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.

P48736

- PK3CG_HUMAN

UniProt

P48736 - PK3CG_HUMAN

(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
Organism
Homo sapiens (Human)
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. 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

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. ephrin receptor binding Source: UniProtKB
  5. phosphatidylinositol 3-kinase activity Source: UniProtKB
  6. phosphatidylinositol-4,5-bisphosphate 3-kinase activity Source: RefGenome
  7. protein binding Source: IntAct
  8. protein kinase activity Source: UniProtKB
  9. protein serine/threonine kinase activity Source: UniProtKB-KW

GO - Biological processi

  1. adaptive immune response Source: UniProtKB
  2. angiogenesis Source: UniProtKB-KW
  3. blood coagulation Source: Reactome
  4. cytokine production Source: UniProtKB
  5. dendritic cell chemotaxis Source: UniProtKB
  6. endocytosis Source: UniProtKB-KW
  7. G-protein coupled receptor signaling pathway Source: UniProtKB
  8. hepatocyte apoptotic process Source: Ensembl
  9. inflammatory response Source: UniProtKB
  10. innate immune response Source: UniProtKB
  11. mast cell degranulation Source: UniProtKB
  12. natural killer cell chemotaxis Source: UniProtKB
  13. negative regulation of cardiac muscle contraction Source: UniProtKB
  14. negative regulation of fibroblast apoptotic process Source: Ensembl
  15. negative regulation of triglyceride catabolic process Source: Ensembl
  16. neutrophil chemotaxis Source: UniProtKB
  17. neutrophil extravasation Source: UniProtKB
  18. phosphatidylinositol 3-kinase signaling Source: UniProtKB
  19. phosphatidylinositol biosynthetic process Source: Reactome
  20. phospholipid metabolic process Source: Reactome
  21. platelet activation Source: Reactome
  22. platelet aggregation Source: UniProtKB
  23. positive regulation of acute inflammatory response Source: Ensembl
  24. positive regulation of cytosolic calcium ion concentration Source: Ensembl
  25. positive regulation of MAP kinase activity Source: UniProtKB
  26. positive regulation of protein kinase B signaling Source: UniProtKB
  27. regulation of cell adhesion mediated by integrin Source: UniProtKB
  28. respiratory burst involved in defense response Source: UniProtKB
  29. secretory granule localization Source: Ensembl
  30. small molecule metabolic process Source: Reactome
  31. T cell activation Source: UniProtKB
  32. T cell chemotaxis Source: UniProtKB
  33. 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.
BRENDAi2.7.1.137. 2681.
ReactomeiREACT_121025. Synthesis of PIPs at the plasma membrane.
REACT_1695. GPVI-mediated activation cascade.
REACT_19290. G beta:gamma signalling through PI3Kgamma.
SignaLinkiP48736.
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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:8978. PIK3CG.

Subcellular locationi

Cytoplasm. Cell membrane 1 Publication

GO - Cellular componenti

  1. 1-phosphatidylinositol-4-phosphate 3-kinase, class IB complex Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: Reactome
  4. mast cell granule Source: GOC
  5. membrane Source: UniProtKB
  6. plasma membrane Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi833 – 8331K → R: Reduced inflammatory reactions but no alterations in cardiac contractility. 1 Publication
Mutagenesisi947 – 9471R → P: Abolishes protein and lipid kinase activity. Does not abolishes interaction with ADRBK1. 1 Publication

Organism-specific databases

PharmGKBiPA33311.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11021102Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoformPRO_0000088792Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1024 – 10241Phosphothreonine; by PKA By similarity
Modified residuei1101 – 11011Phosphoserine; by autocatalysis1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP48736.
PaxDbiP48736.
PRIDEiP48736.

PTM databases

PhosphoSiteiP48736.

Expressioni

Tissue specificityi

Pancreas, skeletal muscle, liver and heart.1 Publication

Gene expression databases

ArrayExpressiP48736.
BgeeiP48736.
CleanExiHS_PIK3CG.
GenevestigatoriP48736.

Interactioni

Subunit structurei

Heterodimer of a catalytic subunit PIK3CG and a PIK3R5 or PIK3R6 regulatory subunit. Interacts with ADRBK1 through the PIK helical domain. Interaction with ADRBK1 is required for targeting to agonist-occupied receptor. Interacts with PDE3B By similarity. Interacts with TPM2. Interacts with EPHA8; regulates integrin-mediated cell adhesion to substrate. Interacts with HRAS; the interaction is required for membrane recruitment and beta-gamma G protein dimer-dependent activation of the PI3K gamma complex PIK3CG:PIK3R6 By similarity.4 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi111312. 17 interactions.
DIPiDIP-37781N.
IntActiP48736. 11 interactions.
MINTiMINT-155782.
STRINGi9606.ENSP00000352121.

