LMPD Database

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LMP002227

UniProt Annotations

Entry Information
Gene Namephosphatidylinositol 3-kinase, regulatory subunit, polypeptide 1 (p85 alpha)
Protein EntryQ3TP23_MOUSE
UniProt IDQ3TP23
SpeciesMouse
Comments
Comment typeDescription
DomainThe SH3 domain mediates the binding to CBLB. {ECO:0000250}.
FunctionBinds 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). {ECO:0000250}.
InteractionQ8IZP0:ABI1 (xeno); NbExp=3; IntAct=EBI-641764, EBI-375446; O88665:Brd7; NbExp=11; IntAct=EBI-641764, EBI-643930; Q62448:Eif4g2; NbExp=3; IntAct=EBI-641764, EBI-296494; P35569:Irs1; NbExp=2; IntAct=EBI-641764, EBI-400825; P42337:Pik3ca; NbExp=6; IntAct=EBI-641764, EBI-641748; Q8BTI9:Pik3cb; NbExp=4; IntAct=EBI-641764, EBI-644672; O35904-2:Pik3cd; NbExp=2; IntAct=EBI-641764, EBI-6470774; Q8R5H6:Wasf1; NbExp=2; IntAct=EBI-641764, EBI-774719;
PtmPhosphorylated. Tyrosine phosphorylated in response to signaling by FGFR1, FGFR2, FGFR3 and FGFR4. 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 (By similarity). Phosphorylated by CSF1R. Phosphorylated by ERBB4. Phosphorylated on tyrosine residues by TEK/TIE2. {ECO:0000250, ECO:0000269|PubMed:10353604, ECO:0000269|PubMed:10521483, ECO:0000269|PubMed:11294897, ECO:0000269|PubMed:17947660, ECO:0000269|PubMed:18034455, ECO:0000269|PubMed:9312046}.
PtmPolyubiquitinated in T-cells by CBLB; which does not promote proteasomal degradation but impairs association with CD28 and CD3Z upon T-cell activation. {ECO:0000269|PubMed:11526404}.
SimilarityBelongs to the PI3K p85 subunit family. {ECO:0000305}.
SimilarityContains 1 Rho-GAP domain. {ECO:0000255|PROSITE- ProRule:PRU00172}.
SimilarityContains 1 SH3 domain. {ECO:0000255|PROSITE- ProRule:PRU00192}.
SimilarityContains 2 SH2 domains. {ECO:0000255|PROSITE- ProRule:PRU00191}.
SubunitHeterodimer of a regulatory subunit PIK3R1 and a p110 catalytic subunit (PIK3CA, PIK3CB or PIK3CD). Interacts with phosphorylated LAT, LAX1 and TRAT1 upon TCR activation. The SH2 domains interact with the YTHM motif of phosphorylated INSR in vitro. Also interacts with tyrosine-phosphorylated IGF1R in vitro. Interacts with IRS1 and phosphorylated IRS4. Interacts with NISCH and RUFY3 (By similarity). Interacts with phosphorylated TOM1L1. Interacts with phosphorylated LIME1 upon TCR or BCR activation. Interacts with CBLB. Interacts with CD28 and CD3Z upon T-cell activation. Interacts with SOCS7 and HCST. Interacts with AXL, FASLG, FGR, HCK, KIT and BCR. Interacts with PTK2/FAK1 (By similarity). Interacts with PDGFRB (tyrosine phosphorylated) (By similarity). Interacts with NTRK1 (phosphorylated upon ligand- binding) (By similarity). Interacts with FER. Interacts with FGFR1, FGFR2, FGFR3 and FGFR4 (phosphorylated) (Probable). Interacts with PDGFRA (tyrosine phosphorylated). Interacts (via SH2 domain) with CSF1R (tyrosine phosphorylated). Interacts with LYN (via SH3 domain); this enhances enzyme activity. Interacts with ERBB4. Interacts (via SH2 domain) with TEK/TIE2 (tyrosine phosphorylated). {ECO:0000250, ECO:0000269|PubMed:10353604, ECO:0000269|PubMed:10521483, ECO:0000269|PubMed:10528161, ECO:0000269|PubMed:10646608, ECO:0000269|PubMed:11006284, ECO:0000269|PubMed:11113178, ECO:0000269|PubMed:11294897, ECO:0000269|PubMed:11526404, ECO:0000269|PubMed:11711534, ECO:0000269|PubMed:12052866, ECO:0000269|PubMed:14610044, ECO:0000269|PubMed:16249387, ECO:0000269|PubMed:1646396, ECO:0000269|PubMed:8128248, ECO:0000269|PubMed:8943348, ECO:0000269|PubMed:9312046, ECO:0000305}.