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PI3R5_MOUSE
ID   PI3R5_MOUSE             Reviewed;         871 AA.
AC   Q5SW28; Q3TU01; Q3UDZ2; Q8C215; Q8CGQ7;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Phosphoinositide 3-kinase regulatory subunit 5;
DE            Short=PI3-kinase regulatory subunit 5;
DE   AltName: Full=PI3-kinase p101 subunit;
DE   AltName: Full=Phosphatidylinositol 4,5-bisphosphate 3-kinase regulatory subunit;
DE            Short=PtdIns-3-kinase regulatory subunit;
DE   AltName: Full=PtdIns-3-kinase p101;
DE   AltName: Full=p101-PI3K;
GN   Name=Pik3r5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ;
RA   Procko E., McColl S.R.;
RT   "Cloning of a murine ortholog of a PI3-kinase gamma regulatory protein.";
RL   Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Lung;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Regulatory subunit of the PI3K gamma complex. Required for
CC       recruitment of the catalytic subunit to the plasma membrane via
CC       interaction with beta-gamma G protein dimers. Required for G protein-
CC       mediated activation of PIK3CG (By similarity). {ECO:0000250}.
CC   -!- ACTIVITY REGULATION: Greatly activated by G gamma proteins.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer of a catalytic subunit (PIK3CG/p120) and a
CC       regulatory (PIK3R5a/p101) subunit. Interacts with beta-gamma G protein
CC       dimers (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O02696}. Cytoplasm
CC       {ECO:0000250|UniProtKB:O02696}. Cell membrane
CC       {ECO:0000250|UniProtKB:O02696}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:O02696}. Note=Predominantly localized in the
CC       nucleus in absence of PIK3CG/p120. Colocalizes with PIK3CG/p120 in the
CC       cytoplasm. Translocated to the plasma membrane in a beta-gamma G
CC       protein-dependent manner. {ECO:0000250|UniProtKB:O02696}.
CC   -!- DOMAIN: The heterodimerization region allows the binding to the
CC       catalytic subunit. {ECO:0000250}.
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DR   EMBL; AY156924; AAN84787.1; -; mRNA.
DR   EMBL; AK089483; BAC40901.2; -; mRNA.
DR   EMBL; AK149847; BAE29119.1; -; mRNA.
DR   EMBL; AK161050; BAE36171.1; -; mRNA.
DR   EMBL; AL606831; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS24865.1; -.
DR   RefSeq; NP_796294.2; NM_177320.2.
DR   RefSeq; XP_006533611.1; XM_006533548.2.
DR   AlphaFoldDB; Q5SW28; -.
DR   SMR; Q5SW28; -.
DR   CORUM; Q5SW28; -.
DR   IntAct; Q5SW28; 2.
DR   STRING; 10090.ENSMUSP00000021283; -.
DR   iPTMnet; Q5SW28; -.
DR   PhosphoSitePlus; Q5SW28; -.
DR   EPD; Q5SW28; -.
DR   jPOST; Q5SW28; -.
DR   MaxQB; Q5SW28; -.
DR   PaxDb; Q5SW28; -.
DR   PRIDE; Q5SW28; -.
DR   ProteomicsDB; 289417; -.
DR   Antibodypedia; 24754; 456 antibodies from 31 providers.
DR   DNASU; 320207; -.
DR   Ensembl; ENSMUST00000021283; ENSMUSP00000021283; ENSMUSG00000020901.
DR   GeneID; 320207; -.
DR   KEGG; mmu:320207; -.
DR   UCSC; uc007jno.1; mouse.
DR   CTD; 23533; -.
DR   MGI; MGI:2443588; Pik3r5.
DR   VEuPathDB; HostDB:ENSMUSG00000020901; -.
DR   eggNOG; ENOG502QV4A; Eukaryota.
DR   GeneTree; ENSGT00530000063753; -.
DR   HOGENOM; CLU_337590_0_0_1; -.
DR   InParanoid; Q5SW28; -.
DR   OMA; PWEDSTN; -.
DR   OrthoDB; 142794at2759; -.
DR   PhylomeDB; Q5SW28; -.
DR   TreeFam; TF102035; -.
DR   Reactome; R-MMU-114604; GPVI-mediated activation cascade.
DR   Reactome; R-MMU-1660499; Synthesis of PIPs at the plasma membrane.
DR   Reactome; R-MMU-392451; G beta:gamma signalling through PI3Kgamma.
DR   Reactome; R-MMU-9027276; Erythropoietin activates Phosphoinositide-3-kinase (PI3K).
