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Protein

40S ribosomal protein S23-A

Gene

RPS23A

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. structural constituent of ribosome Source: SGD

GO - Biological processi

  1. maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: SGD
  2. regulation of translational fidelity Source: SGD
  3. translation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciYEAST:G3O-30825-MONOMER.
ReactomeiREACT_290856. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_302067. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_307259. Formation of a pool of free 40S subunits.
REACT_314339. SRP-dependent cotranslational protein targeting to membrane.
REACT_332565. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_335938. Ribosomal scanning and start codon recognition.
REACT_343353. Peptide chain elongation.
REACT_346847. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_351622. Formation of the ternary complex, and subsequently, the 43S complex.

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S23-A
Alternative name(s):
RP37
S28
YS14
Gene namesi
Name:RPS23A
Synonyms:RPS28A
Ordered Locus Names:YGR118W
ORF Names:G6178
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome VII

Organism-specific databases

CYGDiYGR118w.
SGDiS000003350. RPS23A.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytosolic small ribosomal subunit Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi64 – 641P → A: Lethal mutation. 1 Publication
Mutagenesisi65 – 651N → A: Lethal mutation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14514540S ribosomal protein S23-APRO_0000146482Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei64 – 6413,4-dihydroxyproline1 Publication

Post-translational modificationi

Hydroxylation at Pro-64 affects translation termination efficiency. The stereochemistry of the 3,4-dihydroxyproline has not yet been determined.1 Publication

Keywords - PTMi

Hydroxylation

Proteomic databases

MaxQBiP0CX29.
PRIDEiP0CX29.

Expressioni

Gene expression databases

ExpressionAtlasiP0CX29. differential.

Interactioni

Subunit structurei

Component of the small ribosomal subunit. Mature ribosomes consist of a small (40S) and a large (60S) subunit. The 40S subunit contains 32 different proteins (encoded by 56 genes) and 1 molecule of RNA (18S). The 60S subunit contains 46 different proteins (encoded by 81 genes) and 3 molecules of RNA (25S, 5.8S and 5S).1 Publication

Protein-protein interaction databases

BioGridi33363. 94 interactions.
36298. 23 interactions.

Structurei

Secondary structure

1
145
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni9 – 113Combined sources
Helixi12 – 2312Combined sources
Helixi27 – 348Combined sources
Helixi36 – 394Combined sources
Beta strandi40 – 434Combined sources
Beta strandi45 – 6016Combined sources
Beta strandi68 – 769Combined sources
Turni77 – 793Combined sources
Beta strandi82 – 865Combined sources
Beta strandi89 – 913Combined sources
Turni93 – 953Combined sources
Beta strandi101 – 1066Combined sources
Beta strandi108 – 1125Combined sources
Beta strandi115 – 1173Combined sources
Beta strandi122 – 1276Combined sources
Turni128 – 1303Combined sources
Helixi132 – 1365Combined sources
Beta strandi137 – 1404Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5Xmodel-L28-145[»]
3J6Xelectron microscopy6.10231-145[»]
3J6Yelectron microscopy6.10231-145[»]
3J77electron microscopy6.20231-145[»]
3J78electron microscopy6.30231-145[»]
3V88X-ray3.00X1-145[»]
4U3MX-ray3.00D3/d32-145[»]
4U3NX-ray3.20D3/d32-145[»]
4U3UX-ray2.90D3/d32-145[»]
4U4NX-ray3.10D3/d32-145[»]
4U4OX-ray3.60D3/d32-145[»]
4U4QX-ray3.00D3/d32-145[»]
4U4RX-ray2.80D3/d32-145[»]
4U4UX-ray3.00D3/d32-145[»]
4U4YX-ray3.20D3/d32-145[»]
4U4ZX-ray3.10D3/d32-145[»]
4U50X-ray3.20D3/d32-145[»]
4U51X-ray3.20D3/d32-145[»]
4U52X-ray3.00D3/d32-145[»]
4U53X-ray3.30D3/d32-145[»]
4U55X-ray3.20D3/d32-145[»]
4U56X-ray3.45D3/d32-145[»]
4U6FX-ray3.10D3/d32-145[»]
4V4Belectron microscopy11.70AL28-145[»]
4V6Ielectron microscopy8.80AL1-145[»]
4V7Helectron microscopy8.90L28-145[»]
4V7RX-ray4.00AP/CP1-145[»]
4V88X-ray3.00AX/CX1-145[»]
4V8Yelectron microscopy4.30AX1-145[»]
4V8Zelectron microscopy6.60AX1-145[»]
4V92electron microscopy3.70X2-143[»]
ProteinModelPortaliP0CX29.
SMRiP0CX29. Positions 2-145.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0CX29.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S12P family.Curated

