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Protein

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

Gene

PIK3CG

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 GRK2 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.5 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 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-605240.2 Publications

Pathwayi: phosphatidylinositol phosphate biosynthesis

This protein is involved in the pathway phosphatidylinositol phosphate biosynthesis, which is part of Phospholipid metabolism.
View all proteins of this organism that are known to be involved in the pathway phosphatidylinositol phosphate biosynthesis and in Phospholipid metabolism.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi829 – 838ATPBy similarity10
Nucleotide bindingi864 – 872ATPBy similarity9
Nucleotide bindingi961 – 969ATPBy similarity9

GO - Molecular functioni

  • 1-phosphatidylinositol-3-kinase activity Source: ProtInc
  • 1-phosphatidylinositol-4-phosphate 3-kinase activity Source: GO_Central
  • ATP binding Source: UniProtKB-KW
  • ephrin receptor binding Source: UniProtKB
  • kinase activity Source: MGI
  • phosphatidylinositol 3-kinase activity Source: UniProtKB
  • phosphatidylinositol-4,5-bisphosphate 3-kinase activity Source: GO_Central
  • protein kinase activity Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB-KW

GO - Biological processi

  • adaptive immune response Source: UniProtKB
  • angiogenesis Source: UniProtKB-KW
  • cellular response to cAMP Source: Ensembl
  • cytokine production Source: UniProtKB
  • dendritic cell chemotaxis Source: UniProtKB
  • endocytosis Source: UniProtKB-KW
  • G-protein coupled receptor signaling pathway Source: UniProtKB
  • hepatocyte apoptotic process Source: Ensembl
  • inflammatory response Source: UniProtKB
  • innate immune response Source: UniProtKB
  • mast cell degranulation Source: UniProtKB
  • natural killer cell chemotaxis Source: UniProtKB
  • negative regulation of cardiac muscle contraction Source: UniProtKB
  • negative regulation of fibroblast apoptotic process Source: Ensembl
  • negative regulation of triglyceride catabolic process Source: Ensembl
  • neutrophil chemotaxis Source: UniProtKB
  • neutrophil extravasation Source: UniProtKB
  • phosphatidylinositol 3-kinase signaling Source: UniProtKB
  • phosphatidylinositol biosynthetic process Source: Reactome
  • phosphorylation Source: MGI
  • platelet activation Source: Reactome
  • platelet aggregation Source: UniProtKB
  • positive regulation of acute inflammatory response Source: Ensembl
  • positive regulation of cytosolic calcium ion concentration Source: Ensembl
  • positive regulation of MAP kinase activity Source: UniProtKB
  • positive regulation of protein kinase B signaling Source: UniProtKB
  • regulation of calcium ion transmembrane transport Source: Ensembl
  • regulation of cell adhesion mediated by integrin Source: UniProtKB
  • respiratory burst involved in defense response Source: UniProtKB
  • secretory granule localization Source: Ensembl
  • T cell activation Source: UniProtKB
  • T cell chemotaxis Source: UniProtKB
  • T cell proliferation Source: UniProtKB
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

BioCyciMetaCyc:HS02818-MONOMER.
ZFISH:HS02818-MONOMER.
BRENDAi2.7.1.137. 2681.
2.7.1.153. 2681.
ReactomeiR-HSA-114604. GPVI-mediated activation cascade.
R-HSA-1660499. Synthesis of PIPs at the plasma membrane.
R-HSA-392451. G beta:gamma signalling through PI3Kgamma.
SignaLinkiP48736.
SIGNORiP48736.
UniPathwayiUPA00220.

Chemistry databases

SwissLipidsiSLP:000000909.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:8978. PIK3CG.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • mast cell granule Source: GOC
  • membrane Source: UniProtKB
  • phosphatidylinositol 3-kinase complex, class IB Source: UniProtKB
  • plasma membrane Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi833K → R: Reduced inflammatory reactions but no alterations in cardiac contractility. 1 Publication1
Mutagenesisi947R → P: Abolishes protein and lipid kinase activity. Does not abolishes interaction with GRK2. 1 Publication1

Organism-specific databases

DisGeNETi5294.
OpenTargetsiENSG00000105851.
PharmGKBiPA33311.

Chemistry databases

ChEMBLiCHEMBL3267.
GuidetoPHARMACOLOGYi2156.

Polymorphism and mutation databases

BioMutaiPIK3CG.
DMDMi92090623.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000887921 – 1102Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoformAdd BLAST1102

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1024Phosphothreonine; by PKABy similarity1
Modified residuei1101Phosphoserine; by autocatalysis1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP48736.
MaxQBiP48736.
PaxDbiP48736.
PeptideAtlasiP48736.
PRIDEiP48736.

PTM databases

iPTMnetiP48736.
PhosphoSitePlusiP48736.

Expressioni

Tissue specificityi

Pancreas, skeletal muscle, liver and heart.1 Publication

Gene expression databases

BgeeiENSG00000105851.
CleanExiHS_PIK3CG.
ExpressionAtlasiP48736. baseline and differential.
GenevisibleiP48736. HS.

Interactioni

Subunit structurei

Heterodimer of a catalytic subunit PIK3CG and a PIK3R5 or PIK3R6 regulatory subunit. Interacts with GRK2 through the PIK helical domain. Interaction with GRK2 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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
PDE3BQ133703EBI-1030384,EBI-6172856
PIK3R5O026966EBI-1030384,EBI-6172343From a different organism.

GO - Molecular functioni

  • ephrin receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111312. 22 interactors.
DIPiDIP-37781N.
IntActiP48736. 15 interactors.
MINTiMINT-155782.
STRINGi9606.ENSP00000352121.

Chemistry databases

BindingDBiP48736.

Structurei

Secondary structure

11102
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi145 – 158Combined sources14
Helixi165 – 167Combined sources3
Beta strandi169 – 171Combined sources3
Helixi172 – 179Combined sources8
Helixi181 – 190Combined sources10
Helixi193 – 198Combined sources6
Helixi209 – 212Combined sources4
Helixi213 – 215Combined sources3
Beta strandi216 – 218Combined sources3
Beta strandi220 – 226Combined sources7
Beta strandi229 – 235Combined sources7
Helixi241 – 243Combined sources3
Helixi246 – 252Combined sources7
Helixi256 – 259Combined sources4
Beta strandi263 – 265Combined sources3
Beta strandi271 – 274Combined sources4
Beta strandi283 – 285Combined sources3
Helixi287 – 289Combined sources3
Helixi291 – 298Combined sources8
Beta strandi303 – 308Combined sources6
Helixi313 – 316Combined sources4
Helixi354 – 356Combined sources3
Beta strandi359 – 369Combined sources11
Beta strandi375 – 377Combined sources3
Beta strandi380 – 391Combined sources12
Beta strandi393 – 398Combined sources6
Beta strandi406 – 419Combined sources14
Helixi420 – 422Combined sources3
Beta strandi428 – 434Combined sources7
Beta strandi462 – 469Combined sources8
Beta strandi473 – 475Combined sources3
Beta strandi478 – 483Combined sources6
Helixi499 – 502Combined sources4
Beta strandi511 – 513Combined sources3
Beta strandi515 – 520Combined sources6
Helixi549 – 560Combined sources12
Beta strandi563 – 565Combined sources3
Helixi569 – 577Combined sources9
Helixi579 – 582Combined sources4
Helixi586 – 588Combined sources3
Helixi589 – 593Combined sources5
Helixi601 – 612Combined sources12
Helixi615 – 618Combined sources4
Helixi624 – 630Combined sources7
Beta strandi632 – 634Combined sources3
Helixi638 – 648Combined sources11
Helixi653 – 666Combined sources14
Helixi667 – 669Combined sources3
Beta strandi671 – 674Combined sources4
Helixi676 – 687Combined sources12
Helixi689 – 705Combined sources17
Turni707 – 709Combined sources3
Helixi710 – 721Combined sources12
Turni722 – 724Combined sources3
Helixi726 – 751Combined sources26
Beta strandi755 – 757Combined sources3
Helixi761 – 774Combined sources14
Turni775 – 778Combined sources4
Beta strandi783 – 785Combined sources3
Beta strandi788 – 796Combined sources9
Helixi798 – 800Combined sources3
Beta strandi806 – 808Combined sources3
Beta strandi811 – 818Combined sources8
Beta strandi828 – 836Combined sources9
Helixi838 – 856Combined sources19
Turni857 – 859Combined sources3
Beta strandi869 – 873Combined sources5
Beta strandi876 – 880Combined sources5
Beta strandi885 – 887Combined sources3
Helixi888 – 895Combined sources8
Beta strandi898 – 900Combined sources3
Helixi906 – 914Combined sources9
Beta strandi915 – 917Combined sources3
Helixi918 – 941Combined sources24
Helixi949 – 951Combined sources3
Beta strandi952 – 955Combined sources4
Turni956 – 958Combined sources3
Beta strandi960 – 962Combined sources3
Helixi965 – 970Combined sources6
Helixi989 – 994Combined sources6
Turni998 – 1000Combined sources3
Helixi1004 – 1021Combined sources18
Helixi1024 – 1038Combined sources15
Beta strandi1039 – 1041Combined sources3
Turni1042 – 1045Combined sources4
Helixi1046 – 1054Combined sources9
Turni1055 – 1058Combined sources4
Helixi1061 – 1078Combined sources18
Helixi1081 – 1085Combined sources5
Turni1086 – 1090Combined sources5
Turni1091 – 1093Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4URKX-ray2.90A144-1102[»]
4WWNX-ray2.70A144-1102[»]
4WWOX-ray2.30A144-1102[»]
4WWPX-ray2.40A144-1102[»]
4XX5X-ray2.76A144-1102[»]
4XZ4X-ray2.60A144-1102[»]
5EDSX-ray2.80A144-1102[»]
5G2NX-ray2.68A144-1102[»]
5G55X-ray2.45A144-1102[»]
ProteinModelPortaliP48736.
SMRiP48736.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP48736.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini34 – 141PI3K-ABDPROSITE-ProRule annotationAdd BLAST108
Domaini217 – 309PI3K-RBDPROSITE-ProRule annotationAdd BLAST93
Domaini357 – 521C2 PI3K-typePROSITE-ProRule annotationAdd BLAST165
Domaini541 – 723PIK helicalPROSITE-ProRule annotationAdd BLAST183
Domaini828 – 1073PI3K/PI4KPROSITE-ProRule annotationAdd BLAST246

