40S ribosomal protein S6 - Homo sapiens (Human)

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P62753 (RS6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 87. History...

Clusters with 100%, 90%, 50% identity |

Documents (6) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
40S ribosomal protein S6

Alternative name(s):
Phosphoprotein NP33

Gene names

Name:	RPS6
ORF Names:	OK/SW-cl.2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	249 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Phosphrylated at Ser-235 and Ser-236 by RPS6KA1 and RPS6KA3; phosphorylation at these sites facilitates the assembly of the preinitiation complex. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.20
Sequence similarities	Belongs to the ribosomal protein S6e family.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	TOR signaling cascade Inferred from direct assay. Source: UniProtKB endocrine pancreas development 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 positive regulation of apoptotic process Inferred from direct assay. Source: UniProtKB rRNA processing Inferred from mutant phenotype. Source: UniProtKB translational elongation Traceable author statement. Source: Reactome translational termination Traceable author statement. Source: Reactome viral transcription Traceable author statement. Source: Reactome
Cellular component	cytosolic small ribosomal subunit Inferred from direct assay Ref.7. Source: UniProtKB nucleolus Inferred from direct assay. Source: UniProtKB
Molecular function	protein kinase binding Inferred from physical interaction Ref.20. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NCBP1	Q09161	3	EBI-356625,EBI-464743

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 249

249

40S ribosomal protein S6

PRO_0000137312

Amino acid modifications

Modified residue

N6-acetyllysine Ref.18

Modified residue

Phosphoserine Ref.11

Modified residue

148

Phosphoserine Ref.15

Modified residue

211

N6-acetyllysine Ref.18

Modified residue

235

Phosphoserine; by RPS6KA1, RPS6KA3, DAPK1 and PASK Ref.8 Ref.9 Ref.10 Ref.11 Ref.15 Ref.16 Ref.17 Ref.20

Modified residue

236

Phosphoserine; by RPS6KA1, RPS6KA3, DAPK1 and PASK Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.15 Ref.16 Ref.20

Modified residue

240

Phosphoserine Ref.9 Ref.11 Ref.12 Ref.14 Ref.15 Ref.17

Modified residue

244

Phosphoserine Ref.11 Ref.15

Modified residue

246

Phosphoserine By similarity

Modified residue

247

Phosphoserine Ref.15

Natural variations

Natural variant

221

K → R. Ref.6
Corresponds to variant rs17852447 [ dbSNP | Ensembl ].

VAR_025314

Experimental info

Mutagenesis

235 – 236

SS → AA: Abolishes pohsphorylation by PASK. Ref.20

Sequence conflict

K → T in AAA60288. Ref.1

Sequence conflict

144

L → R in AAA60288. Ref.1

Sequence conflict

155 – 156

QY → EC in AAA60287. Ref.2

Sequence conflict

168

K → R in AAA60287. Ref.2

Sequence conflict

196

K → Q in AAA60288. Ref.1

Sequence conflict

219

E → Q in AAA60287. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P62753 [UniParc].

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

FASTA

249

28,681

        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' referencesShow '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: 2840355] [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: 3279029] [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: 1301164] [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: 1446836] [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: 15489334] [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: 8706699] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-15. Tissue: Placenta.
[8]	"Global phosphoproteome of HT-29 human colon adenocarcinoma cells." Kim J.-E., Tannenbaum S.R., White F.M. J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235 AND SER-236, MASS SPECTROMETRY. Tissue: Colon adenocarcinoma.
[9]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235; SER-236 AND SER-240, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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: 17360704] [Abstract] Cited for: PHOSPHORYLATION AT SER-235 AND SER-236.
[11]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78; SER-235; SER-236; SER-240 AND SER-244, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[12]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148; SER-235; SER-236; SER-240; SER-244 AND SER-247, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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: 18974095] [Abstract] Cited for: PHOSPHORYLATION AT SER-235 AND SER-236 BY DAPK1.
[17]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235 AND SER-240, MASS SPECTROMETRY.
[18]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-30 AND LYS-211, MASS SPECTROMETRY.
[19]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]	"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: 21418524] [Abstract] Cited for: PHOSPHORYLATION AT SER-235 AND SER-236, MUTAGENESIS OF 235-SER-SER-236.
+	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.
IPI	IPI00021840.
PIR	R3HU6. JC1394.
RefSeq	NP_001001.2. NM_001010.2.
UniGene	Hs.408073.
3D structure databases
ProteinModelPortal	P62753.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-31507N.
IntAct	P62753. 22 interactions.
MINT	MINT-1162101.
STRING	P62753.
PTM databases
PhosphoSite	P62753.
Polymorphism databases
DMDM	51338632.
Proteomic databases
PRIDE	P62753.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000380394; ENSP00000369757; ENSG00000137154.
GeneID	6194.
KEGG	hsa:6194.
UCSC	uc003znv.1. human.
Organism-specific databases
CTD	6194.
GeneCards	GC09M019366.
H-InvDB	HIX0007947.
HGNC	HGNC:10429. RPS6.
HPA	CAB004027. HPA031153.
MIM	180460. gene.
neXtProt	NX_P62753.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	HBG316337.
HOVERGEN	HBG011441.
InParanoid	P62753.
OMA	VFYEKRM.
OrthoDB	EOG4KD6N0.
PhylomeDB	P62753.
Enzyme and pathway databases
Pathway_Interaction_DB	il2_pi3kpathway. IL2 signaling events mediated by PI3K. mtor_4pathway. mTOR signaling pathway.
Reactome	REACT_111045. Developmental Biology. REACT_111102. Signal Transduction. REACT_111217. Metabolism. REACT_15380. Diabetes pathways. REACT_17015. Metabolism of proteins. REACT_1762. 3' -UTR-mediated translational regulation. REACT_6167. Influenza Infection. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	P62753.
Bgee	P62753.
CleanEx	HS_RPS6.
Genevestigator	P62753.
GermOnline	ENSG00000137154. Homo sapiens.
Family and domain databases
InterPro	IPR014401. Ribosomal_S6_euk. IPR001377. Ribosomal_S6e. IPR018282. Ribosomal_S6e_CS. [Graphical view]
KO	K02991.
PANTHER	PTHR11502. Ribosomal_S6E. 1 hit.
Pfam	PF01092. Ribosomal_S6e. 1 hit. [Graphical view]
PIRSF	PIRSF002129. Ribosom_S6_euk. 1 hit.
PROSITE	PS00578. RIBOSOMAL_S6E. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	24053.
SOURCE	Search...

Entry information

Entry name

RS6_HUMAN

Accession

Primary (citable) accession number: P62753
Secondary accession number(s): P08227

Q8N6Z7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	January 25, 2012
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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

Ribosomal proteins

Ribosomal proteins families and list of entries

Human chromosome 9

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents