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

 P85B_HUMAN              Reviewed;         728 AA.
O00459; Q5EAT5; Q9UPH9;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 2.
22-NOV-2017, entry version 182.
RecName: Full=Phosphatidylinositol 3-kinase regulatory subunit beta;
Short=PI3-kinase regulatory subunit beta;
Short=PI3K regulatory subunit beta;
Short=PtdIns-3-kinase regulatory subunit beta;
AltName: Full=Phosphatidylinositol 3-kinase 85 kDa regulatory subunit beta;
Short=PI3-kinase subunit p85-beta;
Short=PtdIns-3-kinase regulatory subunit p85-beta;
Name=PIK3R2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-234 AND PRO-313.
PubMed=1314371;
Volinia S., Patracchini P., Otsu M., Hiles I., Gout I., Calzolari E.,
Bernardi F., Rooke L., Waterfield M.D.;
"Chromosomal localization of human p85 alpha, a subunit of
phosphatidylinositol 3-kinase, and its homologue p85 beta.";
Oncogene 7:789-793(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ARG-234 AND PRO-313.
PubMed=9582025; DOI=10.1038/sj.onc.1201695;
Janssen J.W.G., Schleithhoff L., Bartram C.R., Schulz A.S.;
"An oncogenic fusion product of the phosphatidylinositol 3-kinase
p85beta subunit and HUMORF8, a putative deubiquitinating enzyme.";
Oncogene 16:1767-1772(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-234 AND
PRO-313.
TISSUE=Brain, and Placenta;
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).
[5]
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).
[6]
INTERACTION WITH FLT1.
PubMed=9600074; DOI=10.1006/bbrc.1998.8578;
Igarashi K., Isohara T., Kato T., Shigeta K., Yamano T., Uno I.;
"Tyrosine 1213 of Flt-1 is a major binding site of Nck and SHP-2.";
Biochem. Biophys. Res. Commun. 246:95-99(1998).
[7]
INTERACTION WITH FLT4.
PubMed=15102829; DOI=10.1074/jbc.M314015200;
Wang J.F., Zhang X., Groopman J.E.;
"Activation of vascular endothelial growth factor receptor-3 and its
downstream signaling promote cell survival under oxidative stress.";
J. Biol. Chem. 279:27088-27097(2004).
[8]
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).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
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).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-605, AND 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).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-464, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-464, 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).
[15]
FUNCTION, INTERACTION WITH FBXL2 AND PTPN13, PHOSPHORYLATION AT
TYR-655, DEPHOSPHORYLATION AT TYR-655 BY PTPN13, UBIQUITINATION,
DOMAIN, AND MUTAGENESIS OF GLN-651; ARG-652 AND TYR-655.
PubMed=23604317; DOI=10.1038/ncb2731;
Kuchay S., Duan S., Schenkein E., Peschiaroli A., Saraf A.,
Florens L., Washburn M.P., Pagano M.;
"FBXL2- and PTPL1-mediated degradation of p110-free p85beta regulatory
subunit controls the PI(3)K signalling cascade.";
Nat. Cell Biol. 15:472-480(2013).
[16]
INVOLVEMENT IN MPPH1, AND VARIANT MPPH1 PRO-401.
PubMed=23745724; DOI=10.1111/cge.12188;
Nakamura K., Kato M., Tohyama J., Shiohama T., Hayasaka K.,
Nishiyama K., Kodera H., Nakashima M., Tsurusaki Y., Miyake N.,
Matsumoto N., Saitsu H.;
"AKT3 and PIK3R2 mutations in two patients with megalencephaly-related
syndromes: MCAP and MPPH.";
Clin. Genet. 85:396-398(2014).
[17]
INVOLVEMENT IN MPPH1, AND VARIANT MPPH1 ARG-373.
PubMed=22729224; DOI=10.1038/ng.2331;
Riviere J.B., Mirzaa G.M., O'Roak B.J., Beddaoui M., Alcantara D.,
Conway R.L., St-Onge J., Schwartzentruber J.A., Gripp K.W.,
Nikkel S.M., Worthylake T., Sullivan C.T., Ward T.R., Butler H.E.,
Kramer N.A., Albrecht B., Armour C.M., Armstrong L., Caluseriu O.,
Cytrynbaum C., Drolet B.A., Innes A.M., Lauzon J.L., Lin A.E.,
Mancini G.M., Meschino W.S., Reggin J.D., Saggar A.K.,
Lerman-Sagie T., Uyanik G., Weksberg R., Zirn B., Beaulieu C.L.,
Majewski J., Bulman D.E., O'Driscoll M., Shendure J., Graham J.M. Jr.,
Boycott K.M., Dobyns W.B.;
"De novo germline and postzygotic mutations in AKT3, PIK3R2 and PIK3CA
cause a spectrum of related megalencephaly syndromes.";
Nat. Genet. 44:934-940(2012).
[18]
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).
[19]
VARIANTS MPPH1 ARG-373 AND GLU-376.
PubMed=26520804; DOI=10.1016/S1474-4422(15)00278-1;
Mirzaa G.M., Conti V., Timms A.E., Smyser C.D., Ahmed S., Carter M.,
Barnett S., Hufnagel R.B., Goldstein A., Narumi-Kishimoto Y., Olds C.,
Collins S., Johnston K., Deleuze J.F., Nitschke P., Friend K.,
Harris C., Goetsch A., Martin B., Boyle E.A., Parrini E., Mei D.,
Tattini L., Slavotinek A., Blair E., Barnett C., Shendure J.,
Chelly J., Dobyns W.B., Guerrini R.;
"Characterisation of mutations of the phosphoinositide-3-kinase
regulatory subunit, PIK3R2, in perisylvian polymicrogyria: a next-
generation sequencing study.";
Lancet Neurol. 14:1182-1195(2015).
[20]
VARIANT MPPH1 HIS-557.
PubMed=26860062; DOI=10.1038/ejhg.2016.7;
Terrone G., Voisin N., Abdullah Alfaiz A., Cappuccio G., Vitiello G.,
Guex N., D'Amico A., James Barkovich A., Brunetti-Pierri N.,
Del Giudice E., Reymond A.;
"De novo PIK3R2 variant causes polymicrogyria, corpus callosum
hyperplasia and focal cortical dysplasia.";
Eur. J. Hum. Genet. 24:1359-1362(2016).
-!- FUNCTION: Regulatory subunit of phosphoinositide-3-kinase (PI3K),
a kinase that phosphorylates PtdIns(4,5)P2 (Phosphatidylinositol
4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-
trisphosphate (PIP3). PIP3 plays a key role by recruiting PH
domain-containing proteins to the membrane, including AKT1 and
PDPK1, activating signaling cascades involved in cell growth,
survival, proliferation, motility and morphology. Binds to
activated (phosphorylated) protein-tyrosine kinases, through its
SH2 domain, and acts as an adapter, mediating the association of
the p110 catalytic unit to the plasma membrane. Indirectly
regulates autophagy (PubMed:23604317). Promotes 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 (By
similarity). {ECO:0000250|UniProtKB:O08908,
ECO:0000269|PubMed:23604317}.
-!- SUBUNIT: Heterodimer of a regulatory subunit PIK3R2 and a p110
catalytic subunit (PIK3CA, PIK3CB or PIK3CD) (PubMed:23604317).
Interacts with AXL (PubMed:9178760). Interacts with FLT1
(tyrosine-phosphorylated) and FLT4 (tyrosine-phosphorylated)
(PubMed:9600074, PubMed:15102829). Interacts with NYAP1, NYAP2 and
MYO16 (By similarity). Interacts with FBXL2; PIK3R2 is a substrate
of the SCF(FBXL2) complex (PubMed:23604317). Interacts with
PTPN13; dephosphorylates PIK3R2 (PubMed:23604317). 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 (By
similarity). Interacts with PIK3R1; the interaction is dissociated
in an insulin-dependent manner (By similarity).
{ECO:0000250|UniProtKB:O08908, ECO:0000269|PubMed:15102829,
ECO:0000269|PubMed:23604317, ECO:0000269|PubMed:9178760,
ECO:0000269|PubMed:9600074}.
-!- INTERACTION:
P10275:AR; NbExp=14; IntAct=EBI-346930, EBI-608057;
P22681:CBL; NbExp=4; IntAct=EBI-346930, EBI-518228;
Q8WWB3:DYDC1; NbExp=3; IntAct=EBI-346930, EBI-740680;
P00533:EGFR; NbExp=3; IntAct=EBI-346930, EBI-297353;
P04626:ERBB2; NbExp=6; IntAct=EBI-346930, EBI-641062;
P21860:ERBB3; NbExp=16; IntAct=EBI-346930, EBI-720706;
Q13480:GAB1; NbExp=23; IntAct=EBI-346930, EBI-517684;
Q08379:GOLGA2; NbExp=3; IntAct=EBI-346930, EBI-618309;
P62993:GRB2; NbExp=4; IntAct=EBI-346930, EBI-401755;
P42858:HTT; NbExp=6; IntAct=EBI-346930, EBI-466029;
Q9UKT9:IKZF3; NbExp=3; IntAct=EBI-346930, EBI-747204;
P10721:KIT; NbExp=19; IntAct=EBI-346930, EBI-1379503;
P19012:KRT15; NbExp=3; IntAct=EBI-346930, EBI-739566;
P35900:KRT20; NbExp=3; IntAct=EBI-346930, EBI-742094;
O76015:KRT38; NbExp=3; IntAct=EBI-346930, EBI-1047263;
P08581:MET; NbExp=11; IntAct=EBI-346930, EBI-1039152;
Q96HT8:MRFAP1L1; NbExp=4; IntAct=EBI-346930, EBI-748896;
P03496:NS (xeno); NbExp=13; IntAct=EBI-346930, EBI-2547442;
Q82506:NS (xeno); NbExp=2; IntAct=EBI-346930, EBI-6149498;
P42338:PIK3CB; NbExp=3; IntAct=EBI-346930, EBI-2609540;
Q6NUQ1:RINT1; NbExp=3; IntAct=EBI-346930, EBI-726876;
P36406:TRIM23; NbExp=3; IntAct=EBI-346930, EBI-740098;
-!- DOMAIN: The SH2 2 domain is required for interaction with FBXL2
and PTPN13. {ECO:0000269|PubMed:23604317}.
-!- PTM: Phosphorylated in response to signaling from activated
receptor-type protein kinases (PubMed:19690332, PubMed:20068231).
Dephosphorylated by PTPRJ (PubMed:18348712). Dephosphorylated at
Tyr-655 by PTPN13. Phosphorylation of Tyr-655 impairs while its
dephosphorylation promotes interaction with FBXL2 and SCF(FBXL2)-
mediated polyubiquitination (PubMed:23604317).
{ECO:0000269|PubMed:18348712, ECO:0000269|PubMed:23604317}.
-!- PTM: Ubiquitinated. Polyubiquitination by the SCF(FBXL2) complex
probably promotes proteasomal degradation of PIK3R2.
{ECO:0000303|PubMed:23604317}.
-!- DISEASE: Megalencephaly-polymicrogyria-polydactyly-hydrocephalus
syndrome 1 (MPPH1) [MIM:603387]: A syndrome characterized by
megalencephaly, hydrocephalus, and polymicrogyria; polydactyly may
also be seen. There is considerable phenotypic similarity between
this disorder and the megalencephaly-capillary malformation
syndrome. {ECO:0000269|PubMed:22729224,
ECO:0000269|PubMed:23745724, ECO:0000269|PubMed:26520804,
ECO:0000269|PubMed:26860062}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the PI3K p85 subunit family. {ECO:0000305}.
