UniProtKB - P62266 (RS23_HUMAN)
Protein
40S ribosomal protein S23
Gene
RPS23
Organism
Homo sapiens (Human)
Status
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
- viral transcription Source: Reactome
Keywordsi
Molecular function | Ribonucleoprotein, Ribosomal protein |
Enzyme and pathway databases
PathwayCommonsi | P62266 |
Reactomei | R-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-9633012, Response of EIF2AK4 (GCN2) to amino acid deficiency 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 S23Alternative name(s): Small ribosomal subunit protein uS121 Publication |
Gene namesi | Name:RPS23 |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
EuPathDBi | HostDB:ENSG00000186468.12 |
HGNCi | HGNC:10410, RPS23 |
MIMi | 603683, gene |
neXtProti | NX_P62266 |
Subcellular locationi
Endoplasmic reticulum
- Rough endoplasmic reticulum By similarity
Cytosol
- cytosol 1 Publication
Other locations
- Cytoplasm 2 Publications
Note: Detected on cytosolic polysomes (PubMed:25957688). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity).By similarity1 Publication
Cytosol
- cytosol Source: HPA
- cytosolic small ribosomal subunit Source: UniProtKB
Endoplasmic reticulum
- endoplasmic reticulum Source: HPA
- rough endoplasmic reticulum Source: UniProtKB-SubCell
Nucleus
- nucleoplasm Source: Reactome
Other locations
- membrane Source: UniProtKB
- polysomal ribosome Source: UniProtKB
- ribosome Source: GO_Central
Keywords - Cellular componenti
Cytoplasm, Endoplasmic reticulumPathology & 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.
Related information in OMIMFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_079133 | 67 | R → 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 PublicationCorresponds to variant dbSNP:rs1060505034EnsemblClinVar. | 1 | |
Natural variantiVAR_079134 | 120 | F → 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 PublicationCorresponds to variant dbSNP:rs1060505035EnsemblClinVar. | 1 |
Keywords - Diseasei
Deafness, Disease mutation, DwarfismOrganism-specific databases
DisGeNETi | 6228 |
MalaCardsi | RPS23 |
MIMi | 617412, phenotype |
OpenTargetsi | ENSG00000186468 |
PharmGKBi | PA34813 |
Miscellaneous databases
Pharosi | P62266, Tbio |
Polymorphism and mutation databases
BioMutai | RPS23 |
DMDMi | 50403755 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed1 Publication | |||
ChainiPRO_0000146457 | 2 – 143 | 40S ribosomal protein S23Add BLAST | 142 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Cross-linki | 37 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Modified residuei | 54 | N6-succinyllysineBy similarity | 1 | |
Modified residuei | 62 | 3-hydroxyproline3 Publications | 1 | |
Modified residuei | 135 | N6-acetyllysineCombined sources | 1 |
Post-translational modificationi
Hydroxylation at Pro-62 affects translation termination efficiency.3 Publications
Keywords - PTMi
Acetylation, Hydroxylation, Isopeptide bond, Ubl conjugationProteomic databases
EPDi | P62266 |
jPOSTi | P62266 |
MassIVEi | P62266 |
MaxQBi | P62266 |
PaxDbi | P62266 |
PeptideAtlasi | P62266 |
PRIDEi | P62266 |
ProteomicsDBi | 57380 |
TopDownProteomicsi | P62266 |
PTM databases
iPTMneti | P62266 |
PhosphoSitePlusi | P62266 |
SwissPalmi | P62266 |
Expressioni
Gene expression databases
Bgeei | ENSG00000186468, Expressed in female gonad and 201 other tissues |
ExpressionAtlasi | P62266, baseline and differential |
Genevisiblei | P62266, HS |
Organism-specific databases
HPAi | ENSG00000186468, Low tissue specificity |
Interactioni
Subunit structurei
Component of the 40S small ribosomal subunit.