Structurei

Secondary structure

1
1102
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi145 – 15814
Helixi165 – 1673
Beta strandi169 – 1713
Helixi172 – 1798
Helixi181 – 19010
Helixi193 – 1986
Helixi209 – 2124
Helixi213 – 2153
Beta strandi216 – 2183
Beta strandi220 – 2267
Beta strandi229 – 2357
Helixi241 – 2433
Helixi246 – 2527
Helixi256 – 2594
Beta strandi263 – 2653
Beta strandi271 – 2744
Beta strandi283 – 2853
Helixi287 – 2893
Helixi291 – 2988
Beta strandi303 – 3086
Helixi313 – 3164
Helixi354 – 3563
Beta strandi359 – 36911
Beta strandi375 – 3773
Beta strandi380 – 39112
Beta strandi393 – 3986
Beta strandi406 – 41914
Helixi420 – 4223
Beta strandi428 – 4347
Beta strandi462 – 4698
Beta strandi473 – 4753
Beta strandi478 – 4836
Helixi499 – 5024
Beta strandi511 – 5133
Beta strandi515 – 5206
Helixi549 – 56012
Beta strandi563 – 5653
Helixi569 – 5779
Helixi579 – 5824
Helixi586 – 5883
Helixi589 – 5935
Helixi601 – 61212
Helixi615 – 6184
Helixi624 – 6307
Beta strandi632 – 6343
Helixi638 – 64811
Helixi653 – 66614
Helixi667 – 6693
Beta strandi671 – 6744
Helixi676 – 68712
Helixi689 – 70517
Turni707 – 7093
Helixi710 – 72112
Turni722 – 7243
Helixi726 – 75126
Beta strandi755 – 7573
Helixi761 – 77414
Turni775 – 7784
Beta strandi783 – 7853
Beta strandi788 – 7969
Helixi798 – 8003
Beta strandi806 – 8083
Beta strandi811 – 8188
Beta strandi828 – 8369
Helixi838 – 85619
Turni857 – 8593
Beta strandi869 – 8735
Beta strandi876 – 8805
Beta strandi885 – 8873
Helixi888 – 8958
Beta strandi898 – 9003
Helixi906 – 9149
Beta strandi915 – 9173
Helixi918 – 94124
Helixi949 – 9513
Beta strandi952 – 9554
Turni956 – 9583
Beta strandi960 – 9623
Helixi965 – 9706
Helixi989 – 9946
Turni998 – 10003
Helixi1004 – 102118
Helixi1024 – 103815
Beta strandi1039 – 10413
Turni1042 – 10454
Helixi1046 – 10549
Turni1055 – 10584
Helixi1061 – 107818
Helixi1081 – 10855
Turni1086 – 10905
Turni1091 – 10933

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP48736.
SMRiP48736. Positions 144-1089.

Miscellaneous databases

EvolutionaryTraceiP48736.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 141108PI3K-ABDAdd
BLAST
Domaini217 – 30993PI3K-RBDAdd
BLAST
Domaini357 – 521165C2 PI3K-typeAdd
BLAST
Domaini541 – 723183PIK helicalAdd
BLAST
Domaini828 – 1073246PI3K/PI4KAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi19 – 235Poly-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.
HOGENOMiHOG000252912.
HOVERGENiHBG101026.
InParanoidiP48736.
KOiK00922.
OMAiYHEQLTI.
OrthoDBiEOG70CR65.
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

