- PIK3R1
-
Phosphatidylinositol 3-kinase regulatory subunit alpha is an enzyme that in humans is encoded by the PIK3R1 gene.[1]
Phosphatidylinositol 3-kinase phosphorylates the inositol ring of phosphatidylinositol at the 3-prime position. The enzyme comprises a 110 kD catalytic subunit and a regulatory subunit of either 85, 55, or 50 kD. This gene encodes the 85 kD regulatory subunit. Phosphatidylinositol 3-kinase plays an important role in the metabolic actions of insulin, and a mutation in this gene has been associated with insulin resistance. Alternative splicing of this gene results in three transcript variants encoding different isoforms.[2]
Interactions
PIK3R1 has been shown to interact with EPH receptor A2,[3] KHDRBS1,[4][5] Lymphocyte cytosolic protein 2,[6] Janus kinase 2,[7] GAB2,[8][9] CD117,[10][11][12] BCAR1,[13] CD28,[14] SHB,[15] EZR,[16] PIK3CD,[17] GAB1,[18][19][20] HRAS,[21][22] TUBA1B,[23] CD7,[24][25] FCGR2A,[26][27] Grb2,[28][29] IRS2,[30][31][32][33] ADAM12,[34] TYRO3,[35] VAV1,[18][36] ERBB3,[37][38] Wiskott-Aldrich syndrome protein,[39] LTK,[40][41] PTK2,[42] Interleukin 1 receptor, type I,[43] CBLB,[44][45] Erythropoietin receptor,[36][46] Linker of activated T cells,[47] Cbl gene,[48][49][50] IRS1[51][52][53][33] and CENTG1.[54]
References
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- ^ Gual, Philippe; Gonzalez Teresa, Grémeaux Thierry, Barres Romain, Le Marchand-Brustel Yannick, Tanti Jean-François (Jul. 2003). "Hyperosmotic stress inhibits insulin receptor substrate-1 function by distinct mechanisms in 3T3-L1 adipocytes". J. Biol. Chem. (United States) 278 (29): 26550–7. doi:10.1074/jbc.M212273200. ISSN 0021-9258. PMID 12730242.
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Further reading
- Benito M, Valverde AM, Lorenzo M (1996). "IGF-I: a mitogen also involved in differentiation processes in mammalian cells.". Int. J. Biochem. Cell Biol. 28 (5): 499–510. doi:10.1016/1357-2725(95)00168-9. PMID 8697095.
- Snapper SB, Rosen FS (1999). "The Wiskott-Aldrich syndrome protein (WASP): roles in signaling and cytoskeletal organization.". Annu. Rev. Immunol. 17: 905–29. doi:10.1146/annurev.immunol.17.1.905. PMID 10358777.
- Katada T, Kurosu H, Okada T, et al. (1999). "Synergistic activation of a family of phosphoinositide 3-kinase via G-protein coupled and tyrosine kinase-related receptors.". Chem. Phys. Lipids 98 (1-2): 79–86. doi:10.1016/S0009-3084(99)00020-1. PMID 10358930.
- Zhang W, Samelson LE (2000). "The role of membrane-associated adaptors in T cell receptor signalling.". Semin. Immunol. 12 (1): 35–41. doi:10.1006/smim.2000.0205. PMID 10723796.
- Greenway AL, Holloway G, McPhee DA, et al. (2004). "HIV-1 Nef control of cell signalling molecules: multiple strategies to promote virus replication.". J. Biosci. 28 (3): 323–35. doi:10.1007/BF02970151. PMID 12734410.
- Leavitt SA, SchOn A, Klein JC, et al. (2004). "Interactions of HIV-1 proteins gp120 and Nef with cellular partners define a novel allosteric paradigm.". Curr. Protein Pept. Sci. 5 (1): 1–8. doi:10.2174/1389203043486955. PMID 14965316.
- Joseph AM, Kumar M, Mitra D (2005). "Nef: "necessary and enforcing factor" in HIV infection.". Curr. HIV Res. 3 (1): 87–94. doi:10.2174/1570162052773013. PMID 15638726.
PDB gallery 1bfi: SOLUTION STRUCTURE OF THE C-TERMINAL SH2 DOMAIN OF THE P85ALPHA REGULATORY SUBUNIT OF PHOSPHOINOSITIDE 3-KINASE, NMR, 30 STRUCTURES1bfj: SOLUTION STRUCTURE OF THE C-TERMINAL SH2 DOMAIN OF THE P85ALPHA REGULATORY SUBUNIT OF PHOSPHOINOSITIDE 3-KINASE, NMR, MINIMIZED AVERAGE STRUCTURE1fu5: NMR STRUCTURE OF THE N-SH2 DOMAIN OF THE P85 SUBUNIT OF PI3-KINASE COMPLEXED TO A DOUBLY PHOSPHORYLATED PEPTIDE DERIVED FROM POLYOMAVIRUS MIDDLE T ANTIGEN1fu6: NMR STRUCTURE OF THE N-SH2 DOMAIN OF THE P85 SUBUNIT OF PI3-KINASE1h9o: PHOSPHATIDYLINOSITOL 3-KINASE, P85-ALPHA SUBUNIT: C-TERMINAL SH2 DOMAIN COMPLEXED WITH A TYR751 PHOSPHOPEPTIDE FROM THE PDGF RECEPTOR, CRYSTAL STRUCTURE AT 1.79 A1oo3: P395S mutant of the p85 regulatory subunit of the N-terminal src homology 2 domain of PI3-Kinase1oo4: P395S mutant of the p85 regulatory subunit of the N-terminal src homology 2 domain of PI3-Kinase complexed to a peptide derived from PDGFr1pbw: STRUCTURE OF BCR-HOMOLOGY (BH) DOMAIN1pht: PHOSPHATIDYLINOSITOL 3-KINASE P85-ALPHA SUBUNIT SH3 DOMAIN, RESIDUES 1-851pic: PHOSPHATIDYLINOSITOL 3-KINASE, P85-ALPHA SUBUNIT: C-TERMINAL SH2 DOMAIN COMPLEXED WITH A TYR751 PHOSPHOPEPTIDE FROM THE PDGF RECEPTOR, NMR, MINIMIZED MEAN STRUCTURE1pks: STRUCTURE OF THE PI3K SH3 DOMAIN AND ANALYSIS OF THE SH3 FAMILY1pkt: STRUCTURE OF THE PI3K SH3 DOMAIN AND ANALYSIS OF THE SH3 FAMILY1pnj: SOLUTION STRUCTURE AND LIGAND-BINDING SITE OF THE SH3 DOMAIN OF THE P85ALPHA SUBUNIT OF PHOSPHATIDYLINOSITOL 3-KINASE1qad: Crystal Structure of the C-Terminal SH2 Domain of the P85 alpha Regulatory Subunit of Phosphoinositide 3-Kinase: An SH2 domain mimicking its own substrate2iug: CRYSTAL STRUCTURE OF THE PI3-KINASE P85 N-TERMINAL SH2 DOMAIN2iuh: CRYSTAL STRUCTURE OF THE PI3-KINASE P85 N-TERMINAL SH2 DOMAIN IN COMPLEX WITH C-KIT PHOSPHOTYROSYL PEPTIDE2iui: CRYSTAL STRUCTURE OF THE PI3-KINASE P85 N-TERMINAL SH2 DOMAIN IN COMPLEX WITH PDGFR PHOSPHOTYROSYL PEPTIDE2pna: STRUCTURE OF AN SH2 DOMAIN OF THE P85 ALPHA SUBUNIT OF PHOSPHATIDYLINOSITOL-3-OH KINASE2pnb: STRUCTURE OF AN SH2 DOMAIN OF THE P85 ALPHA SUBUNIT OF PHOSPHATIDYLINOSITOL-3-OH KINASE2pni: SOLUTION STRUCTURE AND LIGAND-BINDING SITE OF THE SH3 DOMAIN OF THE P85ALPHA SUBUNIT OF PHOSPHATIDYLINOSITOL 3-KINASECategories:- Human proteins
- Chromosome 5 gene stubs
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