ID   P85B_HUMAN              Reviewed;         728 AA.
AC   O00459; Q5EAT5; Q9UPH9;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   07-JUL-2009, entry version 95.
DE   RecName: Full=Phosphatidylinositol 3-kinase regulatory subunit beta;
DE   AltName: Full=PI3-kinase p85 subunit beta;
DE   AltName: Full=PtdIns-3-kinase p85-beta;
GN   Name=PIK3R2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=98241181; PubMed=9582025; DOI=10.1038/sj.onc.1201695;
RA   Janssen J.W.G., Schleithhoff L., Bartram C.R., Schulz A.S.;
RT   "An oncogenic fusion product of the phosphatidylinositol 3-kinase
RT   p85beta subunit and HUMORF8, a putative deubiquitinating enzyme.";
RL   Oncogene 16:1767-1772(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=92228512; PubMed=1314371;
RA   Volinia S., Patracchini P., Otsu M., Hiles I., Gout I., Calzolari E.,
RA   Bernardi F., Rooke L., Waterfield M.D.;
RT   "Chromosomal localization of human p85 alpha, a subunit of
RT   phosphatidylinositol 3-kinase, and its homologue p85 beta.";
RL   Oncogene 7:789-793(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS SER-234
RP   AND SER-313.
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA   Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA   Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA   Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA   Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA   Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA   Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA   Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA   Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA   Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA   Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA   Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA   Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA   Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA   Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, and Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-464, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Epithelium;
RX   PubMed=15951569; DOI=10.1074/mcp.M500089-MCP200;
RA   Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,
RA   Lauffenburger D.A., White F.M.;
RT   "Time-resolved mass spectrometry of tyrosine phosphorylation sites in
RT   the epidermal growth factor receptor signaling network reveals dynamic
RT   modules.";
RL   Mol. Cell. Proteomics 4:1240-1250(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-464, AND MASS
RP   SPECTROMETRY.
RX   PubMed=15592455; DOI=10.1038/nbt1046;
RA   Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA   Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT   "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT   cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-365; TYR-464 AND
RP   TYR-467, AND MASS SPECTROMETRY.
RX   PubMed=18083107; DOI=10.1016/j.cell.2007.11.025;
RA   Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,
RA   Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,
RA   Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,
RA   Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,
RA   Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
RT   "Global survey of phosphotyrosine signaling identifies oncogenic
RT   kinases in lung cancer.";
RL   Cell 131:1190-1203(2007).
RN   [8]
RP   IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
CC   -!- FUNCTION: Binds to activated (phosphorylated) protein-tyrosine
CC       kinases, through its SH2 domain, and acts as an adapter, mediating
CC       the association of the p110 catalytic unit to the plasma membrane.
CC   -!- SUBUNIT: Heterodimer of a p110 (catalytic) and a p85 (regulatory)
CC       subunits.
CC   -!- INTERACTION:
CC       P08631:HCK; NbExp=1; IntAct=EBI-346930, EBI-346340;
CC   -!- SIMILARITY: Belongs to the PI3K p85 subunit family.
CC   -!- SIMILARITY: Contains 1 Rho-GAP domain.
CC   -!- SIMILARITY: Contains 2 SH2 domains.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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DR   EMBL; X80907; CAA56868.1; -; mRNA.
DR   EMBL; AC007192; AAD22671.1; -; Genomic_DNA.
DR   EMBL; BC070082; AAH70082.1; -; mRNA.
DR   EMBL; BC090249; AAH90249.1; -; mRNA.
DR   IPI; IPI00011736; -.
DR   PIR; H59435; H59435.
DR   RefSeq; NP_005018.1; -.
DR   UniGene; Hs.371344; -.
DR   HSSP; P23727; 2PNB.
DR   SMR; O00459; 324-436, 614-718.
DR   IntAct; O00459; 3.
DR   PhosphoSite; O00459; -.
DR   PRIDE; O00459; -.
DR   Ensembl; ENSG00000105647; Homo sapiens.
DR   GeneID; 5296; -.
DR   KEGG; hsa:5296; -.
DR   UCSC; uc002nia.1; human.
DR   GeneCards; GC19P018089; -.
DR   H-InvDB; HIX0014905; -.
DR   HGNC; HGNC:8980; PIK3R2.
DR   MIM; 603157; gene.
DR   PharmGKB; PA33313; -.
DR   HOGENOM; O00459; -.
DR   HOVERGEN; O00459; -.
DR   Pathway_Interaction_DB; pi3kcipathway; Class I PI3K signaling events.
DR   Pathway_Interaction_DB; trail_pathway; TRAIL signaling pathway.
DR   Reactome; REACT_11044; Signaling by Rho GTPases.
DR   Reactome; REACT_11061; Signalling by NGF.
DR   Reactome; REACT_16888; Signaling by PDGF.
DR   Reactome; REACT_498; Signaling by Insulin receptor.
DR   Reactome; REACT_604; Hemostasis.
DR   Reactome; REACT_6900; Signaling in Immune system.
DR   NextBio; 20470; -.
DR   ArrayExpress; O00459; -.
DR   Bgee; O00459; -.
DR   CleanEx; HS_PIK3R2; -.
DR   GermOnline; ENSG00000105647; Homo sapiens.
DR   GO; GO:0005942; C:phosphoinositide 3-kinase complex; IEA:InterPro.
DR   GO; GO:0035014; F:phosphoinositide 3-kinase regulator activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0019987; P:negative regulation of anti-apoptosis; ISS:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR001720; PI3kinase_P85.
DR   InterPro; IPR000198; RhoGAP.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR001452; SH3_domain.
DR   Gene3D; G3DSA:1.10.555.10; RhoGAP; 1.
DR   Gene3D; G3DSA:3.30.505.10; SH2; 2.
DR   PANTHER; PTHR10155; PI3kinase_P85; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF00017; SH2; 2.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00678; PI3KINASEP85.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   ProDom; PD000093; SH2; 2.
DR   ProDom; PD000066; SH3; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00252; SH2; 2.
DR   SMART; SM00326; SH3; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS50001; SH2; 2.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Phosphoprotein; Polymorphism; Repeat; SH2 domain;
KW   SH3 domain.
FT   CHAIN         1    728       Phosphatidylinositol 3-kinase regulatory
FT                                subunit beta.
FT                                /FTId=PRO_0000080763.
FT   DOMAIN        4     80       SH3.
FT   DOMAIN      109    295       Rho-GAP.
FT   DOMAIN      330    425       SH2 1.
FT   DOMAIN      622    716       SH2 2.
FT   MOD_RES     365    365       Phosphotyrosine.
FT   MOD_RES     464    464       Phosphotyrosine.
FT   MOD_RES     467    467       Phosphotyrosine.
FT   VARIANT     234    234       R -> S (in dbSNP:rs2241088).
FT                                /FTId=VAR_030679.
FT   VARIANT     313    313       P -> S (in dbSNP:rs1011320).
FT                                /FTId=VAR_030680.
SQ   SEQUENCE   728 AA;  81624 MW;  80C2AF244977346B CRC64;
     MAGPEGFQYR ALYPFRRERP EDLELLPGDV LVVSRAALQA LGVAEGGERC PQSVGWMPGL
     NERTRQRGDF PGTYVEFLGP VALARPGPRP RGPRPLPARP RDGAPEPGLT LPDLPEQFSP
     PDVAPPLLVK LVEAIERTGL DSESHYRPEL PAPRTDWSLS DVDQWDTAAL ADGIKSFLLA
     LPAPLVTPEA SAEARRALRE AAGPVGPALE PPTLPLHRAL TLRFLLQHLG RVARRAPALG
     PAVRALGATF GPLLLRAPPP PSSPPPGGAP DGSEPSPDFP ALLVEKLLQE HLEEQEVAPP
     ALPPKPPKAK PAPTVLANGG 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
//