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P23396 (RS3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 163. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
40S ribosomal protein S3
Gene names
Name:RPS3
ORF Names:OK/SW-cl.26
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length243 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Subunit structure

Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Identified in a HCV IRES-mediated translation complex, at least composed of EIF3C, IGF2BP1, RPS3 and HCV RNA-replicon. Ref.17 Ref.22

Subcellular location

Cytoplasm. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Ref.17

Sequence similarities

Belongs to the ribosomal protein S3P family.

Contains 1 KH type-2 domain.

Sequence caution

The sequence BAB93471.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   LigandRNA-binding
   Molecular functionRibonucleoprotein
Ribosomal protein
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA catabolic process, endonucleolytic

Inferred from direct assay PubMed 16737853. Source: GOC

RNA metabolic process

Traceable author statement. Source: Reactome

SRP-dependent cotranslational protein targeting to membrane

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

cellular response to DNA damage stimulus

Inferred from expression pattern PubMed 17560175. Source: UniProtKB

cytoplasmic translation

Inferred from Biological aspect of Ancestor. Source: RefGenome

gene expression

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

negative regulation of DNA repair

Inferred from mutant phenotype PubMed 17049931. Source: UniProtKB

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Traceable author statement. Source: Reactome

nucleic acid phosphodiester bond hydrolysis

Inferred from mutant phenotype PubMed 16584637. Source: GOC

positive regulation of DNA N-glycosylase activity

Inferred from direct assay PubMed 15518571. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Inferred from mutant phenotype PubMed 18045535. Source: UniProtKB

positive regulation of apoptotic signaling pathway

Inferred from direct assay PubMed 14988002. Source: UniProtKB

translation

Non-traceable author statement Ref.2. Source: UniProtKB

translational elongation

Traceable author statement. Source: Reactome

translational initiation

Non-traceable author statement PubMed 15883184. Source: UniProtKB

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 PubMed 14988002. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 16814409PubMed 17560175. Source: UniProtKB

cytosolic small ribosomal subunit

Inferred from direct assay PubMed 15883184Ref.13. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

nucleus

Inferred from direct assay PubMed 14988002PubMed 16814409PubMed 17560175PubMed 18045535. Source: UniProtKB

ribonucleoprotein complex

Inferred from direct assay Ref.17. Source: UniProtKB

ruffle membrane

Inferred from direct assay PubMed 16814409. Source: UniProtKB

   Molecular_functionDNA-(apurinic or apyrimidinic site) lyase activity

Inferred from direct assay PubMed 16737853. Source: UniProtKB

NF-kappaB binding

Inferred from physical interaction PubMed 18045535. Source: UniProtKB

damaged DNA binding

Inferred from direct assay PubMed 16737853PubMed 17560175. Source: UniProtKB

endonuclease activity

Inferred from mutant phenotype PubMed 16584637. Source: UniProtKB

enzyme binding

Inferred from physical interaction PubMed 15518571. Source: UniProtKB

iron-sulfur cluster binding

Non-traceable author statement PubMed 11911468. Source: UniProtKB

mRNA binding

Inferred from direct assay PubMed 18464793. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein kinase A binding

Inferred from physical interaction PubMed 16814409. Source: UniProtKB

protein kinase binding

Inferred from physical interaction PubMed 15950189. Source: UniProtKB

structural constituent of ribosome

Inferred from direct assay PubMed 15883184. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P23396-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P23396-2)

The sequence of this isoform differs from the canonical sequence as follows:
     85-85: E → ELKIMVMVTGYPLLPLK
Note: No experimental confirmation available. Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 24324240S ribosomal protein S3
PRO_0000130320

Regions

Domain21 – 9272KH type-2

Amino acid modifications

Modified residue21N-acetylalanine Ref.10 Ref.20 Ref.28
Modified residue621N6-acetyllysine Ref.24
Modified residue1321N6-succinyllysine By similarity
Modified residue2211Phosphothreonine Ref.12 Ref.15 Ref.19 Ref.23 Ref.25 Ref.27
Modified residue2241Phosphoserine Ref.16
Modified residue2421Phosphothreonine Ref.18
Cross-link90Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link202Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Natural variations

Alternative sequence851E → ELKIMVMVTGYPLLPLK in isoform 2.
VSP_046667

Experimental info

Sequence conflict81K → R in AAB19349. Ref.2
Sequence conflict1041S → C in CAA39248. Ref.1
Sequence conflict2331P → L in CAA39248. Ref.1

Secondary structure

.............. 243
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 1993. Version 2.
Checksum: 6ECBB34A8EE04AAF

FASTA24326,688
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 68FF5C2DF8769693
Show »

FASTA25928,487

References

« Hide 'large scale' references
[1]"Isolation of a cDNA encoding human 40S ribosomal protein s3."
Zhang X.T., Tan Y.M., Tan Y.H.
Nucleic Acids Res. 18:6689-6689(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Ribosomal protein genes are overexpressed in colorectal cancer: isolation of a cDNA clone encoding the human S3 ribosomal protein."
Pogue-Geile K., Geiser J.R., Shu M., Miller C., Wool I.G., Meisler A.I., Pipas J.M.
Mol. Cell. Biol. 11:3842-3849(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"The human ribosomal protein genes: sequencing and comparative analysis of 73 genes."
Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S., Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.
Genome Res. 12:379-390(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]NIEHS SNPs program
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[6]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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] (ISOFORM 1).
Tissue: Adrenal cortex, Liver, Lymph, Skin and Testis.
[9]"A small nucleolar RNA is processed from an intron of the human gene encoding ribosomal protein S3."
Tycowski K.T., Shu M.D., Steitz J.A.
Genes Dev. 7:1176-1190(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 1-94 (ISOFORM 1).
[10]Bienvenut W.V., Murray L., Brunton V.G., Frame M.C., Calvo F., Kolch W.
Submitted (FEB-2008) to UniProtKB
Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Cervix carcinoma and Colon adenocarcinoma.
[11]"Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
Shichijo S., Itoh K.
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-243 (ISOFORM 1).
Tissue: Colon adenocarcinoma.
[12]Bienvenut W.V., Waridel P., Quadroni M.
Submitted (MAR-2009) to UniProtKB
Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[13]"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 188-197.
Tissue: Placenta.
[14]"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.
[15]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Phosphoproteomic analysis of the human pituitary."
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.
Pituitary 9:109-120(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Pituitary.
[17]"Molecular composition of IMP1 ribonucleoprotein granules."
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C.
Mol. Cell. Proteomics 6:798-811(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[18]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-242, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"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 THR-221, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"IGF2BP1 enhances HCV IRES-mediated translation initiation via the 3'UTR."
Weinlich S., Huettelmaier S., Schierhorn A., Behrens S.-E., Ostareck-Lederer A., Ostareck D.H.
RNA 15:1528-1542(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A HCV IRES-MEDIATED TRANSLATION COMPLEX.
[23]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[24]"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-62, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"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 THR-221, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[26]"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].
[27]"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 THR-221, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"Solution structure of the KH domain of human ribosomal protein S3."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2004) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 17-95.
[30]"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.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U14990 mRNA. Translation: AAB60336.1.
U14991 mRNA. Translation: AAB60337.1.
U14992 mRNA. Translation: AAB60338.1.
X55715 mRNA. Translation: CAA39248.1.
S42658 mRNA. Translation: AAB19349.2.
AB061838 Genomic DNA. Translation: BAB79476.1.
AY791291 Genomic DNA. Translation: AAV40835.1.
AK313051 mRNA. Translation: BAG35882.1.
AP000744 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74963.1.
BC003137 mRNA. Translation: AAH03137.1.
BC003577 mRNA. Translation: AAH03577.1.
BC013196 mRNA. Translation: AAH13196.1.
BC034149 mRNA. Translation: AAH34149.1.
BC071917 mRNA. Translation: AAH71917.1.
BC100284 mRNA. Translation: AAI00285.1.
L16016 Genomic DNA. Translation: AAA18095.1.
AB062288 mRNA. Translation: BAB93471.1. Different initiation.
PIRR3HUS3. A41247.
RefSeqNP_000996.2. NM_001005.4.
NP_001243731.1. NM_001256802.1.
NP_001247435.1. NM_001260506.1.
NP_001247436.1. NM_001260507.1.
UniGeneHs.546286.
Hs.740358.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WH9NMR-A17-95[»]
3J3Aelectron microscopy5.00D1-243[»]
ProteinModelPortalP23396.
SMRP23396. Positions 1-227.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112102. 204 interactions.
IntActP23396. 43 interactions.
MINTMINT-4999144.
STRING9606.ENSP00000278572.

PTM databases

PhosphoSiteP23396.

Polymorphism databases

DMDM417719.

Proteomic databases

PaxDbP23396.
PeptideAtlasP23396.
PRIDEP23396.

Protocols and materials databases

DNASU6188.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000278572; ENSP00000278572; ENSG00000149273. [P23396-2]
ENST00000524851; ENSP00000433821; ENSG00000149273. [P23396-1]
ENST00000527446; ENSP00000436971; ENSG00000149273. [P23396-1]
ENST00000531188; ENSP00000434643; ENSG00000149273. [P23396-1]
GeneID6188.
KEGGhsa:6188.
UCSCuc001owh.4. human. [P23396-1]

Organism-specific databases

CTD6188.
GeneCardsGC11P075110.
HGNCHGNC:10420. RPS3.
MIM600454. gene.
neXtProtNX_P23396.
PharmGKBPA34829.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0092.
HOGENOMHOG000210611.
HOVERGENHBG002195.
InParanoidP23396.
KOK02985.
OMACNDYVET.
OrthoDBEOG7F7W9M.
PhylomeDBP23396.
TreeFamTF300901.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_17015. Metabolism of proteins.
REACT_1762. 3' -UTR-mediated translational regulation.
REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP23396.
BgeeP23396.
CleanExHS_RPS3.
GenevestigatorP23396.

Family and domain databases

Gene3D3.30.1140.32. 1 hit.
3.30.300.20. 1 hit.
InterProIPR004087. KH_dom.
IPR015946. KH_dom-like_a/b.
IPR004044. KH_dom_type_2.
IPR009019. KH_prok-type.
IPR001351. Ribosomal_S3_C.
IPR018280. Ribosomal_S3_CS.
IPR005703. Ribosomal_S3_euk/arc.
[Graphical view]
PfamPF07650. KH_2. 1 hit.
PF00189. Ribosomal_S3_C. 1 hit.
[Graphical view]
SMARTSM00322. KH. 1 hit.
[Graphical view]
SUPFAMSSF54814. SSF54814. 1 hit.
SSF54821. SSF54821. 1 hit.
TIGRFAMsTIGR01008. rpsC_E_A. 1 hit.
PROSITEPS50823. KH_TYPE_2. 1 hit.
PS00548. RIBOSOMAL_S3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRpS3. human.
EvolutionaryTraceP23396.
GeneWikiRPS3.
GenomeRNAi6188.
NextBio24029.
PROP23396.
SOURCESearch...

Entry information

Entry nameRS3_HUMAN
AccessionPrimary (citable) accession number: P23396
Secondary accession number(s): B2R7N5 expand/collapse secondary AC list , J3KN86, Q498B5, Q8NI95
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: October 1, 1993
Last modified: April 16, 2014
This is version 163 of the entry and version 2 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 chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM