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Phosphatidylinositol 3-kinase regulatory subunit alpha (PI3-kinase regulatory subunit alpha) (PI3K regulatory subunit alpha) (PtdIns-3-kinase regulatory subunit alpha) (Phosphatidylinositol 3-kinase 85 kDa regulatory subunit alpha) (PI3-kinase subunit p85-alpha) (PtdIns-3-kinase regulatory subunit p85-alpha)

 P85A_HUMAN              Reviewed;         724 AA.
P27986; B3KT19; D3DWA0; E7EX19; Q15747; Q4VBZ7; Q53EM6; Q8IXA2;
Q8N1C5;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
28-NOV-2006, sequence version 2.
30-AUG-2017, entry version 214.
RecName: Full=Phosphatidylinositol 3-kinase regulatory subunit alpha;
Short=PI3-kinase regulatory subunit alpha;
Short=PI3K regulatory subunit alpha;
Short=PtdIns-3-kinase regulatory subunit alpha;
AltName: Full=Phosphatidylinositol 3-kinase 85 kDa regulatory subunit alpha;
Short=PI3-kinase subunit p85-alpha;
Short=PtdIns-3-kinase regulatory subunit p85-alpha;
Name=PIK3R1; Synonyms=GRB1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1849461; DOI=10.1016/0092-8674(91)90410-Z;
Skolnik E.Y., Margolis B., Mohammadi M., Lowenstein E., Fischer R.,
Drepps A., Ullrich A., Schlessinger J.;
"Cloning of PI3 kinase-associated p85 utilizing a novel method for
expression/cloning of target proteins for receptor tyrosine kinases.";
Cell 65:83-90(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4), INTERACTION WITH IRS1,
AND TISSUE SPECIFICITY.
TISSUE=Skeletal muscle;
PubMed=8628286; DOI=10.1128/MCB.16.5.2195;
Antonetti D.A., Algenstaedt P., Kahn C.R.;
"Insulin receptor substrate 1 binds two novel splice variants of the
regulatory subunit of phosphatidylinositol 3-kinase in muscle and
brain.";
Mol. Cell. Biol. 16:2195-2203(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
TISSUE=Skeletal muscle;
Udelhoven M., Kotzka J., Knebel B., Klein E., Krone W.,
Mueller-Wieland D.;
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
ILE-326.
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
LYS-451.
TISSUE=Placenta, and Skeletal muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
INTERACTION WITH PDGFRB.
PubMed=7692233; DOI=10.1128/MCB.13.11.6889;
Nishimura R., Li W., Kashishian A., Mondino A., Zhou M., Cooper J.,
Schlessinger J.;
"Two signaling molecules share a phosphotyrosine-containing binding
site in the platelet-derived growth factor receptor.";
Mol. Cell. Biol. 13:6889-6896(1993).
[10]
INTERACTION WITH INSR.
PubMed=8276809;
Van Horn D.J., Myers M.G. Jr., Backer J.M.;
"Direct activation of the phosphatidylinositol 3'-kinase by the
insulin receptor.";
J. Biol. Chem. 269:29-32(1994).
[11]
FUNCTION IN FGFR4 SIGNALING.
PubMed=7518429;
Vainikka S., Joukov V., Wennstrom S., Bergman M., Pelicci P.G.,
Alitalo K.;
"Signal transduction by fibroblast growth factor receptor-4 (FGFR-4).
Comparison with FGFR-1.";
J. Biol. Chem. 269:18320-18326(1994).
[12]
INTERACTION WITH IGF1R.
PubMed=7541045; DOI=10.1074/jbc.270.26.15639;
Craparo A., O'Neill T.J., Gustafson T.A.;
"Non-SH2 domains within insulin receptor substrate-1 and SHC mediate
their phosphotyrosine-dependent interaction with the NPEY motif of the
insulin-like growth factor I receptor.";
J. Biol. Chem. 270:15639-15643(1995).
[13]
INTERACTION WITH INSR.
PubMed=7537849; DOI=10.1128/MCB.15.5.2500;
Gustafson T.A., He W., Craparo A., Schaub C.D., O'Neill T.J.;
"Phosphotyrosine-dependent interaction of SHC and insulin receptor
substrate 1 with the NPEY motif of the insulin receptor via a novel
non-SH2 domain.";
Mol. Cell. Biol. 15:2500-2508(1995).
[14]
INTERACTION WITH PDGFRA.
PubMed=8940081; DOI=10.1074/jbc.271.48.30942;
Yokote K., Margolis B., Heldin C.H., Claesson-Welsh L.;
"Grb7 is a downstream signaling component of platelet-derived growth
factor alpha- and beta-receptors.";
J. Biol. Chem. 271:30942-30949(1996).
[15]
INTERACTION WITH KIT.
PubMed=9038210; DOI=10.1074/jbc.272.9.5915;
Price D.J., Rivnay B., Fu Y., Jiang S., Avraham S., Avraham H.;
"Direct association of Csk homologous kinase (CHK) with the
diphosphorylated site Tyr568/570 of the activated c-KIT in
megakaryocytes.";
J. Biol. Chem. 272:5915-5920(1997).
[16]
INTERACTION WITH AXL.
PubMed=9178760; DOI=10.1038/sj.onc.1201123;
Braunger J., Schleithoff L., Schulz A.S., Kessler H., Lammers R.,
Ullrich A., Bartram C.R., Janssen J.W.;
"Intracellular signaling of the Ufo/Axl receptor tyrosine kinase is
mediated mainly by a multi-substrate docking-site.";
Oncogene 14:2619-2631(1997).
[17]
INTERACTION WITH LAT.
PubMed=9489702; DOI=10.1016/S0092-8674(00)80901-0;
Zhang W., Sloan-Lancaster J., Kitchen J., Trible R.P., Samelson L.E.;
"LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor
to cellular activation.";
Cell 92:83-92(1998).
[18]
INTERACTION WITH IRS4.
PubMed=9553137; DOI=10.1074/jbc.273.17.10726;
Fantin V.R., Sparling J.D., Slot J.W., Keller S.R., Lienhard G.E.,
Lavan B.E.;
"Characterization of insulin receptor substrate 4 in human embryonic
kidney 293 cells.";
J. Biol. Chem. 273:10726-10732(1998).
[19]
INTERACTION WITH TRAT1.
PubMed=9687533; DOI=10.1084/jem.188.3.561;
Bruyns E., Marie-Cardine A., Kirchgessner H., Sagolla K.,
Shevchenko A., Mann M., Autschbach F., Bensussan A., Meuer S.,
Schraven B.;
"T cell receptor (TCR) interacting molecule (TRIM), a novel disulfide-
linked dimer associated with the TCR-CD3-zeta complex, recruits
intracellular signaling proteins to the plasma membrane.";
J. Exp. Med. 188:561-575(1998).
[20]
INTERACTION WITH HCST.
PubMed=10528161;
Chang C., Dietrich J., Harpur A.G., Lindquist J.A., Haude A.,
Loke Y.W., King A., Colonna M., Trowsdale J., Wilson M.J.;
"KAP10, a novel transmembrane adapter protein genetically linked to
DAP12 but with unique signaling properties.";
J. Immunol. 163:4651-4654(1999).
[21]
INTERACTION WITH CBLB.
