RS6_DROME
ID RS6_DROME Reviewed; 248 AA.
AC P29327; Q94993; Q9W3N4;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=40S ribosomal protein S6;
GN Name=RpS6; Synonyms=hen, l(1)air8; ORFNames=CG10944;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1454811; DOI=10.1073/pnas.89.23.11302;
RA Watson K.L., Konrad K.D., Woods D.F., Bryant P.J.;
RT "Drosophila homolog of the human S6 ribosomal protein is required for tumor
RT suppression in the hematopoietic system.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:11302-11306(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8448211; DOI=10.1016/0167-4781(93)90225-3;
RA Spencer T.A., Mackie G.A.;
RT "The nucleotide sequence of a cloned cDNA encoding ribosomal protein S6
RT from Drosophila melanogaster.";
RL Biochim. Biophys. Acta 1172:332-334(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND ALTERNATIVE SPLICING.
RX PubMed=8412647; DOI=10.1093/oxfordjournals.molbev.a040053;
RA Stewart M.J., Denell R.;
RT "The Drosophila ribosomal protein S6 gene includes a 3' triplication that
RT arose by unequal crossing-over.";
RL Mol. Biol. Evol. 10:1041-1047(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233; SER-235; SER-239;
RP SER-242; SER-244 AND SER-245, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [7]
RP STRUCTURE BY ELECTRON MICROSCOPY (6.0 ANGSTROMS) OF THE 80S RIBOSOME.
RX PubMed=23636399; DOI=10.1038/nature12104;
RA Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
RA Wilson D.N., Beckmann R.;
RT "Structures of the human and Drosophila 80S ribosome.";
RL Nature 497:80-85(2013).
CC -!- FUNCTION: Component of the 40S small ribosomal subunit (By similarity).
CC Plays an important role in controlling cell growth and proliferation
CC through the selective translation of particular classes of mRNA (By
CC similarity). {ECO:0000250|UniProtKB:P62753}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=P29327-1; Sequence=Displayed;
CC Name=B; Synonyms=C;
CC IsoId=P29327-2; Sequence=VSP_005727, VSP_005728;
CC -!- PTM: Ribosomal protein S6 is the major substrate of protein kinases in
CC eukaryote ribosomes. The phosphorylation is stimulated by growth
CC factors, tumor promoting agents, and mitogens. It is dephosphorylated
CC at growth arrest. {ECO:0000250|UniProtKB:P62753}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS6 family.
CC {ECO:0000305}.
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DR EMBL; L01658; AAC34306.1; -; Genomic_DNA.
DR EMBL; L07881; AAA28871.1; -; mRNA.
DR EMBL; L02074; AAB05982.1; -; Genomic_DNA.
DR EMBL; L02074; AAB05983.1; -; Genomic_DNA.
DR EMBL; L02074; AAB05984.1; -; Genomic_DNA.
DR EMBL; L02075; AAB05985.1; -; mRNA.
DR EMBL; AE014298; AAN09218.1; -; Genomic_DNA.
DR PIR; S30194; S30194.
DR RefSeq; NP_511073.1; NM_078518.3. [P29327-1]
DR PDB; 4V6W; EM; 6.00 A; AG=1-248.
DR PDB; 6XU6; EM; 3.50 A; AG=1-231.
DR PDB; 6XU7; EM; 4.90 A; AG=1-231.
DR PDB; 6XU8; EM; 3.00 A; AG=1-231.
DR PDBsum; 4V6W; -.
DR PDBsum; 6XU6; -.
DR PDBsum; 6XU7; -.
DR PDBsum; 6XU8; -.
DR AlphaFoldDB; P29327; -.
DR SMR; P29327; -.
DR BioGRID; 58174; 113.
DR IntAct; P29327; 22.
DR MINT; P29327; -.
DR STRING; 7227.FBpp0071087; -.
DR iPTMnet; P29327; -.
DR PaxDb; P29327; -.
DR PeptideAtlas; P29327; -.
DR PRIDE; P29327; -.
DR DNASU; 31700; -.
DR EnsemblMetazoa; FBtr0071135; FBpp0071087; FBgn0261592. [P29327-1]
DR GeneID; 31700; -.
DR KEGG; dme:Dmel_CG10944; -.
DR CTD; 6194; -.
DR FlyBase; FBgn0261592; RpS6.
DR VEuPathDB; VectorBase:FBgn0261592; -.
DR eggNOG; KOG1646; Eukaryota.
DR GeneTree; ENSGT00390000009819; -.
DR HOGENOM; CLU_046346_0_1_1; -.
DR InParanoid; P29327; -.
DR OMA; FYEKRMS; -.
DR PhylomeDB; P29327; -.
DR Reactome; R-DME-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-DME-166208; mTORC1-mediated signalling.
DR Reactome; R-DME-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-DME-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-DME-72649; Translation initiation complex formation.
DR Reactome; R-DME-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-DME-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-DME-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-DME-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-DME-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-DME-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; P29327; -.
DR BioGRID-ORCS; 31700; 1 hit in 1 CRISPR screen.
DR ChiTaRS; RpS6; fly.
DR GenomeRNAi; 31700; -.
DR PRO; PR:P29327; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0261592; Expressed in seminal fluid secreting gland and 12 other tissues.
DR ExpressionAtlas; P29327; baseline and differential.
DR Genevisible; P29327; DM.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; TAS:FlyBase.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0002181; P:cytoplasmic translation; TAS:FlyBase.
DR InterPro; IPR014401; Ribosomal_S6_euk.
DR InterPro; IPR001377; Ribosomal_S6e.
DR InterPro; IPR018282; Ribosomal_S6e_CS.
DR PANTHER; PTHR11502; PTHR11502; 1.
DR Pfam; PF01092; Ribosomal_S6e; 1.
DR PIRSF; PIRSF002129; Ribosom_S6_euk; 1.
DR SMART; SM01405; Ribosomal_S6e; 1.
DR PROSITE; PS00578; RIBOSOMAL_S6E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..248
FT /note="40S ribosomal protein S6"
FT /id="PRO_0000137323"
FT REGION 215..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 73..200
FT /note="VRLLLKKGHSCYRPRRTGERKRKSVRGCIVDANMSVLALVVLKKGEKDIPGL
FT TDTTIPRRLGPKRASKIRKLYNLSKEDDVRRFVVRRPLPAKDNKKATSKAPKIQRLITP
FT VVLQRKHRRIALKKKRQ -> LRLLKKIHSCFHPRCNKVRKCKTVRKYTVEANVSALTL
FT VVLKKNPSPCRLGPVRSSNISKIYYLCEEDDEVIPVKLQRRHQKKRQNATKEAIAEYVK
FT LLVKRKKESKANRGRYVTIRKPKSSVFSGKK (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_005727"
FT VAR_SEQ 201..248
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_005728"
SQ SEQUENCE 248 AA; 28407 MW; 4E781727C33B3B6D CRC64;
MKLNVSYPAT GCQKLFEVVD EHKLRVFYEK RMGQVVEADI LGDEWKGYQL RIAGGNDKQG
FPMKQGVLTH GRVRLLLKKG HSCYRPRRTG ERKRKSVRGC IVDANMSVLA LVVLKKGEKD
IPGLTDTTIP RRLGPKRASK IRKLYNLSKE DDVRRFVVRR PLPAKDNKKA TSKAPKIQRL
ITPVVLQRKH RRIALKKKRQ IASKEASADY AKLLVQRKKE SKAKREEAKR RRSASIRESK
SSVSSDKK
