P55G_HUMAN
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 03-AUG-2022, entry version 189.
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; P46108: CRK; NbExp=4; 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=9; IntAct=EBI-79893, EBI-641062;
CC Q92569; P21860: ERBB3; NbExp=22; IntAct=EBI-79893, EBI-720706;
CC Q92569; A8MTA8-2: FAM166B; NbExp=3; IntAct=EBI-79893, EBI-12160437;
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=5; 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; Q8NCR6: SMRP1; NbExp=3; IntAct=EBI-79893, EBI-10269322;
CC Q92569; Q8WXH5: SOCS4; NbExp=3; IntAct=EBI-79893, EBI-3942425;
CC Q92569; Q96LK8: SPATA32; NbExp=3; IntAct=EBI-79893, EBI-12849978;
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}.
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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; 188.
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; 188.
DR MINT; Q92569; -.
DR STRING; 9606.ENSP00000262741; -.
DR ChEMBL; CHEMBL3559703; -.
DR DrugBank; DB05210; SF1126.
DR MoonDB; Q92569; Predicted.
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; Q92569; -.
DR PeptideAtlas; Q92569; -.
DR PRIDE; Q92569; -.
DR ProteomicsDB; 75327; -. [Q92569-1]
DR ProteomicsDB; 75328; -. [Q92569-2]
DR ProteomicsDB; 75329; -. [Q92569-3]
DR Antibodypedia; 1490; 288 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 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; VRTCEDE; -.
DR PhylomeDB; Q92569; -.
DR TreeFam; TF102033; -.
DR BioCyc; MetaCyc:ENSG00000117461-MON; -.
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 1075 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 181 other tissues.
DR ExpressionAtlas; Q92569; baseline and differential.
DR Genevisible; Q92569; HS.
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; IC: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; IC:ComplexPortal.
DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; IGI:BHF-UCL.
DR GO; GO:0006955; P:immune response; IC:ComplexPortal.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IBA:GO_Central.
DR GO; GO:2000811; P:negative regulation of anoikis; IC:ComplexPortal.
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:0043491; P:protein kinase B signaling; IMP:BHF-UCL.
DR GO; GO:0043551; P:regulation of phosphatidylinositol 3-kinase activity; IBA:GO_Central.
DR GO; GO:0030217; P:T cell differentiation; IC:ComplexPortal.
DR CDD; cd09930; SH2_cSH2_p85_like; 1.
DR CDD; cd09942; SH2_nSH2_p85_like; 1.
DR Gene3D; 3.30.505.10; -; 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 Pfam; PF16454; PI3K_P85_iSH2; 1.
DR Pfam; PF00017; SH2; 2.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00252; SH2; 2.
DR SUPFAM; SSF55550; SSF55550; 2.
DR PROSITE; PS50001; SH2; 2.
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
