.
DR   GO; GO:0010897; P:negative regulation of triglyceride catabolic process; IEA:Ensembl.
DR   GO; GO:0030593; P:neutrophil chemotaxis; TAS:UniProtKB.
DR   GO; GO:0072672; P:neutrophil extravasation; TAS:UniProtKB.
DR   GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IDA:UniProtKB.
DR   GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
DR   GO; GO:0046854; P:phosphatidylinositol phosphorylation; IBA:GO_Central.
DR   GO; GO:0036092; P:phosphatidylinositol-3-phosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IDA:MGI.
DR   GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR   GO; GO:0070527; P:platelet aggregation; TAS:UniProtKB.
DR   GO; GO:0002675; P:positive regulation of acute inflammatory response; IEA:Ensembl.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
DR   GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:UniProtKB.
DR   GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; TAS:Reactome.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:UniProtKB.
DR   GO; GO:1903169; P:regulation of calcium ion transmembrane transport; IEA:Ensembl.
DR   GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; TAS:UniProtKB.
DR   GO; GO:0002679; P:respiratory burst involved in defense response; TAS:UniProtKB.
DR   GO; GO:0032252; P:secretory granule localization; IEA:Ensembl.
DR   GO; GO:0042110; P:T cell activation; TAS:UniProtKB.
DR   GO; GO:0010818; P:T cell chemotaxis; TAS:UniProtKB.
DR   GO; GO:0042098; P:T cell proliferation; TAS:UniProtKB.
DR   Gene3D; 1.10.1070.11; -; 1.
DR   Gene3D; 1.25.40.70; -; 1.
DR   Gene3D; 2.60.40.150; -; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR   InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR   InterPro; IPR018936; PI3/4_kinase_CS.
DR   InterPro; IPR001263; PI3K_accessory_dom.
DR   InterPro; IPR042236; PI3K_accessory_sf.
DR   InterPro; IPR003113; PI3K_adapt-bd_dom.
DR   InterPro; IPR002420; PI3K_C2_dom.
DR   InterPro; IPR000341; PI3K_Ras-bd_dom.
DR   InterPro; IPR008290; PI3K_Vps34.
DR   InterPro; IPR015433; PI_Kinase.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR10048; PTHR10048; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   Pfam; PF00792; PI3K_C2; 1.
DR   Pfam; PF00794; PI3K_rbd; 1.
DR   Pfam; PF00613; PI3Ka; 1.
DR   PIRSF; PIRSF000587; PI3K_Vps34; 1.
DR   SMART; SM00142; PI3K_C2; 1.
DR   SMART; SM00144; PI3K_rbd; 1.
DR   SMART; SM00145; PI3Ka; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR   PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR   PROSITE; PS51544; PI3K_ABD; 1.
DR   PROSITE; PS51547; PI3K_C2; 1.
DR   PROSITE; PS51546; PI3K_RBD; 1.
DR   PROSITE; PS51545; PIK_HELICAL; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Angiogenesis; ATP-binding; Cell membrane; Chemotaxis;
KW   Cytoplasm; Endocytosis; Immunity; Inflammatory response; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..1102
FT                   /note="Phosphatidylinositol 4,5-bisphosphate 3-kinase
FT                   catalytic subunit gamma isoform"
FT                   /id="PRO_0000088792"
FT   DOMAIN          34..141
FT                   /note="PI3K-ABD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00877"
FT   DOMAIN          217..309
FT                   /note="PI3K-RBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00879"
FT   DOMAIN          357..521
FT                   /note="C2 PI3K-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00880"
FT   DOMAIN          541..723
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00878"
FT   DOMAIN          828..1073
FT                   /note="PI3K/PI4K"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   NP_BIND         829..838
FT                   /note="ATP"
FT                   /evidence="ECO:0000250"
FT   NP_BIND         864..872
FT                   /note="ATP"
FT                   /evidence="ECO:0000250"
FT   NP_BIND         961..969
FT                   /note="ATP"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        19..23
FT                   /note="Poly-Arg"
FT   MOD_RES         1024
FT                   /note="Phosphothreonine; by PKA"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JHG7"
FT   MOD_RES         1101
FT                   /note="Phosphoserine; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:12502714"
FT   MUTAGEN         833
FT                   /note="K->R: Reduced inflammatory reactions but no
FT                   alterations in cardiac contractility."
FT                   /evidence="ECO:0000269|PubMed:15294162"
FT   MUTAGEN         947
FT                   /note="R->P: Abolishes protein and lipid kinase activity.
