LMP012515 UniProt Annotations
Gene Name phosphoinositide-3-kinase, regulatory subunit 1 (alpha) Protein Entry P85A_RAT UniProt ID Q63787 Species Rat
Comment type Description Alternative Products Event=Alternative splicing; Named isoforms=3; Name=p85-alpha; IsoId=Q63787-1; Sequence=Displayed; Name=p55-alpha; IsoId=Q63787-2; Sequence=VSP_004709, VSP_004710; Name=p50-alpha; IsoId=Q63787-3; Sequence=VSP_004711, VSP_004712; Domain The SH3 domain mediates the binding to CBLB Function Binds to activated (phosphorylated) protein-Tyr kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Necessary for the insulin-stimulated increase in glucose uptake and glycogen synthesis in insulin-sensitive tissues. Plays an important role in signaling in response to FGFR1, FGFR2, FGFR3, FGFR4, KITLG/SCF, KIT, PDGFRA and PDGFRB. Likewise, plays a role in ITGB2 signaling (By similarity) Interaction A0MZ67:-; NbExp=2; IntAct=EBI-518443, EBI-1392040; P21575:Dnm1; NbExp=2; IntAct=EBI-518443, EBI-80070; P62813:Gabra1; NbExp=4; IntAct=EBI-518443, EBI-6258192; P35570:Irs1; NbExp=3; IntAct=EBI-518443, EBI-520230; Q91V33:Khdrbs1; NbExp=2; IntAct=EBI-518443, EBI-518436; P18545:PDE6G (xeno); NbExp=2; IntAct=EBI-518443, EBI-2622029; Ptm Phosphorylated. Tyrosine phosphorylated in response to signaling by FGFR1, FGFR2, FGFR3 and FGFR4. Phosphorylated by CSF1R. Phosphorylated on tyrosine residues by TEK/TIE2. Dephosphorylated by PTPRJ. Phosphorylated by PIK3CA at Ser-608; phosphorylation is stimulated by insulin and PDGF. The relevance of phosphorylation by PIK3CA is however unclear. Phosphorylated in response to KIT and KITLG/SCF. Phosphorylated by FGR and ERBB4 (By similarity) Ptm Polyubiquitinated in T-cells by CBLB; which does not promote proteasomal degradation but impairs association with CD28 and CD3Z upon T-cell activation Similarity Belongs to the PI3K p85 subunit family Similarity Contains 1 Rho-GAP domain. {ECO:0000255|PROSITE- ProRule:PRU00172}. Similarity Contains 1 SH3 domain. {ECO:0000255|PROSITE- ProRule:PRU00192}. Similarity Contains 2 SH2 domains. {ECO:0000255|PROSITE- ProRule:PRU00191}. Subunit Heterodimer of a regulatory subunit PIK3R1 and a p110 catalytic subunit (PIK3CA, PIK3CB or PIK3CD). Interacts with phosphorylated LAT, LAX1, TRAT1 and LIME1 upon TCR and/or activation. Interacts with phosphorylated TOM1L1. Interacts with CBLB. The SH2 domains interact with the YTHM motif of phosphorylated INSR in vitro. Also interacts with tyrosine- phosphorylated IGF1R in vitro. Interacts with CD28 and CD3Z upon T-cell activation. Interacts with NISCH, SOCS7 and HCST (By similarity). Interacts with IRS1 and phosphorylated IRS4. Interacts with RUFY3. Interacts with FGFR1, FGFR2, FGFR3 and FGFR4 (phosphorylated) (Probable). Interacts with AXL, FASLG, FER, FGR, HCK, KIT and BCR (By similarity). Interacts with PDGFRA (tyrosine phosphorylated) and PDGFRB (tyrosine phosphorylated). Interacts (via SH2 domain) with CSF1R (tyrosine phosphorylated). Interacts with ERBB4 (phosphorylated). Interacts (via SH2 domain) with TEK/TIE2 (tyrosine phosphorylated). Interacts with LYN (via SH3 domain); this enhances enzyme activity (By similarity). Interacts with NTRK1 (phosphorylated upon ligand-binding) (By similarity). Interacts with PTK2/FAK1. {ECO:0000250, ECO:0000269|PubMed:8628286, ECO:0000269|PubMed:8824286, ECO:0000305}. Tissue Specificity The P85-alpha isoform is widely expressed. Expression of the P55-alpha isoform is highest in brain and skeletal muscle. The P50-alpha isoform is abundant in liver with lower levels in brain and muscle.
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