PIK3CG
entrez
5294
canonical
uniprot
P48736
canonical
ensembl
ENSG00000105851
resolver
ensp
ENSP00000352121
resolver
ensp
ENSP00000392258
resolver
ensp
ENSP00000419260
resolver
enst
ENST00000359195
resolver
enst
ENST00000440650
resolver
enst
ENST00000496166
resolver
genesymbol
PIK3CG
resolver
hgnc
HGNC:8978
resolver
uniprot
A4D0Q6
resolver
uniprot
A8K9G9
resolver
uniprot
Q8IV23
resolver
uniprot
Q9BZC8
resolver
uniprot_entry
A8K9G9_HUMAN
resolver
uniprot_entry
PK3CG_HUMAN
resolver
uniprot_sec
A4D0Q6
resolver
uniprot_sec
Q8IV23
resolver
uniprot_sec
Q9BZC8
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 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. {ECO:0000269|PubMed:16127437, ECO:0000269|PubMed:7624799}.
uniprot
proteins
amino_acid_sequence
MELENYKQPVVLREDNCRRRRRMKPRSAAASLSSMELIPIEFVLPTSQRKCKSPETALLHVAGHGNVEQMKAQVWLRALETSVAADFYHRLGPHHFLLLYQKKGQWYEIYDKYQVVQTLDCLRYWKATHRSPGQIHLVQRHPPSEESQAFQRQLTALIGYDVTDVSNVHDDELEFTRRGLVTPRMAEVASRDPKLYAMHPWVTSKPLPEYLWKKIANNCIFIVIHRSTTSQTIKVSPDDTPGAILQSFFTKMAKKKSLMDIPESQSEQDFVLRVCGRDEYLVGETPIKNFQWVRHCLKNGEEIHVVLDTPPDPALDEVRKEEWPLVDDCTGVTGYHEQLTIHGKDHESVFTVSLWDCDRKFRVKIRGIDIPVLPRNTDLTVFVEANIQHGQQVLCQRRTSPKPFTEEVLWNVWLEFSIKIKDLPKGALLNLQIYCGKAPALSSKASAESPSSESKGKVQLLYYVNLLLIDHRFLLRRGEYVLHMWQISGKGEDQGSFNADKLTSATNPDKENSMSISILLDNYCHPIALPKHQPTPDPEGDRVRAEMPNQLRKQLEAIIATDPLNPLTAEDKELLWHFRYESLKHPKAYPKLFSSVKWGQQEIVAKTYQLLARREVWDQSALDVGLTMQLLDCNFSDENVRAIAVQKLESLEDDDVLHYLLQLVQAVKFEPYHDSALARFLLKRGLRNKRIGHFLFWFLRSEIAQSRHYQQRFAVILEAYLRGCGTAMLHDFTQQVQVIEMLQKVTLDIKSLSAEKYDVSSQVISQLKQKLENLQNSQLPESFRVPYDPGLKAGALAIEKCKVMASKKKPLWLEFKCADPTALSNETIGIIFKHGDDLRQDMLILQILRIMESIWETESLDLCLLPYGCISTGDKIGMIEIVKDATTIAKIQQSTVGNTGAFKDEVLNHWLKEKSPTEEKFQAAVERFVYSCAGYCVATFVLGIGDRHNDNIMITETGNLFHIDFGHILGNYKSFLGINKERVPFVLTPDFLFVMGTSGKKTSPHFQKFQDICVKAYLALRHHTNLLIILFSMMLMTGMPQLTSKEDIEYIRDALTVGKNEEDAKKYFLDQIEVCRDKGWTVQFNWFLHLVLGIKQGEKHSA
uniprot
proteins
disease_involvement
DISEASE: Immunodeficiency 97 with autoinflammation (IMD97) [MIM:619802]: An autosomal recessive disorder with variable features. Affected individuals have childhood-onset antibody defects, cytopenias, and T lymphocytic pneumonitis and colitis. Some patients may have features of hemophagocytic lymphohistiocytosis. {ECO:0000269|PubMed:31554793, ECO:0000269|PubMed:33054089}. Note=The disease is caused by variants affecting the gene represented in this entry.
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). 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, 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. 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. 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 (By similarity). {ECO:0000250|UniProtKB:Q9JHG7, ECO:0000269|PubMed:11277933, ECO:0000269|PubMed:12163475, ECO:0000269|PubMed:15135396, ECO:0000269|PubMed:15294162, ECO:0000269|PubMed:16094730, ECO:0000269|PubMed:16123124, ECO:0000269|PubMed:21393242, ECO:0000269|PubMed:31554793, ECO:0000269|PubMed:33054089, ECO:0000269|PubMed:7624799}.
uniprot
proteins
mass_dalton
126454
uniprot
proteins
mutagenesis
MUTAGEN 833; /note="K->R: Loss of kinase activity. Loss of autophosphorylation. Reduced inflammatory reactions but no alterations in cardiac contractility."; /evidence="ECO:0000269|PubMed:15294162, ECO:0000269|PubMed:16094730"; MUTAGEN 947; /note="R->P: Abolishes protein and lipid kinase activity. Does not abolish interaction with GRK2."; /evidence="ECO:0000269|PubMed:16094730"; MUTAGEN 1101; /note="S->A,Q: Loss of autophosphorylation. No effect on phosphatidylinositol-4,5-bisphosphate 3-kinase activity."; /evidence="ECO:0000269|PubMed:12502714
uniprot
proteins
pathway_participation
PATHWAY: Phospholipid metabolism; phosphatidylinositol phosphate biosynthesis. {ECO:0000305|PubMed:11277933, ECO:0000305|PubMed:15135396, ECO:0000305|PubMed:16123124}.
uniprot
proteins
post_translational_modification
PTM: Autophosphorylation at Ser-1101 has no effect on the phosphatidylinositol-4,5-bisphosphate 3-kinase activity. {ECO:0000269|PubMed:12502714}.
uniprot
proteins
protein_family
PI3/PI4-kinase family
uniprot
proteins
pubmed
10580505
uniprot
proteins
pubmed
11277933
uniprot
proteins
pubmed
11416136
uniprot
proteins
pubmed
12163475
uniprot
proteins
pubmed
12502714
uniprot
proteins
pubmed
12690205
uniprot
proteins
pubmed
12853948
uniprot
proteins
pubmed
15135396
uniprot
proteins
pubmed
15294162
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15797027
uniprot
proteins
pubmed
16094730
uniprot
proteins
pubmed
16123124
uniprot
proteins
pubmed
16127437
uniprot
proteins
pubmed
17290298
uniprot
proteins
pubmed
18278175
uniprot
proteins
pubmed
19147653
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21393242
uniprot
proteins
pubmed
31554793
uniprot
proteins
pubmed
33054089
uniprot
proteins
pubmed
7624799
uniprot
proteins
sequence_length
1102
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12163475}. Cell membrane {ECO:0000269|PubMed:12163475}.
uniprot
proteins