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Protein

40S ribosomal protein S23

Gene

RPS23

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB
  • structural constituent of ribosome Source: InterPro

GO - Biological processi

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_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.

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S23
Gene namesi
Name:RPS23
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:10410. RPS23.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • cytosolic small ribosomal subunit Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleolus Source: HPA
  • ribosome Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34813.

Polymorphism and mutation databases

BioMutaiRPS23.
DMDMi50403755.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 14314240S ribosomal protein S23PRO_0000146457Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei54 – 541N6-succinyllysineBy similarity
Modified residuei62 – 6213-hydroxyproline2 Publications
Modified residuei135 – 1351N6-acetyllysine1 Publication

Post-translational modificationi

Hydroxylation at Pro-62 affects translation termination efficiency.2 Publications

Keywords - PTMi

Acetylation, Hydroxylation

Proteomic databases

MaxQBiP62266.
PaxDbiP62266.
PRIDEiP62266.

PTM databases

PhosphoSiteiP62266.

Expressioni

Gene expression databases

BgeeiP62266.
CleanExiHS_RPS23.
ExpressionAtlasiP62266. baseline and differential.
GenevisibleiP62266. HS.

Organism-specific databases

HPAiHPA054853.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
DCCP431462EBI-353072,EBI-1222919
LRRK2Q5S0072EBI-353072,EBI-5323863

Protein-protein interaction databases

BioGridi112142. 134 interactions.
IntActiP62266. 22 interactions.
MINTiMINT-5000369.
STRINGi9606.ENSP00000296674.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CXGelectron microscopy8.70X1-143[»]
4CXHelectron microscopy8.90X1-143[»]
4V6Xelectron microscopy5.00AX1-143[»]
ProteinModelPortaliP62266.
SMRiP62266. Positions 1-142.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S12P family.Curated

Phylogenomic databases

eggNOGiCOG0048.
GeneTreeiENSGT00550000074784.
HOGENOMiHOG000040064.
HOVERGENiHBG054200.
InParanoidiP62266.
KOiK02973.
OMAiWHDKDYK.
OrthoDBiEOG77DJ7H.
PhylomeDBiP62266.
TreeFamiTF300871.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR006032. Ribosomal_S12/S23.
IPR005680. Ribosomal_S23_euk/arc.
[Graphical view]
PANTHERiPTHR11652. PTHR11652. 1 hit.
PfamiPF00164. Ribosom_S12_S23. 1 hit.
[Graphical view]
PIRSFiPIRSF002133. Ribosomal_S12/S23. 1 hit.
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00982. uS12_E_A. 1 hit.
PROSITEiPS00055. RIBOSOMAL_S12. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P62266-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKCRGLRTA RKLRSHRRDQ KWHDKQYKKA HLGTALKANP FGGASHAKGI
60 70 80 90 100
VLEKVGVEAK QPNSAIRKCV RVQLIKNGKK ITAFVPNDGC LNFIEENDEV
110 120 130 140
LVAGFGRKGH AVGDIPGVRF KVVKVANVSL LALYKGKKER PRS
Length:143
Mass (Da):15,808
Last modified:January 23, 2007 - v3
Checksum:i8417A48B8CF0A8E5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14530 mRNA. Translation: BAA03400.1.
CR456996 mRNA. Translation: CAG33277.1.
BC070221 mRNA. Translation: AAH70221.1.
AB007158 Genomic DNA. Translation: BAA25822.1.
CCDSiCCDS47241.1.
PIRiS42105.
RefSeqiNP_001016.1. NM_001025.4.
UniGeneiHs.527193.

Genome annotation databases

EnsembliENST00000296674; ENSP00000296674; ENSG00000186468.
GeneIDi6228.
KEGGihsa:6228.
UCSCiuc003khu.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14530 mRNA. Translation: BAA03400.1.
CR456996 mRNA. Translation: CAG33277.1.
BC070221 mRNA. Translation: AAH70221.1.
AB007158 Genomic DNA. Translation: BAA25822.1.
CCDSiCCDS47241.1.
PIRiS42105.
RefSeqiNP_001016.1. NM_001025.4.
UniGeneiHs.527193.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CXGelectron microscopy8.70X1-143[»]
4CXHelectron microscopy8.90X1-143[»]
4V6Xelectron microscopy5.00AX1-143[»]
ProteinModelPortaliP62266.
SMRiP62266. Positions 1-142.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112142. 134 interactions.
IntActiP62266. 22 interactions.
MINTiMINT-5000369.
STRINGi9606.ENSP00000296674.

PTM databases

PhosphoSiteiP62266.

Polymorphism and mutation databases

BioMutaiRPS23.
DMDMi50403755.

Proteomic databases

MaxQBiP62266.
PaxDbiP62266.
PRIDEiP62266.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000296674; ENSP00000296674; ENSG00000186468.
GeneIDi6228.
KEGGihsa:6228.
UCSCiuc003khu.3. human.

Organism-specific databases

CTDi6228.
GeneCardsiGC05M081569.
HGNCiHGNC:10410. RPS23.
HPAiHPA054853.
MIMi603683. gene.
neXtProtiNX_P62266.
PharmGKBiPA34813.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0048.
GeneTreeiENSGT00550000074784.
HOGENOMiHOG000040064.
HOVERGENiHBG054200.
InParanoidiP62266.
KOiK02973.
OMAiWHDKDYK.
OrthoDBiEOG77DJ7H.
PhylomeDBiP62266.
TreeFamiTF300871.

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_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.

Miscellaneous databases

ChiTaRSiRPS23. human.
GeneWikiiRPS23.
GenomeRNAii6228.
NextBioi24175.
PROiP62266.
SOURCEiSearch...

Gene expression databases

BgeeiP62266.
CleanExiHS_RPS23.
ExpressionAtlasiP62266. baseline and differential.
GenevisibleiP62266. HS.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR006032. Ribosomal_S12/S23.
IPR005680. Ribosomal_S23_euk/arc.
[Graphical view]
PANTHERiPTHR11652. PTHR11652. 1 hit.
PfamiPF00164. Ribosom_S12_S23. 1 hit.
[Graphical view]
PIRSFiPIRSF002133. Ribosomal_S12/S23. 1 hit.
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00982. uS12_E_A. 1 hit.
PROSITEiPS00055. RIBOSOMAL_S12. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).
  9. Cited for: HYDROXYLATION AT PRO-62.
  10. Cited for: HYDROXYLATION AT PRO-62.

Entry informationi

Entry nameiRS23_HUMAN
AccessioniPrimary (citable) accession number: P62266
Secondary accession number(s): P39028, Q6IB08
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 111 of the entry and version 3 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 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Ribosomal proteins
    Ribosomal proteins families and list of entries
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.