3 PublicationsBinary interactionsi
Hide detailsP62266
With | #Exp. | IntAct |
---|---|---|
DCC [P43146] | 2 | EBI-353072,EBI-1222919 |
LRRK2 [Q5S007] | 2 | EBI-353072,EBI-5323863 |
OGFOD1 [Q8N543] | 3 | EBI-353072,EBI-13327083 |
Protein-protein interaction databases
BioGRIDi | 112142, 207 interactors |
ComplexPortali | CPX-5223, 40S cytosolic small ribosomal subunit |
CORUMi | P62266 |
IntActi | P62266, 47 interactors |
MINTi | P62266 |
STRINGi | 9606.ENSP00000296674 |
Miscellaneous databases
RNActi | P62266, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P62266 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Sequence similaritiesi
Belongs to the universal ribosomal protein uS12 family.Curated
Phylogenomic databases
eggNOGi | KOG1749, Eukaryota |
GeneTreei | ENSGT00550000074784 |
HOGENOMi | CLU_115574_0_1_1 |
InParanoidi | P62266 |
OMAi | KFRWSQR |
OrthoDBi | 1402984at2759 |
PhylomeDBi | P62266 |
TreeFami | TF300871 |
Family and domain databases
CDDi | cd03367, Ribosomal_S23, 1 hit |
InterProi | View protein in InterPro IPR012340, NA-bd_OB-fold IPR006032, Ribosomal_S12/S23 IPR005680, Ribosomal_S23_euk/arc |
PANTHERi | PTHR11652, PTHR11652, 1 hit |
Pfami | View protein in Pfam PF00164, Ribosom_S12_S23, 1 hit |
PIRSFi | PIRSF002133, Ribosomal_S12/S23, 1 hit |
SUPFAMi | SSF50249, SSF50249, 1 hit |
TIGRFAMsi | TIGR00982, uS12_E_A, 1 hit |
PROSITEi | View protein in PROSITE PS00055, RIBOSOMAL_S12, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 4 potential isoforms that are computationally mapped.Show allAlign All
P62266-1 [UniParc]FASTAAdd to basket
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
Computationally mapped potential isoform sequencesi
There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketD6RD47 | D6RD47_HUMAN | 40S ribosomal protein S23 | RPS23 | 134 | Annotation score: | ||
D6RIX0 | D6RIX0_HUMAN | 40S ribosomal protein S23 | RPS23 | 85 | Annotation score: | ||
D6R9I7 | D6R9I7_HUMAN | 40S ribosomal protein S23 | RPS23 | 123 | Annotation score: | ||
D6RDJ2 | D6RDJ2_HUMAN | 40S ribosomal protein S23 | RPS23 | 55 | Annotation score: |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_079133 | 67 | R → 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 PublicationCorresponds to variant dbSNP:rs1060505034EnsemblClinVar. | 1 | |
Natural variantiVAR_079134 | 120 | F → 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 PublicationCorresponds to variant dbSNP:rs1060505035EnsemblClinVar. | 1 |
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 |
CCDSi | CCDS47241.1 |
PIRi | S42105 |
RefSeqi | NP_001016.1, NM_001025.4 |
Genome annotation databases
Ensembli | ENST00000296674; ENSP00000296674; ENSG00000186468 ENST00000651545; ENSP00000498621; ENSG00000186468 |
GeneIDi | 6228 |
KEGGi | hsa:6228 |
UCSCi | uc003khu.4, human |
Similar proteinsi
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 |
CCDSi | CCDS47241.1 |
PIRi | S42105 |
RefSeqi | NP_001016.1, NM_001025.4 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
4CXG | electron microscopy | 8.70 | X | 1-143 | [»] | |
4CXH | electron microscopy | 8.90 | X | 1-143 | [»] | |
4UG0 | electron microscopy | - | SX | 1-143 | [»] | |
4V6X | electron microscopy | 5.00 | AX | 1-143 | [»] | |
5A2Q | electron microscopy | 3.90 | X | 1-143 | [»] | |
5AJ0 | electron microscopy | 3.50 | BX | 1-143 | [»] | |
5FLX | electron microscopy | 3.90 | X | 1-143 | [»] | |
5LKS | electron microscopy | 3.60 | SX | 1-143 | [»] | |
5OA3 | electron microscopy | 4.30 | X | 1-143 | [»] | |
5T2C | electron microscopy | 3.60 | AD | 1-143 | [»] | |
5VYC | X-ray | 6.00 | X1/X2/X3/X4/X5/X6 | 1-143 | [»] | |
6EK0 | electron microscopy | 2.90 | SX | 1-143 | [»] | |
6FEC | electron microscopy | 6.30 | Q | 1-142 | [»] | |
6G18 | electron microscopy | 3.60 | X | 1-143 | [»] | |
6G4S | electron microscopy | 4.00 | X | 1-143 | [»] | |
6G4W | electron microscopy | 4.50 | X | 1-143 | [»] | |
6G51 | electron microscopy | 4.10 | X | 1-143 | [»] | |
6G53 | electron microscopy | 4.50 | X | 1-143 | [»] | |
6G5H | electron microscopy | 3.60 | X | 1-143 | [»] | |
6G5I | electron microscopy | 3.50 | X | 1-143 | [»] | |
6IP5 | electron microscopy | 3.90 | 3B | 1-143 | [»] | |
6IP6 | electron microscopy | 4.50 | 3B | 1-143 | [»] | |
6IP8 | electron microscopy | 3.90 | 3B | 1-143 | [»] | |
6OLE | electron microscopy | 3.10 | SX | 2-142 | [»] | |
6OLF | electron microscopy | 3.90 | SX | 2-142 | [»] | |
