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Protein

40S ribosomal protein S6

Gene

RpS6

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May play an important role in controlling cell growth and proliferation through the selective translation of particular classes of mRNA.

GO - Molecular functioni

  • structural constituent of ribosome Source: FlyBase

GO - Biological processi

  • centrosome duplication Source: FlyBase
  • immune response Source: FlyBase
  • mitotic spindle elongation Source: FlyBase
  • mitotic spindle organization Source: FlyBase
  • translation Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiR-DME-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-DME-166208. mTORC1-mediated signalling.
R-DME-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-DME-72649. Translation initiation complex formation.
R-DME-72689. Formation of a pool of free 40S subunits.
R-DME-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-DME-72702. Ribosomal scanning and start codon recognition.
R-DME-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-DME-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-DME-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S6
Gene namesi
Name:RpS6
Synonyms:hen, l(1)air8
ORF Names:CG10944
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0261592. RpS6.

Subcellular locationi

GO - Cellular componenti

  • cytosolic small ribosomal subunit Source: FlyBase
  • ribosome Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 24824840S ribosomal protein S6PRO_0000137323Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei233 – 2331Phosphoserine1 Publication
Modified residuei235 – 2351Phosphoserine1 Publication
Modified residuei239 – 2391Phosphoserine1 Publication
Modified residuei242 – 2421Phosphoserine1 Publication
Modified residuei244 – 2441Phosphoserine1 Publication
Modified residuei245 – 2451Phosphoserine1 Publication

Post-translational modificationi

Ribosomal protein S6 is the major substrate of protein kinases in eukaryote ribosomes. The phosphorylation is stimulated by growth factors, tumor promoting agents, and mitogens. It is dephosphorylated at growth arrest.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP29327.
PRIDEiP29327.

PTM databases

iPTMnetiP29327.

Expressioni

Gene expression databases

BgeeiP29327.
ExpressionAtlasiP29327. differential.
GenevisibleiP29327. DM.

Interactioni

Protein-protein interaction databases

BioGridi58174. 14 interactions.
IntActiP29327. 22 interactions.
MINTiMINT-277163.
STRINGi7227.FBpp0071087.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00AG1-248[»]
ProteinModelPortaliP29327.
SMRiP29327. Positions 1-227.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S6e family.Curated

Phylogenomic databases

eggNOGiKOG1646. Eukaryota.
COG2125. LUCA.
GeneTreeiENSGT00390000009819.
InParanoidiP29327.
KOiK02991.
OMAiDVVQPKR.
OrthoDBiEOG7Z0JXB.
PhylomeDBiP29327.

Family and domain databases

InterProiIPR014401. Ribosomal_S6_euk.
IPR001377. Ribosomal_S6e.
IPR018282. Ribosomal_S6e_CS.
[Graphical view]
PANTHERiPTHR11502. PTHR11502. 1 hit.
PfamiPF01092. Ribosomal_S6e. 1 hit.
[Graphical view]
PIRSFiPIRSF002129. Ribosom_S6_euk. 1 hit.
SMARTiSM01405. Ribosomal_S6e. 1 hit.
[Graphical view]
PROSITEiPS00578. RIBOSOMAL_S6E. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: P29327-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MKLNVSYPAT GCQKLFEVVD EHKLRVFYEK RMGQVVEADI LGDEWKGYQL
60 70 80 90 100
RIAGGNDKQG FPMKQGVLTH GRVRLLLKKG HSCYRPRRTG ERKRKSVRGC
110 120 130 140 150
IVDANMSVLA LVVLKKGEKD IPGLTDTTIP RRLGPKRASK IRKLYNLSKE
160 170 180 190 200
DDVRRFVVRR PLPAKDNKKA TSKAPKIQRL ITPVVLQRKH RRIALKKKRQ
210 220 230 240
IASKEASADY AKLLVQRKKE SKAKREEAKR RRSASIRESK SSVSSDKK
Length:248
Mass (Da):28,407
Last modified:December 1, 1992 - v1
Checksum:i4E781727C33B3B6D
GO
Isoform B (identifier: P29327-2) [UniParc]FASTAAdd to basket

Also known as: C

The sequence of this isoform differs from the canonical sequence as follows:
     73-200: VRLLLKKGHS...RRIALKKKRQ → LRLLKKIHSC...PKSSVFSGKK
     201-248: Missing.

