ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P23396


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name RS3_HUMAN
Primary accession number P23396
Secondary accession numbers Q498B5 Q8NI95
Integrated into Swiss-Prot on November 1, 1991
Sequence was last modified on October 1, 1993 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 110)
Name and origin of the protein
Protein name 40S ribosomal protein S3
Synonyms None
Gene name
Name: RPS3
ORFNames: OK/SW-cl.26
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1093/nar/18.22.6689; PubMed=2129557 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang X.T., Tan Y.M., Tan Y.H.;
"Isolation of a cDNA encoding human 40S ribosomal protein s3.";
Nucleic Acids Res. 18:6689-6689(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1712897 [NCBI, ExPASy, EBI, Israel, Japan]
Pogue-Geile K., Geiser J.R., Shu M., Miller C., Wool I.G., Meisler A.I., Pipas J.M.;
"Ribosomal protein genes are overexpressed in colorectal cancer: isolation of a cDNA clone encoding the human S3 ribosomal protein.";
Mol. Cell. Biol. 11:3842-3849(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1101/gr.214202; PubMed=11875025 [NCBI, ExPASy, EBI, Israel, Japan]
Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S., Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.;
"The human ribosomal protein genes: sequencing and comparative analysis of 73 genes.";
Genome Res. 12:379-390(2002).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Adrenal cortex, Liver, Lymph, Skin, and Testis;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE OF 1-94.
PubMed=8319909 [NCBI, ExPASy, EBI, Israel, Japan]
Tycowski K.T., Shu M.D., Steitz J.A.;
"A small nucleolar RNA is processed from an intron of the human gene encoding ribosomal protein S3.";
Genes Dev. 7:1176-1190(1993).
[7]
PROTEIN SEQUENCE OF 2-8; 10-64; 68-116; 118-141; 152-173; 186-197 AND 202-243, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
TISSUE=Cervix carcinoma, and Colon adenocarcinoma;
Bienvenut W.V., Murray L., Brunton V.G., Frame M.C., Calvo F., Kolch W.;
Submitted (FEB-2008) to UniProtKB.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-243.
TISSUE=Colon adenocarcinoma;
Shichijo S., Itoh K.;
"Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients.";
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[9]
PROTEIN SEQUENCE OF 10-40; 46-54; 76-90; 95-106; 109-116; 118-132; 152-173; 179-185; 188-197 AND 202-243, PHOSPHORYLATION AT THR-221, AND MASS SPECTROMETRY.
TISSUE=Cervix carcinoma;
Bienvenut W.V., Waridel P., Quadroni M.;
Submitted (MAR-2009) to UniProtKB.
[10]
PROTEIN SEQUENCE OF 188-197.
TISSUE=Placenta;
DOI=10.1111/j.1432-1033.1996.0144u.x; PubMed=8706699 [NCBI, ExPASy, EBI, Israel, Japan]
Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K., Egorov T.A., Thiede B., Wittmann-Liebold B., Otto A.;
"Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry.";
Eur. J. Biochem. 239:144-149(1996).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0507066103; PubMed=16565220 [NCBI, ExPASy, EBI, Israel, Japan]
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
"Phosphoproteome analysis of the human mitotic spindle.";
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, AND MASS SPECTROMETRY.
TISSUE=Pituitary;
DOI=10.1007/s11102-006-8916-x; PubMed=16807684 [NCBI, ExPASy, EBI, Israel, Japan]
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
"Phosphoproteomic analysis of the human pituitary.";
Pituitary 9:109-120(2006).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan]
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan]
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-220; THR-221 AND SER-224, AND MASS SPECTROMETRY.
DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan]
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Anal. Sci. 24:161-166(2008).
[17]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-90 AND LYS-202, AND MASS SPECTROMETRY.
DOI=10.1021/pr800468j; PubMed=18781797 [NCBI, ExPASy, EBI, Israel, Japan]
Meierhofer D., Wang X., Huang L., Kaiser P.;
"Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry.";
J. Proteome Res. 7:4566-4576(2008).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221; SER-224 AND THR-242, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221 AND THR-242, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[20]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[21]
STRUCTURE BY NMR OF 17-95.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the KH domain of human ribosomal protein S3.";
Submitted (NOV-2004) to the PDB data bank.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U14990; AAB60336.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U14991; AAB60337.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U14992; AAB60338.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X55715; CAA39248.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S42658; AAB19349.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB061838; BAB79476.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY791291; AAV40835.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC003137; AAH03137.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC003577; AAH03577.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC013196; AAH13196.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC034149; AAH34149.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC071917; AAH71917.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC100284; AAI00285.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L16016; AAA18095.1; -; Unassigned_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB062288; BAB93471.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00011253; -.
PIR A41247; R3HUS3.
RefSeq NP_000996.2; -.
UniGene Hs.546286
3D structure databases
PDB
1WH9; NMR; -; A=17-95.[ExPASy / RCSB / EBI]
PDBsum 1WH9; -.
SMR P23396; 6-189.
ModBase P23396.
Protein-protein interaction databases
IntAct P23396; 20.
PTM databases
PhosphoSite P23396; -.
Enzyme and pathway databases
Reactome REACT_1762; 3' -UTR-mediated translational regulation.
REACT_6167; Influenza Infection.
REACT_71; Gene Expression.
Organism-specific databases
GeneCards GC11P074788; -.
H-InvDB HIX0009946; -.
HIX0028157; -.
HGNC HGNC:10420; RPS3.
GenAtlas RPS3.
MIM 600454; gene. [NCBI / EBI]
PharmGKB PA31017; -.
Gene expression databases
ArrayExpress P23396; -.
Bgee P23396; -.
CleanEx HS_RPS3; -.
GermOnline ENSG00000149273; Homo sapiens.
Ontologies
GO
GO:0022627; Cellular component: cytosolic small ribosomal subunit (inferred from direct assay from UniProtKB).
GO:0005634; Cellular component: nucleus (inferred from direct assay from UniProtKB).
GO:0032587; Cellular component: ruffle membrane (inferred from direct assay from UniProtKB).
GO:0003684; Molecular function: damaged DNA binding (inferred from direct assay from UniProtKB).
GO:0003906; Molecular function: DNA-(apurinic or apyrimidinic site) lyase activity (inferred from direct assay from UniProtKB).
GO:0004519; Molecular function: endonuclease activity (inferred from mutant phenotype from UniProtKB).
GO:0051536; Molecular function: iron-sulfur cluster binding (non-traceable author statement from UniProtKB).
GO:0003729; Molecular function: mRNA binding (inferred from direct assay from UniProtKB).
GO:0051059; Molecular function: NF-kappaB binding (inferred from physical interaction from UniProtKB).
GO:0019901; Molecular function: protein kinase binding (inferred from physical interaction from UniProtKB).
GO:0003735; Molecular function: structural constituent of ribosome (inferred from direct assay from UniProtKB).
GO:0006919; Biological process: activation of caspase activity (inferred from direct assay from UniProtKB).
GO:0006917; Biological process: induction of apoptosis (inferred from direct assay from UniProtKB).
GO:0045738; Biological process: negative regulation of DNA repair (inferred from mutant phenotype from UniProtKB).
GO:0032088; Biological process: negative regulation of NF-kappaB transcription factor activity (inferred from mutant phenotype from UniProtKB).
GO:0006974; Biological process: response to DNA damage stimulus (inferred from expression pattern from UniProtKB).
GO:0006414; Biological process: translational elongation (inferred from experiment from Reactome).
GO:0006413; Biological process: translational initiation (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR004087; KH.
IPR004044; KH_type_2.
IPR001351; Ribosomal_S3_C.
IPR018280; Ribosomal_S3_CS.
IPR005703; Ribosomal_S3_euk/arc.
Graphical view of domain structure.
Gene3D G3DSA:3.30.1140.32; Ribosomal_S3_C; 1.
Pfam PF07650; KH_2; 1.
PF00189; Ribosomal_S3_C; 1.
Pfam graphical view of domain structure.
SMART SM00322; KH; 1.
SMART graphical view of domain structure.
TIGRFAMs TIGR01008; rpsC_E_A; 1.
PROSITE PS50823; KH_TYPE_2; 1.
PS00548; RIBOSOMAL_S3; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PeptideAtlas P23396; -.
PRIDE P23396; -.
Genome annotation databases
Ensembl ENSG00000149273; Homo sapiens. [Contig view]
GeneID 6188; -.
KEGG hsa:6188; -.
NMPDR fig|9606.3.peg.6308; -.
Phylogenomic databases
HOGENOM P23396; -.
HOVERGEN P23396; -.
OMA P23396; GKLTGER.
Other
NextBio 24029; -.
SOURCE RPS3; Homo sapiens.
ProtoNet P23396.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Direct protein sequencing; Isopeptide bond; Phosphoprotein; Ribonucleoprotein; Ribosomal protein; RNA-binding; Ubl conjugation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   243  242     40S ribosomal protein S3. PRO_0000130320
DOMAIN   21    92  72     KH type-2. 
MOD_RES   2     2        N-acetylalanine. 
MOD_RES   220   220        Phosphothreonine. 
MOD_RES   221   221        Phosphothreonine. 
MOD_RES   224   224        Phosphoserine. 
MOD_RES   242   242        Phosphothreonine. 
CROSSLNK   90    90        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin). 
CROSSLNK   202   202        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin). 
CONFLICT   8     8        K -> R (in Ref. 2; AAB19349). 
CONFLICT   104   104        S -> C (in Ref. 1; CAA39248). 
CONFLICT   233   233        P -> L (in Ref. 1; CAA39248). 
HELIX   17    28  12      
TURN   29    33  5      
STRAND   34    41  8      
STRAND   46    53  8      
HELIX   55    59  5      
HELIX   61    63  3      
HELIX   64    77  14      
STRAND   83    90  8      
Sequence information
Length: 243 AA [This is the length of the unprocessed precursor] Molecular weight: 26688 Da [This is the MW of the unprocessed precursor] CRC64: 6ECBB34A8EE04AAF [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAVQISKKRK FVADGIFKAE LNEFLTRELA EDGYSGVEVR VTPTRTEIII LATRTQNVLG 

        70         80         90        100        110        120 
EKGRRIRELT AVVQKRFGFP EGSVELYAEK VATRGLCAIA QAESLRYKLL GGLAVRRACY 

       130        140        150        160        170        180 
GVLRFIMESG AKGCEVVVSG KLRGQRAKSM KFVDGLMIHS GDPVNYYVDT AVRHVLLRQG 

       190        200        210        220        230        240 
VLGIKVKIML PWDPTGKIGP KKPLPDHVSI VEPKDEILPT TPISEQKGGK PEPPAMPQPV 


PTA 

P23396 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!