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P48736 (PK3CG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform

Short name=PI3-kinase subunit gamma
Short name=PI3K-gamma
Short name=PI3Kgamma
Short name=PtdIns-3-kinase subunit gamma
EC=2.7.1.153
Alternative name(s):
Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit gamma
Short name=PtdIns-3-kinase subunit p110-gamma
Short name=p110gamma
Phosphoinositide-3-kinase catalytic gamma polypeptide
Serine/threonine protein kinase PIK3CG
EC=2.7.11.1
p120-PI3K
Gene names
Name:PIK3CG
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1102 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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 ADRBK1 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. Ref.1 Ref.9 Ref.11 Ref.13 Ref.18

Catalytic activity

ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate.

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. Ref.1 Ref.20

Pathway

Phospholipid metabolism; phosphatidylinositol phosphate biosynthesis.

Subunit structure

Heterodimer of a catalytic subunit PIK3CG and a PIK3R5 or PIK3R6 regulatory subunit. Interacts with ADRBK1 through the PIK helical domain. Interaction with ADRBK1 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. Ref.8 Ref.9 Ref.12 Ref.13

Subcellular location

Cytoplasm. Cell membrane Ref.9.

Tissue specificity

Pancreas, skeletal muscle, liver and heart. Ref.1

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 (Ref.15).

Sequence similarities

Belongs to the PI3/PI4-kinase family.

Contains 1 C2 PI3K-type domain.

Contains 1 PI3K-ABD domain.

Contains 1 PI3K-RBD domain.

Contains 1 PI3K/PI4K domain.

Contains 1 PIK helical domain.

Ontologies

Keywords
   Biological processAngiogenesis
Chemotaxis
Endocytosis
Immunity
Inflammatory response
   Cellular componentCell membrane
Cytoplasm
Membrane
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Inferred from direct assay PubMed 12507995. Source: UniProtKB

T cell activation

Traceable author statement Ref.14. Source: UniProtKB

T cell chemotaxis

Traceable author statement Ref.15. Source: UniProtKB

T cell proliferation

Traceable author statement PubMed 19075988. Source: UniProtKB

adaptive immune response

Traceable author statement Ref.14. Source: UniProtKB

angiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

blood coagulation

Traceable author statement. Source: Reactome

cytokine production

Traceable author statement PubMed 19075988. Source: UniProtKB

dendritic cell chemotaxis

Traceable author statement Ref.15. Source: UniProtKB

endocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

hepatocyte apoptotic process

Inferred from electronic annotation. Source: Ensembl

inflammatory response

Traceable author statement Ref.14. Source: UniProtKB

innate immune response

Traceable author statement Ref.14. Source: UniProtKB

mast cell degranulation

Traceable author statement Ref.14. Source: UniProtKB

natural killer cell chemotaxis

Traceable author statement Ref.15. Source: UniProtKB

negative regulation of cardiac muscle contraction

Traceable author statement Ref.16. Source: UniProtKB

negative regulation of fibroblast apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of triglyceride catabolic process

Inferred from electronic annotation. Source: Ensembl

neutrophil chemotaxis

Traceable author statement Ref.14. Source: UniProtKB

neutrophil extravasation

Traceable author statement Ref.15. Source: UniProtKB

phosphatidylinositol 3-kinase signaling

Inferred from direct assay PubMed 12507995. Source: UniProtKB

phosphatidylinositol biosynthetic process

Traceable author statement. Source: Reactome

phospholipid metabolic process

Traceable author statement. Source: Reactome

platelet activation

Traceable author statement. Source: Reactome

platelet aggregation

Traceable author statement PubMed 21035500. Source: UniProtKB

positive regulation of MAP kinase activity

Inferred from direct assay PubMed 12507995. Source: UniProtKB

positive regulation of acute inflammatory response

Inferred from electronic annotation. Source: Ensembl

positive regulation of cytosolic calcium ion concentration

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein kinase B signaling

Inferred from direct assay PubMed 12507995. Source: UniProtKB

regulation of cell adhesion mediated by integrin

Traceable author statement Ref.15. Source: UniProtKB

respiratory burst involved in defense response

Traceable author statement PubMed 19075988. Source: UniProtKB

secretory granule localization

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_component1-phosphatidylinositol-4-phosphate 3-kinase, class IB complex

Inferred from direct assay PubMed 12507995. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 12507995. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

mast cell granule

Traceable author statement Ref.14. Source: GOC

membrane

Inferred from direct assay PubMed 12507995. Source: UniProtKB

plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_function1-phosphatidylinositol-3-kinase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

1-phosphatidylinositol-4-phosphate 3-kinase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ephrin receptor binding

Inferred from physical interaction Ref.8. Source: UniProtKB

phosphatidylinositol 3-kinase activity

Traceable author statement Ref.14. Source: UniProtKB

phosphatidylinositol-4,5-bisphosphate 3-kinase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein binding

Inferred from physical interaction PubMed 12507995Ref.18. Source: IntAct

protein kinase activity

Traceable author statement PubMed 19376709. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PDE3BQ133703EBI-1030384,EBI-6172856
PIK3R5O026966EBI-1030384,EBI-6172343From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11021102Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
PRO_0000088792

Regions

Domain34 – 141108PI3K-ABD
Domain217 – 30993PI3K-RBD
Domain357 – 521165C2 PI3K-type
Domain541 – 723183PIK helical
Domain828 – 1073246PI3K/PI4K
Nucleotide binding829 – 83810ATP By similarity
Nucleotide binding864 – 8729ATP By similarity
Nucleotide binding961 – 9699ATP By similarity
Compositional bias19 – 235Poly-Arg

Amino acid modifications

Modified residue10241Phosphothreonine; by PKA By similarity
Modified residue11011Phosphoserine; by autocatalysis Ref.10

Experimental info

Mutagenesis8331K → R: Reduced inflammatory reactions but no alterations in cardiac contractility. Ref.11
Mutagenesis9471R → P: Abolishes protein and lipid kinase activity. Does not abolishes interaction with ADRBK1. Ref.13
Sequence conflict301Missing in CAA58284. Ref.1
Sequence conflict4591Q → R in CAA58284. Ref.1
Sequence conflict4591Q → R in AAG61115. Ref.3

Secondary structure

.................................................................................................................................................................. 1102
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P48736 [UniParc].

Last modified April 4, 2006. Version 3.
Checksum: EF2B1A0E1CBEF406

FASTA1,102126,454
        10         20         30         40         50         60 
MELENYKQPV VLREDNCRRR RRMKPRSAAA SLSSMELIPI EFVLPTSQRK CKSPETALLH 

        70         80         90        100        110        120 
VAGHGNVEQM KAQVWLRALE TSVAADFYHR LGPHHFLLLY QKKGQWYEIY DKYQVVQTLD 

       130        140        150        160        170        180 
CLRYWKATHR SPGQIHLVQR HPPSEESQAF QRQLTALIGY DVTDVSNVHD DELEFTRRGL 

       190        200        210        220        230        240 
VTPRMAEVAS RDPKLYAMHP WVTSKPLPEY LWKKIANNCI FIVIHRSTTS QTIKVSPDDT 

       250        260        270        280        290        300 
PGAILQSFFT KMAKKKSLMD IPESQSEQDF VLRVCGRDEY LVGETPIKNF QWVRHCLKNG 

       310        320        330        340        350        360 
EEIHVVLDTP PDPALDEVRK EEWPLVDDCT GVTGYHEQLT IHGKDHESVF TVSLWDCDRK 

       370        380        390        400        410        420 
FRVKIRGIDI PVLPRNTDLT VFVEANIQHG QQVLCQRRTS PKPFTEEVLW NVWLEFSIKI 

       430        440        450        460        470        480 
KDLPKGALLN LQIYCGKAPA LSSKASAESP SSESKGKVQL LYYVNLLLID HRFLLRRGEY 

       490        500        510        520        530        540 
VLHMWQISGK GEDQGSFNAD KLTSATNPDK ENSMSISILL DNYCHPIALP KHQPTPDPEG 

       550        560        570        580        590        600 
DRVRAEMPNQ LRKQLEAIIA TDPLNPLTAE DKELLWHFRY ESLKHPKAYP KLFSSVKWGQ 

       610        620        630        640        650        660 
QEIVAKTYQL LARREVWDQS ALDVGLTMQL LDCNFSDENV RAIAVQKLES LEDDDVLHYL 

       670        680        690        700        710        720 
LQLVQAVKFE PYHDSALARF LLKRGLRNKR IGHFLFWFLR SEIAQSRHYQ QRFAVILEAY 

       730        740        750        760        770        780 
LRGCGTAMLH DFTQQVQVIE MLQKVTLDIK SLSAEKYDVS SQVISQLKQK LENLQNSQLP 

       790        800        810        820        830        840 
ESFRVPYDPG LKAGALAIEK CKVMASKKKP LWLEFKCADP TALSNETIGI IFKHGDDLRQ 

       850        860        870        880        890        900 
DMLILQILRI MESIWETESL DLCLLPYGCI STGDKIGMIE IVKDATTIAK IQQSTVGNTG 

       910        920        930        940        950        960 
AFKDEVLNHW LKEKSPTEEK FQAAVERFVY SCAGYCVATF VLGIGDRHND NIMITETGNL 

       970        980        990       1000       1010       1020 
FHIDFGHILG NYKSFLGINK ERVPFVLTPD FLFVMGTSGK KTSPHFQKFQ DICVKAYLAL 

      1030       1040       1050       1060       1070       1080 
RHHTNLLIIL FSMMLMTGMP QLTSKEDIEY IRDALTVGKN EEDAKKYFLD QIEVCRDKGW 

      1090       1100 
TVQFNWFLHL VLGIKQGEKH SA 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of a G protein-activated human phosphoinositide-3 kinase."
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.
Science 269:690-693(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, TISSUE SPECIFICITY.
[2]Waterfield M.D.
Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Regulation of a G-protein-activated phosphoinositide-3-kinase."
Michalke M., Schaefer M., Stoyanov B., Wetzker R., Nuernberg B.
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"The DNA sequence of human chromosome 7."
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. expand/collapse author list , 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.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"Human chromosome 7: DNA sequence and biology."
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. expand/collapse author list , 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.
Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Pancreas.
[8]"The EphA8 receptor regulates integrin activity through p110gamma phosphatidylinositol-3 kinase in a tyrosine kinase activity-independent manner."
Gu C., Park S.
Mol. Cell. Biol. 21:4579-4597(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EPHA8.
[9]"Phosphoinositide 3-kinase regulates beta2-adrenergic receptor endocytosis by AP-2 recruitment to the receptor/beta-arrestin complex."
Naga Prasad S.V., Laporte S.A., Chamberlain D., Caron M.G., Barak L., Rockman H.A.
J. Cell Biol. 158:563-575(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ADRBK1.
[10]"Identification and characterization of the autophosphorylation sites of phosphoinositide 3-kinase isoforms beta and gamma."
Czupalla C., Culo M., Muller E.C., Brock C., Reusch H.P., Spicher K., Krause E., Nurnberg B.
J. Biol. Chem. 278:11536-11545(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-1101.
[11]"PI3Kgamma modulates the cardiac response to chronic pressure overload by distinct kinase-dependent and -independent effects."
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.
Cell 118:375-387(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CARDIAC CONTRACTILITY, MUTAGENESIS OF LYS-833.
[12]"p84, a new Gbetagamma-activated regulatory subunit of the type IB phosphoinositide 3-kinase p110gamma."
Suire S., Coadwell J., Ferguson G.J., Davidson K., Hawkins P., Stephens L.
Curr. Biol. 15:566-570(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PIK3R5.
[13]"Protein kinase activity of phosphoinositide 3-kinase regulates beta-adrenergic receptor endocytosis."
Naga Prasad S.V., Jayatilleke A., Madamanchi A., Rockman H.A.
Nat. Cell Biol. 7:785-796(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A PROTEIN KINASE, INTERACTION WITH ADRBK1 AND TPM2, MUTAGENESIS OF ARG-947.
[14]"PI3K delta and PI3K gamma: partners in crime in inflammation in rheumatoid arthritis and beyond?"
Rommel C., Camps M., Ji H.
Nat. Rev. Immunol. 7:191-201(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[15]"Targeting phosphoinositide 3-kinase gamma to fight inflammation and more."
Barberis L., Hirsch E.
Thromb. Haemost. 99:279-285(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION IN LEUKOCYTES AND ENDOTHELIAL CELLS, REVIEW ON ANTINFLAMMATORY THERAPY TARGET.
[16]"Cardiac regulation by phosphoinositide 3-kinases and PTEN."
Oudit G.Y., Penninger J.M.
Cardiovasc. Res. 82:250-260(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION IN CARDIAC CONTRACTILITY.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"A phosphodiesterase 3B-based signaling complex integrates exchange protein activated by cAMP 1 and phosphatidylinositol 3-kinase signals in human arterial endothelial cells."
Wilson L.S., Baillie G.S., Pritchard L.M., Umana B., Terrin A., Zaccolo M., Houslay M.D., Maurice D.H.
J. Biol. Chem. 286:16285-16296(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[19]"Structural insights into phosphoinositide 3-kinase catalysis and signalling."
Walker E.H., Perisic O., Ried C., Stephens L., Williams R.L.
Nature 402:313-320(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 144-1102.
[20]"Blockade of PI3Kgamma suppresses joint inflammation and damage in mouse models of rheumatoid arthritis."
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.
Nat. Med. 11:936-943(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 144-1101 IN A COMPLEX WITH AS-604850 AND AS-605240, ENZYME REGULATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X83368 mRNA. Translation: CAA58284.1.
AF327656 mRNA. Translation: AAG61115.1.
AC005018 Genomic DNA. Translation: AAQ96873.1.
CH236947 Genomic DNA. Translation: EAL24396.1.
CH471070 Genomic DNA. Translation: EAW83387.1.
BC035683 mRNA. Translation: AAH35683.1.
CCDSCCDS5739.1.
RefSeqNP_001269355.1. NM_001282426.1.
NP_001269356.1. NM_001282427.1.
NP_002640.2. NM_002649.3.
XP_005250500.1. XM_005250443.1.
UniGeneHs.32942.
Hs.561747.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E8YX-ray2.00A144-1102[»]
1E8ZX-ray2.40A144-1102[»]
1HE8X-ray3.00A144-1102[»]
2A4ZX-ray2.90A144-1102[»]
2A5UX-ray2.70A144-1102[»]
2CHWX-ray2.60A144-1102[»]
2CHXX-ray2.50A144-1102[»]
2CHZX-ray2.60A144-1102[»]
2V4LX-ray2.50A144-1102[»]
3APCX-ray2.54A144-1102[»]
3APDX-ray2.55A144-1102[»]
3APFX-ray2.82A144-1102[»]
3CSFX-ray2.80A144-1102[»]
3CSTX-ray3.20A144-1102[»]
3DBSX-ray2.80A144-1102[»]
3DPDX-ray2.85A144-1102[»]
3ENEX-ray2.40A144-1102[»]
3IBEX-ray2.80A144-1102[»]
3L08X-ray2.70A144-1102[»]
3L13X-ray3.00A144-1102[»]
3L16X-ray2.90A144-1102[»]
3L17X-ray3.00A144-1102[»]
3L54X-ray2.30A144-1102[»]
3LJ3X-ray2.43A144-1102[»]
3MJWX-ray2.87A144-1102[»]
3ML8X-ray2.70A144-1102[»]
3ML9X-ray2.55A144-1102[»]
3NZSX-ray2.75A147-1094[»]
3NZUX-ray2.60A147-1094[»]
3OAWX-ray2.75A144-1102[»]
3P2BX-ray3.20A144-1102[»]
3PREX-ray2.91A144-1102[»]
3PRZX-ray2.60A144-1102[»]
3PS6X-ray2.60A144-1102[»]
3QAQX-ray2.90A144-1102[»]
3QARX-ray2.65A144-1102[»]
3QJZX-ray2.90A144-1102[»]
3QK0X-ray2.85A144-1102[»]
3R7QX-ray2.50A144-1102[»]
3R7RX-ray2.90A144-1102[»]
3S2AX-ray2.55A144-1102[»]
3SD5X-ray3.20A144-1102[»]
3T8MX-ray2.50A144-1102[»]
3TJPX-ray2.70A144-1102[»]
3TL5X-ray2.79A144-1102[»]
3ZVVX-ray2.50A144-1102[»]
3ZW3X-ray2.80A144-1102[»]
4ANUX-ray2.81A144-1102[»]
4ANVX-ray2.13A144-1102[»]
4ANWX-ray2.31A144-1102[»]
4ANXX-ray2.73A144-1102[»]
4AOFX-ray3.30A144-1102[»]
4DK5X-ray2.95A144-1102[»]
4EZJX-ray2.67A144-1102[»]
4EZKX-ray2.80A144-1102[»]
4EZLX-ray2.94A144-1102[»]
4F1SX-ray3.00A144-1102[»]
4FA6X-ray2.70A144-1102[»]
4FADX-ray2.70A144-1102[»]
4FHJX-ray2.60A144-1102[»]
4FHKX-ray3.00A144-1102[»]
4FJYX-ray2.90A144-1102[»]
4FJZX-ray3.00A144-1102[»]
4FLHX-ray2.60A144-1102[»]
4FULX-ray2.47A144-1102[»]
4G11X-ray3.40A144-1102[»]
4GB9X-ray2.44A144-1102[»]
4HLEX-ray2.78A144-1102[»]
4HVBX-ray2.35A144-1102[»]
4J6IX-ray2.90A144-1102[»]
4KZ0X-ray2.87A144-1102[»]
4KZCX-ray3.25A144-1102[»]
4PS3X-ray2.90A144-1102[»]
4PS7X-ray2.69A144-1102[»]
4PS8X-ray2.99A144-1102[»]
ProteinModelPortalP48736.
SMRP48736. Positions 144-1089.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111312. 17 interactions.
DIPDIP-37781N.
IntActP48736. 11 interactions.
MINTMINT-155782.
STRING9606.ENSP00000352121.

Chemistry

BindingDBP48736.
ChEMBLCHEMBL3267.
GuidetoPHARMACOLOGY2156.

PTM databases

PhosphoSiteP48736.

Polymorphism databases

DMDM92090623.

Proteomic databases

MaxQBP48736.
PaxDbP48736.
PRIDEP48736.

Protocols and materials databases

DNASU5294.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000359195; ENSP00000352121; ENSG00000105851.
ENST00000440650; ENSP00000392258; ENSG00000105851.
ENST00000496166; ENSP00000419260; ENSG00000105851.
GeneID5294.
KEGGhsa:5294.
UCSCuc003vdu.3. human.

Organism-specific databases

CTD5294.
GeneCardsGC07P106505.
HGNCHGNC:8978. PIK3CG.
MIM601232. gene.
neXtProtNX_P48736.
PharmGKBPA33311.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5032.
HOGENOMHOG000252912.
HOVERGENHBG101026.
InParanoidP48736.
KOK00922.
OMAYHEQLTI.
OrthoDBEOG70CR65.
PhylomeDBP48736.
TreeFamTF102031.

Enzyme and pathway databases

BioCycMetaCyc:HS02818-MONOMER.
BRENDA2.7.1.137. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_604. Hemostasis.
SignaLinkP48736.
UniPathwayUPA00220.

Gene expression databases

ArrayExpressP48736.
BgeeP48736.
CleanExHS_PIK3CG.
GenevestigatorP48736.

Family and domain databases

Gene3D1.10.1070.11. 1 hit.
1.25.40.70. 1 hit.
2.60.40.150. 1 hit.
InterProIPR016024. ARM-type_fold.
IPR000008. C2_dom.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR003113. PI3K_adapt-bd_dom.
IPR002420. PI3K_C2_dom.
IPR000341. PI3K_Ras-bd_dom.
IPR015433. PI_Kinase.
IPR001263. PInositide-3_kin_accessory_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERPTHR10048. PTHR10048. 1 hit.
PfamPF00454. PI3_PI4_kinase. 1 hit.
PF00792. PI3K_C2. 1 hit.
PF00794. PI3K_rbd. 1 hit.
PF00613. PI3Ka. 1 hit.
[Graphical view]
SMARTSM00142. PI3K_C2. 1 hit.
SM00144. PI3K_rbd. 1 hit.
SM00145. PI3Ka. 1 hit.
SM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
SSF49562. SSF49562. 1 hit.
SSF54236. SSF54236. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00915. PI3_4_KINASE_1. 1 hit.
PS00916. PI3_4_KINASE_2. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
PS51544. PI3K_ABD. 1 hit.
PS51547. PI3K_C2. 1 hit.
PS51546. PI3K_RBD. 1 hit.
PS51545. PIK_HELICAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP48736.
GeneWikiPIK3CG.
GenomeRNAi5294.
NextBio20458.
PROP48736.
SOURCESearch...

Entry information

Entry namePK3CG_HUMAN
AccessionPrimary (citable) accession number: P48736
Secondary accession number(s): A4D0Q6, Q8IV23, Q9BZC8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: April 4, 2006
Last modified: July 9, 2014
This is version 149 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM