SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9JHG7

- PK3CG_MOUSE

UniProt

Q9JHG7 - PK3CG_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
Gene
Pik3cg, Pi3kg1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.10 Publications

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 – 83810ATP By similarity
Nucleotide bindingi864 – 8729ATP By similarity
Nucleotide bindingi961 – 9699ATP By 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. G-protein coupled receptor signaling pathway Source: Ensembl
  2. angiogenesis Source: UniProtKB-KW
  3. chemotaxis Source: UniProtKB-KW
  4. endocytosis Source: UniProtKB-KW
  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 MAP kinase activity Source: Ensembl
  12. positive regulation of acute inflammatory response Source: Ensembl
  13. positive regulation of cytosolic calcium ion concentration Source: Ensembl
  14. positive regulation of protein kinase B signaling Source: Ensembl
  15. protein phosphorylation Source: MGI
  16. secretory granule localization Source: Ensembl
Complete GO annotation...

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
Complete GO annotation...

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 isoform
PRO_0000088793Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1024 – 10241Phosphothreonine; by PKA1 Publication
Modified residuei1101 – 11011Phosphoserine; by autocatalysis By 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:PIK3R6.3 Publications

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ9JHG7.
SMRiQ9JHG7. Positions 144-1094.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 141108PI3K-ABD
Add
BLAST
Domaini217 – 30993PI3K-RBD
Add
BLAST
Domaini357 – 521165C2 PI3K-type
Add
BLAST
Domaini541 – 723183PIK helical
Add
BLAST
Domaini828 – 1073246PI3K/PI4K
Add
BLAST

Compositional bias

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

Sequence similaritiesi

Belongs to the PI3/PI4-kinase family.
Contains 1 PI3K-ABD domain.
Contains 1 PI3K-RBD domain.
Contains 1 PI3K/PI4K domain.
Contains 1 PIK helical domain.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti262 – 2621S → P in CAB89686. 1 Publication
Sequence conflicti262 – 2621S → P in CAB89851. 1 Publication
Sequence conflicti350 – 3501F → V in CAB89686. 1 Publication
Sequence conflicti350 – 3501F → V in CAB89851. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 119 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

Similar proteinsi