Primary Information | |
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BoMiProt ID | Bomi7938 |
Protein Name | Phosphatidylinositol 3-kinase regulatory subunit alpha/Phosphatidylinositol 3-kinase 85 kDa regulatory subunit alpha |
Organism | Bos taurus |
Uniprot ID | P23727 |
Milk Fraction | Exosomes |
Ref Sequence ID | NP_777000.1 |
Aminoacid Length | 724 |
Molecular Weight | 83497 |
FASTA Sequence | Download |
Gene Name | PIK3R1 |
Gene ID | 282307 |
Protein Existence Status | Reviewed |
Secondary Information | |
Presence in other biological fluids/tissue/cells | mammary gland |
Protein Function | PI 3-kinases catalyze the transfer of phosphate to the 3′-OH position of inositol lipids to produce phosphatidylinositol-3,4-bisphosphate and phosphatidylinositol-3,4,5-trisphosphate (PIP3), which in turn act as second messengers by recruiting proteins containing pleckstrin homology (PH) domains to the plasma membrane to assemble signaling complexes. |
Biochemical Properties | The SH2 domains are of fundamental importance for the enzymatic function of PI 3-kinase, since they bind to phosphotyrosine residues of activated growth factor receptors and adapter molecules such as the platelet-derived growth factor (PDGF) receptors and the insulin receptor substrate IRS-1. |
PTMs | N-Acetylation at Ser, Phosphorylation at Ser/Tyr, Ubl conjugation |
Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation | >sp|P23727|P85A_BOVIN Phosphatidylinositol 3-kinase regulatory subunit alpha OS=Bos taurus OX=9913 GN=PIK3R1 PE=1 SV=1 MSAEGYQYRALYDYKKEREEDIDLHLGDILTVNKGSLVALGFSDGQEAKPEEIGWLNGYN ETTGERGDFPGTYVEYIGRKKISPPTPKPRPPRPLPVAPGPSKTEADSEQQASTLPDLAE QFAPPDVAPPLLIKLVEAIEKKGLECSTLYRTQS*154SSNPAELRQLLDCDTASLDLEMFDVH VLADAFKRYLLDLPNPVIPVAVSSELISLAPEVQSSEEYIQLLKKLIRSPSIPHQYWLTL QYLLKHFFKLSQTSSKNLLNARVLSELFSPLLFRFPAAS*279SENTEHLIKIIEILISTEWNE RQPAPALPPKPPKPTTVANNGMNNNMSLQDAEWYWGDISREEVNEKLRDTADGTFLVRDA STKMHGDYTLTLRKGGNNKLIKIFHRDGKYGFSDPLTFNSVVELINHYRNESLAQYNPKL DVKLLYPVSKYQQDQVVKEDNIEAVGKKLHEYNTQFQEKSREYDRLY*467EDYTRTSQEIQMK RTAIEAFNETIKIFEEQCQTQERYSKEYIEKFKREGNETEIQRIMHNYEKLKSRISEIVD SRRRLEEDLKKQAAEYREIDKRMNSIKPDLIQLRKTRDQY*580LMWLTQKGVRQKKLNEWLGN ENTEDQYSLVEDDEDLPHHDEKTWNVGSSNRNKAENLLRGKRDGTFLVRESSKQGCYACS VVVDGEVKHCVINKTATGYGFAEPYNLYSSLKELVLHYQHTS*608LVQHNDSLNVTLAYPVYA QQRR |
SCOP | Class : Alpha and beta proteins (a+b) Fold : SH2-like Superfamily : SH2 domain Family : SH2 domain Domain Name : 1BFJ A:1-111 Class : All beta proteins Fold : SH3-like barrel Superfamily : SH3-domain Family : SH3-domain Domain Name : 2PNI A:5-80 Class : All alpha proteins Fold : Left-handed antiparallel coiled-coil Superfamily : PI3K inter-SH2 coiled-coil domain Family : PI3K inter-SH2 coiled-coil domain Domain Name : DXU B:431-599 Class : All alpha proteins Fold : GTPase activation domain, GAP Superfamily : GTPase activation domain, GAP Family : BCR-homology GTPase activation domain (RhoGAP-domain) Domain Name : 6D81 A:113-298 |
CATH | Matched CATH superfamily 3.30.505.10 2.30.30.40 |
Predicted Disorder Regions | NA |
DisProt Annotation | |
TM Helix Prediction | No TM helices |
Significance of PTMs | Phosphorylation of Ser608 plays a role as a shutoff switch in growth factor signaling and contributes to the differences in functional properties of different PI 3-kinase isoforms in vivo. |
PDB ID | 1BFI, 1BFJ, 1OO3, 1OO4, 1PNJ, 1QAD, 2PNA, 2PNB, 2PNI, 5DXH, 5DXU, 5T8F, 6D81, 6D82, 6D85, 6D86, 6D87, 6G6W, 6MRP, 6OCO, 6OCU, 6R4R, 7JIS, |
Bibliography | 1.Foukas LC, Beeton CA, Jensen J, Phillips WA, Shepherd PR. Regulation of phosphoinositide 3-kinase by its intrinsic serine kinase activity in vivo. Mol Cell Biol. 2004 Feb;24(3):966-75. doi:10.1128/MCB.24.3.966-975.2004. PMID: 14729945; PMCID: PMC321424. 2.Synthesis and function of 3-phosphorylated inositol lipids.Vanhaesebroeck B, Leevers SJ, Ahmadi K, Timms J, Katso R, Driscoll PC, Woscholski R, Parker PJ, Waterfield MD.Annu Rev Biochem. 2001; 70():535-602. 3.Regulation of phosphatidylinositol 3'-kinase by tyrosyl phosphoproteins. Full activation requires occupancy of both SH2 domains in the 85-kDa regulatory subunit.Rordorf-Nikolic T, Van Horn DJ, Chen D, White MF, Backer JM.J Biol Chem. 1995 Feb 24; 270(8):3662-6. |