PubMed=10086340; DOI=10.1038/sj.onc.1202499;
Ettenberg S.A., Keane M.M., Nau M.M., Frankel M., Wang L.-M.,
Pierce J.H., Lipkowitz S.;
"cbl-b inhibits epidermal growth factor receptor signaling.";
Oncogene 18:1855-1866(1999).
[22]
INTERACTION WITH FGR AND HCK.
PubMed=10739672; DOI=10.1006/excr.2000.4816;
Axelsson L., Hellberg C., Melander F., Smith D., Zheng L.,
Andersson T.;
"Clustering of beta(2)-integrins on human neutrophils activates dual
signaling pathways to PtdIns 3-kinase.";
Exp. Cell Res. 256:257-263(2000).
[23]
INTERACTION WITH ERBB4.
PubMed=10867024; DOI=10.1074/jbc.C901015199;
Sweeney C., Lai C., Riese D.J. II, Diamonti A.J., Cantley L.C.,
Carraway K.L. III;
"Ligand discrimination in signaling through an ErbB4 receptor
homodimer.";
J. Biol. Chem. 275:19803-19807(2000).
[24]
INTERACTION WITH CBLB, AND UBIQUITINATION.
PubMed=11087752; DOI=10.1074/jbc.M008901200;
Fang D., Wang H.-Y., Fang N., Altman Y., Elly C., Liu Y.-C.;
"Cbl-b, a RING-type E3 ubiquitin ligase, targets phosphatidylinositol
3-kinase for ubiquitination in T cells.";
J. Biol. Chem. 276:4872-4878(2001).
[25]
INTERACTION WITH CD3Z AND CD28, AND UBIQUITINATION.
PubMed=11526404; DOI=10.1038/ni0901-870;
Fang D., Liu Y.-C.;
"Proteolysis-independent regulation of PI3K by Cbl-b-mediated
ubiquitination in T cells.";
Nat. Immunol. 2:870-875(2001).
[26]
INTERACTION WITH NISCH.
PubMed=11912194; DOI=10.1074/jbc.M111838200;
Sano H., Liu S.C.H., Lane W.S., Piletz J.E., Lienhard G.E.;
"Insulin receptor substrate 4 associates with the protein IRAS.";
J. Biol. Chem. 277:19439-19447(2002).
[27]
INTERACTION WITH LAX1.
PubMed=12359715; DOI=10.1074/jbc.M208946200;
Zhu M., Janssen E., Leung K., Zhang W.;
"Molecular cloning of a novel gene encoding a membrane-associated
adaptor protein (LAX) in lymphocyte signaling.";
J. Biol. Chem. 277:46151-46158(2002).
[28]
INTERACTION WITH HIV-1 NEF.
PubMed=12009866; DOI=10.1006/viro.2002.1365;
Linnemann T., Zheng Y.-H., Mandic R., Peterlin B.M.;
"Interaction between Nef and phosphatidylinositol-3-kinase leads to
activation of p21-activated kinase and increased production of HIV.";
Virology 294:246-255(2002).
[29]
INTERACTION WITH HCV NS5A.
PubMed=12186904; DOI=10.1128/JVI.76.18.9207-9217.2002;
He Y., Nakao H., Tan S.-L., Polyak S.J., Neddermann P., Vijaysri S.,
Jacobs B.L., Katze M.G.;
"Subversion of cell signaling pathways by hepatitis C virus
nonstructural 5A protein via interaction with Grb2 and P85
phosphatidylinositol 3-kinase.";
J. Virol. 76:9207-9217(2002).
[30]
INTERACTION WITH NTRK1.
PubMed=15488758; DOI=10.1016/j.ccr.2004.09.011;
Tacconelli A., Farina A.R., Cappabianca L., Desantis G., Tessitore A.,
Vetuschi A., Sferra R., Rucci N., Argenti B., Screpanti I., Gulino A.,
Mackay A.R.;
"TrkA alternative splicing: a regulated tumor-promoting switch in
human neuroblastoma.";
Cancer Cell 6:347-360(2004).
[31]
REVIEW ON INTERACTION WITH KIT AND ROLE IN KIT SIGNALING.
PubMed=15526160; DOI=10.1007/s00018-004-4189-6;
Ronnstrand L.;
"Signal transduction via the stem cell factor receptor/c-Kit.";
Cell. Mol. Life Sci. 61:2535-2548(2004).
[32]
INTERACTION WITH BCR.
PubMed=15302586; DOI=10.1016/j.yexcr.2004.05.010;
Laurent C.E., Smithgall T.E.;
"The c-Fes tyrosine kinase cooperates with the breakpoint cluster
region protein (Bcr) to induce neurite extension in a Rac- and Cdc42-
dependent manner.";
Exp. Cell Res. 299:188-198(2004).
[33]
PHOSPHORYLATION BY FGR.
PubMed=15561106; DOI=10.1016/j.yexcr.2004.09.005;
Continolo S., Baruzzi A., Majeed M., Caveggion E., Fumagalli L.,
Lowell C.A., Berton G.;
"The proto-oncogene Fgr regulates cell migration and this requires its
plasma membrane localization.";
Exp. Cell Res. 302:253-269(2005).
[34]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[35]
PHOSPHORYLATION, AND DEPHOSPHORYLATION BY PTPRJ.
PubMed=18348712; DOI=10.1042/BJ20071317;
Tsuboi N., Utsunomiya T., Roberts R.L., Ito H., Takahashi K., Noda M.,
Takahashi T.;
"The tyrosine phosphatase CD148 interacts with the p85 regulatory
subunit of phosphoinositide 3-kinase.";
Biochem. J. 413:193-200(2008).
[36]
INTERACTION WITH ERBB4.
PubMed=18721752; DOI=10.1016/j.chembiol.2008.07.006;
Kaushansky A., Gordus A., Budnik B.A., Lane W.S., Rush J.,
MacBeath G.;
"System-wide investigation of ErbB4 reveals 19 sites of Tyr
phosphorylation that are unusually selective in their recruitment
properties.";
Chem. Biol. 15:808-817(2008).
[37]
INTERACTION WITH FASLG.
PubMed=19807924; DOI=10.1186/1471-2172-10-53;
Voss M., Lettau M., Janssen O.;
"Identification of SH3 domain interaction partners of human FasL
(CD178) by phage display screening.";
BMC Immunol. 10:53-53(2009).
[38]
INTERACTION WITH FGFR3.
PubMed=19286672; DOI=10.1093/hmg/ddp116;
Salazar L., Kashiwada T., Krejci P., Muchowski P., Donoghue D.,
Wilcox W.R., Thompson L.M.;
"A novel interaction between fibroblast growth factor receptor 3 and
the p85 subunit of phosphoinositide 3-kinase: activation-dependent
regulation of ERK by p85 in multiple myeloma cells.";
Hum. Mol. Genet. 18:1951-1961(2009).
[39]
REVIEW ON ROLE IN FGFR1 SIGNALING.
PubMed=15863030; DOI=10.1016/j.cytogfr.2005.01.001;
Eswarakumar V.P., Lax I., Schlessinger J.;
"Cellular signaling by fibroblast growth factor receptors.";
Cytokine Growth Factor Rev. 16:139-149(2005).
[40]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-580, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[41]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[42]
FUNCTION, AND INTERACTION WITH XBP1.
PubMed=20348923; DOI=10.1038/nm.2121;
Winnay J.N., Boucher J., Mori M.A., Ueki K., Kahn C.R.;
"A regulatory subunit of phosphoinositide 3-kinase increases the
nuclear accumulation of X-box-binding protein-1 to modulate the
unfolded protein response.";
Nat. Med. 16:438-445(2010).
[43]
INTERACTION WITH HERPES SIMPLEX VIRUS 1 UL46.
PubMed=21228233; DOI=10.1128/JVI.01877-10;
Wagner M.J., Smiley J.R.;
"Herpes simplex virus requires VP11/12 to activate Src family kinase-
phosphoinositide 3-kinase-Akt signaling.";
J. Virol. 85:2803-2812(2011).
[44]
INVOLVEMENT IN AGM7.
PubMed=22351933; DOI=10.1084/jem.20112533;
Conley M.E., Dobbs A.K., Quintana A.M., Bosompem A., Wang Y.D.,
Coustan-Smith E., Smith A.M., Perez E.E., Murray P.J.;
"Agammaglobulinemia and absent B lineage cells in a patient lacking
the p85? subunit of PI3K.";
J. Exp. Med. 209:463-470(2012).
[45]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[46]
INVOLVEMENT IN SHORTS, AND VARIANT SHORTS TRP-649.
PubMed=23810382; DOI=10.1016/j.ajhg.2013.06.005;
FORGE Canada Consortium;
Dyment D.A., Smith A.C., Alcantara D., Schwartzentruber J.A.,
Basel-Vanagaite L., Curry C.J., Temple I.K., Reardon W., Mansour S.,
Haq M.R., Gilbert R., Lehmann O.J., Vanstone M.R., Beaulieu C.L.,
Majewski J., Bulman D.E., O'Driscoll M., Boycott K.M., Innes A.M.,
Friedman J., Michaud J., Bernier F., Brudno M., Fernandez B.,
Knoppers B., Samuels M., Scherer S.;
"Mutations in PIK3R1 cause SHORT syndrome.";
Am. J. Hum. Genet. 93:158-166(2013).
[47]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154 AND SER-279, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[48]
INTERACTION WITH VARICELLA VIRUS ORF12.
PubMed=23192871; DOI=10.1128/JVI.02395-12;
Liu X., Cohen J.I.;
"Varicella-zoster virus ORF12 protein activates the
phosphatidylinositol 3-kinase/Akt pathway to regulate cell cycle
progression.";
J. Virol. 87:1842-1848(2013).
[49]
INTERACTION WITH FAM83B.
PubMed=23676467;
Cipriano R., Miskimen K.L., Bryson B.L., Foy C.R., Bartel C.A.,
Jackson M.W.;
"FAM83B-mediated activation of PI3K/AKT and MAPK signaling cooperates
to promote epithelial cell transformation and resistance to targeted
therapies.";
Oncotarget 4:729-738(2013).
[50]
INVOLVEMENT IN IMD36.
PubMed=25133428; DOI=10.1172/JCI75746;
Deau M.C., Heurtier L., Frange P., Suarez F., Bole-Feysot C.,
Nitschke P., Cavazzana M., Picard C., Durandy A., Fischer A.,
Kracker S.;
"A human immunodeficiency caused by mutations in the PIK3R1 gene.";
J. Clin. Invest. 124:3923-3928(2014).
[51]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[52]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-85.
PubMed=8648629; DOI=10.1006/jmbi.1996.0190;
Liang J., Chen J.K., Schreiber S.L., Clardy J.;
"Crystal structure of P13K SH3 domain at 2.0-A resolution.";
J. Mol. Biol. 257:632-643(1996).
[53]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 324-434.
PubMed=8599763; DOI=10.1038/nsb0496-364;
Nolte R.T., Eck M.J., Schlessinger J., Shoelson S.E., Harrison S.C.;
"Crystal structure of the PI 3-kinase p85 amino-terminal SH2 domain
and its phosphopeptide complexes.";
Nat. Struct. Biol. 3:364-373(1996).
[54]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 115-298.
PubMed=8962058; DOI=10.1073/pnas.93.25.14373;
Musacchio A., Cantley L.C., Harrison S.C.;
"Crystal structure of the breakpoint cluster region-homology domain
from phosphoinositide 3-kinase p85 alpha subunit.";
Proc. Natl. Acad. Sci. U.S.A. 93:14373-14378(1996).
[55]
X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 617-724 IN COMPLEX WITH
PDGFRB.
PubMed=11567151; DOI=10.1107/S0907444901012434;
Pauptit R.A., Dennis C.A., Derbyshire D.J., Breeze A.L., Weston S.A.,
Rowsell S., Murshudov G.N.;
"NMR trial models: experiences with the colicin immunity protein Im7
and the p85alpha C-terminal SH2-peptide complex.";
Acta Crystallogr. D 57:1397-1404(2001).
[56]
STRUCTURE BY NMR OF 1-79.
PubMed=7681364; DOI=10.1016/0092-8674(93)90582-B;
Koyama S., Yu H., Dalgarno D.C., Shin T.B., Zydowsky L.D.,
Schreiber S.L.;
"Structure of the PI3K SH3 domain and analysis of the SH3 family.";
Cell 72:945-952(1993).
[57]
STRUCTURE BY NMR OF 91-104.
PubMed=8961927; DOI=10.1021/bi9620969;
Renzoni D.A., Pugh D.J., Siligardi G., Das P., Morton C.J., Rossi C.,
Waterfield M.D., Campbell I.D., Ladbury J.E.;
"Structural and thermodynamic characterization of the interaction of
the SH3 domain from Fyn with the proline-rich binding site on the p85
subunit of PI3-kinase.";
Biochemistry 35:15646-15653(1996).
[58]
STRUCTURE BY NMR OF 617-724.
PubMed=8670861;
Breeze A.L., Kara B.V., Barratt D.G., Anderson M., Smith J.C.,
Luke R.W., Best J.R., Cartlidge S.A.;
"Structure of a specific peptide complex of the carboxy-terminal SH2
domain from the p85 alpha subunit of phosphatidylinositol 3-kinase.";
EMBO J. 15:3579-3589(1996).
[59]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 431-600, AND FUNCTION.
PubMed=17626883; DOI=10.1126/science.1135394;
Miled N., Yan Y., Hon W.C., Perisic O., Zvelebil M., Inbar Y.,
Schneidman-Duhovny D., Wolfson H.J., Backer J.M., Williams R.L.;
"Mechanism of two classes of cancer mutations in the phosphoinositide
3-kinase catalytic subunit.";
Science 317:239-242(2007).
[60]
X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 322-600.
PubMed=18079394; DOI=10.1126/science.1150799;
Huang C.-H., Mandelker D., Schmidt-Kittler O., Samuels Y.,
Velculescu V.E., Kinzler K.W., Vogelstein B., Gabelli S.B.,
Amzel L.M.;
"The structure of a human p110alpha/p85alpha complex elucidates the
effects of oncogenic PI3Kalpha mutations.";
Science 318:1744-1748(2007).
[61]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 322-694, FUNCTION, AND
SUBUNIT.
PubMed=19805105; DOI=10.1073/pnas.0908444106;
Mandelker D., Gabelli S.B., Schmidt-Kittler O., Zhu J., Cheong I.,
Huang C.H., Kinzler K.W., Vogelstein B., Amzel L.M.;
"A frequent kinase domain mutation that changes the interaction
between PI3Kalpha and the membrane.";
Proc. Natl. Acad. Sci. U.S.A. 106:16996-17001(2009).
[62]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-83.
PubMed=19919182; DOI=10.1515/BC.2010.003;
Batra-Safferling R., Granzin J., Modder S., Hoffmann S., Willbold D.;
"Structural studies of the phosphatidylinositol 3-kinase (PI3K) SH3
domain in complex with a peptide ligand: role of the anchor residue in
ligand binding.";
Biol. Chem. 391:33-42(2010).
[63]
VARIANT ILE-326.
PubMed=9032108; DOI=10.2337/diab.46.3.494;
Hansen T., Andersen C.B., Echwald S.M., Urhammer S.A., Clausen J.O.,
Vestergaard H., Owens D., Hansen L., Pedersen O.;
"Identification of a common amino acid polymorphism in the p85alpha
regulatory subunit of phosphatidylinositol 3-kinase: effects on
glucose disappearance constant, glucose effectiveness, and the insulin
sensitivity index.";
Diabetes 46:494-501(1997).
[64]
VARIANTS ILE-326 AND GLN-409, AND CHARACTERIZATION OF VARIANTS ILE-326
AND GLN-409.
PubMed=10768093; DOI=10.1007/s001250050050;
Baynes K.C.R., Beeton C.A., Panayotou G., Stein R., Soos M.,
Hansen T., Simpson H., O'Rahilly S., Shepherd P.R., Whitehead J.P.;
"Natural variants of human p85 alpha phosphoinositide 3-kinase in
severe insulin resistance: a novel variant with impaired insulin-
stimulated lipid kinase activity.";
Diabetologia 43:321-331(2000).
[65]
VARIANTS SHORTS LYS-489 AND ILE-539 DEL.
PubMed=23810378; DOI=10.1016/j.ajhg.2013.05.019;
Thauvin-Robinet C., Auclair M., Duplomb L., Caron-Debarle M.,
Avila M., St-Onge J., Le Merrer M., Le Luyer B., Heron D.,
Mathieu-Dramard M., Bitoun P., Petit J.M., Odent S., Amiel J.,
Picot D., Carmignac V., Thevenon J., Callier P., Laville M.,
Reznik Y., Fagour C., Nunes M.L., Capeau J., Lascols O., Huet F.,
Faivre L., Vigouroux C., Riviere J.B.;
"PIK3R1 mutations cause syndromic insulin resistance with
lipoatrophy.";
Am. J. Hum. Genet. 93:141-149(2013).
[66]
VARIANT SHORTS TRP-649.
PubMed=23810379; DOI=10.1016/j.ajhg.2013.05.023;
Chudasama K.K., Winnay J., Johansson S., Claudi T., Konig R.,
Haldorsen I., Johansson B., Woo J.R., Aarskog D., Sagen J.V.,
Kahn C.R., Molven A., Njolstad P.R.;
"SHORT syndrome with partial lipodystrophy due to impaired
phosphatidylinositol 3 kinase signaling.";
Am. J. Hum. Genet. 93:150-157(2013).
-!- 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 (PubMed:17626883, PubMed:19805105,
PubMed:7518429). Modulates the cellular response to ER stress by
promoting nuclear translocation of XBP1 isoform 2 in a ER
stress- and/or insulin-dependent manner during metabolic
overloading in the liver and hence plays a role in glucose
tolerance improvement (PubMed:20348923).
{ECO:0000269|PubMed:17626883, ECO:0000269|PubMed:19805105,
ECO:0000269|PubMed:20348923, ECO:0000269|PubMed:7518429}.
-!- SUBUNIT: Interacts (via SH2 domain) with CSF1R (tyrosine
phosphorylated). Interacts with PIK3R2; the interaction is
dissociated in an insulin-dependent manner (By similarity).
Interacts with XBP1 isoform 2; the interaction is direct and
induces translocation of XBP1 isoform 2 into the nucleus in a ER
stress- and/or insulin-dependent but PI3K-independent manner
(PubMed:20348923). Heterodimer 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). Interacts with
herpes simplex virus 1 UL46 and varicella virus ORF12; these
interactions activate the PI3K/AKT pathway. Interacts with FAM83B;
activates the PI3K/AKT signaling cascade (PubMed:23676467).
{ECO:0000250|UniProtKB:P23727, ECO:0000250|UniProtKB:P26450,
ECO:0000250|UniProtKB:Q63787, ECO:0000269|PubMed:10086340,
ECO:0000269|PubMed:10528161, ECO:0000269|PubMed:10739672,
ECO:0000269|PubMed:10867024, ECO:0000269|PubMed:11087752,
ECO:0000269|PubMed:11526404, ECO:0000269|PubMed:11567151,
ECO:0000269|PubMed:11912194, ECO:0000269|PubMed:12009866,
ECO:0000269|PubMed:12186904, ECO:0000269|PubMed:12359715,
ECO:0000269|PubMed:15302586, ECO:0000269|PubMed:15488758,
ECO:0000269|PubMed:18721752, ECO:0000269|PubMed:19286672,
ECO:0000269|PubMed:19805105, ECO:0000269|PubMed:19807924,
ECO:0000269|PubMed:20348923, ECO:0000269|PubMed:21228233,
ECO:0000269|PubMed:23676467, ECO:0000269|PubMed:7537849,
ECO:0000269|PubMed:7541045, ECO:0000269|PubMed:7692233,
ECO:0000269|PubMed:8276809, ECO:0000269|PubMed:8628286,
ECO:0000269|PubMed:8940081, ECO:0000269|PubMed:9038210,
ECO:0000269|PubMed:9178760, ECO:0000269|PubMed:9489702,
ECO:0000269|PubMed:9553137, ECO:0000269|PubMed:9687533}.
-!- INTERACTION:
Q8IZP0: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;
Q13111:CHAF1A; NbExp=2; IntAct=EBI-79464, EBI-1020839;
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;
P41970:ELK3; NbExp=2; IntAct=EBI-79464, EBI-1758534;
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=4; 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=3; 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=6; IntAct=EBI-79464, EBI-286483;
P08581:MET; NbExp=6; IntAct=EBI-79464, EBI-1039152;
Q8WX92:NELFB; NbExp=2; IntAct=EBI-79464, EBI-347721;
P03496:NS (xeno); NbExp=6; IntAct=EBI-79464, EBI-2547442;
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=14; IntAct=EBI-79464, EBI-2116585;
P42338:PIK3CB; NbExp=3; IntAct=EBI-9090282, EBI-2609540;
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;
Q9NP31:SH2D2A; NbExp=3; IntAct=EBI-9090282, EBI-490630;
Q9UPX8:SHANK2; NbExp=2; IntAct=EBI-79464, EBI-1570571;
P29353:SHC1; NbExp=3; IntAct=EBI-79464, EBI-78835;
Q9H0K1:SIK2; NbExp=7; IntAct=EBI-79464, EBI-1181664;
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;
-!- ALTERNATIVE PRODUCTS:
Event=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.;
-!- TISSUE SPECIFICITY: Isoform 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).
{ECO:0000269|PubMed:8628286}.
-!- DOMAIN: The SH3 domain mediates the binding to CBLB, and to HIV-1
Nef.
-!- PTM: Polyubiquitinated 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:11087752,
ECO:0000269|PubMed:11526404}.
-!- PTM: Phosphorylated. 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:0000250,
ECO:0000269|PubMed:15561106, ECO:0000269|PubMed:18348712}.
-!- DISEASE: Agammaglobulinemia 7, autosomal recessive (AGM7)
[MIM:615214]: A primary immunodeficiency characterized by
profoundly low or absent serum antibodies and low or absent
circulating B-cells due to an early block of B-cell development.
Affected individuals develop severe infections in the first years
of life. {ECO:0000269|PubMed:22351933}. Note=The disease is caused
by mutations affecting the gene represented in this entry.
-!- DISEASE: SHORT syndrome (SHORTS) [MIM:269880]: A rare, multisystem
disease characterized by short stature, anomalies of the anterior
chamber of the eye, characteristic facial features such as
triangular facies, lack of facial fat, and hypoplastic nasal alae
with overhanging columella, partial lipodystrophy, hernias,
hyperextensibility, and delayed dentition. The clinical phenotype
can include insulin resistance, nephrocalcinosis, and hearing
deficits. Developmental milestones and cognition are normal.
{ECO:0000269|PubMed:23810378, ECO:0000269|PubMed:23810379,
ECO:0000269|PubMed:23810382}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Immunodeficiency 36 (IMD36) [MIM:616005]: A primary
immunodeficiency characterized by impaired B-cell function,
hypogammaglobulinemia and recurrent infections.
{ECO:0000269|PubMed:25133428}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the PI3K p85 subunit family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PIK3R1ID41717ch5q13.html";
-----------------------------------------------------------------------
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EMBL; M61906; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; U49349; AAB04140.1; -; mRNA.
EMBL; AF279367; AAO15359.1; -; mRNA.
EMBL; AK094785; BAG52931.1; -; mRNA.
EMBL; AK223613; BAD97333.1; -; mRNA.
EMBL; AC016564; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC104120; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471137; EAW51312.1; -; Genomic_DNA.
EMBL; CH471137; EAW51313.1; -; Genomic_DNA.
EMBL; BC030815; AAH30815.1; -; mRNA.
EMBL; BC094795; AAH94795.1; -; mRNA.
CCDS; CCDS3993.1; -. [P27986-1]
CCDS; CCDS3994.1; -. [P27986-3]
CCDS; CCDS3995.1; -. [P27986-2]
CCDS; CCDS56374.1; -. [P27986-5]
PIR; A38748; A38748.
RefSeq; NP_001229395.1; NM_001242466.1. [P27986-5]
RefSeq; NP_852556.2; NM_181504.3. [P27986-2]
RefSeq; NP_852664.1; NM_181523.2. [P27986-1]
RefSeq; NP_852665.1; NM_181524.1. [P27986-3]
RefSeq; XP_005248599.1; XM_005248542.3. [P27986-1]
RefSeq; XP_016865074.1; XM_017009585.1. [P27986-1]
UniGene; Hs.132225; -.
UniGene; Hs.604502; -.
UniGene; Hs.734132; -.
PDB; 1A0N; NMR; -; A=91-104.
PDB; 1AZG; NMR; -; A=91-104.
PDB; 1H9O; X-ray; 1.79 A; A=617-724.
PDB; 1PBW; X-ray; 2.00 A; A/B=105-319.
PDB; 1PHT; X-ray; 2.00 A; A=1-85.
PDB; 1PIC; NMR; -; A=617-724.
PDB; 1PKS; NMR; -; A=1-79.
PDB; 1PKT; NMR; -; A=1-79.
PDB; 2IUG; X-ray; 1.89 A; A=321-440.
PDB; 2IUH; X-ray; 2.00 A; A=321-440.
PDB; 2IUI; X-ray; 2.40 A; A/B=321-440.
PDB; 2RD0; X-ray; 3.05 A; B=322-600.
PDB; 2V1Y; X-ray; 2.40 A; B=431-600.
PDB; 3HHM; X-ray; 2.80 A; B=322-694.
PDB; 3HIZ; X-ray; 3.30 A; B=322-694.
PDB; 3I5R; X-ray; 1.70 A; A=1-83.
PDB; 3I5S; X-ray; 3.00 A; A/B/C/D=1-83.
PDB; 4A55; X-ray; 3.50 A; B=322-600.
PDB; 4JPS; X-ray; 2.20 A; B=307-593.
PDB; 4L1B; X-ray; 2.59 A; B=318-615.
PDB; 4L23; X-ray; 2.50 A; B=318-615.
PDB; 4L2Y; X-ray; 2.80 A; B=318-615.
PDB; 4OVU; X-ray; 2.96 A; B=322-600.
PDB; 4OVV; X-ray; 3.50 A; B=322-600.
PDB; 4WAF; X-ray; 2.39 A; B=306-617.
PDB; 4YKN; X-ray; 2.90 A; A=318-615.
PDB; 4ZOP; X-ray; 2.62 A; B=307-590.
PDB; 5AUL; X-ray; 1.10 A; A=614-720.
PDB; 5FI4; X-ray; 2.50 A; B=306-617.
PDB; 5GJI; X-ray; 0.90 A; A=325-430.
PDB; 5ITD; X-ray; 3.02 A; B=307-617.
PDB; 5M6U; X-ray; 2.85 A; B=1-724.
PDB; 5SW8; X-ray; 3.30 A; B=322-600.
PDB; 5SWG; X-ray; 3.11 A; B=322-600.
PDB; 5SWO; X-ray; 3.50 A; B=322-600.
PDB; 5SWP; X-ray; 3.41 A; B=322-600.
PDB; 5SWR; X-ray; 3.31 A; B=322-600.
PDB; 5SWT; X-ray; 3.49 A; B=322-600.
PDB; 5SX8; X-ray; 3.47 A; B=322-600.
PDB; 5SX9; X-ray; 3.52 A; B=322-600.
PDB; 5SXA; X-ray; 3.35 A; B=322-600.
PDB; 5SXB; X-ray; 3.30 A; B=322-600.
PDB; 5SXC; X-ray; 3.55 A; B=322-600.
PDB; 5SXD; X-ray; 3.50 A; B=322-600.
PDB; 5SXE; X-ray; 3.51 A; B=322-600.
PDB; 5SXF; X-ray; 3.46 A; B=322-600.
PDB; 5SXI; X-ray; 3.40 A; B=322-600.
PDB; 5SXJ; X-ray; 3.42 A; B=322-600.
PDB; 5SXK; X-ray; 3.55 A; B=322-600.
PDB; 5UBT; X-ray; 2.83 A; B=432-599.
PDB; 5UK8; X-ray; 2.50 A; B=306-593.
PDB; 5UKJ; X-ray; 2.80 A; B=306-593.
PDB; 5UL1; X-ray; 3.00 A; B=306-593.
PDB; 5VLR; X-ray; 2.80 A; B=431-600.
PDBsum; 1A0N; -.
PDBsum; 1AZG; -.
PDBsum; 1H9O; -.
PDBsum; 1PBW; -.
PDBsum; 1PHT; -.
PDBsum; 1PIC; -.
PDBsum; 1PKS; -.
PDBsum; 1PKT; -.
PDBsum; 2IUG; -.
PDBsum; 2IUH; -.
PDBsum; 2IUI; -.