MELENYKQPV VLREDNCRRR RRMKPRSAAA SLSSMELIPI EFVLPTSQRK     50
CKSPETALLH VAGHGNVEQM KAQVWLRALE TSVAADFYHR LGPHHFLLLY 100
QKKGQWYEIY DKYQVVQTLD CLRYWKATHR SPGQIHLVQR HPPSEESQAF 150
QRQLTALIGY DVTDVSNVHD DELEFTRRGL VTPRMAEVAS RDPKLYAMHP 200
WVTSKPLPEY LWKKIANNCI FIVIHRSTTS QTIKVSPDDT PGAILQSFFT 250
KMAKKKSLMD IPESQSEQDF VLRVCGRDEY LVGETPIKNF QWVRHCLKNG 300
EEIHVVLDTP PDPALDEVRK EEWPLVDDCT GVTGYHEQLT IHGKDHESVF 350
TVSLWDCDRK FRVKIRGIDI PVLPRNTDLT VFVEANIQHG QQVLCQRRTS 400
PKPFTEEVLW NVWLEFSIKI KDLPKGALLN LQIYCGKAPA LSSKASAESP 450
SSESKGKVQL LYYVNLLLID HRFLLRRGEY VLHMWQISGK GEDQGSFNAD 500
KLTSATNPDK ENSMSISILL DNYCHPIALP KHQPTPDPEG DRVRAEMPNQ 550
LRKQLEAIIA TDPLNPLTAE DKELLWHFRY ESLKHPKAYP KLFSSVKWGQ 600
QEIVAKTYQL LARREVWDQS ALDVGLTMQL LDCNFSDENV RAIAVQKLES 650
LEDDDVLHYL LQLVQAVKFE PYHDSALARF LLKRGLRNKR IGHFLFWFLR 700
SEIAQSRHYQ QRFAVILEAY LRGCGTAMLH DFTQQVQVIE MLQKVTLDIK 750
SLSAEKYDVS SQVISQLKQK LENLQNSQLP ESFRVPYDPG LKAGALAIEK 800
CKVMASKKKP LWLEFKCADP TALSNETIGI IFKHGDDLRQ DMLILQILRI 850
MESIWETESL DLCLLPYGCI STGDKIGMIE IVKDATTIAK IQQSTVGNTG 900
AFKDEVLNHW LKEKSPTEEK FQAAVERFVY SCAGYCVATF VLGIGDRHND 950
NIMITETGNL FHIDFGHILG NYKSFLGINK ERVPFVLTPD FLFVMGTSGK 1000
KTSPHFQKFQ DICVKAYLAL RHHTNLLIIL FSMMLMTGMP QLTSKEDIEY 1050
IRDALTVGKN EEDAKKYFLD QIEVCRDKGW TVQFNWFLHL VLGIKQGEKH 1100
SA 1102
Length:1,102
Mass (Da):126,454
Last modified:April 4, 2006 - v3
Checksum:iEF2B1A0E1CBEF406
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301Missing in CAA58284. 1 Publication
Sequence conflicti459 – 4591Q → R in CAA58284. 1 Publication
Sequence conflicti459 – 4591Q → R in AAG61115. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_005250443.1.
UniGeneiHs.32942.
Hs.561747.

Genome annotation databases

EnsembliENST00000359195; ENSP00000352121; ENSG00000105851.
ENST00000440650; ENSP00000392258; ENSG00000105851.
ENST00000496166; ENSP00000419260; ENSG00000105851.
GeneIDi5294.
KEGGihsa:5294.
UCSCiuc003vdu.3. human.

Polymorphism databases

DMDMi92090623.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS5739.1.
RefSeqi NP_001269355.1. NM_001282426.1.
NP_001269356.1. NM_001282427.1.
NP_002640.2. NM_002649.3.
XP_005250500.1. XM_005250443.1.
UniGenei Hs.32942.
Hs.561747.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1E8Y X-ray 2.00 A 144-1102 [» ]
1E8Z X-ray 2.40 A 144-1102 [» ]
1HE8 X-ray 3.00 A 144-1102 [» ]
2A4Z X-ray 2.90 A 144-1102 [» ]
2A5U X-ray 2.70 A 144-1102 [» ]
2CHW X-ray 2.60 A 144-1102 [» ]
2CHX X-ray 2.50 A 144-1102 [» ]
2CHZ X-ray 2.60 A 144-1102 [» ]
2V4L X-ray 2.50 A 144-1102 [» ]
3APC X-ray 2.54 A 144-1102 [» ]
3APD X-ray 2.55 A 144-1102 [» ]
3APF X-ray 2.82 A 144-1102 [» ]
3CSF X-ray 2.80 A 144-1102 [» ]
3CST X-ray 3.20 A 144-1102 [» ]
3DBS X-ray 2.80 A 144-1102 [» ]
3DPD X-ray 2.85 A 144-1102 [» ]
3ENE X-ray 2.40 A 144-1102 [» ]
3IBE X-ray 2.80 A 144-1102 [» ]
3L08 X-ray 2.70 A 144-1102 [» ]
3L13 X-ray 3.00 A 144-1102 [» ]
3L16 X-ray 2.90 A 144-1102 [» ]
3L17 X-ray 3.00 A 144-1102 [» ]
3L54 X-ray 2.30 A 144-1102 [» ]
3LJ3 X-ray 2.43 A 144-1102 [» ]
3MJW X-ray 2.87 A 144-1102 [» ]
3ML8 X-ray 2.70 A 144-1102 [» ]
3ML9 X-ray 2.55 A 144-1102 [» ]
3NZS X-ray 2.75 A 147-1094 [» ]
3NZU X-ray 2.60 A 147-1094 [» ]
3OAW X-ray 2.75 A 144-1102 [» ]
3P2B X-ray 3.20 A 144-1102 [» ]
3PRE X-ray 2.91 A 144-1102 [» ]
3PRZ X-ray 2.60 A 144-1102 [» ]
3PS6 X-ray 2.60 A 144-1102 [» ]
3QAQ X-ray 2.90 A 144-1102 [» ]
3QAR X-ray 2.65 A 144-1102 [» ]
3QJZ X-ray 2.90 A 144-1102 [» ]
3QK0 X-ray 2.85 A 144-1102 [» ]
3R7Q X-ray 2.50 A 144-1102 [» ]
3R7R X-ray 2.90 A 144-1102 [» ]
3S2A X-ray 2.55 A 144-1102 [» ]
3SD5 X-ray 3.20 A 144-1102 [» ]
3T8M X-ray 2.50 A 144-1102 [» ]
3TJP X-ray 2.70 A 144-1102 [» ]
3TL5 X-ray 2.79 A 144-1102 [» ]
3ZVV X-ray 2.50 A 144-1102 [» ]
3ZW3 X-ray 2.80 A 144-1102 [» ]
4ANU X-ray 2.81 A 144-1102 [» ]
4ANV X-ray 2.13 A 144-1102 [» ]
4ANW X-ray 2.31 A 144-1102 [» ]
4ANX X-ray 2.73 A 144-1102 [» ]
4AOF X-ray 3.30 A 144-1102 [» ]
4DK5 X-ray 2.95 A 144-1102 [» ]
4EZJ X-ray 2.67 A 144-1102 [» ]
4EZK X-ray 2.80 A 144-1102 [» ]
4EZL X-ray 2.94 A 144-1102 [» ]
4F1S X-ray 3.00 A 144-1102 [» ]
4FA6 X-ray 2.70 A 144-1102 [» ]
4FAD X-ray 2.70 A 144-1102 [» ]
4FHJ X-ray 2.60 A 144-1102 [» ]
4FHK X-ray 3.00 A 144-1102 [» ]
4FJY X-ray 2.90 A 144-1102 [» ]
4FJZ X-ray 3.00 A 144-1102 [» ]
4FLH X-ray 2.60 A 144-1102 [» ]
4FUL X-ray 2.47 A 144-1102 [» ]
4G11 X-ray 3.40 A 144-1102 [» ]
4GB9 X-ray 2.44 A 144-1102 [» ]
4HLE X-ray 2.78 A 144-1102 [» ]
4HVB X-ray 2.35 A 144-1102 [» ]
4J6I X-ray 2.90 A 144-1102 [» ]
4KZ0 X-ray 2.87 A 144-1102 [» ]
4KZC X-ray 3.25 A 144-1102 [» ]
4PS3 X-ray 2.90 A 144-1102 [» ]
4PS7 X-ray 2.69 A 144-1102 [» ]
4PS8 X-ray 2.99 A 144-1102 [» ]
ProteinModelPortali P48736.
SMRi P48736. Positions 144-1089.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111312. 17 interactions.
DIPi DIP-37781N.
IntActi P48736. 11 interactions.
MINTi MINT-155782.
STRINGi 9606.ENSP00000352121.

Chemistry

BindingDBi P48736.
ChEMBLi CHEMBL3267.
GuidetoPHARMACOLOGYi 2156.

PTM databases

PhosphoSitei P48736.

Polymorphism databases

DMDMi 92090623.

Proteomic databases

MaxQBi P48736.
PaxDbi P48736.
PRIDEi P48736.

Protocols and materials databases

DNASUi 5294.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000359195 ; ENSP00000352121 ; ENSG00000105851 .
ENST00000440650 ; ENSP00000392258 ; ENSG00000105851 .
ENST00000496166 ; ENSP00000419260 ; ENSG00000105851 .
GeneIDi 5294.
KEGGi hsa:5294.
UCSCi uc003vdu.3. human.

Organism-specific databases

CTDi 5294.
GeneCardsi GC07P106505.
HGNCi HGNC:8978. PIK3CG.
MIMi 601232. gene.
neXtProti NX_P48736.
PharmGKBi PA33311.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5032.
HOGENOMi HOG000252912.
HOVERGENi HBG101026.
InParanoidi P48736.
KOi K00922.
OMAi YHEQLTI.
OrthoDBi EOG70CR65.
PhylomeDBi P48736.
TreeFami TF102031.

Enzyme and pathway databases

UniPathwayi UPA00220 .
BioCyci MetaCyc:HS02818-MONOMER.
BRENDAi 2.7.1.137. 2681.
Reactomei REACT_121025. Synthesis of PIPs at the plasma membrane.
REACT_1695. GPVI-mediated activation cascade.
REACT_19290. G beta:gamma signalling through PI3Kgamma.
SignaLinki P48736.

Miscellaneous databases

EvolutionaryTracei P48736.
GeneWikii PIK3CG.
GenomeRNAii 5294.
NextBioi 20458.
PROi P48736.
SOURCEi Search...

Gene expression databases

ArrayExpressi P48736.
Bgeei P48736.
CleanExi HS_PIK3CG.
Genevestigatori P48736.

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 [MRNA], FUNCTION, ENZYME REGULATION, TISSUE SPECIFICITY.
  2. Waterfield M.D.
    Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "Regulation of a G-protein-activated phosphoinositide-3-kinase."
    Michalke M., Schaefer M., Stoyanov B., Wetzker R., Nuernberg B.
    Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pancreas.
  8. "The EphA8 receptor regulates integrin activity through p110gamma phosphatidylinositol-3 kinase in a tyrosine kinase activity-independent manner."
    Gu C., Park S.
    Mol. Cell. Biol. 21:4579-4597(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EPHA8.
  9. "Phosphoinositide 3-kinase regulates beta2-adrenergic receptor endocytosis by AP-2 recruitment to the receptor/beta-arrestin complex."
    Naga Prasad S.V., Laporte S.A., Chamberlain D., Caron M.G., Barak L., Rockman H.A.
    J. Cell Biol. 158:563-575(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ADRBK1.
  10. "Identification and characterization of the autophosphorylation sites of phosphoinositide 3-kinase isoforms beta and gamma."
    Czupalla C., Culo M., Muller E.C., Brock C., Reusch H.P., Spicher K., Krause E., Nurnberg B.
    J. Biol. Chem. 278:11536-11545(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-1101.
  11. "PI3Kgamma modulates the cardiac response to chronic pressure overload by distinct kinase-dependent and -independent effects."
    Patrucco E., Notte A., Barberis L., Selvetella G., Maffei A., Brancaccio M., Marengo S., Russo G., Azzolino O., Rybalkin S.D., Silengo L., Altruda F., Wetzker R., Wymann M.P., Lembo G., Hirsch E.
    Cell 118:375-387(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CARDIAC CONTRACTILITY, MUTAGENESIS OF LYS-833.
  12. "p84, a new Gbetagamma-activated regulatory subunit of the type IB phosphoinositide 3-kinase p110gamma."
    Suire S., Coadwell J., Ferguson G.J., Davidson K., Hawkins P., Stephens L.
    Curr. Biol. 15:566-570(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PIK3R5.
  13. "Protein kinase activity of phosphoinositide 3-kinase regulates beta-adrenergic receptor endocytosis."
    Naga Prasad S.V., Jayatilleke A., Madamanchi A., Rockman H.A.
    Nat. Cell Biol. 7:785-796(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A PROTEIN KINASE, INTERACTION WITH ADRBK1 AND TPM2, MUTAGENESIS OF ARG-947.
  14. "PI3K delta and PI3K gamma: partners in crime in inflammation in rheumatoid arthritis and beyond?"
    Rommel C., Camps M., Ji H.
    Nat. Rev. Immunol. 7:191-201(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  15. "Targeting phosphoinositide 3-kinase gamma to fight inflammation and more."
    Barberis L., Hirsch E.
    Thromb. Haemost. 99:279-285(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION IN LEUKOCYTES AND ENDOTHELIAL CELLS, REVIEW ON ANTINFLAMMATORY THERAPY TARGET.
  16. "Cardiac regulation by phosphoinositide 3-kinases and PTEN."
    Oudit G.Y., Penninger J.M.
    Cardiovasc. Res. 82:250-260(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION IN CARDIAC CONTRACTILITY.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "A phosphodiesterase 3B-based signaling complex integrates exchange protein activated by cAMP 1 and phosphatidylinositol 3-kinase signals in human arterial endothelial cells."
    Wilson L.S., Baillie G.S., Pritchard L.M., Umana B., Terrin A., Zaccolo M., Houslay M.D., Maurice D.H.
    J. Biol. Chem. 286:16285-16296(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  19. "Structural insights into phosphoinositide 3-kinase catalysis and signalling."
    Walker E.H., Perisic O., Ried C., Stephens L., Williams R.L.
    Nature 402:313-320(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 144-1102.
  20. Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 144-1101 IN A COMPLEX WITH AS-604850 AND AS-605240, ENZYME REGULATION.

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: September 3, 2014
This is version 150 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 (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

External Data

Dasty 3

Similar proteinsi