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Q9JHG7

- PK3CG_MOUSE

UniProt

Q9JHG7 - PK3CG_MOUSE

Protein

Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform

Gene

Pik3cg

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    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. Contribute 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 By similarity.By similarity

    Catalytic activityi

    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 regulationi

    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 subunit PIK3R5 leading to the translocation from the cytosol to the plasma membrane and to kinase activation; the respective activation involving PIK3R6 requires HRAS for membrane recruitment. Wortmannin sensitive in nM range. Inhibited by AS252424.2 Publications

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi829 – 83810ATPBy similarity
    Nucleotide bindingi864 – 8729ATPBy similarity
    Nucleotide bindingi961 – 9699ATPBy similarity

    GO - Molecular functioni

    1. 1-phosphatidylinositol-3-kinase activity Source: RefGenome
    2. 1-phosphatidylinositol-4-phosphate 3-kinase activity Source: RefGenome
    3. ATP binding Source: UniProtKB-KW
    4. phosphatidylinositol-4,5-bisphosphate 3-kinase activity Source: RefGenome
    5. protein serine/threonine kinase activity Source: UniProtKB-KW

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. chemotaxis Source: UniProtKB-KW
    3. endocytosis Source: UniProtKB-KW
    4. G-protein coupled receptor signaling pathway Source: Ensembl
    5. hepatocyte apoptotic process Source: Ensembl
    6. immune system process Source: UniProtKB-KW
    7. inflammatory response Source: UniProtKB-KW
    8. negative regulation of fibroblast apoptotic process Source: MGI
    9. negative regulation of triglyceride catabolic process Source: Ensembl
    10. phosphatidylinositol 3-kinase signaling Source: Ensembl
    11. positive regulation of acute inflammatory response Source: Ensembl
    12. positive regulation of cytosolic calcium ion concentration Source: Ensembl
    13. positive regulation of MAP kinase activity Source: Ensembl
    14. positive regulation of protein kinase B signaling Source: Ensembl
    15. protein phosphorylation Source: MGI
    16. secretory granule localization Source: Ensembl

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Angiogenesis, Chemotaxis, Endocytosis, Immunity, Inflammatory response

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.1.153. 3474.
    ReactomeiREACT_198973. Synthesis of PIPs at the plasma membrane.
    REACT_220092. GPVI-mediated activation cascade.
    REACT_223974. G beta:gamma signalling through PI3Kgamma.
    UniPathwayiUPA00220.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform (EC:2.7.1.153)
    Short name:
    PI3-kinase subunit gamma
    Short name:
    PI3K-gamma
    Short name:
    PI3Kgamma
    Short name:
    PtdIns-3-kinase subunit gamma
    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 namesi
    Name:Pik3cg
    Synonyms:Pi3kg1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 12

    Organism-specific databases

    MGIiMGI:1353576. Pik3cg.

    Subcellular locationi

    Cytoplasm By similarity. Cell membrane By similarity

    GO - Cellular componenti

    1. 1-phosphatidylinositol-4-phosphate 3-kinase, class IB complex Source: Ensembl
    2. phosphatidylinositol 3-kinase complex Source: RefGenome
    3. plasma membrane Source: RefGenome

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Viable and fertile. Display abnormalities when the immune system is stressed. Reduced leukocyte migration in response to chemotactic agents and towards the site of inflammation. Reduced neutrophil oxidative burst in response to chemotactic agents. Reduced thymocyte survival and defective T lymphocyte activation. Protected from leukocyte infiltration of synovia in a model of rheumatoid arthritis. Dendritic cell showed reduced response to chemokines and migration to draining lymph nodes under inflammatory conditions. Platelets have defects in thrombus formation. Increased cardiac contractility. Display myocardial damage after transverse aortic constriction.7 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11021102Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoformPRO_0000088793Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1024 – 10241Phosphothreonine; by PKA1 Publication
    Modified residuei1101 – 11011Phosphoserine; by autocatalysisBy similarity

    Post-translational modificationi

    Phosphorylated at Thr-1024 by PKA. Phosphorylation inhibits lipid kinase activity.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiQ9JHG7.

    PTM databases

    PhosphoSiteiQ9JHG7.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9JHG7.
    BgeeiQ9JHG7.
    GenevestigatoriQ9JHG7.

    Interactioni

    Subunit structurei

    Heterodimer of a catalytic subunit PIK3CG and a PIK3R5 or PIK3R6 regulatory subunit. Interacts with ADRBK1 through the PIK helical domain By similarity. Interaction with ADRBK1 is required for targeting to agonist-occupied receptor. Interacts with PDE3B. Interacts with TPM2 By similarity. 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 similarity3 Publications

    Protein-protein interaction databases

    BioGridi206031. 2 interactions.
    DIPiDIP-41862N.
    IntActiQ9JHG7. 6 interactions.
    MINTiMINT-1612546.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9JHG7.
    SMRiQ9JHG7. Positions 144-1094.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini34 – 141108PI3K-ABDPROSITE-ProRule annotationAdd
    BLAST
    Domaini217 – 30993PI3K-RBDPROSITE-ProRule annotationAdd
    BLAST
    Domaini357 – 521165C2 PI3K-typePROSITE-ProRule annotationAdd
    BLAST
    Domaini541 – 723183PIK helicalPROSITE-ProRule annotationAdd
    BLAST
    Domaini828 – 1073246PI3K/PI4KPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi18 – 225Poly-Arg

    Sequence similaritiesi

    Belongs to the PI3/PI4-kinase family.PROSITE-ProRule annotation
    Contains 1 C2 PI3K-type domain.PROSITE-ProRule annotation
    Contains 1 PI3K-ABD domain.PROSITE-ProRule annotation
    Contains 1 PI3K-RBD domain.PROSITE-ProRule annotation
    Contains 1 PI3K/PI4K domain.PROSITE-ProRule annotation
    Contains 1 PIK helical domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5032.
    GeneTreeiENSGT00620000087742.
    HOGENOMiHOG000252912.
    HOVERGENiHBG101026.
    KOiK00922.
    OMAiYHEQLTI.
    OrthoDBiEOG70CR65.
    PhylomeDBiQ9JHG7.
    TreeFamiTF102031.

    Family and domain databases

    Gene3Di1.10.1070.11. 1 hit.
    1.25.40.70. 1 hit.
    2.60.40.150. 1 hit.
    InterProiIPR016024. 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]
    PANTHERiPTHR10048. PTHR10048. 1 hit.
    PfamiPF00454. PI3_PI4_kinase. 1 hit.
    PF00792. PI3K_C2. 1 hit.
    PF00794. PI3K_rbd. 1 hit.
    PF00613. PI3Ka. 1 hit.
    [Graphical view]
    SMARTiSM00142. PI3K_C2. 1 hit.
    SM00144. PI3K_rbd. 1 hit.
    SM00145. PI3Ka. 1 hit.
    SM00146. PI3Kc. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 1 hit.
    SSF49562. SSF49562. 1 hit.
    SSF54236. SSF54236. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS00915. 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]

    Sequencei

    Sequence statusi: Complete.

    Q9JHG7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MELENYEQPV VLREDNLRRR RRMKPRSAAG SLSSMELIPI EFVLPTSQRI     50
    SKTPETALLH VAGHGNVEQM KAQVWLRALE TSVAAEFYHR LGPDQFLLLY 100
    QKKGQWYEIY DRYQVVQTLD CLHYWKLMHK SPGQIHVVQR HVPSEETLAF 150
    QKQLTSLIGY DVTDISNVHD DELEFTRRRL VTPRMAEVAG RDAKLYAMHP 200
    WVTSKPLPDY LSKKIANNCI FIVIHRGTTS QTIKVSADDT PGTILQSFFT 250
    KMAKKKSLMN ISESQSEQDF VLRVCGRDEY LVGETPLKNF QWVRQCLKNG 300
    DEIHLVLDTP PDPALDEVRK EEWPLVDDCT GVTGYHEQLT IHGKDHESVF 350
    TVSLWDCDRK FRVKIRGIDI PVLPRNTDLT VFVEANIQHG QQVLCQRRTS 400
    PKPFAEEVLW NVWLEFGIKI KDLPKGALLN LQIYCCKTPS LSSKASAETP 450
    GSESKGKAQL LYYVNLLLID HRFLLRHGDY VLHMWQISGK AEEQGSFNAD 500
    KLTSATNPDK ENSMSISILL DNYCHPIALP KHRPTPDPEG DRVRAEMPNQ 550
    LRKQLEAIIA TDPLNPLTAE DKELLWHFRY ESLKHPKAYP KLFSSVKWGQ 600
    QEIVAKTYQL LARREIWDQS ALDVGLTMQL LDCNFSDENV RAIAVQKLES 650
    LEDDDVLHYL LQLVQAVKFE PYHDSALARF LLKRGLRNKR IGHFLFWFLR 700
    SEIAQSRHYQ QRFAVILEAY LRGCGTAMLQ DFTQQVHVIE MLQKVTIDIK 750
    SLSAEKYDVS SQVISQLKQK LESLQNSNLP ESFRVPYDPG LKAGTLVIEK 800
    CKVMASKKKP LWLEFKCADP TVLSNETIGI IFKHGDDLRQ DMLILQILRI 850
    MESIWETESL DLCLLPYGCI STGDKIGMIE IVKDATTIAQ IQQSTVGNTG 900
    AFKDEVLNHW LKEKCPIEEK FQAAVERFVY SCAGYCVATF VLGIGDRHND 950
    NIMISETGNL FHIDFGHILG NYKSFLGINK ERVPFVLTPD FLFVMGSSGK 1000
    KTSPHFQKFQ DVCVRAYLAL RHHTNLLIIL FSMMLMTGMP QLTSKEDIEY 1050
    IRDALTVGKS EEDAKKYFLD QIEVCRDKGW TVQFNWFLHL VLGIKQGEKH 1100
    SA 1102
    Length:1,102
    Mass (Da):126,400
    Last modified:July 27, 2011 - v2
    Checksum:i7675848792D76734
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti262 – 2621S → P in CAB89686. (PubMed:11054537)Curated
    Sequence conflicti262 – 2621S → P in CAB89851. (PubMed:11054537)Curated
    Sequence conflicti350 – 3501F → V in CAB89686. (PubMed:11054537)Curated
    Sequence conflicti350 – 3501F → V in CAB89851. (PubMed:11054537)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ249280 mRNA. Translation: CAB89686.1.
    AJ249413
    , AJ249414, AJ249415, AJ249416, AJ249417, AJ249418, AJ249419, AJ249420 Genomic DNA. Translation: CAB89851.1.
    BC051246 mRNA. Translation: AAH51246.1.
    CCDSiCCDS25870.1.
    RefSeqiNP_001139672.1. NM_001146200.1.
    NP_001139673.1. NM_001146201.1.
    NP_064668.2. NM_020272.2.
    XP_006515175.1. XM_006515112.1.
    UniGeneiMm.101369.
    Mm.404021.

    Genome annotation databases

    EnsembliENSMUST00000053215; ENSMUSP00000062864; ENSMUSG00000020573.
    ENSMUST00000085469; ENSMUSP00000082596; ENSMUSG00000020573.
    ENSMUST00000156904; ENSMUSP00000123539; ENSMUSG00000020573.
    GeneIDi30955.
    KEGGimmu:30955.
    UCSCiuc007nib.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ249280 mRNA. Translation: CAB89686.1 .
    AJ249413
    , AJ249414 , AJ249415 , AJ249416 , AJ249417 , AJ249418 , AJ249419 , AJ249420 Genomic DNA. Translation: CAB89851.1 .
    BC051246 mRNA. Translation: AAH51246.1 .
    CCDSi CCDS25870.1.
    RefSeqi NP_001139672.1. NM_001146200.1.
    NP_001139673.1. NM_001146201.1.
    NP_064668.2. NM_020272.2.
    XP_006515175.1. XM_006515112.1.
    UniGenei Mm.101369.
    Mm.404021.

    3D structure databases

    ProteinModelPortali Q9JHG7.
    SMRi Q9JHG7. Positions 144-1094.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 206031. 2 interactions.
    DIPi DIP-41862N.
    IntActi Q9JHG7. 6 interactions.
    MINTi MINT-1612546.

    Chemistry

    ChEMBLi CHEMBL2189158.

    PTM databases

    PhosphoSitei Q9JHG7.

    Proteomic databases

    PRIDEi Q9JHG7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000053215 ; ENSMUSP00000062864 ; ENSMUSG00000020573 .
    ENSMUST00000085469 ; ENSMUSP00000082596 ; ENSMUSG00000020573 .
    ENSMUST00000156904 ; ENSMUSP00000123539 ; ENSMUSG00000020573 .
    GeneIDi 30955.
    KEGGi mmu:30955.
    UCSCi uc007nib.2. mouse.

    Organism-specific databases

    CTDi 5294.
    MGIi MGI:1353576. Pik3cg.

    Phylogenomic databases

    eggNOGi COG5032.
    GeneTreei ENSGT00620000087742.
    HOGENOMi HOG000252912.
    HOVERGENi HBG101026.
    KOi K00922.
    OMAi YHEQLTI.
    OrthoDBi EOG70CR65.
    PhylomeDBi Q9JHG7.
    TreeFami TF102031.

