Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

40S ribosomal protein S6

Gene

RPS6

Organism
Homo sapiens (Human)
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

  • poly(A) RNA binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • structural constituent of ribosome Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciZFISH:ENSG00000137154-MONOMER.
ReactomeiR-HSA-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-HSA-156902. Peptide chain elongation.
R-HSA-166208. mTORC1-mediated signalling.
R-HSA-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-HSA-192823. Viral mRNA Translation.
R-HSA-2408557. Selenocysteine synthesis.
R-HSA-6790901. rRNA modification in the nucleus and cytosol.
R-HSA-6791226. Major pathway of rRNA processing in the nucleolus and cytosol.
R-HSA-72649. Translation initiation complex formation.
R-HSA-72689. Formation of a pool of free 40S subunits.
R-HSA-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-HSA-72702. Ribosomal scanning and start codon recognition.
R-HSA-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-HSA-72764. Eukaryotic Translation Termination.
R-HSA-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-HSA-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
SignaLinkiP62753.
SIGNORiP62753.

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S6
Alternative name(s):
Phosphoprotein NP33
Gene namesi
Name:RPS6
ORF Names:OK/SW-cl.2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:10429. RPS6.

Subcellular locationi

GO - Cellular componenti

  • cell body Source: ParkinsonsUK-UCL
  • cytoplasm Source: HPA
  • cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
  • cytosol Source: Reactome
  • cytosolic small ribosomal subunit Source: UniProtKB
  • dendrite Source: ParkinsonsUK-UCL
  • intracellular ribonucleoprotein complex Source: MGI
  • membrane Source: UniProtKB
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: Ensembl
  • polysome Source: Ensembl
  • small ribosomal subunit Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi235 – 236SS → AA: Abolishes phosphorylation by PASK. 1 Publication2

Organism-specific databases

DisGeNETi6194.
OpenTargetsiENSG00000137154.
PharmGKBiPA34844.

Chemistry databases

ChEMBLiCHEMBL3351215.

Polymorphism and mutation databases

BioMutaiRPS6.
DMDMi51338632.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001373121 – 24940S ribosomal protein S6Add BLAST249

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei148PhosphoserineCombined sources1
Modified residuei211N6-acetyllysineCombined sources1
Modified residuei235Phosphoserine; by RPS6KA1, RPS6KA3, DAPK1 and PASKCombined sources3 Publications1
Modified residuei236Phosphoserine; by RPS6KA1, RPS6KA3, DAPK1 and PASKCombined sources3 Publications1
Modified residuei240PhosphoserineCombined sources1
Modified residuei242PhosphoserineCombined sources1
Modified residuei244PhosphoserineCombined sources1
Modified residuei247PhosphoserineCombined sources1

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.3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP62753.
MaxQBiP62753.
PaxDbiP62753.
PeptideAtlasiP62753.
PRIDEiP62753.
TopDownProteomicsiP62753.

PTM databases

iPTMnetiP62753.
PhosphoSitePlusiP62753.
SwissPalmiP62753.

Expressioni

Gene expression databases

BgeeiENSG00000137154.
CleanExiHS_RPS6.
ExpressionAtlasiP62753. baseline and differential.
GenevisibleiP62753. HS.

Organism-specific databases

HPAiCAB004027.
HPA031153.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
NCBP1Q091613EBI-356625,EBI-464743
PASKQ96RG23EBI-356625,EBI-1042651

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi112108. 208 interactors.
DIPiDIP-31507N.
IntActiP62753. 58 interactors.
MINTiMINT-1162101.
STRINGi9606.ENSP00000369757.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4UG0electron microscopy-SG1-249[»]
4V6Xelectron microscopy5.00AG1-249[»]
5A2Qelectron microscopy3.90G1-249[»]
5AJ0electron microscopy3.50BG1-249[»]
5FLXelectron microscopy3.90G1-249[»]
ProteinModelPortaliP62753.
SMRiP62753.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S6e family.Curated

Phylogenomic databases

eggNOGiKOG1646. Eukaryota.
COG2125. LUCA.
GeneTreeiENSGT00390000009819.
HOGENOMiHOG000190952.
HOVERGENiHBG011441.
InParanoidiP62753.
KOiK02991.
OMAiEGKKERF.
OrthoDBiEOG091G089B.
PhylomeDBiP62753.
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.

