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P62753

- RS6_HUMAN

UniProt

P62753 - RS6_HUMAN

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Protein
40S ribosomal protein S6
Gene
RPS6, OK/SW-cl.2
Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. poly(A) RNA binding Source: UniProtKB
  2. protein binding Source: UniProtKB
  3. protein kinase binding Source: UniProtKB
  4. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. RNA metabolic process Source: Reactome
  2. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  3. TOR signaling Source: UniProtKB
  4. cellular protein metabolic process Source: Reactome
  5. gene expression Source: Reactome
  6. glucose homeostasis Source: UniProtKB
  7. insulin receptor signaling pathway Source: Reactome
  8. mRNA metabolic process Source: Reactome
  9. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  10. positive regulation of apoptotic process Source: UniProtKB
  11. rRNA processing Source: UniProtKB
  12. ribosomal small subunit biogenesis Source: UniProtKB
  13. translation Source: UniProtKB
  14. translational elongation Source: Reactome
  15. translational initiation Source: Reactome
  16. translational termination Source: Reactome
  17. viral life cycle Source: Reactome
  18. viral process Source: Reactome
  19. viral transcription Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiREACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1979. Translation initiation complex formation.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_6772. S6K1 signalling.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.
REACT_9491. Viral mRNA Translation.
SignaLinkiP62753.

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
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:10429. RPS6.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. cytosolic small ribosomal subunit Source: UniProtKB
  4. nucleolus Source: UniProtKB
  5. nucleus Source: UniProtKB
  6. ribonucleoprotein complex Source: MGI
  7. small ribosomal subunit Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi235 – 2362SS → AA: Abolishes phosphorylation by PASK. 1 Publication

Organism-specific databases

PharmGKBiPA34844.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 24924940S ribosomal protein S6
PRO_0000137312Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei211 – 2111N6-acetyllysine1 Publication
Modified residuei235 – 2351Phosphoserine; by RPS6KA1, RPS6KA3, DAPK1 and PASK4 Publications
Modified residuei236 – 2361Phosphoserine; by RPS6KA1, RPS6KA3, DAPK1 and PASK5 Publications
Modified residuei240 – 2401Phosphoserine3 Publications
Modified residuei242 – 2421Phosphoserine1 Publication
Modified residuei244 – 2441Phosphoserine1 Publication
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.3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP62753.
PaxDbiP62753.
PRIDEiP62753.

PTM databases

PhosphoSiteiP62753.

Expressioni

Gene expression databases

ArrayExpressiP62753.
BgeeiP62753.
CleanExiHS_RPS6.
GenevestigatoriP62753.

Organism-specific databases

HPAiCAB004027.
HPA031153.

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

BioGridi112108. 165 interactions.
DIPiDIP-31507N.
IntActiP62753. 40 interactions.
MINTiMINT-1162101.
STRINGi9606.ENSP00000369757.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Aelectron microscopy5.00G1-249[»]
ProteinModelPortaliP62753.
SMRiP62753. Positions 1-237.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2125.
HOGENOMiHOG000190952.
HOVERGENiHBG011441.
InParanoidiP62753.
KOiK02991.
OMAiCQKLFEV.
OrthoDBiEOG7Z0JXB.
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.
PROSITEiPS00578. RIBOSOMAL_S6E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P62753-1 [UniParc]FASTAAdd to Basket

« Hide

MKLNISFPAT GCQKLIEVDD ERKLRTFYEK RMATEVAADA LGEEWKGYVV    50
RISGGNDKQG FPMKQGVLTH GRVRLLLSKG HSCYRPRRTG ERKRKSVRGC 100
IVDANLSVLN LVIVKKGEKD IPGLTDTTVP RRLGPKRASR IRKLFNLSKE 150
DDVRQYVVRK PLNKEGKKPR TKAPKIQRLV TPRVLQHKRR RIALKKQRTK 200
KNKEEAAEYA KLLAKRMKEA KEKRQEQIAK RRRLSSLRAS TSKSESSQK 249
Length:249
Mass (Da):28,681
Last modified:August 1, 1988 - v1
Checksum:iA61E435884E636AE
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti221 – 2211K → R.1 Publication
Corresponds to variant rs17852447 [ dbSNP | Ensembl ].
VAR_025314

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 231K → T in AAA60288. 1 Publication
Sequence conflicti144 – 1441L → R in AAA60288. 1 Publication
Sequence conflicti155 – 1562QY → EC in AAA60287. 1 Publication
Sequence conflicti168 – 1681K → R in AAA60287. 1 Publication
Sequence conflicti196 – 1961K → Q in AAA60288. 1 Publication
Sequence conflicti219 – 2191E → Q in AAA60287. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.1. human.

Polymorphism databases

DMDMi51338632.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS6492.1.
PIRi JC1394. R3HU6.
RefSeqi NP_001001.2. NM_001010.2.
UniGenei Hs.408073.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3J3A electron microscopy 5.00 G 1-249 [» ]
ProteinModelPortali P62753.
SMRi P62753. Positions 1-237.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112108. 165 interactions.
DIPi DIP-31507N.
IntActi P62753. 40 interactions.
MINTi MINT-1162101.
STRINGi 9606.ENSP00000369757.

PTM databases

PhosphoSitei P62753.

Polymorphism databases

DMDMi 51338632.

Proteomic databases

MaxQBi P62753.
PaxDbi P62753.
PRIDEi P62753.

Protocols and materials databases

DNASUi 6194.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000380394 ; ENSP00000369757 ; ENSG00000137154 .
GeneIDi 6194.
KEGGi hsa:6194.
UCSCi uc003znv.1. human.

Organism-specific databases

CTDi 6194.
GeneCardsi GC09M019366.
HGNCi HGNC:10429. RPS6.
HPAi CAB004027.
HPA031153.
MIMi 180460. gene.
neXtProti NX_P62753.
PharmGKBi PA34844.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2125.
HOGENOMi HOG000190952.
HOVERGENi HBG011441.
InParanoidi P62753.
KOi K02991.
OMAi CQKLFEV.
OrthoDBi EOG7Z0JXB.
PhylomeDBi P62753.
TreeFami TF300035.

Enzyme and pathway databases

Reactomei REACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1979. Translation initiation complex formation.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_6772. S6K1 signalling.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.
REACT_9491. Viral mRNA Translation.
SignaLinki P62753.

Miscellaneous databases

ChiTaRSi RPS6. human.
GenomeRNAii 6194.
NextBioi 24053.
PROi P62753.
SOURCEi Search...

Gene expression databases

ArrayExpressi P62753.
Bgeei P62753.
CleanExi HS_RPS6.
Genevestigatori P62753.

Family and domain databases

InterProi IPR014401. Ribosomal_S6_euk.
IPR001377. Ribosomal_S6e.
IPR018282. Ribosomal_S6e_CS.
[Graphical view ]
PANTHERi PTHR11502. PTHR11502. 1 hit.
Pfami PF01092. Ribosomal_S6e. 1 hit.
[Graphical view ]
PIRSFi PIRSF002129. Ribosom_S6_euk. 1 hit.
PROSITEi PS00578. RIBOSOMAL_S6E. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.

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: September 3, 2014
This is version 116 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

External Data

Dasty 3

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