Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P62753 (RS6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
40S ribosomal protein S6
Alternative name(s):
Phosphoprotein NP33
Gene names
Name:RPS6
ORF Names:OK/SW-cl.2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length249 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Post-translational modification

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. Ref.9 Ref.12 Ref.16

Sequence similarities

Belongs to the ribosomal protein S6e family.

Ontologies

Keywords
   Coding sequence diversityPolymorphism
   Molecular functionRibonucleoprotein
Ribosomal protein
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

SRP-dependent cotranslational protein targeting to membrane

Traceable author statement. Source: Reactome

TOR signaling

Inferred from direct assay PubMed 16428328. Source: UniProtKB

cellular protein metabolic process

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

glucose homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

insulin receptor signaling pathway

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Traceable author statement. Source: Reactome

positive regulation of apoptotic process

Inferred from direct assay PubMed 18362888. Source: UniProtKB

rRNA processing

Inferred from mutant phenotype PubMed 18697920. Source: UniProtKB

ribosomal small subunit biogenesis

Inferred from mutant phenotype PubMed 18697920. Source: UniProtKB

translation

Inferred by curator PubMed 15883184Ref.7. Source: UniProtKB

translational elongation

Traceable author statement. Source: Reactome

translational initiation

Traceable author statement. Source: Reactome

translational termination

Traceable author statement. Source: Reactome

viral life cycle

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

viral transcription

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

cytosolic small ribosomal subunit

Inferred from direct assay PubMed 15883184Ref.7. Source: UniProtKB

nucleolus

Inferred from direct assay PubMed 8590812. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 2334893. Source: UniProtKB

ribonucleoprotein complex

Inferred from direct assay PubMed 18809582. Source: MGI

small ribosomal subunit

Inferred from direct assay PubMed 15590835. Source: UniProtKB

   Molecular_functionpoly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 16314389. Source: UniProtKB

protein kinase binding

Inferred from physical interaction Ref.16. Source: UniProtKB

structural constituent of ribosome

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 24924940S ribosomal protein S6
PRO_0000137312

Amino acid modifications

Modified residue2111N6-acetyllysine Ref.13
Modified residue2351Phosphoserine; by RPS6KA1, RPS6KA3, DAPK1 and PASK Ref.9 Ref.11 Ref.12 Ref.16
Modified residue2361Phosphoserine; by RPS6KA1, RPS6KA3, DAPK1 and PASK Ref.9 Ref.11 Ref.12 Ref.16 Ref.17
Modified residue2401Phosphoserine Ref.11 Ref.14 Ref.17
Modified residue2421Phosphoserine Ref.17
Modified residue2441Phosphoserine Ref.11
Modified residue2471Phosphoserine Ref.11

Natural variations

Natural variant2211K → R. Ref.6
Corresponds to variant rs17852447 [ dbSNP | Ensembl ].
VAR_025314

Experimental info

Mutagenesis235 – 2362SS → AA: Abolishes phosphorylation by PASK. Ref.16
Sequence conflict231K → T in AAA60288. Ref.1
Sequence conflict1441L → R in AAA60288. Ref.1
Sequence conflict155 – 1562QY → EC in AAA60287. Ref.2
Sequence conflict1681K → R in AAA60287. Ref.2
Sequence conflict1961K → Q in AAA60288. Ref.1
Sequence conflict2191E → Q in AAA60287. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P62753 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: A61E435884E636AE

FASTA24928,681
        10         20         30         40         50         60 
MKLNISFPAT GCQKLIEVDD ERKLRTFYEK RMATEVAADA LGEEWKGYVV RISGGNDKQG 

        70         80         90        100        110        120 
FPMKQGVLTH GRVRLLLSKG HSCYRPRRTG ERKRKSVRGC IVDANLSVLN LVIVKKGEKD 

       130        140        150        160        170        180 
IPGLTDTTVP RRLGPKRASR IRKLFNLSKE DDVRQYVVRK PLNKEGKKPR TKAPKIQRLV 

       190        200        210        220        230        240 
TPRVLQHKRR RIALKKQRTK KNKEEAAEYA KLLAKRMKEA KEKRQEQIAK RRRLSSLRAS 


TSKSESSQK 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of cloned cDNAs that code for human ribosomal protein S6."
Lott J.B., Mackie G.A.
Gene 65:31-39(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The primary structure of the human ribosomal protein S6 derived from a cloned cDNA."
Heinze H., Arnold H.H., Fischer D., Kruppa J.
J. Biol. Chem. 263:4139-4144(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The organization of the intron-containing human S6 ribosomal protein (rpS6) gene and determination of its location at chromosome 9p21."
Antoine M., Fried M.
Hum. Mol. Genet. 1:565-570(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"The human ribosomal protein S6 gene: isolation, primary structure and location in chromosome 9."
Pata I., Hoth S., Kruppa J., Metspalu A.
Gene 121:387-392(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
Shichijo S., Itoh K.
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Colon adenocarcinoma.
[6]"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], VARIANT ARG-221.
Tissue: Colon, Muscle, Pancreas, Skin and Testis.
[7]"Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry."
Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K., Egorov T.A., Thiede B., Wittmann-Liebold B., Otto A.
Eur. J. Biochem. 239:144-149(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-15.
Tissue: Placenta.
[8]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"RAS/ERK signaling promotes site-specific ribosomal protein S6 phosphorylation via RSK and stimulates cap-dependent translation."
Roux P.P., Shahbazian D., Vu H., Holz M.K., Cohen M.S., Taunton J., Sonenberg N., Blenis J.
J. Biol. Chem. 282:14056-14064(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-235 AND SER-236.
[10]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235; SER-236; SER-240; SER-244 AND SER-247, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Peptide combinatorial libraries identify TSC2 as a death-associated protein kinase (DAPK) death domain-binding protein and reveal a stimulatory role for DAPK in mTORC1 signaling."
Stevens C., Lin Y., Harrison B., Burch L., Ridgway R.A., Sansom O., Hupp T.
J. Biol. Chem. 284:334-344(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-235 AND SER-236 BY DAPK1.
[13]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-211, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Substrate preference and phosphatidylinositol monophosphate inhibition of the catalytic domain of the Per-Arnt-Sim domain kinase PASKIN."
Schlafli P., Troger J., Eckhardt K., Borter E., Spielmann P., Wenger R.H.
FEBS J. 278:1757-1768(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-235 AND SER-236, MUTAGENESIS OF 235-SER-SER-236.
[17]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236; SER-240 AND SER-242, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Structures of the human and Drosophila 80S ribosome."
Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M., Wilson D.N., Beckmann R.
Nature 497:80-85(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS6492.1.
PIRR3HU6. JC1394.
RefSeqNP_001001.2. NM_001010.2.
UniGeneHs.408073.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Aelectron microscopy5.00G1-249[»]
ProteinModelPortalP62753.
SMRP62753. Positions 1-237.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112108. 186 interactions.
DIPDIP-31507N.
IntActP62753. 40 interactions.
MINTMINT-1162101.
STRING9606.ENSP00000369757.

PTM databases

PhosphoSiteP62753.

Polymorphism databases

DMDM51338632.

Proteomic databases

MaxQBP62753.
PaxDbP62753.
PRIDEP62753.

Protocols and materials databases

DNASU6194.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000380394; ENSP00000369757; ENSG00000137154.
GeneID6194.
KEGGhsa:6194.
UCSCuc003znv.1. human.

Organism-specific databases

CTD6194.
GeneCardsGC09M019366.
HGNCHGNC:10429. RPS6.
HPACAB004027.
HPA031153.
MIM180460. gene.
neXtProtNX_P62753.
PharmGKBPA34844.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2125.
HOGENOMHOG000190952.
HOVERGENHBG011441.
InParanoidP62753.
KOK02991.
OMACQKLFEV.
OrthoDBEOG7Z0JXB.
PhylomeDBP62753.
TreeFamTF300035.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_17015. Metabolism of proteins.
REACT_1762. 3' -UTR-mediated translational regulation.
REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.
SignaLinkP62753.

Gene expression databases

ArrayExpressP62753.
BgeeP62753.
CleanExHS_RPS6.
GenevestigatorP62753.

Family and domain databases

InterProIPR014401. Ribosomal_S6_euk.
IPR001377. Ribosomal_S6e.
IPR018282. Ribosomal_S6e_CS.
[Graphical view]
PANTHERPTHR11502. PTHR11502. 1 hit.
PfamPF01092. Ribosomal_S6e. 1 hit.
[Graphical view]
PIRSFPIRSF002129. Ribosom_S6_euk. 1 hit.
PROSITEPS00578. RIBOSOMAL_S6E. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRPS6. human.
GenomeRNAi6194.
NextBio24053.
PROP62753.
SOURCESearch...

Entry information

Entry nameRS6_HUMAN
AccessionPrimary (citable) accession number: P62753
Secondary accession number(s): P08227 expand/collapse secondary AC list , P10660, Q4VBY7, Q8N6Z7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: July 9, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM