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Protein

40S ribosomal protein S6

Gene

Rps6

Organism
Mus musculus (Mouse)
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

GO - Biological processi

  • activation-induced cell death of T cells Source: MGI
  • erythrocyte development Source: MGI
  • G1/S transition of mitotic cell cycle Source: MGI
  • gastrulation Source: MGI
  • glucose homeostasis Source: UniProtKB
  • mitotic cell cycle checkpoint Source: MGI
  • mitotic nuclear division Source: MGI
  • negative regulation of apoptotic process Source: MGI
  • oogenesis stage Source: MGI
  • placenta development Source: MGI
  • positive regulation of apoptotic process Source: MGI
  • ribosomal small subunit biogenesis Source: MGI
  • rRNA processing Source: MGI
  • T cell differentiation in thymus Source: MGI
  • T cell proliferation involved in immune response Source: MGI
  • TOR signaling Source: MGI
  • translation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiR-MMU-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-MMU-166208. mTORC1-mediated signalling.
R-MMU-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-MMU-6791226. Major pathway of rRNA processing in the nucleolus.
R-MMU-72649. Translation initiation complex formation.
R-MMU-72689. Formation of a pool of free 40S subunits.
R-MMU-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-MMU-72702. Ribosomal scanning and start codon recognition.
R-MMU-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-MMU-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-MMU-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S6
Alternative name(s):
Phosphoprotein NP33
Gene namesi
Name:Rps6
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:98159. Rps6.

Subcellular locationi

GO - Cellular componenti

  • cell body Source: MGI
  • cytoplasm Source: MGI
  • cytoplasmic ribonucleoprotein granule Source: MGI
  • cytosolic small ribosomal subunit Source: MGI
  • dendrite Source: MGI
  • intracellular ribonucleoprotein complex Source: MGI
  • membrane Source: MGI
  • nucleolus Source: MGI
  • nucleus Source: MGI
  • perinuclear region of cytoplasm Source: MGI
  • polysome Source: MGI
  • ribosome Source: MGI
  • small ribosomal subunit Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 24924940S ribosomal protein S6PRO_0000137313Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei148 – 1481PhosphoserineBy similarity
Modified residuei211 – 2111N6-acetyllysineCombined sources
Modified residuei235 – 2351Phosphoserine; by RPS6KA1, RPS6KA3, DAPK1 and PASKBy similarity
Modified residuei236 – 2361Phosphoserine; by RPS6KA1, RPS6KA3, DAPK1 and PASKBy similarity
Modified residuei240 – 2401Phosphoserine2 Publications
Modified residuei242 – 2421PhosphoserineBy similarity
Modified residuei244 – 2441PhosphoserineCombined sources2 Publications
Modified residuei247 – 2471Phosphoserine1 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. Phosphorylated at Ser-235 and Ser-236 by RPS6KA1 and RPS6KA3; phosphorylation at these sites facilitates the assembly of the preinitiation complex.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP62754.
PaxDbiP62754.
PeptideAtlasiP62754.
PRIDEiP62754.

PTM databases

iPTMnetiP62754.
PhosphoSiteiP62754.
SwissPalmiP62754.

Expressioni

Gene expression databases

BgeeiP62754.
CleanExiMM_RPS6.
ExpressionAtlasiP62754. baseline and differential.
GenevisibleiP62754. MM.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

BioGridi203013. 6 interactions.
DIPiDIP-42772N.
IntActiP62754. 12 interactions.
MINTiMINT-1865522.
STRINGi10090.ENSMUSP00000099878.

Structurei

3D structure databases

ProteinModelPortaliP62754.
SMRiP62754. Positions 1-230.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S6e family.Curated

Phylogenomic databases

eggNOGiKOG1646. Eukaryota.
COG2125. LUCA.
HOGENOMiHOG000190952.
HOVERGENiHBG011441.
InParanoidiP62754.
KOiK02991.
OMAiEGKKERF.
OrthoDBiEOG7Z0JXB.
PhylomeDBiP62754.
TreeFamiTF300035.

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]

Sequencei

Sequence statusi: Complete.

P62754-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLNISFPAT GCQKLIEVDD ERKLRTFYEK RMATEVAADA LGEEWKGYVV
60 70 80 90 100
RISGGNDKQG FPMKQGVLTH GRVRLLLSKG HSCYRPRRTG ERKRKSVRGC
110 120 130 140 150
IVDANLSVLN LVIVKKGEKD IPGLTDTTVP RRLGPKRASR IRKLFNLSKE
160 170 180 190 200
DDVRQYVVRK PLNKEGKKPR TKAPKIQRLV TPRVLQHKRR RIALKKQRTK
210 220 230 240
KNKEEAAEYA KLLAKRMKEA KEKRQEQIAK RRRLSSLRAS TSKSESSQK
Length:249
Mass (Da):28,681
Last modified:August 1, 1988 - v1
Checksum:iA61E435884E636AE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00348 mRNA. Translation: CAA68430.1.
Z54209 Genomic DNA. Translation: CAA90936.1.
AK012284 mRNA. Translation: BAB28142.1.
AK012828 mRNA. Translation: BAB28498.1.
AK013333 mRNA. Translation: BAB28796.1.
AK050609 mRNA. Translation: BAC34340.1.
BC010604 mRNA. Translation: AAH10604.1.
CCDSiCCDS18310.1.
PIRiS00660. R3MS6.
RefSeqiNP_033122.1. NM_009096.3.
XP_011238179.1. XM_011239877.1.
UniGeneiMm.379007.
Mm.425090.

Genome annotation databases

EnsembliENSMUST00000102814; ENSMUSP00000099878; ENSMUSG00000028495.
GeneIDi105244208.
20104.
KEGGimmu:105244208.
mmu:20104.
UCSCiuc008tme.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00348 mRNA. Translation: CAA68430.1.
Z54209 Genomic DNA. Translation: CAA90936.1.
AK012284 mRNA. Translation: BAB28142.1.
AK012828 mRNA. Translation: BAB28498.1.
AK013333 mRNA. Translation: BAB28796.1.
AK050609 mRNA. Translation: BAC34340.1.
BC010604 mRNA. Translation: AAH10604.1.
CCDSiCCDS18310.1.
PIRiS00660. R3MS6.
RefSeqiNP_033122.1. NM_009096.3.
XP_011238179.1. XM_011239877.1.
UniGeneiMm.379007.
Mm.425090.

3D structure databases

ProteinModelPortaliP62754.
SMRiP62754. Positions 1-230.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203013. 6 interactions.
DIPiDIP-42772N.
IntActiP62754. 12 interactions.
MINTiMINT-1865522.
STRINGi10090.ENSMUSP00000099878.

PTM databases

iPTMnetiP62754.
PhosphoSiteiP62754.
SwissPalmiP62754.

Proteomic databases

EPDiP62754.
PaxDbiP62754.
PeptideAtlasiP62754.
PRIDEiP62754.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000102814; ENSMUSP00000099878; ENSMUSG00000028495.
GeneIDi105244208.
20104.
KEGGimmu:105244208.
mmu:20104.
UCSCiuc008tme.1. mouse.

Organism-specific databases

CTDi6194.
MGIiMGI:98159. Rps6.

Phylogenomic databases

eggNOGiKOG1646. Eukaryota.
COG2125. LUCA.
HOGENOMiHOG000190952.
HOVERGENiHBG011441.
InParanoidiP62754.
KOiK02991.
OMAiEGKKERF.
OrthoDBiEOG7Z0JXB.
PhylomeDBiP62754.
TreeFamiTF300035.

Enzyme and pathway databases

ReactomeiR-MMU-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-MMU-166208. mTORC1-mediated signalling.
R-MMU-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-MMU-6791226. Major pathway of rRNA processing in the nucleolus.
R-MMU-72649. Translation initiation complex formation.
R-MMU-72689. Formation of a pool of free 40S subunits.
R-MMU-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-MMU-72702. Ribosomal scanning and start codon recognition.
R-MMU-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-MMU-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-MMU-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

PROiP62754.
SOURCEiSearch...

Gene expression databases

BgeeiP62754.
CleanExiMM_RPS6.
ExpressionAtlasiP62754. baseline and differential.
GenevisibleiP62754. MM.

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. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Structural characterization of the mouse ribosomal protein S6-encoding gene."
    Pata I., Metspalu A.
    Gene 175:241-245(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/Sv.
    Tissue: Liver.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Thymus.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Mammary tumor.
  5. "Mitogen-activated 70K S6 kinase. Identification of in vitro 40 S ribosomal S6 phosphorylation sites."
    Ferrari S., Bandi H.R., Hofsteenge J., Bussian B.M., Thomas G.
    J. Biol. Chem. 266:22770-22775(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, PHOSPHORYLATION AT SER-235; SER-236; SER-240 AND SER-244.
  6. "Identification of 40 S ribosomal protein S6 phosphorylation sites in Swiss mouse 3T3 fibroblasts stimulated with serum."
    Bandi H.R., Ferrari S., Krieg J., Meyer H.E., Thomas G.
    J. Biol. Chem. 268:4530-4533(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, PHOSPHORYLATION AT SER-235; SER-240; SER-244 AND SER-247.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  8. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-211, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiRS6_MOUSE
AccessioniPrimary (citable) accession number: P62754
Secondary accession number(s): P08227, P10660
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: July 6, 2016
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Ribosomal proteins
    Ribosomal proteins families and list of entries
  3. 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.