Show »
Length:200
Mass (Da):23,072
Checksum:iCEFD9B4CE67B2971
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei73 – 200128VRLLL…KKKRQ → LRLLKKIHSCFHPRCNKVRK CKTVRKYTVEANVSALTLVV LKKNPSPCRLGPVRSSNISK IYYLCEEDDEVIPVKLQRRH QKKRQNATKEAIAEYVKLLV KRKKESKANRGRYVTIRKPK SSVFSGKK in isoform B. CuratedVSP_005727Add
BLAST
Alternative sequencei201 – 24848Missing in isoform B. CuratedVSP_005728Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L01658 Genomic DNA. Translation: AAC34306.1.
L07881 mRNA. Translation: AAA28871.1.
L02074 Genomic DNA. Translation: AAB05982.1.
L02074 Genomic DNA. Translation: AAB05983.1.
L02074 Genomic DNA. Translation: AAB05984.1.
L02075 mRNA. Translation: AAB05985.1.
AE014298 Genomic DNA. Translation: AAN09218.1.
PIRiS30194.
RefSeqiNP_511073.1. NM_078518.3. [P29327-1]
UniGeneiDm.2623.

Genome annotation databases

EnsemblMetazoaiFBtr0071135; FBpp0071087; FBgn0261592. [P29327-1]
GeneIDi31700.
KEGGidme:Dmel_CG10944.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L01658 Genomic DNA. Translation: AAC34306.1.
L07881 mRNA. Translation: AAA28871.1.
L02074 Genomic DNA. Translation: AAB05982.1.
L02074 Genomic DNA. Translation: AAB05983.1.
L02074 Genomic DNA. Translation: AAB05984.1.
L02075 mRNA. Translation: AAB05985.1.
AE014298 Genomic DNA. Translation: AAN09218.1.
PIRiS30194.
RefSeqiNP_511073.1. NM_078518.3. [P29327-1]
UniGeneiDm.2623.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00AG1-248[»]
ProteinModelPortaliP29327.
SMRiP29327. Positions 1-227.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi58174. 14 interactions.
IntActiP29327. 22 interactions.
MINTiMINT-277163.
STRINGi7227.FBpp0071087.

PTM databases

iPTMnetiP29327.

Proteomic databases

PaxDbiP29327.
PRIDEiP29327.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0071135; FBpp0071087; FBgn0261592. [P29327-1]
GeneIDi31700.
KEGGidme:Dmel_CG10944.

Organism-specific databases

CTDi6194.
FlyBaseiFBgn0261592. RpS6.

Phylogenomic databases

eggNOGiKOG1646. Eukaryota.
COG2125. LUCA.
GeneTreeiENSGT00390000009819.
InParanoidiP29327.
KOiK02991.
OMAiDVVQPKR.
OrthoDBiEOG7Z0JXB.
PhylomeDBiP29327.

Enzyme and pathway databases

ReactomeiR-DME-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-DME-166208. mTORC1-mediated signalling.
R-DME-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-DME-72649. Translation initiation complex formation.
R-DME-72689. Formation of a pool of free 40S subunits.
R-DME-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-DME-72702. Ribosomal scanning and start codon recognition.
R-DME-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-DME-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-DME-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

ChiTaRSiRpS6. fly.
GenomeRNAii31700.
NextBioi774900.
PROiP29327.

Gene expression databases

BgeeiP29327.
ExpressionAtlasiP29327. differential.
GenevisibleiP29327. DM.

Family and domain databases

InterProiIPR014401. Ribosomal_S6_euk.
IPR001377. Ribosomal_S6e.
IPR018282. Ribosomal_S6e_CS.
[Graphical view]
PANTHERiPTHR11502. PTHR11502. 1 hit.
PfamiPF01092. Ribosomal_S6e. 1 hit.
[Graphical view]
PIRSFiPIRSF002129. Ribosom_S6_euk. 1 hit.
SMARTiSM01405. Ribosomal_S6e. 1 hit.
[Graphical view]
PROSITEiPS00578. RIBOSOMAL_S6E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Drosophila homolog of the human S6 ribosomal protein is required for tumor suppression in the hematopoietic system."
    Watson K.L., Konrad K.D., Woods D.F., Bryant P.J.
    Proc. Natl. Acad. Sci. U.S.A. 89:11302-11306(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of a cloned cDNA encoding ribosomal protein S6 from Drosophila melanogaster."
    Spencer T.A., Mackie G.A.
    Biochim. Biophys. Acta 1172:332-334(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The Drosophila ribosomal protein S6 gene includes a 3' triplication that arose by unequal crossing-over."
    Stewart M.J., Denell R.
    Mol. Biol. Evol. 10:1041-1047(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ALTERNATIVE SPLICING.
  4. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  5. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  6. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233; SER-235; SER-239; SER-242; SER-244 AND SER-245, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  7. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (6.0 ANGSTROMS) OF THE 80S RIBOSOME.

Entry informationi

Entry nameiRS6_DROME
AccessioniPrimary (citable) accession number: P29327
Secondary accession number(s): Q94993, Q9W3N4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: May 11, 2016
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Ribosomal proteins
    Ribosomal proteins families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.