DR   BioGRID-ORCS; 320207; 6 hits in 73 CRISPR screens.
DR   ChiTaRS; Pik3r5; mouse.
DR   PRO; PR:Q5SW28; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q5SW28; protein.
DR   Bgee; ENSMUSG00000020901; Expressed in granulocyte and 80 other tissues.
DR   ExpressionAtlas; Q5SW28; baseline and differential.
DR   Genevisible; Q5SW28; MM.
DR   GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; ISO:MGI.
DR   GO; GO:0005944; C:phosphatidylinositol 3-kinase complex, class IB; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046935; F:1-phosphatidylinositol-3-kinase regulator activity; ISO:MGI.
DR   GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; ISS:UniProtKB.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
DR   GO; GO:0043406; P:positive regulation of MAP kinase activity; ISS:UniProtKB.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:UniProtKB.
DR   GO; GO:0043551; P:regulation of phosphatidylinositol 3-kinase activity; ISO:MGI.
DR   InterPro; IPR019522; PIK3R5/6.
DR   PANTHER; PTHR15593; PTHR15593; 1.
DR   Pfam; PF10486; PI3K_1B_p101; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cell membrane; Cytoplasm; Membrane; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..871
FT                   /note="Phosphoinositide 3-kinase regulatory subunit 5"
FT                   /id="PRO_0000058422"
FT   REGION          25..101
FT                   /note="Heterodimerization"
FT                   /evidence="ECO:0000250"
FT   REGION          381..413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          646..746
FT                   /note="Interaction with beta-gamma G protein dimers"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:O02696"
FT   MOD_RES         451
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         500
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WYR1"
FT   CONFLICT        65
FT                   /note="K -> E (in Ref. 2; BAE29119)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        269
FT                   /note="I -> T (in Ref. 2; BAC40901)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        369
FT                   /note="M -> V (in Ref. 1; AAN84787)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        642
FT                   /note="A -> V (in Ref. 1; AAN84787)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        647
FT                   /note="I -> T (in Ref. 1; AAN84787)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        651
FT                   /note="M -> V (in Ref. 1; AAN84787)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        796
FT                   /note="D -> G (in Ref. 2; BAE29119)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   871 AA;  96954 MW;  1D0F36A3D4042D62 CRC64;
     MQPAATTCTE DRIQHALERC LHGLSLGRRS APWSAGLCLN CWSLQELVSR DPGHFLILLE
     QILQKTQEVQ EKGTYDLLAP LALLFYSTVL CTPHFPPDSD LLLKAASTYH CFLTWPVPYC
     SICREMLTFI DAELKAPGIS YQRLVRAEQG LPVRSHRSST VTVLLLNPVE VQAEFLAVAD
     KLSTPGQSPH GTYTTLLLHA FQATFGAHCD LPKLHRKLQS KTIEELEDIF TETTEAQELA
     SGIGDVAEAR EWLRTKLQAV GEKAGFPGIL DTASPGKLHT IPIPVARCYT YSWNQDSFDI
     LQEVLLKEQE LLQPGILGDD EEEEEEDLEM DRHCAERDSL LSTSSLVSHD STLLLTSSQA
     SEPVLSRQML TTFVSGLSDG MDSGYVEDSE ENSEWPQKPG SQKRQGHRRP GQKFNRFYKL
     LKSTSQLVLR RDSRSLESSV DPTLPLRRAG SLCSPLDCPA QLPSRAQRSR SLPQAKLTTQ
     LPRWLLAPPS HHQRRRPFLS GDEDPKASTL RVVVFGSDRI SGKVARAYSK LRRLETSHPI
     LTRFFKLQFF YVPVKRSHGT SPSACPSSLS QASPLPADSL KYPSPTDLGM APWEDSTNDI
     SHYLGMLDPW YERNVLGLMH LPPEVLCQQS LKADSRPLEG SATQLPILAD MLLYYCRFAA
     RPVLLQVYQT ELTFVTGEKT TEIFIQSLEL GHSATTRAIK ASGRGRKRLG IDDDREAVPL
     TLQIIYSKGA ISGRSRWSNL EKVCTSVNLS KACQKPEELD SSMEALTLTL TEVVKRQNPK
     SKKGFNQIST SYIKVDKVQI IGSSSCPFAV CLDQDERKIL QSVVRCEVSP CYKPEKSSLP
     PERSFSQPAE TGSDLCSLLC LPIMTFSGAL P
 
 
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