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Gene Symbol |
PIK3CG |
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Aliases |
PI3CG, PI3K, PI3Kgamma, PIK3, p110gamma, p120-PI3K |
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Entrez Gene ID |
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Gene Name |
Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit gamma |
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Chromosomal Location |
7q22.3 |
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HGNC ID |
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Summary |
Phosphoinositide 3-kinases (PI3Ks) phosphorylate inositol lipids and are involved in the immune response. The protein encoded by this gene is a class I catalytic subunit of PI3K. Like other class I catalytic subunits (p110-alpha p110-beta, and p110-delta), the encoded protein binds a p85 regulatory subunit to form PI3K. This gene is located in a commonly deleted segment of chromosome 7 previously identified in myeloid leukemias. Several transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jun 2015]
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RefSeq DNA |
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RefSeq mRNA |
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e!Ensembl
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Protein Information |
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Protein Name |
Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform, 1-phosphatidylinositol 3-kinase, PI3-kinase subunit gamma, phosphatidylinositol 3 kinase gamma, p110 gamma, phosphatidylinositol 3-kinase catalytic 110-kD gamma, phosphatidylinositol-4,5-bisphosphate 3-kinase 110 kDa catalytic subunit gamma, phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit gamma isoform, phosphoinositide-3-kinase gamma catalytic subunit, ptdIns-3-kinase subunit gamma, ptdIns-3-kinase subunit p110-gamma, serine/threonine protein kinase PIK3CG |
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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 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. |
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UniProt |
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PDB |
1E8Y, 1E8Z, 1HE8, 2A4Z, 2A5U, 2CHW, 2CHX, 2CHZ, 2V4L, 3APC, 3APD, 3APF, 3CSF, 3CST, 3DBS, 3DPD, 3ENE, 3IBE, 3L08, 3L13, 3L16, 3L17, 3L54, 3LJ3, 3MJW, 3ML8, 3ML9, 3NZS, 3NZU, 3OAW, 3P2B, 3PRE, 3PRZ, 3PS6, 3QAQ, 3QAR, 3QJZ, 3QK0, 3R7Q, 3R7R, 3S2A, 3SD5, 3T8M, 3TJP, 3TL5, 3ZVV, 3ZW3, 4ANU, 4ANV, 4ANW, 4ANX, |
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Interactions |
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STRING |
MINT |
IntAct |
ENSP00000378517 |
P10451 |
P10451 |
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View interactions
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Associated Diseases
Disease group | Disease Name | References |
Cardiovascular Diseases |
Heart Failure |
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Myocardial Failure |
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Endocrine System Diseases |
PCOS |
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Neoplasms |
Medulloblastoma |
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Lymphoma |
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Psychiatric/Brain disorders |
Autistic Disorder |
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References |
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Ma Xiang, Fan Lu, Meng Yan, Hou Zheng, Mao Yun-Dong, Wang Wei, Ding Wei, Liu Jia-Yin |
Laboratory of Reproductive Medicine, Nanjing Medical University, and The Center of Clinical Reproductive Medicine, The First Affiliated Hospital of Nanjing Medical University, People's Republic of China. |
Mol Hum Reprod. 2007 Aug;13(8):527-35. doi: 10.1093/molehr/gam036. Epub 2007 Jun |
Abstract
Polycystic ovary syndrome (PCOS) is the most common cause of anovulatory infertility, affecting 5-10% of females of reproductive age. Currently, little is known about the changes in whole proteins between PCOS and normal ovaries. In the present study, a proteomic approach comprised two-dimensional gel electrophoresis (2DE) analysis and mass spectroscopy was used to identify proteins and examine expression patterns in three PCOS and normal ovaries. One hundred and ten protein spots were separated and showed different intensities between PCOS and normal ovaries. Sixty-nine proteins associated with cellular metabolism and physiological process were identified from 72 spots. Fifty-four proteins were up-regulated in PCOS ovaries and 15 other proteins were up-regulated in normal ovaries. These data demonstrate, for the first time, the complexity in the regulation of ovarian protein expression in human PCOS, and will provide important insight for a better understanding of the pathogenetic mechanisms underlying this clinical disorder. |
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National Institute for Research in Reproductive Health, Jehangir Merwanji Street, Parel, Mumbai-400 012
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