Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
| Name | Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform |
|---|---|
| Synonyms |
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| Gene Name | PIK3CG |
| Organism | Human |
| Amino acid sequence | >lcl|BSEQ0019096|Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform MELENYKQPVVLREDNCRRRRRMKPRSAAASLSSMELIPIEFVLPTSQRKCKSPETALLH VAGHGNVEQMKAQVWLRALETSVAADFYHRLGPHHFLLLYQKKGQWYEIYDKYQVVQTLD CLRYWKATHRSPGQIHLVQRHPPSEESQAFQRQLTALIGYDVTDVSNVHDDELEFTRRGL VTPRMAEVASRDPKLYAMHPWVTSKPLPEYLWKKIANNCIFIVIHRSTTSQTIKVSPDDT PGAILQSFFTKMAKKKSLMDIPESQSEQDFVLRVCGRDEYLVGETPIKNFQWVRHCLKNG EEIHVVLDTPPDPALDEVRKEEWPLVDDCTGVTGYHEQLTIHGKDHESVFTVSLWDCDRK FRVKIRGIDIPVLPRNTDLTVFVEANIQHGQQVLCQRRTSPKPFTEEVLWNVWLEFSIKI KDLPKGALLNLQIYCGKAPALSSKASAESPSSESKGKVQLLYYVNLLLIDHRFLLRRGEY VLHMWQISGKGEDQGSFNADKLTSATNPDKENSMSISILLDNYCHPIALPKHQPTPDPEG DRVRAEMPNQLRKQLEAIIATDPLNPLTAEDKELLWHFRYESLKHPKAYPKLFSSVKWGQ QEIVAKTYQLLARREVWDQSALDVGLTMQLLDCNFSDENVRAIAVQKLESLEDDDVLHYL LQLVQAVKFEPYHDSALARFLLKRGLRNKRIGHFLFWFLRSEIAQSRHYQQRFAVILEAY LRGCGTAMLHDFTQQVQVIEMLQKVTLDIKSLSAEKYDVSSQVISQLKQKLENLQNSQLP ESFRVPYDPGLKAGALAIEKCKVMASKKKPLWLEFKCADPTALSNETIGIIFKHGDDLRQ DMLILQILRIMESIWETESLDLCLLPYGCISTGDKIGMIEIVKDATTIAKIQQSTVGNTG AFKDEVLNHWLKEKSPTEEKFQAAVERFVYSCAGYCVATFVLGIGDRHNDNIMITETGNL FHIDFGHILGNYKSFLGINKERVPFVLTPDFLFVMGTSGKKTSPHFQKFQDICVKAYLAL RHHTNLLIILFSMMLMTGMPQLTSKEDIEYIRDALTVGKNEEDAKKYFLDQIEVCRDKGW TVQFNWFLHLVLGIKQGEKHSA |
| Number of residues | 1102 |
| Molecular Weight | 126452.625 |
| Theoretical pI | 7.53 |
| GO Classification | Functions
Processes
Components
|
| General Function | Protein serine/threonine kinase activity |
| Specific 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 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. |
| Pfam Domain Function | |
| Transmembrane Regions | Not Available |
| GenBank Protein ID | 1507822 |
| UniProtKB ID | P48736 |
| UniProtKB Entry Name | PK3CG_HUMAN |
| Cellular Location | Cytoplasm |
| Gene sequence | >lcl|BSEQ0019097|Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform (PIK3CG) ATGGAGCTGGAGAACTATAAACAGCCCGTGGTGCTGAGAGAGGACAACTGCCGAAGGCGC CGGAGGATGAAGCCGCGCAGTGCTGCGGCCAGCCTGTCCTCCATGGAGCTCATCCCCATC GAGTTCGTGCTGCCCACCAGCCAGCGCAAATGCAAGAGCCCCGAAACGGCGCTGCTGCAC GTGGCCGGCCACGGCAACGTGGAGCAGATGAAGGCCCAGGTGTGGCTGCGAGCGCTGGAG ACCAGCGTGGCGGCGGACTTCTACCACCGGCTGGGACCGCATCACTTCCTCCTGCTCTAT CAGAAGAAGGGGCAGTGGTACGAGATCTACGACAAGTACCAGGTGGTGCAGACTCTGGAC TGCCTGCGCTACTGGAAGGCCACGCACCGGAGCCCGGGCCAGATCCACCTGGTGCAGCGG CACCCGCCCTCCGAGGAGTCCCAAGCCTTCCAGCGGCAGCTCACGGCGCTGATTGGCTAT GACGTCACTGACGTCAGCAACGTGCACGACGATGAGCTGGAGTTCACGCGCCGTGGCTTG GTGACCCCGCGCATGGCGGAGGTGGCCAGCCGCGACCCCAAGCTCTACGCCATGCACCCG TGGGTGACGTCCAAGCCCCTCCCGGAGTACCTGTGGAAGAAGATTGCCAACAACTGCATC TTCATCGTCATTCACCGCAGCACCACCAGCCAGACCATTAAGGTCTCACCCGACGACACC CCCGGCGCCATCCTGCAGAGCTTCTTCACCAAGATGGCCAAGAAGAAATCTCTGATGGAT ATTCCCGAAAGCCAAAGCGAACAGGATTTTGTGCTGCGCGTCTGTGGCCGGGATGAGTAC CTGGTGGGCGAAACGCCCATCAAAAACTTCCAGTGGGTGAGGCACTGCCTCAAGAACGGA GAAGAGATTCACGTGGTACTGGACACGCCTCCAGACCCGGCCCTAGACGAGGTGAGGAAG GAAGAGTGGCCACTGGTGGATGACTGCACGGGAGTCACCGGCTACCATGAGCAGCTTACC ATCCACGGCAAGGACCACGAGAGTGTGTTCACCGTGTCCCTGTGGGACTGCGACCGCAAG TTCAGGGTCAAGATCAGAGGCATTGATATCCCCGTCCTGCCTCGGAACACCGACCTCACA GTTTTTGTAGAGGCAAACATCCAGCATGGGCAACAAGTCCTTTGCCAAAGGAGAACCAGC CCCAAACCCTTCACAGAGGAGGTGCTGTGGAATGTGTGGCTTGAGTTCAGTATCAAAATC AAAGACTTGCCCAAAGGGGCTCTACTGAACCTCCAGATCTACTGCGGTAAAGCTCCAGCA CTGTCCAGCAAGGCCTCTGCAGAGTCCCCCAGTTCTGAGTCCAAGGGCAAAGTTCAGCTT CTCTATTATGTGAACCTGCTGCTGATAGACCACCGTTTCCTCCTGCGCCGTGGAGAATAC GTCCTCCACATGTGGCAGATATCTGGGAAGGGAGAAGACCAAGGAAGCTTCAATGCTGAC AAACTCACGTCTGCAACTAACCCAGACAAGGAGAACTCAATGTCCATCTCCATTCTTCTG GACAATTACTGCCACCCGATAGCCCTGCCTAAGCATCAGCCCACCCCTGACCCGGAAGGG GACCGGGTTCGAGCAGAAATGCCCAACCAGCTTCGCAAGCAATTGGAGGCGATCATAGCC ACTGATCCACTTAACCCTCTCACAGCAGAGGACAAAGAATTGCTCTGGCATTTTAGATAC GAAAGCCTTAAGCACCCAAAAGCATATCCTAAGCTATTTAGTTCAGTGAAATGGGGACAG CAAGAAATTGTGGCCAAAACATACCAATTGTTGGCCAGAAGGGAAGTCTGGGATCAAAGT GCTTTGGATGTTGGGTTAACAATGCAGCTCCTGGACTGCAACTTCTCAGATGAAAATGTA AGAGCCATTGCAGTTCAGAAACTGGAGAGCTTGGAGGACGATGATGTTCTGCATTACCTT CTACAATTGGTCCAGGCTGTGAAATTTGAACCATACCATGATAGCGCCCTTGCCAGATTT CTGCTGAAGCGTGGTTTAAGAAACAAAAGAATTGGTCACTTTTTGTTTTGGTTCTTGAGA AGTGAGATAGCCCAGTCCAGACACTATCAGCAGAGGTTCGCTGTGATTCTGGAAGCCTAT CTGAGGGGCTGTGGCACAGCCATGCTGCACGACTTTACCCAACAAGTCCAAGTAATCGAG ATGTTACAAAAAGTCACCCTTGATATTAAATCGCTCTCTGCTGAAAAGTATGACGTCAGT TCCCAAGTTATTTCACAACTTAAACAAAAGCTTGAAAACCTGCAGAATTCTCAACTCCCC GAAAGCTTTAGAGTTCCATATGATCCTGGACTGAAAGCAGGAGCGCTGGCAATTGAAAAA TGTAAAGTAATGGCCTCCAAGAAAAAACCACTATGGCTTGAGTTTAAATGTGCCGATCCT ACAGCCCTATCAAATGAAACAATTGGAATTATCTTTAAACATGGTGATGATCTGCGCCAA GACATGCTTATTTTACAGATTCTACGAATCATGGAGTCTATTTGGGAGACTGAATCTTTG GATCTATGCCTCCTGCCATATGGTTGCATTTCAACTGGTGACAAAATAGGAATGATCGAG ATTGTGAAAGACGCCACGACAATTGCCAAAATTCAGCAAAGCACAGTGGGCAACACGGGA GCATTTAAAGATGAAGTCCTGAATCACTGGCTCAAAGAAAAATCCCCTACTGAAGAAAAG TTTCAGGCAGCAGTGGAGAGATTTGTTTATTCCTGTGCAGGCTACTGTGTGGCAACCTTT GTTCTTGGAATAGGCGACAGACACAATGACAATATTATGATCACCGAGACAGGAAACCTA TTTCATATTGACTTCGGGCACATTCTTGGGAATTACAAAAGTTTCCTGGGCATTAATAAA GAGAGAGTGCCATTTGTGCTAACCCCTGACTTCCTCTTTGTGATGGGAACTTCTGGAAAG AAGACAAGCCCACACTTCCAGAAATTTCAGGACATCTGTGTTAAGGCTTATCTAGCCCTT CGTCATCACACAAACCTACTGATCATCCTGTTCTCCATGATGCTGATGACAGGAATGCCC CAGTTAACAAGCAAAGAAGACATTGAATATATCCGGGATGCCCTCACAGTGGGGAAAAAT GAGGAGGATGCTAAAAAGTATTTTCTTGATCAGATCGAAGTTTGCAGAGACAAAGGATGG ACTGTGCAGTTTAATTGGTTTCTACATCTTGTTCTTGGCATCAAACAAGGAGAGAAACAT TCAGCCTAA |
| GenBank Gene ID | X83368 |
| GeneCard ID | Not Available |
| GenAtlas ID | PIK3CG |
| HGNC ID | HGNC:8978 |
| Chromosome Location | 7 |
| Locus | 7q22.3 |
| References |
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