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Protein

40S ribosomal protein S23

Gene

RPS23

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

Functioni

Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:28257692, PubMed:23636399, PubMed:25957688, PubMed:25901680). The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (PubMed:23636399, PubMed:25957688, PubMed:25901680). Plays an important role in translational accuracy (PubMed:28257692).4 Publications

GO - Molecular functioni

  • RNA binding Source: UniProtKB
  • structural constituent of ribosome Source: UniProtKB

GO - Biological processi

  • cytoplasmic translation Source: UniProtKB
  • maintenance of translational fidelity Source: UniProtKB
  • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  • SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  • stress granule assembly Source: UniProtKB
  • translation Source: UniProtKB
  • translational initiation Source: Reactome

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiR-HSA-156827 L13a-mediated translational silencing of Ceruloplasmin expression
R-HSA-156902 Peptide chain elongation
R-HSA-1799339 SRP-dependent cotranslational protein targeting to membrane
R-HSA-192823 Viral mRNA Translation
R-HSA-2408557 Selenocysteine synthesis
R-HSA-6791226 Major pathway of rRNA processing in the nucleolus and cytosol
R-HSA-72649 Translation initiation complex formation
R-HSA-72689 Formation of a pool of free 40S subunits
R-HSA-72695 Formation of the ternary complex, and subsequently, the 43S complex
R-HSA-72702 Ribosomal scanning and start codon recognition
R-HSA-72706 GTP hydrolysis and joining of the 60S ribosomal subunit
R-HSA-72764 Eukaryotic Translation Termination
R-HSA-9010553 Regulation of expression of SLITs and ROBOs
R-HSA-975956 Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC)
R-HSA-975957 Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S23
Alternative name(s):
Small ribosomal subunit protein uS121 Publication
Gene namesi
Name:RPS23
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

EuPathDBiHostDB:ENSG00000186468.12
HGNCiHGNC:10410 RPS23
MIMi603683 gene
neXtProtiNX_P62266

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum

Pathology & Biotechi

Involvement in diseasei

Brachycephaly, trichomegaly, and developmental delay (BTDD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant developmental disorder characterized by brachycephaly, ciliary trichomegaly, dysmorphic features of the face and hands, hearing loss, and developmental delay with short stature. Intellectual disability and autism spectrum disorder may be present in some patients.
See also OMIM:617412
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07913367R → K in BTDD; decreases hydroxylation of the protein; decreases the accuracy of translation; decreases levels of incorporation of the mutant protein into ribosomes and polysomes; patient cells become highly sensitive to oxidative stress. 1 Publication1
Natural variantiVAR_079134120F → I in BTDD; decreases hydroxylation of the protein; decreases the accuracy of translation; decreases levels of incorporation of the mutant protein into polysomes; patient cells become highly sensitive to oxidative stress. 1 Publication1

Keywords - Diseasei

Deafness, Disease mutation, Dwarfism

Organism-specific databases

DisGeNETi6228
MalaCardsiRPS23
MIMi617412 phenotype
OpenTargetsiENSG00000186468
PharmGKBiPA34813

Polymorphism and mutation databases

BioMutaiRPS23
DMDMi50403755

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001464572 – 14340S ribosomal protein S23Add BLAST142

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki37Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei54N6-succinyllysineBy similarity1
Modified residuei623-hydroxyproline3 Publications1
Modified residuei135N6-acetyllysineCombined sources1

Post-translational modificationi

Hydroxylation at Pro-62 affects translation termination efficiency.3 Publications

Keywords - PTMi

Acetylation, Hydroxylation, Isopeptide bond, Ubl conjugation

Proteomic databases

EPDiP62266
MaxQBiP62266
PaxDbiP62266
PeptideAtlasiP62266
PRIDEiP62266
ProteomicsDBi57380
TopDownProteomicsiP62266

PTM databases

iPTMnetiP62266
PhosphoSitePlusiP62266
SwissPalmiP62266

Expressioni

Gene expression databases

BgeeiENSG00000186468
CleanExiHS_RPS23
ExpressionAtlasiP62266 baseline and differential
GenevisibleiP62266 HS

Organism-specific databases

HPAiHPA054853

Interactioni

Subunit structurei

Component of the 40S small ribosomal subunit.3 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi112142, 155 interactors
CORUMiP62266
IntActiP62266, 34 interactors
MINTiP62266
STRINGi9606.ENSP00000296674

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4CXGelectron microscopy8.70X1-143[»]
4CXHelectron microscopy8.90X1-143[»]
4UG0electron microscopy-SX1-143[»]
4V6Xelectron microscopy5.00AX1-143[»]
5A2Qelectron microscopy3.90X1-143[»]
5AJ0electron microscopy3.50BX1-143[»]
5FLXelectron microscopy3.90X1-143[»]
5LKSelectron microscopy3.60SX1-143[»]
5OA3electron microscopy4.30X1-143[»]
5T2Celectron microscopy3.60AD1-143[»]
5VYCX-ray6.00X1/X2/X3/X4/X5/X61-143[»]
6EK0electron microscopy2.90SX1-143[»]
6FECelectron microscopy6.30Q1-142[»]
ProteinModelPortaliP62266
SMRiP62266
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1749 Eukaryota
COG0048 LUCA
GeneTreeiENSGT00550000074784
HOGENOMiHOG000040064
HOVERGENiHBG054200
InParanoidiP62266
KOiK02973
OMAiKFRWSQR
OrthoDBiEOG091G0R2G
PhylomeDBiP62266
TreeFamiTF300871

Family and domain databases

CDDicd03367 Ribosomal_S23, 1 hit
InterProiView protein in InterPro
IPR012340 NA-bd_OB-fold
IPR006032 Ribosomal_S12/S23
IPR005680 Ribosomal_S23_euk/arc
PANTHERiPTHR11652 PTHR11652, 1 hit
PfamiView protein in Pfam
PF00164 Ribosom_S12_S23, 1 hit
PIRSFiPIRSF002133 Ribosomal_S12/S23, 1 hit
SUPFAMiSSF50249 SSF50249, 1 hit
TIGRFAMsiTIGR00982 uS12_E_A, 1 hit
PROSITEiView protein in PROSITE
PS00055 RIBOSOMAL_S12, 1 hit

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

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07913367R → K in BTDD; decreases hydroxylation of the protein; decreases the accuracy of translation; decreases levels of incorporation of the mutant protein into ribosomes and polysomes; patient cells become highly sensitive to oxidative stress. 1 Publication1
Natural variantiVAR_079134120F → I in BTDD; decreases hydroxylation of the protein; decreases the accuracy of translation; decreases levels of incorporation of the mutant protein into polysomes; patient cells become highly sensitive to oxidative stress. 1 Publication1

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.4 human

Similar proteinsi

Entry informationi

Entry nameiRS23_HUMAN
AccessioniPrimary (citable) accession number: P62266
Secondary accession number(s): P39028, Q6IB08
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: January 23, 2007
Last modified: June 20, 2018
This is version 141 of the entry and version 3 of the sequence. See 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. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Ribosomal proteins
    Ribosomal proteins families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

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