LMPD Database

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LMP002617

UniProt Annotations

Entry Information
Gene Namephosphoinositide-3-kinase, regulatory subunit 1 (alpha)
Protein EntryP85A_HUMAN
UniProt IDP27986
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=5; Name=1; IsoId=P27986-1; Sequence=Displayed; Name=2; Synonyms=AS53; IsoId=P27986-2; Sequence=VSP_021842, VSP_021843; Name=3; Synonyms=p46; IsoId=P27986-3; Sequence=VSP_021841, VSP_021844; Name=4; Synonyms=p85I; IsoId=P27986-4; Sequence=VSP_021845; Name=5; IsoId=P27986-5; Sequence=VSP_045903; Note=No experimental confirmation available.;
DiseaseAgammaglobulinemia 7, autosomal recessive (AGM7) [MIM
DiseaseSHORT syndrome (SHORTS) [MIM
DomainThe SH3 domain mediates the binding to CBLB, and to HIV-1 Nef.
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. {ECO
InteractionQ8IZP0:ABI1; NbExp=8; IntAct=EBI-79464, EBI-375446; P42684:ABL2; NbExp=2; IntAct=EBI-79464, EBI-1102694; P10275:AR; NbExp=5; IntAct=EBI-79464, EBI-608057; P22681:CBL; NbExp=5; IntAct=EBI-79464, EBI-518228; P10747:CD28; NbExp=8; IntAct=EBI-79464, EBI-4314301; Q8IY22:CMIP; NbExp=2; IntAct=EBI-79464, EBI-7689652; P46108:CRK; NbExp=2; IntAct=EBI-79464, EBI-886; P46109:CRKL; NbExp=2; IntAct=EBI-79464, EBI-910; P16410:CTLA4; NbExp=3; IntAct=EBI-79464, EBI-1030991; Q9Y2H0:DLGAP4; NbExp=2; IntAct=EBI-79464, EBI-722139; P00533:EGFR; NbExp=5; IntAct=EBI-79464, EBI-297353; P04626:ERBB2; NbExp=11; IntAct=EBI-79464, EBI-641062; P21860:ERBB3; NbExp=40; IntAct=EBI-79464, EBI-720706; P03372:ESR1; NbExp=6; IntAct=EBI-79464, EBI-78473; P48023:FASLG; NbExp=2; IntAct=EBI-79464, EBI-495538; P11362:FGFR1; NbExp=5; IntAct=EBI-79464, EBI-1028277; P17948:FLT1; NbExp=2; IntAct=EBI-79464, EBI-1026718; P36888:FLT3; NbExp=2; IntAct=EBI-79464, EBI-3946257; Q13480:GAB1; NbExp=33; IntAct=EBI-79464, EBI-517684; P62993:GRB2; NbExp=3; IntAct=EBI-79464, EBI-401755; P42858:HTT; NbExp=7; IntAct=EBI-79464, EBI-466029; P08069:IGF1R; NbExp=4; IntAct=EBI-79464, EBI-475981; P06213:INSR; NbExp=3; IntAct=EBI-79464, EBI-475899; P35568:IRS1; NbExp=12; IntAct=EBI-79464, EBI-517592; P35570:Irs1 (xeno); NbExp=2; IntAct=EBI-79464, EBI-520230; Q9Y4H2:IRS2; NbExp=2; IntAct=EBI-79464, EBI-1049582; P10721:KIT; NbExp=19; IntAct=EBI-79464, EBI-1379503; Q86VI4-3:LAPTM4B; NbExp=2; IntAct=EBI-79464, EBI-3267286; O43561:LAT; NbExp=4; IntAct=EBI-79464, EBI-1222766; Q92918:MAP4K1; NbExp=2; IntAct=EBI-79464, EBI-881; P45983:MAPK8; NbExp=2; IntAct=EBI-79464, EBI-286483; P08581:MET; NbExp=6; IntAct=EBI-79464, EBI-1039152; Q8WX92:NELFB; NbExp=2; IntAct=EBI-79464, EBI-347721; Q6PFX7:Nyap1 (xeno); NbExp=4; IntAct=EBI-79464, EBI-7447489; Q8BM65-4:Nyap2 (xeno); NbExp=3; IntAct=EBI-79464, EBI-7447598; P09619:PDGFRB; NbExp=19; IntAct=EBI-79464, EBI-641237; P42336:PIK3CA; NbExp=13; IntAct=EBI-79464, EBI-2116585; P16885:PLCG2; NbExp=2; IntAct=EBI-79464, EBI-617403; P49023:PXN; NbExp=2; IntAct=EBI-79464, EBI-702209; Q13905:RAPGEF1; NbExp=2; IntAct=EBI-79464, EBI-976876; P26373:RPL13; NbExp=2; IntAct=EBI-79464, EBI-356849; P19793:RXRA; NbExp=8; IntAct=EBI-79464, EBI-78598; Q9UPX8:SHANK2; NbExp=2; IntAct=EBI-79464, EBI-1570571; P29353:SHC1; NbExp=3; IntAct=EBI-79464, EBI-78835; Q96EB6:SIRT1; NbExp=3; IntAct=EBI-79464, EBI-1802965; Q07889:SOS1; NbExp=3; IntAct=EBI-79464, EBI-297487; P12931:SRC; NbExp=6; IntAct=EBI-79464, EBI-621482; P30874:SSTR2; NbExp=5; IntAct=EBI-79464, EBI-6266898; P58753:TIRAP; NbExp=3; IntAct=EBI-79464, EBI-528644; O15455:TLR3; NbExp=2; IntAct=EBI-79464, EBI-6116630; Q15661:TPSAB1; NbExp=2; IntAct=EBI-79464, EBI-1761369; Q9ULW0:TPX2; NbExp=2; IntAct=EBI-79464, EBI-1037322; Q9UKW4:VAV3; NbExp=2; IntAct=EBI-79464, EBI-297568; Q99152:VP3 (xeno); NbExp=3; IntAct=EBI-79464, EBI-1776808; Q8IUH5:ZDHHC17; NbExp=2; IntAct=EBI-9090282, EBI-524753;
PtmPhosphorylated. Tyrosine phosphorylated in response to signaling by FGFR1, FGFR2, FGFR3 and FGFR4. Phosphorylated by CSF1R. Phosphorylated by ERBB4. 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 (By similarity). Phosphorylated in response to KIT and KITLG/SCF. Phosphorylated by FGR. {ECO
PtmPolyubiquitinated in T-cells by CBLB; which does not promote proteasomal degradation but impairs association with CD28 and CD3Z upon T-cell activation. {ECO
SimilarityBelongs to the PI3K p85 subunit family.
SimilarityContains 1 Rho-GAP domain. {ECO
SimilarityContains 1 SH3 domain. {ECO
SimilarityContains 2 SH2 domains. {ECO
SubunitHeterodimer of a regulatory subunit PIK3R1 and a p110 catalytic subunit (PIK3CA, PIK3CB or PIK3CD). Interacts with FER. Interacts (via SH2 domain) with TEK/TIE2 (tyrosine phosphorylated). Interacts with PTK2/FAK1 (By similarity). Interacts with phosphorylated TOM1L1. Interacts with phosphorylated LIME1 upon TCR and/or BCR activation. Interacts with SOCS7. Interacts with RUFY3. Interacts (via SH2 domain) with CSF1R (tyrosine phosphorylated). Interacts with LYN (via SH3 domain); this enhances enzyme activity (By similarity). Interacts with phosphorylated LAT, LAX1 and TRAT1 upon TCR activation. Interacts with CBLB. Interacts with HIV-1 Nef to activate the Nef associated p21-activated kinase (PAK). This interaction depends on the C-terminus of both proteins and leads to increased production of HIV. Interacts with HCV NS5A. 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 IRS1 and phosphorylated IRS4, as well as with NISCH and HCST. Interacts with FASLG, KIT and BCR. Interacts with AXL, FGFR1, FGFR2, FGFR3 and FGFR4 (phosphorylated). Interacts with FGR and HCK. Interacts with PDGFRA (tyrosine phosphorylated) and PDGFRB (tyrosine phosphorylated). Interacts with ERBB4 (phosphorylated). Interacts with NTRK1 (phosphorylated upon ligand-binding). {ECO
Tissue SpecificityIsoform 2 is expressed in skeletal muscle and brain, and at lower levels in kidney and cardiac muscle. Isoform 2 and isoform 4 are present in skeletal muscle (at protein level).
Web ResourceName=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/PIK3R1ID41717ch5q13.html";