FT                   Does not abolishes interaction with GRK2."
FT                   /evidence="ECO:0000269|PubMed:16094730"
FT   CONFLICT        30
FT                   /note="Missing (in Ref. 1; CAA58284)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        459
FT                   /note="Q -> R (in Ref. 1; CAA58284 and 3; AAG61115)"
FT                   /evidence="ECO:0000305"
FT   HELIX           145..158
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   HELIX           165..167
FT                   /evidence="ECO:0000244|PDB:3APC"
FT   STRAND          169..171
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   HELIX           172..179
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   HELIX           181..190
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   HELIX           193..198
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   HELIX           209..212
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   HELIX           213..215
FT                   /evidence="ECO:0000244|PDB:5G2N"
FT   STRAND          216..218
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   STRAND          220..226
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   STRAND          229..235
FT                   /evidence="ECO:0000244|PDB:6AUD"
FT   HELIX           241..243
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   HELIX           246..252
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   HELIX           256..259
FT                   /evidence="ECO:0000244|PDB:1HE8"
FT   STRAND          263..265
FT                   /evidence="ECO:0000244|PDB:1HE8"
FT   STRAND          271..274
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   STRAND          283..285
FT                   /evidence="ECO:0000244|PDB:6AUD"
FT   HELIX           287..289
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   HELIX           291..298
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   STRAND          303..308
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   HELIX           313..316
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   HELIX           354..356
FT                   /evidence="ECO:0000244|PDB:4ANV"
FT   STRAND          359..369
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   STRAND          375..377
FT                   /evidence="ECO:0000244|PDB:4ANW"
FT   STRAND          380..391
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   STRAND          393..398
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   STRAND          406..419
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   HELIX           420..422
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   STRAND          428..434
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   STRAND          462..469
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   STRAND          473..475
FT                   /evidence="ECO:0000244|PDB:4ANV"
FT   STRAND          478..483
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   STRAND          484..486
FT                   /evidence="ECO:0000244|PDB:5T23"
FT   HELIX           499..502
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   STRAND          511..513
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   STRAND          515..520
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   HELIX           549..560
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   STRAND          563..565
FT                   /evidence="ECO:0000244|PDB:4XX5"
FT   HELIX           569..577
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   HELIX           579..582
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   HELIX           586..588
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   HELIX           589..593
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   HELIX           601..612
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   HELIX           615..618
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   HELIX           624..630
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   STRAND          632..634
FT                   /evidence="ECO:0000244|PDB:1HE8"
FT   HELIX           638..648
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   HELIX           653..666
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   HELIX           667..669
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   STRAND          671..674
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   HELIX           676..687
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   HELIX           689..705
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   TURN            707..709
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   HELIX           710..721
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   TURN            722..724
FT                   /evidence="ECO:0000244|PDB:3ML8"
FT   HELIX           726..751
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   STRAND          755..757
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   HELIX           761..774
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   TURN            775..778
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   STRAND          783..785
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   STRAND          788..796
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   HELIX           798..800
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   STRAND          806..808
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   STRAND          811..818
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   STRAND          828..836
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   HELIX           838..856
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   TURN            857..859
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   STRAND          869..873
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   STRAND          876..880
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   STRAND          885..887
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   HELIX           888..895
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   STRAND          898..900
FT                   /evidence="ECO:0000244|PDB:3LJ3"
FT   HELIX           906..914
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   STRAND          915..917
FT                   /evidence="ECO:0000244|PDB:2A4Z"
FT   HELIX           918..941
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   HELIX           949..951
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   STRAND          952..955
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   TURN            956..958
FT                   /evidence="ECO:0000244|PDB:1HE8"
FT   STRAND          960..962
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   HELIX           965..970
FT                   /evidence="ECO:0000244|PDB:3L54"
FT   HELIX           989..994
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   TURN            998..1000
FT                   /evidence="ECO:0000244|PDB:4ANV"
FT   HELIX           1004..1021
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   HELIX           1024..1038
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   STRAND          1039..1041
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   TURN            1042..1045
FT                   /evidence="ECO:0000244|PDB:3PRE"
FT   HELIX           1046..1054
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   TURN            1055..1058
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   HELIX           1061..1078
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   HELIX           1081..1085
FT                   /evidence="ECO:0000244|PDB:1E8Y"
FT   TURN            1090..1092
FT                   /evidence="ECO:0000244|PDB:5G55"
SQ   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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