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Protein

40S ribosomal protein S6-1

Gene

RPS6A

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 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.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S6-1
Gene namesi
Name:RPS6A
Ordered Locus Names:At4g31700
ORF Names:F28M20.110
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G31700.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • cytosol Source: TAIR
  • cytosolic ribosome Source: TAIR
  • cytosolic small ribosomal subunit Source: TAIR
  • membrane Source: TAIR
  • nucleolus Source: TAIR
  • plasma membrane Source: TAIR
  • plasmodesma Source: TAIR
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 25025040S ribosomal protein S6-1PRO_0000137329Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei237 – 2371PhosphoserineCombined sources
Modified residuei247 – 2471PhosphoserineCombined sources

Post-translational modificationi

Ribosomal protein S6 is the major substrate of protein kinases in eukaryote ribosomes.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO48549.
PRIDEiO48549.

PTM databases

iPTMnetiO48549.

Expressioni

Gene expression databases

ExpressionAtlasiO48549. baseline and differential.
GenevisibleiO48549. AT.

Interactioni

Protein-protein interaction databases

BioGridi14584. 8 interactions.
IntActiO48549. 2 interactions.
STRINGi3702.AT4G31700.1.

Structurei

3D structure databases

ProteinModelPortaliO48549.
SMRiO48549. Positions 1-241.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S6e family.Curated

Phylogenomic databases

eggNOGiKOG1646. Eukaryota.
COG2125. LUCA.
HOGENOMiHOG000190952.
InParanoidiO48549.
KOiK02991.
OMAiSARGCIV.
PhylomeDBiO48549.

Family and domain databases

InterProiIPR014401. Ribosomal_S6_euk.
IPR001377. Ribosomal_S6e.
[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]

Sequencei

Sequence statusi: Complete.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: O48549-1) [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
MKFNVANPTT GCQKKLEIDD DQKLRAFYDK RISQEVSGDA LGEEFKGYVF
60 70 80 90 100
KIKGGCDKQG FPMKQGVLTP GRVRLLLHRG TPCFRGHGRR TGERRRKSVR
110 120 130 140 150
GCIVSPDLSV LNLVIVKKGE NDLPGLTDTE KPRMRGPKRA SKIRKLFNLK
160 170 180 190 200
KEDDVRTYVN TYRRKFTNKK GKEVSKAPKI QRLVTPLTLQ RKRARIADKK
210 220 230 240 250
KKIAKANSDA ADYQKLLASR LKEQRDRRSE SLAKKRSRLS SAAAKPSVTA
Length:250
Mass (Da):28,367
Last modified:August 30, 2005 - v2
Checksum:i3956C5084E53A85A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti129 – 1335TEKPR → HESK in AAB88298 (Ref. 1) Curated
Sequence conflicti235 – 2351K → E in AAB88298 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF034217 mRNA. Translation: AAB88298.1.
AL031004 Genomic DNA. Translation: CAA19753.1.
AL161579 Genomic DNA. Translation: CAB79888.1.
CP002687 Genomic DNA. Translation: AEE85946.1.
AY050803 mRNA. Translation: AAK92738.1.
AY113983 mRNA. Translation: AAM45031.1.
BT000693 mRNA. Translation: AAN31838.1.
PIRiT05100.
RefSeqiNP_194898.1. NM_119319.4. [O48549-1]
UniGeneiAt.22261.

Genome annotation databases

EnsemblPlantsiAT4G31700.1; AT4G31700.1; AT4G31700. [O48549-1]
GeneIDi829298.
KEGGiath:AT4G31700.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF034217 mRNA. Translation: AAB88298.1.
AL031004 Genomic DNA. Translation: CAA19753.1.
AL161579 Genomic DNA. Translation: CAB79888.1.
CP002687 Genomic DNA. Translation: AEE85946.1.
AY050803 mRNA. Translation: AAK92738.1.
AY113983 mRNA. Translation: AAM45031.1.
BT000693 mRNA. Translation: AAN31838.1.
PIRiT05100.
RefSeqiNP_194898.1. NM_119319.4. [O48549-1]
UniGeneiAt.22261.

3D structure databases

ProteinModelPortaliO48549.
SMRiO48549. Positions 1-241.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi14584. 8 interactions.
IntActiO48549. 2 interactions.
STRINGi3702.AT4G31700.1.

PTM databases

iPTMnetiO48549.

Proteomic databases

PaxDbiO48549.
PRIDEiO48549.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G31700.1; AT4G31700.1; AT4G31700. [O48549-1]
GeneIDi829298.
KEGGiath:AT4G31700.

Organism-specific databases

TAIRiAT4G31700.

Phylogenomic databases

eggNOGiKOG1646. Eukaryota.
COG2125. LUCA.
HOGENOMiHOG000190952.
InParanoidiO48549.
KOiK02991.
OMAiSARGCIV.
PhylomeDBiO48549.

Enzyme and pathway databases

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

Miscellaneous databases

PROiO48549.

Gene expression databases

ExpressionAtlasiO48549. baseline and differential.
GenevisibleiO48549. AT.

Family and domain databases

InterProiIPR014401. Ribosomal_S6_euk.
IPR001377. Ribosomal_S6e.
[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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "S6 ribosomal protein of Arabidopsis thaliana."
    Bonham-Smith P.C.
    Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
  2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "The organization of cytoplasmic ribosomal protein genes in the Arabidopsis genome."
    Barakat A., Szick-Miranda K., Chang I.-F., Guyot R., Blanc G., Cooke R., Delseny M., Bailey-Serres J.
    Plant Physiol. 127:398-415(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY ORGANIZATION, NOMENCLATURE.
  6. "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
    Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
    J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: cv. Columbia.
  7. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
    Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
    Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237 AND SER-247, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRS61_ARATH
AccessioniPrimary (citable) accession number: O48549
Secondary accession number(s): O81777
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: August 30, 2005
Last modified: June 8, 2016
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  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.