ID P55G_HUMAN Reviewed; 461 AA. AC Q92569; B2R9C1; D3DQ12; O60482; Q5T4P1; Q5T4P2; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2011, sequence version 2. DT 24-JAN-2024, entry version 197. DE RecName: Full=Phosphatidylinositol 3-kinase regulatory subunit gamma; DE Short=PI3-kinase regulatory subunit gamma; DE Short=PI3K regulatory subunit gamma; DE Short=PtdIns-3-kinase regulatory subunit gamma; DE AltName: Full=Phosphatidylinositol 3-kinase 55 kDa regulatory subunit gamma; DE Short=PI3-kinase subunit p55-gamma; DE Short=PtdIns-3-kinase regulatory subunit p55-gamma; DE AltName: Full=p55PIK; GN Name=PIK3R3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT LYS-283. RC TISSUE=Fetal brain; RX PubMed=9524259; DOI=10.1016/s0378-1119(98)00045-6; RA Dey B.R., Furlanetto R.W., Nissley S.P.; RT "Cloning of human p55 gamma, a regulatory subunit of phosphatidylinositol RT 3-kinase, by a yeast two-hybrid library screen with the insulin-like growth RT factor-I receptor."; RL Gene 209:175-183(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT LYS-283. RA Suzuki T.; RT "Molecular cloning of human p55pik."; RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LYS-283. RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LYS-283. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP INTERACTION WITH AXL. RX PubMed=12470648; DOI=10.1016/s0006-291x(02)02718-3; RA Hafizi S., Alindri F., Karlsson R., Dahlbaeck B.; RT "Interaction of Axl receptor tyrosine kinase with C1-TEN, a novel C1 RT domain-containing protein with homology to tensin."; RL Biochem. Biophys. Res. Commun. 299:793-800(2002). CC -!- FUNCTION: Binds to activated (phosphorylated) protein-tyrosine kinases CC through its SH2 domain and regulates their kinase activity. During CC insulin stimulation, it also binds to IRS-1. CC -!- SUBUNIT: Heterodimer of a regulatory subunit PIK3R3 and a p110 CC catalytic subunit (PIK3CA, PIK3CB or PIK3CD). Interacts with AXL. CC {ECO:0000269|PubMed:12470648}. CC -!- INTERACTION: CC Q92569; Q8IZP0: ABI1; NbExp=2; IntAct=EBI-79893, EBI-375446; CC Q92569; Q9BQD7: ANTKMT; NbExp=3; IntAct=EBI-79893, EBI-713602; CC Q92569; P10275: AR; NbExp=37; IntAct=EBI-79893, EBI-608057; CC Q92569; Q4LE39-3: ARID4B; NbExp=3; IntAct=EBI-79893, EBI-11957452; CC Q92569; Q66PJ3-4: ARL6IP4; NbExp=3; IntAct=EBI-79893, EBI-5280499; CC Q92569; P51451: BLK; NbExp=3; IntAct=EBI-79893, EBI-2105445; CC Q92569; Q9H2G9: BLZF1; NbExp=5; IntAct=EBI-79893, EBI-2548012; CC Q92569; Q3SXR2: C3orf36; NbExp=3; IntAct=EBI-79893, EBI-18036948; CC Q92569; P22681: CBL; NbExp=4; IntAct=EBI-79893, EBI-518228; CC Q92569; A0A1B0GWI1: CCDC196; NbExp=3; IntAct=EBI-79893, EBI-10181422; CC Q92569; Q8N998: CCDC89; NbExp=3; IntAct=EBI-79893, EBI-12814117; CC Q92569; Q96LK0: CEP19; NbExp=4; IntAct=EBI-79893, EBI-741885; CC Q92569; Q6WN34-2: CHRDL2; NbExp=3; IntAct=EBI-79893, EBI-12593838; CC Q92569; A8MTA8-2: CIMIP2B; NbExp=3; IntAct=EBI-79893, EBI-12160437; CC Q92569; P46108: CRK; NbExp=3; IntAct=EBI-79893, EBI-886; CC Q92569; P53672: CRYBA2; NbExp=4; IntAct=EBI-79893, EBI-750444; CC Q92569; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-79893, EBI-11988027; CC Q92569; Q14919: DRAP1; NbExp=4; IntAct=EBI-79893, EBI-712941; CC Q92569; P00533: EGFR; NbExp=7; IntAct=EBI-79893, EBI-297353; CC Q92569; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-79893, EBI-744099; CC Q92569; P04626: ERBB2; NbExp=10; IntAct=EBI-79893, EBI-641062; CC Q92569; P21860: ERBB3; NbExp=22; IntAct=EBI-79893, EBI-720706; CC Q92569; Q8TC99: FNDC8; NbExp=3; IntAct=EBI-79893, EBI-12903902; CC Q92569; O43559: FRS3; NbExp=3; IntAct=EBI-79893, EBI-725515; CC Q92569; Q13480: GAB1; NbExp=36; IntAct=EBI-79893, EBI-517684; CC Q92569; P62993: GRB2; NbExp=4; IntAct=EBI-79893, EBI-401755; CC Q92569; P08631-2: HCK; NbExp=4; IntAct=EBI-79893, EBI-9834454; CC Q92569; P42858: HTT; NbExp=18; IntAct=EBI-79893, EBI-466029; CC Q92569; P35568: IRS1; NbExp=4; IntAct=EBI-79893, EBI-517592; CC Q92569; Q13352: ITGB3BP; NbExp=3; IntAct=EBI-79893, EBI-712105; CC Q92569; Q6ZU52: KIAA0408; NbExp=3; IntAct=EBI-79893, EBI-739493; CC Q92569; P10721: KIT; NbExp=31; IntAct=EBI-79893, EBI-1379503; CC Q92569; Q96JM7-2: L3MBTL3; NbExp=3; IntAct=EBI-79893, EBI-11985629; CC Q92569; P28838: LAP3; NbExp=3; IntAct=EBI-79893, EBI-2339312; CC Q92569; P08581: MET; NbExp=11; IntAct=EBI-79893, EBI-1039152; CC Q92569; Q8N6F8: METTL27; NbExp=3; IntAct=EBI-79893, EBI-8487781; CC Q92569; Q15742: NAB2; NbExp=3; IntAct=EBI-79893, EBI-8641936; CC Q92569; O76041: NEBL; NbExp=3; IntAct=EBI-79893, EBI-2880203; CC Q92569; Q14511-2: NEDD9; NbExp=3; IntAct=EBI-79893, EBI-11746523; CC Q92569; Q8TAK6: OLIG1; NbExp=2; IntAct=EBI-79893, EBI-3867416; CC Q92569; Q6GQQ9: OTUD7B; NbExp=3; IntAct=EBI-79893, EBI-527784; CC Q92569; Q9NPB6-2: PARD6A; NbExp=3; IntAct=EBI-79893, EBI-10693102; CC Q92569; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-79893, EBI-10302990; CC Q92569; Q8N2H9: PELI3; NbExp=3; IntAct=EBI-79893, EBI-448457; CC Q92569; P42336: PIK3CA; NbExp=45; IntAct=EBI-79893, EBI-2116585; CC Q92569; P42338: PIK3CB; NbExp=3; IntAct=EBI-79893, EBI-2609540; CC Q92569; O00329: PIK3CD; NbExp=4; IntAct=EBI-79893, EBI-718309; CC Q92569; Q9UL19: PLAAT4; NbExp=3; IntAct=EBI-79893, EBI-10323452; CC Q92569; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-79893, EBI-742388; CC Q92569; Q5SXH7-1: PLEKHS1; NbExp=4; IntAct=EBI-79893, EBI-26412802; CC Q92569; O60237-2: PPP1R12B; NbExp=2; IntAct=EBI-79893, EBI-10700351; CC Q92569; P31321: PRKAR1B; NbExp=3; IntAct=EBI-79893, EBI-2805516; CC Q92569; I6L996: PTK2; NbExp=3; IntAct=EBI-79893, EBI-10181089; CC Q92569; Q05397: PTK2; NbExp=3; IntAct=EBI-79893, EBI-702142; CC Q92569; Q96R05: RBP7; NbExp=3; IntAct=EBI-79893, EBI-2856326; CC Q92569; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-79893, EBI-6257312; CC Q92569; Q14140: SERTAD2; NbExp=3; IntAct=EBI-79893, EBI-2822051; CC Q92569; Q9NP31: SH2D2A; NbExp=4; IntAct=EBI-79893, EBI-490630; CC Q92569; Q8WXH5: SOCS4; NbExp=3; IntAct=EBI-79893, EBI-3942425; CC Q92569; Q96LK8: SPATA32; NbExp=3; IntAct=EBI-79893, EBI-12849978; CC Q92569; Q8NCR6: SPMIP6; NbExp=3; IntAct=EBI-79893, EBI-10269322; CC Q92569; Q99619: SPSB2; NbExp=3; IntAct=EBI-79893, EBI-2323209; CC Q92569; P12931: SRC; NbExp=3; IntAct=EBI-79893, EBI-621482; CC Q92569; Q9BWG4: SSBP4; NbExp=3; IntAct=EBI-79893, EBI-744719; CC Q92569; P51692: STAT5B; NbExp=3; IntAct=EBI-79893, EBI-1186119; CC Q92569; Q5VWN6: TASOR2; NbExp=5; IntAct=EBI-79893, EBI-745958; CC Q92569; Q07912-2: TNK2; NbExp=3; IntAct=EBI-79893, EBI-11994780; CC Q92569; P19237: TNNI1; NbExp=3; IntAct=EBI-79893, EBI-746692; CC Q92569; P04637: TP53; NbExp=5; IntAct=EBI-79893, EBI-366083; CC Q92569; O60636: TSPAN2; NbExp=3; IntAct=EBI-79893, EBI-3914288; CC Q92569; Q8IZQ1: WDFY3; NbExp=2; IntAct=EBI-79893, EBI-1569256; CC Q92569; P07947: YES1; NbExp=3; IntAct=EBI-79893, EBI-515331; CC Q92569; Q99592: ZBTB18; NbExp=3; IntAct=EBI-79893, EBI-3232046; CC Q92569; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-79893, EBI-4395669; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q92569-1; Sequence=Displayed; CC Name=2; CC IsoId=Q92569-2; Sequence=VSP_004714; CC Name=3; CC IsoId=Q92569-3; Sequence=VSP_004713, VSP_004714; CC -!- TISSUE SPECIFICITY: Highest levels in brain and testis. Lower levels in CC adipose tissue, kidney, heart, lung and skeletal muscle. CC -!- SIMILARITY: Belongs to the PI3K p85 subunit family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF028785; AAC39696.1; -; mRNA. DR EMBL; D88532; BAA13636.1; -; mRNA. DR EMBL; AK313726; BAG36468.1; -; mRNA. DR EMBL; AL358075; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471059; EAX06946.1; -; Genomic_DNA. DR EMBL; CH471059; EAX06947.1; -; Genomic_DNA. DR EMBL; CH471059; EAX06944.1; -; Genomic_DNA. DR EMBL; CH471059; EAX06945.1; -; Genomic_DNA. DR CCDS; CCDS529.1; -. [Q92569-1] DR CCDS; CCDS76154.1; -. [Q92569-2] DR RefSeq; NP_001107644.1; NM_001114172.1. [Q92569-1] DR RefSeq; NP_001290358.1; NM_001303429.1. [Q92569-2] DR RefSeq; NP_003620.3; NM_003629.3. [Q92569-1] DR RefSeq; XP_016858103.1; XM_017002614.1. DR AlphaFoldDB; Q92569; -. DR SMR; Q92569; -. DR BioGRID; 114075; 200. DR ComplexPortal; CPX-1918; Phosphatidylinositol 3-kinase complex class IA, p110alpha/p55gamma. DR ComplexPortal; CPX-5977; Phosphatidylinositol 3-kinase complex class IA, p110beta/p55gamma. DR ComplexPortal; CPX-5978; Phosphatidylinositol 3-kinase complex class IA, p110delta/p55gamma. DR DIP; DIP-30925N; -. DR IntAct; Q92569; 196. DR MINT; Q92569; -. DR STRING; 9606.ENSP00000262741; -. DR ChEMBL; CHEMBL3559703; -. DR DrugBank; DB05210; SF1126. DR MoonDB; Q92569; Predicted. DR GlyGen; Q92569; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q92569; -. DR PhosphoSitePlus; Q92569; -. DR BioMuta; PIK3R3; -. DR DMDM; 317373310; -. DR EPD; Q92569; -. DR jPOST; Q92569; -. DR MassIVE; Q92569; -. DR MaxQB; Q92569; -. DR PaxDb; 9606-ENSP00000262741; -. DR PeptideAtlas; Q92569; -. DR ProteomicsDB; 75327; -. [Q92569-1] DR ProteomicsDB; 75328; -. [Q92569-2] DR ProteomicsDB; 75329; -. [Q92569-3] DR Pumba; Q92569; -. DR Antibodypedia; 1490; 336 antibodies from 35 providers. DR DNASU; 8503; -. DR Ensembl; ENST00000262741.10; ENSP00000262741.5; ENSG00000117461.15. [Q92569-1] DR Ensembl; ENST00000372006.5; ENSP00000361075.1; ENSG00000117461.15. [Q92569-1] DR Ensembl; ENST00000420542.5; ENSP00000412546.1; ENSG00000117461.15. [Q92569-1] DR Ensembl; ENST00000423209.5; ENSP00000391431.1; ENSG00000117461.15. [Q92569-2] DR GeneID; 8503; -. DR KEGG; hsa:8503; -. DR MANE-Select; ENST00000262741.10; ENSP00000262741.5; NM_003629.4; NP_003620.3. DR UCSC; uc001cpb.5; human. [Q92569-1] DR AGR; HGNC:8981; -. DR CTD; 8503; -. DR DisGeNET; 8503; -. DR GeneCards; PIK3R3; -. DR HGNC; HGNC:8981; PIK3R3. DR HPA; ENSG00000117461; Low tissue specificity. DR MIM; 606076; gene. DR neXtProt; NX_Q92569; -. DR OpenTargets; ENSG00000117461; -. DR PharmGKB; PA33314; -. DR VEuPathDB; HostDB:ENSG00000117461; -. DR eggNOG; KOG4637; Eukaryota. DR GeneTree; ENSGT00940000156259; -. DR HOGENOM; CLU_041839_0_0_1; -. DR InParanoid; Q92569; -. DR OMA; AQPHEKN; -. DR OrthoDB; 2880119at2759; -. DR PhylomeDB; Q92569; -. DR TreeFam; TF102033; -. DR BioCyc; MetaCyc:ENSG00000117461-MONOMER; -. DR PathwayCommons; Q92569; -. DR Reactome; R-HSA-114604; GPVI-mediated activation cascade. DR Reactome; R-HSA-1257604; PIP3 activates AKT signaling. DR Reactome; R-HSA-1266695; Interleukin-7 signaling. DR Reactome; R-HSA-1433557; Signaling by SCF-KIT. DR Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane. DR Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer. DR Reactome; R-HSA-388841; Costimulation by the CD28 family. DR Reactome; R-HSA-389357; CD28 dependent PI3K/Akt signaling. DR Reactome; R-HSA-416476; G alpha (q) signalling events. DR Reactome; R-HSA-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling. DR Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling. DR Reactome; R-HSA-8853659; RET signaling. DR Reactome; R-HSA-9009391; Extra-nuclear estrogen signaling. DR Reactome; R-HSA-9013149; RAC1 GTPase cycle. DR Reactome; R-HSA-9013404; RAC2 GTPase cycle. DR Reactome; R-HSA-912526; Interleukin receptor SHC signaling. DR Reactome; R-HSA-912631; Regulation of signaling by CBL. DR Reactome; R-HSA-9670439; Signaling by phosphorylated juxtamembrane, extracellular and kinase domain KIT mutants. DR SignaLink; Q92569; -. DR SIGNOR; Q92569; -. DR BioGRID-ORCS; 8503; 13 hits in 1163 CRISPR screens. DR ChiTaRS; PIK3R3; human. DR GeneWiki; PIK3R3; -. DR GenomeRNAi; 8503; -. DR Pharos; Q92569; Tbio. DR PRO; PR:Q92569; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q92569; Protein. DR Bgee; ENSG00000117461; Expressed in cerebellar vermis and 182 other cell types or tissues. DR ExpressionAtlas; Q92569; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IBA:GO_Central. DR GO; GO:0005943; C:phosphatidylinositol 3-kinase complex, class IA; NAS:ComplexPortal. DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; TAS:ProtInc. DR GO; GO:0046935; F:1-phosphatidylinositol-3-kinase regulator activity; IBA:GO_Central. DR GO; GO:0001784; F:phosphotyrosine residue binding; IPI:CAFA. DR GO; GO:0030183; P:B cell differentiation; NAS:ComplexPortal. DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; IGI:BHF-UCL. DR GO; GO:0006955; P:immune response; NAS:ComplexPortal. DR GO; GO:0008286; P:insulin receptor signaling pathway; IBA:GO_Central. DR GO; GO:2000811; P:negative regulation of anoikis; NAS:ComplexPortal. DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IMP:BHF-UCL. DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central. DR GO; GO:0030335; P:positive regulation of cell migration; NAS:ARUK-UCL. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:BHF-UCL. DR GO; GO:0030217; P:T cell differentiation; NAS:ComplexPortal. DR CDD; cd09930; SH2_cSH2_p85_like; 1. DR CDD; cd09942; SH2_nSH2_p85_like; 1. DR Gene3D; 1.10.287.1490; -; 1. DR Gene3D; 3.30.505.10; SH2 domain; 2. DR InterPro; IPR032498; PI3K_P85_iSH2. DR InterPro; IPR035020; PI3kinase_P85_cSH2. DR InterPro; IPR035022; PI3kinase_P85_nSH2. DR InterPro; IPR000980; SH2. DR InterPro; IPR036860; SH2_dom_sf. DR PANTHER; PTHR10155; PHOSPHATIDYLINOSITOL 3-KINASE REGULATORY SUBUNIT; 1. DR PANTHER; PTHR10155:SF10; PI3K21B, ISOFORM B; 1. DR Pfam; PF16454; PI3K_P85_iSH2; 1. DR Pfam; PF00017; SH2; 2. DR PRINTS; PR00678; PI3KINASEP85. DR PRINTS; PR00401; SH2DOMAIN. DR SMART; SM00252; SH2; 2. DR SUPFAM; SSF55550; SH2 domain; 2. DR PROSITE; PS50001; SH2; 2. DR Genevisible; Q92569; HS. PE 1: Evidence at protein level; KW Alternative splicing; Phosphoprotein; Reference proteome; Repeat; KW SH2 domain. FT CHAIN 1..461 FT /note="Phosphatidylinositol 3-kinase regulatory subunit FT gamma" FT /id="PRO_0000080767" FT DOMAIN 65..160 FT /note="SH2 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191" FT DOMAIN 358..452 FT /note="SH2 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191" FT MOD_RES 341 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q64143" FT VAR_SEQ 36..71 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:9524259" FT /id="VSP_004713" FT VAR_SEQ 256..314 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:9524259" FT /id="VSP_004714" FT VARIANT 283 FT /note="N -> K (in dbSNP:rs785467)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:9524259, ECO:0000269|Ref.2, FT ECO:0000269|Ref.5" FT /id="VAR_047153" FT CONFLICT 21 FT /note="P -> L (in Ref. 1; AAC39696)" FT /evidence="ECO:0000305" SQ SEQUENCE 461 AA; 54448 MW; 303BCC2F9EEE5364 CRC64; MYNTVWSMDR DDADWREVMM PYSTELIFYI EMDPPALPPK PPKPMTSAVP NGMKDSSVSL QDAEWYWGDI SREEVNDKLR DMPDGTFLVR DASTKMQGDY TLTLRKGGNN KLIKIYHRDG KYGFSDPLTF NSVVELINHY HHESLAQYNP KLDVKLMYPV SRYQQDQLVK EDNIDAVGKK LQEYHSQYQE KSKEYDRLYE EYTRTSQEIQ MKRTAIEAFN ETIKIFEEQC HTQEQHSKEY IERFRREGNE KEIERIMMNY DKLKSRLGEI HDSKMRLEQD LKNQALDNRE IDKKMNSIKP DLIQLRKIRD QHLVWLNHKG VRQKRLNVWL GIKNEDADEN YFINEEDENL PHYDEKTWFV EDINRVQAED LLYGKPDGAF LIRESSKKGC YACSVVADGE VKHCVIYSTA RGYGFAEPYN LYSSLKELVL HYQQTSLVQH NDSLNVRLAY PVHAQMPSLC R //