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi19 – 23Poly-Arg5

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

eggNOGiKOG0904. Eukaryota.
COG5032. LUCA.
GeneTreeiENSGT00760000119110.
HOGENOMiHOG000252912.
HOVERGENiHBG101026.
InParanoidiP48736.
KOiK00922.
OMAiFTEEVLW.
OrthoDBiEOG091G027R.
PhylomeDBiP48736.
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.

P48736-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELENYKQPV VLREDNCRRR RRMKPRSAAA SLSSMELIPI EFVLPTSQRK
60 70 80 90 100
CKSPETALLH VAGHGNVEQM KAQVWLRALE TSVAADFYHR LGPHHFLLLY
110 120 130 140 150
QKKGQWYEIY DKYQVVQTLD CLRYWKATHR SPGQIHLVQR HPPSEESQAF
160 170 180 190 200
QRQLTALIGY DVTDVSNVHD DELEFTRRGL VTPRMAEVAS RDPKLYAMHP
210 220 230 240 250
WVTSKPLPEY LWKKIANNCI FIVIHRSTTS QTIKVSPDDT PGAILQSFFT
260 270 280 290 300
KMAKKKSLMD IPESQSEQDF VLRVCGRDEY LVGETPIKNF QWVRHCLKNG
310 320 330 340 350
EEIHVVLDTP PDPALDEVRK EEWPLVDDCT GVTGYHEQLT IHGKDHESVF
360 370 380 390 400
TVSLWDCDRK FRVKIRGIDI PVLPRNTDLT VFVEANIQHG QQVLCQRRTS
410 420 430 440 450
PKPFTEEVLW NVWLEFSIKI KDLPKGALLN LQIYCGKAPA LSSKASAESP
460 470 480 490 500
SSESKGKVQL LYYVNLLLID HRFLLRRGEY VLHMWQISGK GEDQGSFNAD
510 520 530 540 550
KLTSATNPDK ENSMSISILL DNYCHPIALP KHQPTPDPEG DRVRAEMPNQ
560 570 580 590 600
LRKQLEAIIA TDPLNPLTAE DKELLWHFRY ESLKHPKAYP KLFSSVKWGQ
610 620 630 640 650
QEIVAKTYQL LARREVWDQS ALDVGLTMQL LDCNFSDENV RAIAVQKLES
660 670 680 690 700
LEDDDVLHYL LQLVQAVKFE PYHDSALARF LLKRGLRNKR IGHFLFWFLR
710 720 730 740 750
SEIAQSRHYQ QRFAVILEAY LRGCGTAMLH DFTQQVQVIE MLQKVTLDIK
760 770 780 790 800
SLSAEKYDVS SQVISQLKQK LENLQNSQLP ESFRVPYDPG LKAGALAIEK
810 820 830 840 850
CKVMASKKKP LWLEFKCADP TALSNETIGI IFKHGDDLRQ DMLILQILRI
860 870 880 890 900
MESIWETESL DLCLLPYGCI STGDKIGMIE IVKDATTIAK IQQSTVGNTG
910 920 930 940 950
AFKDEVLNHW LKEKSPTEEK FQAAVERFVY SCAGYCVATF VLGIGDRHND
960 970 980 990 1000
NIMITETGNL FHIDFGHILG NYKSFLGINK ERVPFVLTPD FLFVMGTSGK
1010 1020 1030 1040 1050
KTSPHFQKFQ DICVKAYLAL RHHTNLLIIL FSMMLMTGMP QLTSKEDIEY
1060 1070 1080 1090 1100
IRDALTVGKN EEDAKKYFLD QIEVCRDKGW TVQFNWFLHL VLGIKQGEKH

SA
Length:1,102
Mass (Da):126,454
Last modified:April 4, 2006 - v3
Checksum:iEF2B1A0E1CBEF406
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti30Missing in CAA58284 (PubMed:7624799).Curated1
Sequence conflicti459Q → R in CAA58284 (PubMed:7624799).Curated1
Sequence conflicti459Q → R in AAG61115 (Ref. 3) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS5739.1.
RefSeqiNP_001269355.1. NM_001282426.1.
NP_001269356.1. NM_001282427.1.
NP_002640.2. NM_002649.3.
XP_005250500.1. XM_005250443.3.
UniGeneiHs.32942.
Hs.561747.

Genome annotation databases

EnsembliENST00000359195; ENSP00000352121; ENSG00000105851.
ENST00000440650; ENSP00000392258; ENSG00000105851.
ENST00000496166; ENSP00000419260; ENSG00000105851.
GeneIDi5294.
KEGGihsa:5294.
UCSCiuc003vdu.5. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS5739.1.
RefSeqiNP_001269355.1. NM_001282426.1.
NP_001269356.1. NM_001282427.1.
NP_002640.2. NM_002649.3.
XP_005250500.1. XM_005250443.3.
UniGeneiHs.32942.
Hs.561747.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4URKX-ray2.90A144-1102[»]
4WWNX-ray2.70A144-1102[»]
4WWOX-ray2.30A144-1102[»]
4WWPX-ray2.40A144-1102[»]
4XX5X-ray2.76A144-1102[»]
4XZ4X-ray2.60A144-1102[»]
5EDSX-ray2.80A144-1102[»]
5G2NX-ray2.68A144-1102[»]
5G55X-ray2.45A144-1102[»]
ProteinModelPortaliP48736.
SMRiP48736.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111312. 22 interactors.
DIPiDIP-37781N.
IntActiP48736. 15 interactors.
MINTiMINT-155782.
STRINGi9606.ENSP00000352121.

Chemistry databases

BindingDBiP48736.
ChEMBLiCHEMBL3267.
GuidetoPHARMACOLOGYi2156.
SwissLipidsiSLP:000000909.

PTM databases

iPTMnetiP48736.
PhosphoSitePlusiP48736.

Polymorphism and mutation databases

BioMutaiPIK3CG.
DMDMi92090623.

Proteomic databases

EPDiP48736.
MaxQBiP48736.
PaxDbiP48736.
PeptideAtlasiP48736.
PRIDEiP48736.

Protocols and materials databases

DNASUi5294.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000359195; ENSP00000352121; ENSG00000105851.
ENST00000440650; ENSP00000392258; ENSG00000105851.
ENST00000496166; ENSP00000419260; ENSG00000105851.
GeneIDi5294.
KEGGihsa:5294.
UCSCiuc003vdu.5. human.

Organism-specific databases

CTDi5294.
DisGeNETi5294.
GeneCardsiPIK3CG.
HGNCiHGNC:8978. PIK3CG.
MIMi601232. gene.
neXtProtiNX_P48736.
OpenTargetsiENSG00000105851.
PharmGKBiPA33311.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0904. Eukaryota.
COG5032. LUCA.
GeneTreeiENSGT00760000119110.
HOGENOMiHOG000252912.
HOVERGENiHBG101026.
InParanoidiP48736.
KOiK00922.
OMAiFTEEVLW.
OrthoDBiEOG091G027R.
PhylomeDBiP48736.
TreeFamiTF102031.

Enzyme and pathway databases

UniPathwayiUPA00220.
BioCyciMetaCyc:HS02818-MONOMER.
ZFISH:HS02818-MONOMER.
BRENDAi2.7.1.137. 2681.
2.7.1.153. 2681.
ReactomeiR-HSA-114604. GPVI-mediated activation cascade.
R-HSA-1660499. Synthesis of PIPs at the plasma membrane.
R-HSA-392451. G beta:gamma signalling through PI3Kgamma.
SignaLinkiP48736.
SIGNORiP48736.

Miscellaneous databases

EvolutionaryTraceiP48736.
GeneWikiiPIK3CG.
GenomeRNAii5294.
PROiP48736.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000105851.
CleanExiHS_PIK3CG.
ExpressionAtlasiP48736. baseline and differential.
GenevisibleiP48736. HS.

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]
ProtoNetiSearch...

Entry informationi

Entry nameiPK3CG_HUMAN
AccessioniPrimary (citable) accession number: P48736
Secondary accession number(s): A4D0Q6, Q8IV23, Q9BZC8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: April 4, 2006
Last modified: November 30, 2016
This is version 174 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

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 (PubMed:18278175).1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.