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P62266 (RS23_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
40S ribosomal protein S23
Gene names
Name:RPS23
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length143 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Post-translational modification

Hydroxylation at Pro-62 affects translation termination efficiency.

Sequence similarities

Belongs to the ribosomal protein S12P family.

Ontologies

Keywords
   Molecular functionRibonucleoprotein
Ribosomal protein
   PTMAcetylation
Hydroxylation
   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

cellular protein metabolic process

Traceable author statement. Source: Reactome

gene expression

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

translation

Inferred by curator PubMed 15883184Ref.4. 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.4. Source: UniProtKB

nucleolus

Inferred from direct assay. Source: HPA

ribosome

Non-traceable author statement Ref.1. Source: UniProtKB

   Molecular_functionpoly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 20434207. Source: IntAct

structural constituent of ribosome

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DCCP431462EBI-353072,EBI-1222919

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 14314240S ribosomal protein S23
PRO_0000146457

Amino acid modifications

Modified residue541N6-succinyllysine By similarity
Modified residue6213-hydroxyproline Ref.9 Ref.10
Modified residue1351N6-acetyllysine Ref.6

Sequences

Sequence LengthMass (Da)Tools
P62266 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 8417A48B8CF0A8E5

FASTA14315,808
        10         20         30         40         50         60 
MGKCRGLRTA RKLRSHRRDQ KWHDKQYKKA HLGTALKANP FGGASHAKGI VLEKVGVEAK 

        70         80         90        100        110        120 
QPNSAIRKCV RVQLIKNGKK ITAFVPNDGC LNFIEENDEV LVAGFGRKGH AVGDIPGVRF 

       130        140 
KVVKVANVSL LALYKGKKER PRS 

« Hide

References

« Hide 'large scale' references
[1]"A cDNA sequence of human ribosomal protein, homologue of yeast S28."
Hori N., Murakawa K., Matoba R., Fukushima A., Okubo K., Matsubara K.
Nucleic Acids Res. 21:4394-4394(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"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].
Tissue: Testis.
[4]"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 2-10.
Tissue: Placenta.
[5]"A map of 75 human ribosomal protein genes."
Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J., Tanaka T., Page D.C.
Genome Res. 8:509-523(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 84-142.
[6]"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-135, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"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].
[8]"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).
[9]"Hydroxylation of the eukaryotic ribosomal decoding center affects translational accuracy."
Loenarz C., Sekirnik R., Thalhammer A., Ge W., Spivakovsky E., Mackeen M.M., McDonough M.A., Cockman M.E., Kessler B.M., Ratcliffe P.J., Wolf A., Schofield C.J.
Proc. Natl. Acad. Sci. U.S.A. 111:4019-4024(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: HYDROXYLATION AT PRO-62.
[10]"OGFOD1 catalyzes prolyl hydroxylation of RPS23 and is involved in translation control and stress granule formation."
Singleton R.S., Liu-Yi P., Formenti F., Ge W., Sekirnik R., Fischer R., Adam J., Pollard P.J., Wolf A., Thalhammer A., Loenarz C., Flashman E., Yamamoto A., Coleman M.L., Kessler B.M., Wappner P., Schofield C.J., Ratcliffe P.J., Cockman M.E.
Proc. Natl. Acad. Sci. U.S.A. 111:4031-4036(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: HYDROXYLATION AT PRO-62.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D14530 mRNA. Translation: BAA03400.1.
CR456996 mRNA. Translation: CAG33277.1.
BC070221 mRNA. Translation: AAH70221.1.
AB007158 Genomic DNA. Translation: BAA25822.1.
CCDSCCDS47241.1.
PIRS42105.
RefSeqNP_001016.1. NM_001025.4.
UniGeneHs.527193.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Aelectron microscopy5.00X1-143[»]
ProteinModelPortalP62266.
SMRP62266. Positions 1-142.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112142. 158 interactions.
IntActP62266. 20 interactions.
MINTMINT-5000369.
STRING9606.ENSP00000296674.

PTM databases

PhosphoSiteP62266.

Polymorphism databases

DMDM50403755.

Proteomic databases

MaxQBP62266.
PaxDbP62266.
PRIDEP62266.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296674; ENSP00000296674; ENSG00000186468.
GeneID6228.
KEGGhsa:6228.
UCSCuc003khu.3. human.

Organism-specific databases

CTD6228.
GeneCardsGC05M081569.
HGNCHGNC:10410. RPS23.
HPAHPA054853.
MIM603683. gene.
neXtProtNX_P62266.
PharmGKBPA34813.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0048.
HOGENOMHOG000040064.
HOVERGENHBG054200.
InParanoidP62266.
KOK02973.
OMAWHDKDYK.
OrthoDBEOG77DJ7H.
PhylomeDBP62266.
TreeFamTF300871.

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

ArrayExpressP62266.
BgeeP62266.
CleanExHS_RPS23.
GenevestigatorP62266.

Family and domain databases

Gene3D2.40.50.140. 1 hit.
InterProIPR012340. NA-bd_OB-fold.
IPR006032. Ribosomal_S12/S23.
IPR005680. Ribosomal_S23_euk/arc.
[Graphical view]
PANTHERPTHR11652. PTHR11652. 1 hit.
PfamPF00164. Ribosom_S12_S23. 1 hit.
[Graphical view]
PIRSFPIRSF002133. Ribosomal_S12/S23. 1 hit.
SUPFAMSSF50249. SSF50249. 1 hit.
TIGRFAMsTIGR00982. S23_S12_E_A. 1 hit.
PROSITEPS00055. RIBOSOMAL_S12. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRPS23. human.
GeneWikiRPS23.
GenomeRNAi6228.
NextBio24175.
PROP62266.
SOURCESearch...

Entry information

Entry nameRS23_HUMAN
AccessionPrimary (citable) accession number: P62266
Secondary accession number(s): P39028, Q6IB08
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 103 of the entry and version 3 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 5

Human chromosome 5: entries, gene names and cross-references to MIM