6OLG | electron microscopy | 3.40 | BX | 2-140 | [»] | |
6OLI | electron microscopy | 3.50 | SX | 2-142 | [»] | |
6OLZ | electron microscopy | 3.90 | BX | 2-140 | [»] | |
6OM0 | electron microscopy | 3.10 | SX | 2-142 | [»] | |
6OM7 | electron microscopy | 3.70 | SX | 2-142 | [»] | |
6QZP | electron microscopy | 2.90 | SX | 2-142 | [»] | |
6Y0G | electron microscopy | 3.20 | SX | 1-143 | [»] | |
6Y2L | electron microscopy | 3.00 | SX | 1-143 | [»] | |
6Y57 | electron microscopy | 3.50 | SX | 1-143 | [»] | |
6Z6L | electron microscopy | 3.00 | SX | 1-143 | [»] | |
6Z6M | electron microscopy | 3.10 | SX | 1-143 | [»] | |
6Z6N | electron microscopy | 2.90 | SX | 1-143 | [»] | |
6ZLW | electron microscopy | 2.60 | X | 1-143 | [»] | |
6ZM7 | electron microscopy | 2.70 | SX | 1-143 | [»] | |
6ZME | electron microscopy | 3.00 | SX | 1-143 | [»] | |
6ZMI | electron microscopy | 2.60 | SX | 1-143 | [»] | |
6ZMO | electron microscopy | 3.10 | SX | 1-143 | [»] | |
6ZMT | electron microscopy | 3.00 | X | 1-143 | [»] | |
6ZN5 | electron microscopy | 3.20 | X | 2-142 | [»] | |
6ZOJ | electron microscopy | 2.80 | X | 1-143 | [»] | |
6ZOK | electron microscopy | 2.80 | X | 1-143 | [»] | |
6ZON | electron microscopy | 3.00 | j | 1-143 | [»] | |
6ZP4 | electron microscopy | 2.90 | j | 1-143 | [»] | |
6ZVH | electron microscopy | 2.90 | X | 2-142 | [»] | |
SMRi | P62266 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 112142, 207 interactors |
ComplexPortali | CPX-5223, 40S cytosolic small ribosomal subunit |
CORUMi | P62266 |
IntActi | P62266, 47 interactors |
MINTi | P62266 |
STRINGi | 9606.ENSP00000296674 |
PTM databases
iPTMneti | P62266 |
PhosphoSitePlusi | P62266 |
SwissPalmi | P62266 |
Polymorphism and mutation databases
BioMutai | RPS23 |
DMDMi | 50403755 |
Proteomic databases
EPDi | P62266 |
jPOSTi | P62266 |
MassIVEi | P62266 |
MaxQBi | P62266 |
PaxDbi | P62266 |
PeptideAtlasi | P62266 |
PRIDEi | P62266 |
ProteomicsDBi | 57380 |
TopDownProteomicsi | P62266 |
Protocols and materials databases
Antibodypediai | 24716, 130 antibodies |
Genome annotation databases
Ensembli | ENST00000296674; ENSP00000296674; ENSG00000186468 ENST00000651545; ENSP00000498621; ENSG00000186468 |
GeneIDi | 6228 |
KEGGi | hsa:6228 |
UCSCi | uc003khu.4, human |
Organism-specific databases
CTDi | 6228 |
DisGeNETi | 6228 |
EuPathDBi | HostDB:ENSG00000186468.12 |
GeneCardsi | RPS23 |
HGNCi | HGNC:10410, RPS23 |
HPAi | ENSG00000186468, Low tissue specificity |
MalaCardsi | RPS23 |
MIMi | 603683, gene 617412, phenotype |
neXtProti | NX_P62266 |
OpenTargetsi | ENSG00000186468 |
PharmGKBi | PA34813 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG1749, Eukaryota |
GeneTreei | ENSGT00550000074784 |
HOGENOMi | CLU_115574_0_1_1 |
InParanoidi | P62266 |
OMAi | KFRWSQR |
OrthoDBi | 1402984at2759 |
PhylomeDBi | P62266 |
TreeFami | TF300871 |
Enzyme and pathway databases
PathwayCommonsi | P62266 |
Reactomei | R-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-9633012, Response of EIF2AK4 (GCN2) to amino acid deficiency 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) |
Miscellaneous databases
BioGRID-ORCSi | 6228, 748 hits in 827 CRISPR screens |
ChiTaRSi | RPS23, human |
GeneWikii | RPS23 |
GenomeRNAii | 6228 |
Pharosi | P62266, Tbio |
PROi | PR:P62266 |
RNActi | P62266, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000186468, Expressed in female gonad and 201 other tissues |
ExpressionAtlasi | P62266, baseline and differential |
Genevisiblei | P62266, HS |
Family and domain databases
CDDi | cd03367, Ribosomal_S23, 1 hit |
InterProi | View protein in InterPro IPR012340, NA-bd_OB-fold IPR006032, Ribosomal_S12/S23 IPR005680, Ribosomal_S23_euk/arc |
PANTHERi | PTHR11652, PTHR11652, 1 hit |
Pfami | View protein in Pfam PF00164, Ribosom_S12_S23, 1 hit |
PIRSFi | PIRSF002133, Ribosomal_S12/S23, 1 hit |
SUPFAMi | SSF50249, SSF50249, 1 hit |
TIGRFAMsi | TIGR00982, uS12_E_A, 1 hit |
PROSITEi | View protein in PROSITE PS00055, RIBOSOMAL_S12, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | RS23_HUMAN | |
Accessioni | P62266Primary (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: | December 2, 2020 | |
This is version 161 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 5
Human chromosome 5: entries, gene names and cross-references to MIM - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Ribosomal proteins
Ribosomal proteins families and list of entries