Pik3cg
entrez
30955
canonical
uniprot
Q9JHG7
canonical
ensembl
ENSMUSG00000020573
resolver
ensp
ENSMUSP00000062864
resolver
ensp
ENSMUSP00000082596
resolver
ensp
ENSMUSP00000123539
resolver
ensp
ENSMUSP00000151400
resolver
ensp
ENSMUSP00000152007
resolver
ensp
ENSMUSP00000217589
resolver
enst
ENSMUST00000053215
resolver
enst
ENSMUST00000085469
resolver
enst
ENSMUST00000156904
resolver
enst
ENSMUST00000220366
resolver
genesymbol
Pik3cg
resolver
genesymbol_syn
Pi3kg1
resolver
uniprot
Q3UVA4
resolver
uniprot
Q80V09
resolver
uniprot
Q8C5Q7
resolver
uniprot_entry
PK3CG_MOUSE
resolver
uniprot_entry
Q3UVA4_MOUSE
resolver
uniprot_entry
Q8C5Q7_MOUSE
resolver
uniprot_sec
Q80V09
resolver
activity_regulation
ACTIVITY 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. {ECO:0000269|PubMed:11054537, ECO:0000269|PubMed:19297623}.
uniprot
proteins
amino_acid_sequence
MELENYEQPVVLREDNLRRRRRMKPRSAAGSLSSMELIPIEFVLPTSQRISKTPETALLHVAGHGNVEQMKAQVWLRALETSVAAEFYHRLGPDQFLLLYQKKGQWYEIYDRYQVVQTLDCLHYWKLMHKSPGQIHVVQRHVPSEETLAFQKQLTSLIGYDVTDISNVHDDELEFTRRRLVTPRMAEVAGRDAKLYAMHPWVTSKPLPDYLSKKIANNCIFIVIHRGTTSQTIKVSADDTPGTILQSFFTKMAKKKSLMNISESQSEQDFVLRVCGRDEYLVGETPLKNFQWVRQCLKNGDEIHLVLDTPPDPALDEVRKEEWPLVDDCTGVTGYHEQLTIHGKDHESVFTVSLWDCDRKFRVKIRGIDIPVLPRNTDLTVFVEANIQHGQQVLCQRRTSPKPFAEEVLWNVWLEFGIKIKDLPKGALLNLQIYCCKTPSLSSKASAETPGSESKGKAQLLYYVNLLLIDHRFLLRHGDYVLHMWQISGKAEEQGSFNADKLTSATNPDKENSMSISILLDNYCHPIALPKHRPTPDPEGDRVRAEMPNQLRKQLEAIIATDPLNPLTAEDKELLWHFRYESLKHPKAYPKLFSSVKWGQQEIVAKTYQLLARREIWDQSALDVGLTMQLLDCNFSDENVRAIAVQKLESLEDDDVLHYLLQLVQAVKFEPYHDSALARFLLKRGLRNKRIGHFLFWFLRSEIAQSRHYQQRFAVILEAYLRGCGTAMLQDFTQQVHVIEMLQKVTIDIKSLSAEKYDVSSQVISQLKQKLESLQNSNLPESFRVPYDPGLKAGTLVIEKCKVMASKKKPLWLEFKCADPTVLSNETIGIIFKHGDDLRQDMLILQILRIMESIWETESLDLCLLPYGCISTGDKIGMIEIVKDATTIAQIQQSTVGNTGAFKDEVLNHWLKEKCPIEEKFQAAVERFVYSCAGYCVATFVLGIGDRHNDNIMISETGNLFHIDFGHILGNYKSFLGINKERVPFVLTPDFLFVMGSSGKKTSPHFQKFQDVCVRAYLALRHHTNLLIILFSMMLMTGMPQLTSKEDIEYIRDALTVGKSEEDAKKYFLDQIEVCRDKGWTVQFNWFLHLVLGIKQGEKHSA
uniprot
proteins
ec_number
2.7.1.137
uniprot
proteins
ec_number
2.7.1.153
uniprot
proteins
ec_number
2.7.1.154
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
function
FUNCTION: Phosphoinositide-3-kinase (PI3K) that phosphorylates PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3) (PubMed:10669418, PubMed:11054537). 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 (PubMed:10669416). Links G protein-coupled receptor activation to PIP3 production (PubMed:10669416). Involved in immune, inflammatory and allergic responses (PubMed:10669416, PubMed:10669418, PubMed:16127437, PubMed:31554793). 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 (PubMed:10669416). Controls motility of dendritic cells (PubMed:15318168). Together with PIK3CD is involved in natural killer (NK) cell development and migration towards the sites of inflammation (PubMed:16116162, PubMed:19297623). Participates in T-lymphocyte migration (PubMed:19297623). Regulates T-lymphocyte proliferation, activation 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 (PubMed:17673465). Regulates alpha-IIb/beta-3 integrins (ITGA2B/ ITGB3) adhesive function in platelets downstream of P2Y12 through a lipid kinase activity-independent mechanism (PubMed:17673465). May have also a lipid kinase activity-dependent function in platelet aggregation (PubMed:17673465). Involved in endothelial progenitor cell migration. Negative regulator of cardiac contractility (PubMed:12297047). Modulates cardiac contractility by anchoring protein kinase A (PKA) and PDE3B activation, reducing cAMP levels (PubMed:12297047, PubMed:15294162, PubMed:21474070). Regulates cardiac contractility also by promoting beta-adrenergic receptor internalization by binding to GRK2 and by non-muscle tropomyosin phosphorylation (PubMed:21474070). Also has serine/threonine protein kinase activity: both lipid and protein kinase activities are required for beta-adrenergic receptor endocytosis (By similarity). 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). In neutrophils, participates in a phospholipase C-activating N-formyl peptide-activated GPCR (G protein-coupled receptor) signaling pathway downstream of RASGRP4-mediated Ras-activation, to promote neutrophil functional responses (PubMed:22728827). {ECO:0000250|UniProtKB:P48736, ECO:0000269|PubMed:10669416, ECO:0000269|PubMed:10669418, ECO:0000269|PubMed:11054537, ECO:0000269|PubMed:12297047, ECO:0000269|PubMed:15294162, ECO:0000269|PubMed:15318168, ECO:0000269|PubMed:16116162, ECO:0000269|PubMed:16127437, ECO:0000269|PubMed:17673465, ECO:0000269|PubMed:19297623, ECO:0000269|PubMed:21474070, ECO:0000269|PubMed:22728827, ECO:0000269|PubMed:31554793}.
uniprot
proteins
mass_dalton
126400
uniprot
proteins
pathway_participation
PATHWAY: Phospholipid metabolism; phosphatidylinositol phosphate biosynthesis.
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at Thr-1024 by PKA. Phosphorylation inhibits lipid kinase activity. {ECO:0000269|PubMed:21474070}.; PTM: Autophosphorylation at Ser-1101 has no effect on the phosphatidylinositol-4,5-bisphosphate 3-kinase activity. {ECO:0000250|UniProtKB:P48736}.
uniprot
proteins
protein_family
PI3/PI4-kinase family
uniprot
proteins
pubmed
10669416
uniprot
proteins
pubmed
10669418
uniprot
proteins
pubmed
11054537
uniprot
proteins
pubmed
11416136
uniprot
proteins
pubmed
12297047
uniprot
proteins
pubmed
15294162
uniprot
proteins
pubmed
15318168
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16116162
uniprot
proteins
pubmed
16127437
uniprot
proteins
pubmed
17673465
uniprot
proteins
pubmed
19297623
uniprot
proteins
pubmed
19906996
uniprot
proteins
pubmed
21474070
uniprot
proteins
pubmed
22728827
uniprot
proteins
pubmed
31554793
uniprot
proteins
sequence_length
1102
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P48736}. Cell membrane {ECO:0000250|UniProtKB:P48736}.
uniprot
proteins