Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform

Details

Name
Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
Synonyms
  • 2.7.1.153
  • p110gamma
  • p120-PI3K
  • Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit gamma
  • Phosphoinositide-3-kinase catalytic gamma polypeptide
  • PI3-kinase subunit gamma
  • PtdIns-3-kinase subunit p110-gamma
  • Serine/threonine protein kinase PIK3CG
Gene Name
PIK3CG
Organism
Humans
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
1-phosphatidylinositol-3-kinase activity / 1-phosphatidylinositol-4-phosphate 3-kinase activity / ATP binding / ephrin receptor binding / phosphatidylinositol 3-kinase activity / phosphatidylinositol-4,5-bisphosphate 3-kinase activity / protein kinase activity / protein serine/threonine kinase activity
Processes
adaptive immune response / angiogenesis / blood coagulation / cellular response to cAMP / cytokine production / dendritic cell chemotaxis / endocytosis / G-protein coupled receptor signaling pathway / hepatocyte apoptotic process / inflammatory response / innate immune response / mast cell degranulation / natural killer cell chemotaxis / negative regulation of cardiac muscle contraction / negative regulation of fibroblast apoptotic process / negative regulation of triglyceride catabolic process / neutrophil chemotaxis / neutrophil extravasation / phosphatidylinositol 3-kinase signaling / phosphatidylinositol biosynthetic process / phospholipid metabolic process / platelet activation / platelet aggregation / positive regulation of acute inflammatory response / positive regulation of cytosolic calcium ion concentration / positive regulation of MAP kinase activity / positive regulation of protein kinase B signaling / regulation of calcium ion transmembrane transport / regulation of cell adhesion mediated by integrin / respiratory burst involved in defense response / secretory granule localization / small molecule metabolic process / T cell activation / T cell chemotaxis / T cell proliferation
Components
cytoplasm / cytosol / mast cell granule / membrane / phosphatidylinositol 3-kinase complex, class IB / plasma membrane
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
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
Chromosome Location
7
Locus
7q22.3
External Identifiers
ResourceLink
UniProtKB IDP48736
UniProtKB Entry NamePK3CG_HUMAN
GenBank Protein ID1507822
GenBank Gene IDX83368
GenAtlas IDPIK3CG
HGNC IDHGNC:8978
General References
  1. Stoyanov B, Volinia S, Hanck T, Rubio I, Loubtchenkov M, Malek D, Stoyanova S, Vanhaesebroeck B, Dhand R, Nurnberg B, et al.: Cloning and characterization of a G protein-activated human phosphoinositide-3 kinase. Science. 1995 Aug 4;269(5224):690-3. [Article]
  2. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, 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 CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, 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 WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [Article]
  3. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [Article]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  5. Gu C, Park S: The EphA8 receptor regulates integrin activity through p110gamma phosphatidylinositol-3 kinase in a tyrosine kinase activity-independent manner. Mol Cell Biol. 2001 Jul;21(14):4579-97. [Article]
  6. Naga Prasad SV, Laporte SA, Chamberlain D, Caron MG, Barak L, Rockman HA: Phosphoinositide 3-kinase regulates beta2-adrenergic receptor endocytosis by AP-2 recruitment to the receptor/beta-arrestin complex. J Cell Biol. 2002 Aug 5;158(3):563-75. Epub 2002 Aug 5. [Article]
  7. Czupalla C, Culo M, Muller EC, Brock C, Reusch HP, Spicher K, Krause E, Nurnberg B: Identification and characterization of the autophosphorylation sites of phosphoinositide 3-kinase isoforms beta and gamma. J Biol Chem. 2003 Mar 28;278(13):11536-45. Epub 2002 Dec 26. [Article]
  8. Patrucco E, Notte A, Barberis L, Selvetella G, Maffei A, Brancaccio M, Marengo S, Russo G, Azzolino O, Rybalkin SD, Silengo L, Altruda F, Wetzker R, Wymann MP, Lembo G, Hirsch E: PI3Kgamma modulates the cardiac response to chronic pressure overload by distinct kinase-dependent and -independent effects. Cell. 2004 Aug 6;118(3):375-87. [Article]
  9. Suire S, Coadwell J, Ferguson GJ, Davidson K, Hawkins P, Stephens L: p84, a new Gbetagamma-activated regulatory subunit of the type IB phosphoinositide 3-kinase p110gamma. Curr Biol. 2005 Mar 29;15(6):566-70. [Article]
  10. Naga Prasad SV, Jayatilleke A, Madamanchi A, Rockman HA: Protein kinase activity of phosphoinositide 3-kinase regulates beta-adrenergic receptor endocytosis. Nat Cell Biol. 2005 Aug;7(8):785-96. [Article]
  11. Rommel C, Camps M, Ji H: PI3K delta and PI3K gamma: partners in crime in inflammation in rheumatoid arthritis and beyond? Nat Rev Immunol. 2007 Mar;7(3):191-201. Epub 2007 Feb 9. [Article]
  12. Barberis L, Hirsch E: Targeting phosphoinositide 3-kinase gamma to fight inflammation and more. Thromb Haemost. 2008 Feb;99(2):279-85. doi: 10.1160/TH07-10-0632. [Article]
  13. Oudit GY, Penninger JM: Cardiac regulation by phosphoinositide 3-kinases and PTEN. Cardiovasc Res. 2009 May 1;82(2):250-60. doi: 10.1093/cvr/cvp014. Epub 2009 Jan 15. [Article]
  14. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
  15. Wilson LS, Baillie GS, Pritchard LM, Umana B, Terrin A, Zaccolo M, Houslay MD, Maurice DH: A phosphodiesterase 3B-based signaling complex integrates exchange protein activated by cAMP 1 and phosphatidylinositol 3-kinase signals in human arterial endothelial cells. J Biol Chem. 2011 May 6;286(18):16285-96. doi: 10.1074/jbc.M110.217026. Epub 2011 Mar 10. [Article]
  16. Walker EH, Perisic O, Ried C, Stephens L, Williams RL: Structural insights into phosphoinositide 3-kinase catalysis and signalling. Nature. 1999 Nov 18;402(6759):313-20. [Article]
  17. Camps M, Ruckle T, Ji H, Ardissone V, Rintelen F, Shaw J, Ferrandi C, Chabert C, Gillieron C, Francon B, Martin T, Gretener D, Perrin D, Leroy D, Vitte PA, Hirsch E, Wymann MP, Cirillo R, Schwarz MK, Rommel C: Blockade of PI3Kgamma suppresses joint inflammation and damage in mouse models of rheumatoid arthritis. Nat Med. 2005 Sep;11(9):936-43. Epub 2005 Aug 28. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02010StaurosporineexperimentalunknownDetails
DB02375MyricetinexperimentalunknownDetails
DB05241XL765investigationalunknownDetails
DB047695-QUINOXALIN-6-YLMETHYLENE-THIAZOLIDINE-2,4-DIONEexperimentalunknownDetails
DB068312-((9H-PURIN-6-YLTHIO)METHYL)-5-CHLORO-3-(2-METHOXYPHENYL)QUINAZOLIN-4(3H)-ONEexperimentalunknownDetails
DB06836N-(5-{4-Chloro-3-[(2-hydroxyethyl)sulfamoyl]phenyl}-4-methyl-1,3-thiazol-2-yl)acetamideexperimentalunknownDetails
DB070735,5-dimethyl-2-morpholin-4-yl-5,6-dihydro-1,3-benzothiazol-7(4H)-oneexperimentalunknownDetails
DB073353-[4-AMINO-1-(1-METHYLETHYL)-1H-PYRAZOLO[3,4-D]PYRIMIDIN-3-YL]PHENOLexperimentalunknownDetails
DB07503(5E)-5-[(2,2-DIFLUORO-1,3-BENZODIOXOL-5-YL)METHYLENE]-1,3-THIAZOLIDINE-2,4-DIONEexperimentalunknownDetails
DB08059WortmanninexperimentalunknownDetails
DB02656LY-294002experimentalunknownDetails
DB083001-methyl-3-naphthalen-2-yl-1H-pyrazolo[3,4-d]pyrimidin-4-amineexperimentalunknownDetails
DB04216Quercetinexperimental, investigationalunknownDetails
DB12010Fostamatinibapproved, investigationalunknowninhibitorDetails
DB05552TG100-115investigationalyesinhibitorDetails
DB11952Duvelisibapproved, investigationalyesinhibitorDetails
DB12483Copanlisibapproved, investigationalunknowninhibitorDetails