    Enzyme and pathway databases

    UniPathwayi UPA00220 .
    BRENDAi 2.7.1.153. 3474.
    Reactomei REACT_198973. Synthesis of PIPs at the plasma membrane.
    REACT_220092. GPVI-mediated activation cascade.
    REACT_223974. G beta:gamma signalling through PI3Kgamma.

    Miscellaneous databases

    ChiTaRSi PIK3CG. mouse.
    NextBioi 307436.
    PROi Q9JHG7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9JHG7.
    Bgeei Q9JHG7.
    Genevestigatori Q9JHG7.

    Family and domain databases

    Gene3Di 1.10.1070.11. 1 hit.
    1.25.40.70. 1 hit.
    2.60.40.150. 1 hit.
    InterProi IPR016024. 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 ]
    PANTHERi PTHR10048. PTHR10048. 1 hit.
    Pfami PF00454. PI3_PI4_kinase. 1 hit.
    PF00792. PI3K_C2. 1 hit.
    PF00794. PI3K_rbd. 1 hit.
    PF00613. PI3Ka. 1 hit.
    [Graphical view ]
    SMARTi SM00142. PI3K_C2. 1 hit.
    SM00144. PI3K_rbd. 1 hit.
    SM00145. PI3Ka. 1 hit.
    SM00146. PI3Kc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 1 hit.
    SSF49562. SSF49562. 1 hit.
    SSF54236. SSF54236. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS00915. 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 ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ENZYME REGULATION.
    2. "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].
      Strain: FVB/N-3.
      Tissue: Mammary tumor.
    3. Lubec G., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1060-1065, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: OF1.
      Tissue: Hippocampus.
    4. Cited for: FUNCTION ON INFLAMMATION AND CHEMOTACTIC RESPONSE, DISRUPTION PHENOTYPE.
    5. "Central role for G protein-coupled phosphoinositide 3-kinase gamma in inflammation."
      Hirsch E., Katanaev V.L., Garlanda C., Azzolino O., Pirola L., Silengo L., Sozzani S., Mantovani A., Altruda F., Wymann M.P.
      Science 287:1049-1053(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION ON INFLAMMATION AND CHEMOTACTIC RESPONSE, DISRUPTION PHENOTYPE.
    6. "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.
    7. Cited for: FUNCTION ON CARDIAC CONTRACTILITY, DISRUPTION PHENOTYPE.
    8. "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, INTERACTION WITH PDE3B, DISRUPTION PHENOTYPE.
    9. Cited for: FUNCTION ON IMMUNE RESPONSE, DISRUPTION PHENOTYPE.
    10. "T cell development requires the combined activities of the p110gamma and p110delta catalytic isoforms of phosphatidylinositol 3-kinase."
      Webb L.M.C., Vigorito E., Wymann M.P., Hirsch E., Turner M.
      J. Immunol. 175:2783-2787(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN T-CELL DEVELOPMENT.
    11. Cited for: FUNCTION ON INFLAMMATION AND CHEMOTACTIC RESPONSE, DISRUPTION PHENOTYPE.
    12. "Identification of a unique co-operative phosphoinositide 3-kinase signaling mechanism regulating integrin alpha IIb beta 3 adhesive function in platelets."
      Schoenwaelder S.M., Ono A., Sturgeon S., Chan S.M., Mangin P., Maxwell M.J., Turnbull S., Mulchandani M., Anderson K., Kauffenstein G., Rewcastle G.W., Kendall J., Gachet C., Salem H.H., Jackson S.P.
      J. Biol. Chem. 282:28648-28658(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION ON PLATELET AGGREGATION, DISRUPTION PHENOTYPE.
    13. "p110gamma and p110delta isoforms of phosphoinositide 3-kinase differentially regulate natural killer cell migration in health and disease."
      Saudemont A., Garcon F., Yadi H., Roche-Molina M., Kim N., Segonds-Pichon A., Martin-Fontecha A., Okkenhaug K., Colucci F.
      Proc. Natl. Acad. Sci. U.S.A. 106:5795-5800(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NATURAL KILLER CELL MIGRATION, ENZYME REGULATION.
    14. Cited for: INTERACTION WITH HRAS.
    15. Cited for: FUNCTION ON CARDIAC CONTRACTILITY, PHOSPHORYLATION AT THR-1024.

    Entry informationi

    Entry nameiPK3CG_MOUSE
    AccessioniPrimary (citable) accession number: Q9JHG7
    Secondary accession number(s): Q80V09
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 120 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3