PDBsum; 2RD0; -.
PDBsum; 2V1Y; -.
PDBsum; 3HHM; -.
PDBsum; 3HIZ; -.
PDBsum; 3I5R; -.
PDBsum; 3I5S; -.
PDBsum; 4A55; -.
PDBsum; 4JPS; -.
PDBsum; 4L1B; -.
PDBsum; 4L23; -.
PDBsum; 4L2Y; -.
PDBsum; 4OVU; -.
PDBsum; 4OVV; -.
PDBsum; 4WAF; -.
PDBsum; 4YKN; -.
PDBsum; 4ZOP; -.
PDBsum; 5AUL; -.
PDBsum; 5FI4; -.
PDBsum; 5GJI; -.
PDBsum; 5ITD; -.
PDBsum; 5M6U; -.
PDBsum; 5SW8; -.
PDBsum; 5SWG; -.
PDBsum; 5SWO; -.
PDBsum; 5SWP; -.
PDBsum; 5SWR; -.
PDBsum; 5SWT; -.
PDBsum; 5SX8; -.
PDBsum; 5SX9; -.
PDBsum; 5SXA; -.
PDBsum; 5SXB; -.
PDBsum; 5SXC; -.
PDBsum; 5SXD; -.
PDBsum; 5SXE; -.
PDBsum; 5SXF; -.
PDBsum; 5SXI; -.
PDBsum; 5SXJ; -.
PDBsum; 5SXK; -.
PDBsum; 5UBT; -.
PDBsum; 5UK8; -.
PDBsum; 5UKJ; -.
PDBsum; 5UL1; -.
PDBsum; 5VLR; -.
ProteinModelPortal; P27986; -.
SMR; P27986; -.
BioGrid; 111313; 172.
DIP; DIP-119N; -.
IntAct; P27986; 230.
MINT; MINT-93751; -.
STRING; 9606.ENSP00000274335; -.
BindingDB; P27986; -.
ChEMBL; CHEMBL2506; -.
DrugBank; DB01064; Isoprenaline.
DrugBank; DB05210; SF1126.
iPTMnet; P27986; -.
PhosphoSitePlus; P27986; -.
BioMuta; PIK3R1; -.
DMDM; 118572681; -.
EPD; P27986; -.
MaxQB; P27986; -.
PaxDb; P27986; -.
PeptideAtlas; P27986; -.
PRIDE; P27986; -.
DNASU; 5295; -.
Ensembl; ENST00000320694; ENSP00000323512; ENSG00000145675. [P27986-3]
Ensembl; ENST00000336483; ENSP00000338554; ENSG00000145675. [P27986-2]
Ensembl; ENST00000521381; ENSP00000428056; ENSG00000145675. [P27986-1]
Ensembl; ENST00000521657; ENSP00000429277; ENSG00000145675. [P27986-1]
Ensembl; ENST00000523872; ENSP00000430098; ENSG00000145675. [P27986-5]
GeneID; 5295; -.
KEGG; hsa:5295; -.
UCSC; uc003jva.4; human. [P27986-1]
CTD; 5295; -.
DisGeNET; 5295; -.
GeneCards; PIK3R1; -.
HGNC; HGNC:8979; PIK3R1.
HPA; CAB004268; -.
HPA; HPA001216; -.
MalaCards; PIK3R1; -.
MIM; 171833; gene.
MIM; 269880; phenotype.
MIM; 615214; phenotype.
MIM; 616005; phenotype.
neXtProt; NX_P27986; -.
OpenTargets; ENSG00000145675; -.
Orphanet; 397596; Activated PIK3-delta syndrome.
Orphanet; 33110; Autosomal agammaglobulinemia.
Orphanet; 3163; SHORT syndrome.
PharmGKB; PA33312; -.
eggNOG; KOG4637; Eukaryota.
eggNOG; ENOG410XP6R; LUCA.
GeneTree; ENSGT00390000010431; -.
HOGENOM; HOG000008438; -.
HOVERGEN; HBG082100; -.
InParanoid; P27986; -.
KO; K02649; -.
OMA; LNGYNET; -.
OrthoDB; EOG091G0C3Z; -.
PhylomeDB; P27986; -.
TreeFam; TF102033; -.
BioCyc; MetaCyc:ENSG00000145675-MONOMER; -.
BRENDA; 2.7.1.153; 2681.
Reactome; R-HSA-109704; PI3K Cascade.
Reactome; R-HSA-114604; GPVI-mediated activation cascade.
Reactome; R-HSA-1236382; Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants.
Reactome; R-HSA-1250342; PI3K events in ERBB4 signaling.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-1266695; Interleukin-7 signaling.
Reactome; R-HSA-1433557; Signaling by SCF-KIT.
Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
Reactome; R-HSA-180292; GAB1 signalosome.
Reactome; R-HSA-1839117; Signaling by cytosolic FGFR1 fusion mutants.
Reactome; R-HSA-186763; Downstream signal transduction.
Reactome; R-HSA-1963642; PI3K events in ERBB2 signaling.
Reactome; R-HSA-198203; PI3K/AKT activation.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-2029485; Role of phospholipids in phagocytosis.
Reactome; R-HSA-210993; Tie2 Signaling.
Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
Reactome; R-HSA-2424491; DAP12 signaling.
Reactome; R-HSA-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
Reactome; R-HSA-373753; Nephrin interactions.
Reactome; R-HSA-388841; Costimulation by the CD28 family.
Reactome; R-HSA-389357; CD28 dependent PI3K/Akt signaling.
Reactome; R-HSA-392451; G beta:gamma signalling through PI3Kgamma.
Reactome; R-HSA-416476; G alpha (q) signalling events.
Reactome; R-HSA-416482; G alpha (12/13) signalling events.
Reactome; R-HSA-430116; GP1b-IX-V activation signalling.
Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-HSA-512988; Interleukin-3, 5 and GM-CSF signaling.
Reactome; R-HSA-5637810; Constitutive Signaling by EGFRvIII.
Reactome; R-HSA-5654689; PI-3K cascade:FGFR1.
Reactome; R-HSA-5654695; PI-3K cascade:FGFR2.
Reactome; R-HSA-5654710; PI-3K cascade:FGFR3.
Reactome; R-HSA-5654720; PI-3K cascade:FGFR4.
Reactome; R-HSA-5655253; Signaling by FGFR2 in disease.
Reactome; R-HSA-5655291; Signaling by FGFR4 in disease.
Reactome; R-HSA-5655302; Signaling by FGFR1 in disease.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-HSA-8851907; MET activates PI3K/AKT signaling.
Reactome; R-HSA-8853334; Signaling by FGFR3 fusions in cancer.
Reactome; R-HSA-8853338; Signaling by FGFR3 point mutants in cancer.
Reactome; R-HSA-8853659; RET signaling.
Reactome; R-HSA-912526; Interleukin receptor SHC signaling.
Reactome; R-HSA-912631; Regulation of signaling by CBL.
Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
SignaLink; P27986; -.
SIGNOR; P27986; -.
ChiTaRS; PIK3R1; human.
EvolutionaryTrace; P27986; -.
GeneWiki; PIK3R1; -.
GenomeRNAi; 5295; -.
PRO; PR:P27986; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000145675; -.
CleanEx; HS_PIK3R1; -.
ExpressionAtlas; P27986; baseline and differential.
Genevisible; P27986; HS.
GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
GO; GO:0005801; C:cis-Golgi network; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:1990578; C:perinuclear endoplasmic reticulum membrane; IEA:Ensembl.
GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; ISS:BHF-UCL.
GO; GO:0005943; C:phosphatidylinositol 3-kinase complex, class IA; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; TAS:Reactome.
GO; GO:0046935; F:1-phosphatidylinositol-3-kinase regulator activity; IBA:GO_Central.
GO; GO:0043125; F:ErbB-3 class receptor binding; IDA:UniProtKB.
GO; GO:0043559; F:insulin binding; IDA:UniProtKB.
GO; GO:0005158; F:insulin receptor binding; IPI:UniProtKB.
GO; GO:0043560; F:insulin receptor substrate binding; ISS:BHF-UCL.
GO; GO:0005159; F:insulin-like growth factor receptor binding; IPI:UniProtKB.
GO; GO:0005168; F:neurotrophin TRKA receptor binding; IPI:UniProtKB.
GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; ISS:BHF-UCL.
GO; GO:0035014; F:phosphatidylinositol 3-kinase regulator activity; ISS:UniProtKB.
GO; GO:0036312; F:phosphatidylinositol 3-kinase regulatory subunit binding; IEA:Ensembl.
GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; TAS:Reactome.
GO; GO:0001784; F:phosphotyrosine residue binding; IPI:CAFA.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0005068; F:transmembrane receptor protein tyrosine kinase adaptor activity; ISS:BHF-UCL.
GO; GO:0007411; P:axon guidance; TAS:Reactome.
GO; GO:0030183; P:B cell differentiation; IEA:Ensembl.
GO; GO:0001678; P:cellular glucose homeostasis; ISS:UniProtKB.
GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
GO; GO:0034644; P:cellular response to UV; IEA:Ensembl.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0038128; P:ERBB2 signaling pathway; TAS:Reactome.
GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
GO; GO:0060396; P:growth hormone receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0008286; P:insulin receptor signaling pathway; IBA:GO_Central.
GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0001953; P:negative regulation of cell-matrix adhesion; IEA:Ensembl.
GO; GO:0045671; P:negative regulation of osteoclast differentiation; IEA:Ensembl.
GO; GO:0051531; P:NFAT protein import into nucleus; IEA:Ensembl.
GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IDA:BHF-UCL.
GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
GO; GO:0046854; P:phosphatidylinositol phosphorylation; ISS:UniProtKB.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome.
GO; GO:0030168; P:platelet activation; TAS:Reactome.
GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
GO; GO:1900103; P:positive regulation of endoplasmic reticulum unfolded protein response; IMP:UniProtKB.
GO; GO:0090004; P:positive regulation of establishment of protein localization to plasma membrane; ISS:BHF-UCL.
GO; GO:0046326; P:positive regulation of glucose import; ISS:BHF-UCL.
GO; GO:2001275; P:positive regulation of glucose import in response to insulin stimulus; ISS:AgBase.
GO; GO:0033120; P:positive regulation of RNA splicing; IMP:UniProtKB.
GO; GO:0042993; P:positive regulation of transcription factor import into nucleus; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
GO; GO:0046626; P:regulation of insulin receptor signaling pathway; IEA:Ensembl.
GO; GO:0043551; P:regulation of phosphatidylinositol 3-kinase activity; ISS:BHF-UCL.
GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; TAS:Reactome.
GO; GO:0051492; P:regulation of stress fiber assembly; IEA:Ensembl.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:UniProtKB.
GO; GO:0031295; P:T cell costimulation; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd09930; SH2_cSH2_p85_like; 1.
CDD; cd09942; SH2_nSH2_p85_like; 1.
CDD; cd11910; SH3_PI3K_p85alpha; 1.
Gene3D; 3.30.505.10; -; 2.
InterPro; IPR032498; PI3K_P85_iSH2.
InterPro; IPR035591; PI3K_p85alpha_SH3.
InterPro; IPR035020; PI3kinase_P85_cSH2.
InterPro; IPR035022; PI3kinase_P85_nSH2.
InterPro; IPR001720; PI3kinase_P85_p55.
InterPro; IPR008936; Rho_GTPase_activation_prot.
InterPro; IPR000198; RhoGAP_dom.
InterPro; IPR000980; SH2.
InterPro; IPR001452; SH3_domain.
PANTHER; PTHR10155; PTHR10155; 1.
Pfam; PF16454; PI3K_P85_iSH2; 1.
Pfam; PF00620; RhoGAP; 1.
Pfam; PF00017; SH2; 2.
PRINTS; PR00401; SH2DOMAIN.
SMART; SM00324; RhoGAP; 1.
SMART; SM00252; SH2; 2.
SMART; SM00326; SH3; 1.
SUPFAM; SSF48350; SSF48350; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF55550; SSF55550; 2.
PROSITE; PS50238; RHOGAP; 1.
PROSITE; PS50001; SH2; 2.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Disease mutation; Dwarfism; Host-virus interaction; Phosphoprotein;
Polymorphism; Protein transport; Reference proteome; Repeat;
SH2 domain; SH3 domain; Stress response; Transport; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 724 Phosphatidylinositol 3-kinase regulatory
subunit alpha.
/FTId=PRO_0000080758.
DOMAIN 3 79 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 113 301 Rho-GAP. {ECO:0000255|PROSITE-
ProRule:PRU00172}.
DOMAIN 333 428 SH2 1. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 624 718 SH2 2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 154 154 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 279 279 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 467 467 Phosphotyrosine.
{ECO:0000250|UniProtKB:P26450}.
MOD_RES 580 580 Phosphotyrosine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 608 608 Phosphoserine.
{ECO:0000250|UniProtKB:P23727}.
VAR_SEQ 1 363 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045903.
VAR_SEQ 1 300 Missing (in isoform 3).
{ECO:0000303|Ref.3}.
/FTId=VSP_021841.
VAR_SEQ 1 270 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8628286,
ECO:0000303|Ref.5}.
/FTId=VSP_021842.
VAR_SEQ 271 304 MLFRFSAASSDNTENLIKVIEILISTEWNERQPA -> MYN
TVWNMEDLDLEYAKTDINCGTDLMFYIEMDP (in
isoform 2). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8628286,
ECO:0000303|Ref.5}.
/FTId=VSP_021843.
VAR_SEQ 301 306 RQPAPA -> MHNLQT (in isoform 3).
{ECO:0000303|Ref.3}.
/FTId=VSP_021844.
VAR_SEQ 605 605 D -> ENFLSCLPS (in isoform 4).
{ECO:0000303|PubMed:8628286}.
/FTId=VSP_021845.
VARIANT 326 326 M -> I (does not affect insulin-
stimulated lipid kinase activity;
dbSNP:rs3730089).
{ECO:0000269|PubMed:10768093,
ECO:0000269|PubMed:9032108,
ECO:0000269|Ref.5}.
/FTId=VAR_010023.
VARIANT 409 409 R -> Q (in a patient with severe insulin
resistance; lower insulin-stimulated
lipid kinase activity compared with wild-
type; dbSNP:rs748784250).
{ECO:0000269|PubMed:10768093}.
/FTId=VAR_010024.
VARIANT 451 451 E -> K (in dbSNP:rs17852841).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_029562.
VARIANT 489 489 E -> K (in SHORTS; there is 70 to 90%
reduction in the effect of insulin on
AKT1 activation, glycogen synthesis and
glucose uptake, indicating severe insulin
resistance for both proximal and distal
PI3K-dependent signaling;
dbSNP:rs397514047).
{ECO:0000269|PubMed:23810378}.
/FTId=VAR_070221.
VARIANT 539 539 Missing (in SHORTS; there is 70 to 90%
reduction in the effect of insulin on
AKT1 activation, glycogen synthesis and
glucose uptake, indicating severe insulin
resistance for both proximal and distal
PI3K-dependent signaling).
{ECO:0000269|PubMed:23810378}.
/FTId=VAR_070222.
VARIANT 649 649 R -> W (in SHORTS; impairs interaction
between PIK3R1 and IRS1 and reduces AKT1-
mediated insulin signaling;
dbSNP:rs397515453).
{ECO:0000269|PubMed:23810379,
ECO:0000269|PubMed:23810382}.
/FTId=VAR_070223.
CONFLICT 330 330 D -> N (in Ref. 1; M61906).
{ECO:0000305}.
CONFLICT 460 460 S -> G (in Ref. 4; BAG52931).
{ECO:0000305}.
STRAND 4 10 {ECO:0000244|PDB:3I5R}.
STRAND 29 33 {ECO:0000244|PDB:3I5R}.
HELIX 34 40 {ECO:0000244|PDB:3I5R}.
TURN 43 45 {ECO:0000244|PDB:3I5R}.
HELIX 46 48 {ECO:0000244|PDB:3I5R}.
HELIX 50 53 {ECO:0000244|PDB:3I5R}.
STRAND 55 60 {ECO:0000244|PDB:3I5R}.
TURN 61 64 {ECO:0000244|PDB:3I5R}.
STRAND 65 70 {ECO:0000244|PDB:3I5R}.
HELIX 71 73 {ECO:0000244|PDB:3I5R}.
STRAND 74 81 {ECO:0000244|PDB:3I5R}.
TURN 100 102 {ECO:0000244|PDB:1AZG}.
HELIX 118 121 {ECO:0000244|PDB:1PBW}.
HELIX 130 143 {ECO:0000244|PDB:1PBW}.
TURN 147 150 {ECO:0000244|PDB:1PBW}.
HELIX 160 164 {ECO:0000244|PDB:1PBW}.
STRAND 167 170 {ECO:0000244|PDB:1PBW}.
HELIX 174 176 {ECO:0000244|PDB:1PBW}.
HELIX 179 191 {ECO:0000244|PDB:1PBW}.
STRAND 193 195 {ECO:0000244|PDB:1PBW}.
HELIX 200 209 {ECO:0000244|PDB:1PBW}.
HELIX 210 212 {ECO:0000244|PDB:1PBW}.
HELIX 216 227 {ECO:0000244|PDB:1PBW}.
HELIX 234 252 {ECO:0000244|PDB:1PBW}.
HELIX 254 257 {ECO:0000244|PDB:1PBW}.
HELIX 261 273 {ECO:0000244|PDB:1PBW}.
HELIX 280 295 {ECO:0000244|PDB:1PBW}.
HELIX 323 325 {ECO:0000244|PDB:4L23}.
HELIX 328 330 {ECO:0000244|PDB:5GJI}.
STRAND 334 337 {ECO:0000244|PDB:4WAF}.
HELIX 340 347 {ECO:0000244|PDB:5GJI}.
STRAND 354 359 {ECO:0000244|PDB:5GJI}.
HELIX 363 365 {ECO:0000244|PDB:2IUG}.
STRAND 368 374 {ECO:0000244|PDB:5GJI}.
STRAND 377 386 {ECO:0000244|PDB:5GJI}.
STRAND 389 395 {ECO:0000244|PDB:5GJI}.
STRAND 398 400 {ECO:0000244|PDB:5GJI}.
HELIX 401 409 {ECO:0000244|PDB:5GJI}.
HELIX 413 415 {ECO:0000244|PDB:5GJI}.
HELIX 418 420 {ECO:0000244|PDB:5GJI}.
TURN 430 432 {ECO:0000244|PDB:2IUG}.
HELIX 433 436 {ECO:0000244|PDB:4WAF}.
HELIX 442 515 {ECO:0000244|PDB:4JPS}.
HELIX 518 587 {ECO:0000244|PDB:4JPS}.
HELIX 591 598 {ECO:0000244|PDB:2V1Y}.
HELIX 617 619 {ECO:0000244|PDB:5AUL}.
HELIX 621 623 {ECO:0000244|PDB:5AUL}.
STRAND 625 629 {ECO:0000244|PDB:1PIC}.
HELIX 631 638 {ECO:0000244|PDB:5AUL}.
STRAND 645 650 {ECO:0000244|PDB:5AUL}.
STRAND 652 655 {ECO:0000244|PDB:1PIC}.
STRAND 657 663 {ECO:0000244|PDB:5AUL}.
STRAND 666 675 {ECO:0000244|PDB:5AUL}.
STRAND 678 682 {ECO:0000244|PDB:5AUL}.
STRAND 688 690 {ECO:0000244|PDB:5AUL}.
HELIX 691 698 {ECO:0000244|PDB:5AUL}.
HELIX 703 705 {ECO:0000244|PDB:5AUL}.
TURN 708 710 {ECO:0000244|PDB:1PIC}.
STRAND 716 719 {ECO:0000244|PDB:1PIC}.
SEQUENCE 724 AA; 83598 MW; B9DAD8416C33140F CRC64;
MSAEGYQYRA LYDYKKEREE DIDLHLGDIL TVNKGSLVAL GFSDGQEARP EEIGWLNGYN
ETTGERGDFP GTYVEYIGRK KISPPTPKPR PPRPLPVAPG SSKTEADVEQ QALTLPDLAE
QFAPPDIAPP LLIKLVEAIE KKGLECSTLY RTQSSSNLAE LRQLLDCDTP SVDLEMIDVH
VLADAFKRYL LDLPNPVIPA AVYSEMISLA PEVQSSEEYI QLLKKLIRSP SIPHQYWLTL
QYLLKHFFKL SQTSSKNLLN ARVLSEIFSP MLFRFSAASS DNTENLIKVI EILISTEWNE
RQPAPALPPK PPKPTTVANN GMNNNMSLQD AEWYWGDISR EEVNEKLRDT ADGTFLVRDA
STKMHGDYTL TLRKGGNNKL IKIFHRDGKY GFSDPLTFSS VVELINHYRN ESLAQYNPKL
DVKLLYPVSK YQQDQVVKED NIEAVGKKLH EYNTQFQEKS REYDRLYEEY TRTSQEIQMK
RTAIEAFNET IKIFEEQCQT QERYSKEYIE KFKREGNEKE IQRIMHNYDK LKSRISEIID
SRRRLEEDLK KQAAEYREID KRMNSIKPDL IQLRKTRDQY LMWLTQKGVR QKKLNEWLGN
ENTEDQYSLV EDDEDLPHHD EKTWNVGSSN RNKAENLLRG KRDGTFLVRE SSKQGCYACS
VVVDGEVKHC VINKTATGYG FAEPYNLYSS LKELVLHYQH TSLVQHNDSL NVTLAYPVYA
QQRR


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