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EMBL; X80907; CAA56868.1; -; mRNA.
EMBL; AC007192; AAD22671.1; -; Genomic_DNA.
EMBL; BC070082; AAH70082.1; -; mRNA.
EMBL; BC090249; AAH90249.1; -; mRNA.
CCDS; CCDS12371.1; -.
PIR; H59435; H59435.
RefSeq; NP_005018.1; NM_005027.3.
UniGene; Hs.371344; -.
PDB; 2KT1; NMR; -; A=1-80.
PDB; 2XS6; X-ray; 2.09 A; A=108-298.
PDB; 3MTT; X-ray; 3.30 A; A=433-610.
PDB; 3O5Z; X-ray; 2.01 A; A/B=1-85.
PDBsum; 2KT1; -.
PDBsum; 2XS6; -.
PDBsum; 3MTT; -.
PDBsum; 3O5Z; -.
ProteinModelPortal; O00459; -.
SMR; O00459; -.
BioGrid; 111314; 124.
DIP; DIP-31811N; -.
IntAct; O00459; 71.
MINT; MINT-1210047; -.
STRING; 9606.ENSP00000471914; -.
BindingDB; O00459; -.
ChEMBL; CHEMBL3559703; -.
DrugBank; DB01064; Isoprenaline.
DrugBank; DB05210; SF1126.
iPTMnet; O00459; -.
PhosphoSitePlus; O00459; -.
EPD; O00459; -.
MaxQB; O00459; -.
PaxDb; O00459; -.
PeptideAtlas; O00459; -.
PRIDE; O00459; -.
Ensembl; ENST00000222254; ENSP00000222254; ENSG00000105647.
Ensembl; ENST00000617130; ENSP00000477864; ENSG00000105647.
GeneID; 5296; -.
KEGG; hsa:5296; -.
UCSC; uc002nia.3; human.
CTD; 5296; -.
DisGeNET; 5296; -.
EuPathDB; HostDB:ENSG00000105647.14; -.
GeneCards; PIK3R2; -.
HGNC; HGNC:8980; PIK3R2.
HPA; HPA069291; -.
MalaCards; PIK3R2; -.
MIM; 603157; gene.
MIM; 603387; phenotype.
neXtProt; NX_O00459; -.
OpenTargets; ENSG00000105647; -.
OpenTargets; ENSG00000268173; -.
Orphanet; 83473; Megalencephaly - polymicrogyria - postaxial polydactyly - hydrocephalus.
PharmGKB; PA33313; -.
eggNOG; KOG4637; Eukaryota.
eggNOG; ENOG410XP6R; LUCA.
GeneTree; ENSGT00390000010431; -.
HOGENOM; HOG000008438; -.
HOVERGEN; HBG082100; -.
InParanoid; O00459; -.
KO; K02649; -.
OMA; HCVIYKT; -.
OrthoDB; EOG091G0C3Z; -.
PhylomeDB; O00459; -.
TreeFam; TF102033; -.
BioCyc; MetaCyc:ENSG00000105647-MONOMER; -.
Reactome; R-HSA-109704; PI3K Cascade.
Reactome; R-HSA-114604; GPVI-mediated activation cascade.
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-186763; Downstream signal transduction.
Reactome; R-HSA-194840; Rho GTPase cycle.
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 family 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-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-HSA-512988; Interleukin-3, 5 and GM-CSF signaling.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-HSA-8853659; RET signaling.
Reactome; R-HSA-912526; Interleukin receptor SHC signaling.
Reactome; R-HSA-912631; Regulation of signaling by CBL.
SignaLink; O00459; -.
SIGNOR; O00459; -.
ChiTaRS; PIK3R2; human.
EvolutionaryTrace; O00459; -.
GeneWiki; PIK3R2; -.
GenomeRNAi; 5296; -.
PRO; PR:O00459; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000105647; -.
CleanEx; HS_PIK3R2; -.
ExpressionAtlas; O00459; baseline and differential.
Genevisible; O00459; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IBA:GO_Central.
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:0005096; F:GTPase activator activity; TAS:Reactome.
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; ISS:ParkinsonsUK-UCL.
GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:UniProtKB.
GO; GO:0001678; P:cellular glucose homeostasis; ISS:UniProtKB.
GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
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:0008286; P:insulin receptor signaling pathway; IBA:GO_Central.
GO; GO:0038111; P:interleukin-7-mediated signaling pathway; TAS:Reactome.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0043409; P:negative regulation of MAPK cascade; IMP:BHF-UCL.
GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IDA:UniProtKB.
GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
GO; GO:0046854; P:phosphatidylinositol phosphorylation; IBA:GO_Central.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome.
GO; GO:2001275; P:positive regulation of glucose import in response to insulin stimulus; ISS:AgBase.
GO; GO:0042993; P:positive regulation of transcription factor import into nucleus; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0010506; P:regulation of autophagy; IMP:UniProtKB.
GO; GO:0043551; P:regulation of phosphatidylinositol 3-kinase activity; IBA:GO_Central.
GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; TAS:Reactome.
GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
CDD; cd09930; SH2_cSH2_p85_like; 1.
CDD; cd09942; SH2_nSH2_p85_like; 1.
CDD; cd11909; SH3_PI3K_p85beta; 1.
Gene3D; 1.10.555.10; -; 1.
Gene3D; 3.30.505.10; -; 2.
InterPro; IPR032498; PI3K_P85_iSH2.
InterPro; IPR035586; PI3K_p85beta_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; IPR036860; SH2_dom_sf.
InterPro; IPR036028; SH3-like_dom_sf.
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; Complete proteome; Disease mutation; Phosphoprotein;
Polymorphism; Protein transport; Reference proteome; Repeat;
SH2 domain; SH3 domain; Stress response; Transport; Ubl conjugation.
CHAIN 1 728 Phosphatidylinositol 3-kinase regulatory
subunit beta.
/FTId=PRO_0000080763.
DOMAIN 4 80 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 109 295 Rho-GAP. {ECO:0000255|PROSITE-
ProRule:PRU00172}.
DOMAIN 330 425 SH2 1. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 622 716 SH2 2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
MOD_RES 464 464 Phosphotyrosine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 605 605 Phosphotyrosine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 655 655 Phosphotyrosine.
{ECO:0000269|PubMed:23604317}.
VARIANT 234 234 S -> R (in dbSNP:rs2241088).
{ECO:0000269|PubMed:1314371,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9582025}.
/FTId=VAR_030679.
VARIANT 313 313 S -> P (in dbSNP:rs1011320).
{ECO:0000269|PubMed:1314371,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9582025}.
/FTId=VAR_030680.
VARIANT 373 373 G -> R (in MPPH1; dbSNP:rs587776934).
{ECO:0000269|PubMed:22729224,
ECO:0000269|PubMed:26520804}.
/FTId=VAR_069262.
VARIANT 376 376 K -> E (in MPPH1; unknown pathological
significance).
{ECO:0000269|PubMed:26520804}.
/FTId=VAR_075556.
VARIANT 401 401 L -> P (in MPPH1; dbSNP:rs587777624).
{ECO:0000269|PubMed:23745724}.
/FTId=VAR_075683.
VARIANT 557 557 D -> H (in MPPH1; dbSNP:rs372272045).
{ECO:0000269|PubMed:26860062}.
/FTId=VAR_075684.
MUTAGEN 651 651 Q->A: Loss of interaction with FBXL2 and
increased half-life; when associated with
A-652. {ECO:0000269|PubMed:23604317}.
MUTAGEN 652 652 R->A: Loss of interaction with FBXL2 and
increased half-life; when associated with
A-651. {ECO:0000269|PubMed:23604317}.
MUTAGEN 655 655 Y->A: Stabilized interaction with FBXL2
and decreased half-life.
{ECO:0000269|PubMed:23604317}.
STRAND 5 11 {ECO:0000244|PDB:3O5Z}.
STRAND 30 34 {ECO:0000244|PDB:3O5Z}.
HELIX 35 40 {ECO:0000244|PDB:3O5Z}.
HELIX 47 49 {ECO:0000244|PDB:3O5Z}.
HELIX 51 54 {ECO:0000244|PDB:3O5Z}.
STRAND 56 61 {ECO:0000244|PDB:3O5Z}.
TURN 62 64 {ECO:0000244|PDB:3O5Z}.
STRAND 67 71 {ECO:0000244|PDB:3O5Z}.
HELIX 72 74 {ECO:0000244|PDB:3O5Z}.
STRAND 75 81 {ECO:0000244|PDB:3O5Z}.
HELIX 114 117 {ECO:0000244|PDB:2XS6}.
HELIX 126 138 {ECO:0000244|PDB:2XS6}.
HELIX 144 146 {ECO:0000244|PDB:2XS6}.
HELIX 162 164 {ECO:0000244|PDB:2XS6}.
HELIX 167 180 {ECO:0000244|PDB:2XS6}.
STRAND 181 183 {ECO:0000244|PDB:2XS6}.
HELIX 188 199 {ECO:0000244|PDB:2XS6}.
HELIX 206 209 {ECO:0000244|PDB:2XS6}.
TURN 211 213 {ECO:0000244|PDB:2XS6}.
HELIX 216 235 {ECO:0000244|PDB:2XS6}.
HELIX 239 255 {ECO:0000244|PDB:2XS6}.
HELIX 279 293 {ECO:0000244|PDB:2XS6}.
HELIX 439 512 {ECO:0000244|PDB:3MTT}.
HELIX 515 583 {ECO:0000244|PDB:3MTT}.
HELIX 588 594 {ECO:0000244|PDB:3MTT}.
SEQUENCE 728 AA; 81545 MW; ADAC3E4B61F3F44A CRC64;
MAGPEGFQYR ALYPFRRERP EDLELLPGDV LVVSRAALQA LGVAEGGERC PQSVGWMPGL
NERTRQRGDF PGTYVEFLGP VALARPGPRP RGPRPLPARP RDGAPEPGLT LPDLPEQFSP
PDVAPPLLVK LVEAIERTGL DSESHYRPEL PAPRTDWSLS DVDQWDTAAL ADGIKSFLLA
LPAPLVTPEA SAEARRALRE AAGPVGPALE PPTLPLHRAL TLRFLLQHLG RVASRAPALG
PAVRALGATF GPLLLRAPPP PSSPPPGGAP DGSEPSPDFP ALLVEKLLQE HLEEQEVAPP
ALPPKPPKAK PASTVLANGG SPPSLQDAEW YWGDISREEV NEKLRDTPDG TFLVRDASSK
IQGEYTLTLR KGGNNKLIKV FHRDGHYGFS EPLTFCSVVD LINHYRHESL AQYNAKLDTR
LLYPVSKYQQ DQIVKEDSVE AVGAQLKVYH QQYQDKSREY DQLYEEYTRT SQELQMKRTA
IEAFNETIKI FEEQGQTQEK CSKEYLERFR REGNEKEMQR ILLNSERLKS RIAEIHESRT
KLEQQLRAQA SDNREIDKRM NSLKPDLMQL RKIRDQYLVW LTQKGARQKK INEWLGIKNE
TEDQYALMED EDDLPHHEER TWYVGKINRT QAEEMLSGKR DGTFLIRESS QRGCYACSVV
VDGDTKHCVI YRTATGFGFA EPYNLYGSLK ELVLHYQHAS LVQHNDALTV TLAHPVRAPG
PGPPPAAR


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