P62753-1 [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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti23K → T in AAA60288 (PubMed:2840355).Curated1
Sequence conflicti144L → R in AAA60288 (PubMed:2840355).Curated1
Sequence conflicti155 – 156QY → EC in AAA60287 (PubMed:3279029).Curated2
Sequence conflicti168K → R in AAA60287 (PubMed:3279029).Curated1
Sequence conflicti196K → Q in AAA60288 (PubMed:2840355).Curated1
Sequence conflicti219E → Q in AAA60287 (PubMed:3279029).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_025314221K → R.1 PublicationCorresponds to variant rs17852447dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20020 mRNA. Translation: AAA60288.1.
J03537 mRNA. Translation: AAA60287.1.
X67309 Genomic DNA. Translation: CAA47719.1.
M77232 Genomic DNA. Translation: AAA60289.1.
AB062123 mRNA. Translation: BAB93455.1.
BC000524 mRNA. Translation: AAH00524.1.
BC009427 mRNA. Translation: AAH09427.2.
BC027620 mRNA. Translation: AAH27620.1.
BC071907 mRNA. Translation: AAH71907.1.
BC071908 mRNA. Translation: AAH71908.1.
BC094826 mRNA. Translation: AAH94826.1.
CCDSiCCDS6492.1.
PIRiJC1394. R3HU6.
RefSeqiNP_001001.2. NM_001010.2.
UniGeneiHs.408073.

Genome annotation databases

EnsembliENST00000380394; ENSP00000369757; ENSG00000137154.
GeneIDi6194.
KEGGihsa:6194.
UCSCiuc003znv.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20020 mRNA. Translation: AAA60288.1.
J03537 mRNA. Translation: AAA60287.1.
X67309 Genomic DNA. Translation: CAA47719.1.
M77232 Genomic DNA. Translation: AAA60289.1.
AB062123 mRNA. Translation: BAB93455.1.
BC000524 mRNA. Translation: AAH00524.1.
BC009427 mRNA. Translation: AAH09427.2.
BC027620 mRNA. Translation: AAH27620.1.
BC071907 mRNA. Translation: AAH71907.1.
BC071908 mRNA. Translation: AAH71908.1.
BC094826 mRNA. Translation: AAH94826.1.
CCDSiCCDS6492.1.
PIRiJC1394. R3HU6.
RefSeqiNP_001001.2. NM_001010.2.
UniGeneiHs.408073.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4UG0electron microscopy-SG1-249[»]
4V6Xelectron microscopy5.00AG1-249[»]
5A2Qelectron microscopy3.90G1-249[»]
5AJ0electron microscopy3.50BG1-249[»]
5FLXelectron microscopy3.90G1-249[»]
ProteinModelPortaliP62753.
SMRiP62753.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112108. 208 interactors.
DIPiDIP-31507N.
IntActiP62753. 58 interactors.
MINTiMINT-1162101.
STRINGi9606.ENSP00000369757.

Chemistry databases

ChEMBLiCHEMBL3351215.

PTM databases

iPTMnetiP62753.
PhosphoSitePlusiP62753.
SwissPalmiP62753.

Polymorphism and mutation databases

BioMutaiRPS6.
DMDMi51338632.

Proteomic databases

EPDiP62753.
MaxQBiP62753.
PaxDbiP62753.
PeptideAtlasiP62753.
PRIDEiP62753.
TopDownProteomicsiP62753.

Protocols and materials databases

DNASUi6194.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000380394; ENSP00000369757; ENSG00000137154.
GeneIDi6194.
KEGGihsa:6194.
UCSCiuc003znv.2. human.

Organism-specific databases

CTDi6194.
DisGeNETi6194.
GeneCardsiRPS6.
HGNCiHGNC:10429. RPS6.
HPAiCAB004027.
HPA031153.
MIMi180460. gene.
neXtProtiNX_P62753.
OpenTargetsiENSG00000137154.
PharmGKBiPA34844.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1646. Eukaryota.
COG2125. LUCA.
GeneTreeiENSGT00390000009819.
HOGENOMiHOG000190952.
HOVERGENiHBG011441.
InParanoidiP62753.
KOiK02991.
OMAiEGKKERF.
OrthoDBiEOG091G089B.
PhylomeDBiP62753.
TreeFamiTF300035.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000137154-MONOMER.
ReactomeiR-HSA-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-HSA-156902. Peptide chain elongation.
R-HSA-166208. mTORC1-mediated signalling.
R-HSA-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-HSA-192823. Viral mRNA Translation.
R-HSA-2408557. Selenocysteine synthesis.
R-HSA-6790901. rRNA modification in the nucleus and cytosol.
R-HSA-6791226. Major pathway of rRNA processing in the nucleolus and cytosol.
R-HSA-72649. Translation initiation complex formation.
R-HSA-72689. Formation of a pool of free 40S subunits.
R-HSA-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-HSA-72702. Ribosomal scanning and start codon recognition.
R-HSA-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-HSA-72764. Eukaryotic Translation Termination.
R-HSA-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-HSA-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
SignaLinkiP62753.
SIGNORiP62753.

Miscellaneous databases

ChiTaRSiRPS6. human.
GenomeRNAii6194.
PROiP62753.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000137154.
CleanExiHS_RPS6.
ExpressionAtlasiP62753. baseline and differential.
GenevisibleiP62753. HS.

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...

Entry informationi

Entry nameiRS6_HUMAN
AccessioniPrimary (citable) accession number: P62753
Secondary accession number(s): P08227
, P10660, Q4VBY7, Q8N6Z7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: November 2, 2016
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Ribosomal proteins
    Ribosomal proteins families and list of entries
  7. 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.