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Q9JHG7 (PK3CG_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
Synonyms:Pi3kg1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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. 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. Ref.4 Ref.5 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15

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 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. Ref.1 Ref.13

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 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. Ref.6 Ref.8 Ref.14

Subcellular location

Cytoplasm By similarity. Cell membrane By similarity.

Post-translational modification

Phosphorylated at Thr-1024 by PKA. Phosphorylation inhibits lipid kinase activity. Ref.15

Disruption phenotype

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. Ref.4 Ref.5 Ref.7 Ref.8 Ref.9 Ref.11 Ref.12

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 termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

angiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

chemotaxis

Inferred from electronic annotation. Source: UniProtKB-KW

endocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

hepatocyte apoptotic process

Inferred from electronic annotation. Source: Ensembl

immune system process

Inferred from electronic annotation. Source: UniProtKB-KW

inflammatory response

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of fibroblast apoptotic process

Inferred from direct assay PubMed 15192701. Source: MGI

negative regulation of triglyceride catabolic process

Inferred from electronic annotation. Source: Ensembl

phosphatidylinositol 3-kinase signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of MAP kinase activity

Inferred from electronic annotation. Source: Ensembl

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 electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from direct assay PubMed 15192701. Source: MGI

secretory granule localization

Inferred from electronic annotation. Source: Ensembl

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

Inferred from electronic annotation. Source: Ensembl

phosphatidylinositol 3-kinase complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

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

phosphatidylinositol-4,5-bisphosphate 3-kinase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein serine/threonine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11021102Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
PRO_0000088793

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 bias18 – 225Poly-Arg

Amino acid modifications

Modified residue10241Phosphothreonine; by PKA Ref.15
Modified residue11011Phosphoserine; by autocatalysis By similarity

Experimental info

Sequence conflict2621S → P in CAB89686. Ref.1
Sequence conflict2621S → P in CAB89851. Ref.1
Sequence conflict3501F → V in CAB89686. Ref.1
Sequence conflict3501F → V in CAB89851. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9JHG7 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 7675848792D76734

FASTA1,102126,400
        10         20         30         40         50         60 
MELENYEQPV VLREDNLRRR RRMKPRSAAG SLSSMELIPI EFVLPTSQRI SKTPETALLH 

        70         80         90        100        110        120 
VAGHGNVEQM KAQVWLRALE TSVAAEFYHR LGPDQFLLLY QKKGQWYEIY DRYQVVQTLD 

       130        140        150        160        170        180 
CLHYWKLMHK SPGQIHVVQR HVPSEETLAF QKQLTSLIGY DVTDISNVHD DELEFTRRRL 

       190        200        210        220        230        240 
VTPRMAEVAG RDAKLYAMHP WVTSKPLPDY LSKKIANNCI FIVIHRGTTS QTIKVSADDT 

       250        260        270        280        290        300 
PGTILQSFFT KMAKKKSLMN ISESQSEQDF VLRVCGRDEY LVGETPLKNF QWVRQCLKNG 

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

       370        380        390        400        410        420 
FRVKIRGIDI PVLPRNTDLT VFVEANIQHG QQVLCQRRTS PKPFAEEVLW NVWLEFGIKI 

       430        440        450        460        470        480 
KDLPKGALLN LQIYCCKTPS LSSKASAETP GSESKGKAQL LYYVNLLLID HRFLLRHGDY 

       490        500        510        520        530        540 
VLHMWQISGK AEEQGSFNAD KLTSATNPDK ENSMSISILL DNYCHPIALP KHRPTPDPEG 

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

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

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

       730        740        750        760        770        780 
LRGCGTAMLQ DFTQQVHVIE MLQKVTIDIK SLSAEKYDVS SQVISQLKQK LESLQNSNLP 

       790        800        810        820        830        840 
ESFRVPYDPG LKAGTLVIEK CKVMASKKKP LWLEFKCADP TVLSNETIGI IFKHGDDLRQ 

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

       910        920        930        940        950        960 
AFKDEVLNHW LKEKCPIEEK FQAAVERFVY SCAGYCVATF VLGIGDRHND NIMISETGNL 

       970        980        990       1000       1010       1020 
FHIDFGHILG NYKSFLGINK ERVPFVLTPD FLFVMGSSGK KTSPHFQKFQ DVCVRAYLAL 

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

      1090       1100 
TVQFNWFLHL VLGIKQGEKH SA 

« Hide

References

« Hide 'large scale' references
[1]"Analysis of the murine phosphoinositide 3-kinase gamma gene."
Hirsch E., Wymann M.P., Patrucco E., Tolosano E., Bulgarelli-Leva G., Marengo S., Rocchi M., Altruda F.
Gene 256:69-81(2000) [PubMed] [Europe PMC] [Abstract]
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]"Function of PI3Kgamma in thymocyte development, T cell activation, and neutrophil migration."
Sasaki T., Irie-Sasaki J., Jones R.G., Oliveira-dos-Santos A.J., Stanford W.L., Bolon B., Wakeham A., Itie A., Bouchard D., Kozieradzki I., Joza N., Mak T.W., Ohashi P.S., Suzuki A., Penninger J.M.
Science 287:1040-1046(2000) [PubMed] [Europe PMC] [Abstract]
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]"Regulation of myocardial contractility and cell size by distinct PI3K-PTEN signaling pathways."
Crackower M.A., Oudit G.Y., Kozieradzki I., Sarao R., Sun H., Sasaki T., Hirsch E., Suzuki A., Shioi T., Irie-Sasaki J., Sah R., Cheng H.-Y.M., Rybin V.O., Lembo G., Fratta L., Oliveira-dos-Santos A.J., Benovic J.L., Kahn C.R. expand/collapse author list , Izumo S., Steinberg S.F., Wymann M.P., Backx P.H., Penninger J.M.
Cell 110:737-749(2002) [PubMed] [Europe PMC] [Abstract]
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]"Defective dendritic cell migration and activation of adaptive immunity in PI3Kgamma-deficient mice."
Del Prete A., Vermi W., Dander E., Otero K., Barberis L., Luini W., Bernasconi S., Sironi M., Santoro A., Garlanda C., Facchetti F., Wymann M.P., Vecchi A., Hirsch E., Mantovani A., Sozzani S.
EMBO J. 23:3505-3515(2004) [PubMed] [Europe PMC] [Abstract]
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]"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: 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]"Ras is an indispensable coregulator of the class IB phosphoinositide 3-kinase p87/p110gamma."
Kurig B., Shymanets A., Bohnacker T., Prajwal X., Brock C., Ahmadian M.R., Schaefer M., Gohla A., Harteneck C., Wymann M.P., Jeanclos E., Nurnberg B.
Proc. Natl. Acad. Sci. U.S.A. 106:20312-20317(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HRAS.
[15]"Integrating cardiac PIP3 and cAMP signaling through a PKA anchoring function of p110gamma."
Perino A., Ghigo A., Ferrero E., Morello F., Santulli G., Baillie G.S., Damilano F., Dunlop A.J., Pawson C., Walser R., Levi R., Altruda F., Silengo L., Langeberg L.K., Neubauer G., Heymans S., Lembo G., Wymann M.P. expand/collapse author list , Wetzker R., Houslay M.D., Iaccarino G., Scott J.D., Hirsch E.
Mol. Cell 42:84-95(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION ON CARDIAC CONTRACTILITY, PHOSPHORYLATION AT THR-1024.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ249280 mRNA. Translation: CAB89686.1.
AJ249413 expand/collapse EMBL AC list , AJ249414, AJ249415, AJ249416, AJ249417, AJ249418, AJ249419, AJ249420 Genomic DNA. Translation: CAB89851.1.
BC051246 mRNA. Translation: AAH51246.1.
RefSeqNP_001139672.1. NM_001146200.1.
NP_001139673.1. NM_001146201.1.
NP_064668.2. NM_020272.2.
XP_006515175.1. XM_006515112.1.
UniGeneMm.101369.
Mm.404021.

3D structure databases

ProteinModelPortalQ9JHG7.
SMRQ9JHG7. Positions 144-1094.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid206031. 2 interactions.
DIPDIP-41862N.
IntActQ9JHG7. 6 interactions.
MINTMINT-1612546.

Chemistry

ChEMBLCHEMBL2189158.

PTM databases

PhosphoSiteQ9JHG7.

Proteomic databases

PRIDEQ9JHG7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000053215; ENSMUSP00000062864; ENSMUSG00000020573.
ENSMUST00000085469; ENSMUSP00000082596; ENSMUSG00000020573.
ENSMUST00000156904; ENSMUSP00000123539; ENSMUSG00000020573.
GeneID30955.
KEGGmmu:30955.
UCSCuc007nib.2. mouse.

Organism-specific databases

CTD5294.
MGIMGI:1353576. Pik3cg.

Phylogenomic databases

eggNOGCOG5032.
GeneTreeENSGT00620000087742.
HOGENOMHOG000252912.
HOVERGENHBG101026.
KOK00922.
OMAYHEQLTI.
OrthoDBEOG70CR65.
PhylomeDBQ9JHG7.
TreeFamTF102031.

Enzyme and pathway databases

BRENDA2.7.1.153. 3474.
UniPathwayUPA00220.

Gene expression databases

ArrayExpressQ9JHG7.
BgeeQ9JHG7.
GenevestigatorQ9JHG7.

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.
[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.
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

ChiTaRSPIK3CG. mouse.
NextBio307436.
PROQ9JHG7.
SOURCESearch...

Entry information

Entry namePK3CG_MOUSE
AccessionPrimary (citable) accession number: Q9JHG7
Secondary accession number(s): Q80V09
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot