Search by BoMiProt ID - Bomi7938


Primary Information

BoMiProt ID Bomi7938
Protein Name Phosphatidylinositol 3-kinase regulatory subunit alpha/Phosphatidylinositol 3-kinase 85 kDa regulatory subunit alpha
Organism Bos taurus
Uniprot IDP23727
Milk FractionExosomes
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.