Phylogenomic databases

InParanoidiP0CX29.
KOiK02973.
OrthoDBiEOG7SN8R7.

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. S23_S12_E_A. 1 hit.
PROSITEiPS00055. RIBOSOMAL_S12. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0CX29-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKGKPRGLN SARKLRVHRR NNRWAENNYK KRLLGTAFKS SPFGGSSHAK
60 70 80 90 100
GIVLEKLGIE SKQPNSAIRK CVRVQLIKNG KKVTAFVPND GCLNFVDEND
110 120 130 140
EVLLAGFGRK GKAKGDIPGV RFKVVKVSGV SLLALWKEKK EKPRS
Length:145
Mass (Da):16,038
Last modified:June 28, 2011 - v1
Checksum:i5A89ADF540DA1311
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96570 Unassigned RNA. Translation: AAA16235.1.
Z72903 Genomic DNA. Translation: CAA97128.1.
BK006941 Genomic DNA. Translation: DAA08210.1.
PIRiA46703.
RefSeqiNP_011633.3. NM_001181247.3.
NP_015457.1. NM_001184229.1.

Genome annotation databases

EnsemblFungiiYGR118W; YGR118W; YGR118W.
YPR132W; YPR132W; YPR132W.
GeneIDi853015.
856250.
KEGGisce:YGR118W.
sce:YPR132W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96570 Unassigned RNA. Translation: AAA16235.1.
Z72903 Genomic DNA. Translation: CAA97128.1.
BK006941 Genomic DNA. Translation: DAA08210.1.
PIRiA46703.
RefSeqiNP_011633.3. NM_001181247.3.
NP_015457.1. NM_001184229.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5Xmodel-L28-145[»]
3J6Xelectron microscopy6.10231-145[»]
3J6Yelectron microscopy6.10231-145[»]
3J77electron microscopy6.20231-145[»]
3J78electron microscopy6.30231-145[»]
3V88X-ray3.00X1-145[»]
4U3MX-ray3.00D3/d32-145[»]
4U3NX-ray3.20D3/d32-145[»]
4U3UX-ray2.90D3/d32-145[»]
4U4NX-ray3.10D3/d32-145[»]
4U4OX-ray3.60D3/d32-145[»]
4U4QX-ray3.00D3/d32-145[»]
4U4RX-ray2.80D3/d32-145[»]
4U4UX-ray3.00D3/d32-145[»]
4U4YX-ray3.20D3/d32-145[»]
4U4ZX-ray3.10D3/d32-145[»]
4U50X-ray3.20D3/d32-145[»]
4U51X-ray3.20D3/d32-145[»]
4U52X-ray3.00D3/d32-145[»]
4U53X-ray3.30D3/d32-145[»]
4U55X-ray3.20D3/d32-145[»]
4U56X-ray3.45D3/d32-145[»]
4U6FX-ray3.10D3/d32-145[»]
4V4Belectron microscopy11.70AL28-145[»]
4V6Ielectron microscopy8.80AL1-145[»]
4V7Helectron microscopy8.90L28-145[»]
4V7RX-ray4.00AP/CP1-145[»]
4V88X-ray3.00AX/CX1-145[»]
4V8Yelectron microscopy4.30AX1-145[»]
4V8Zelectron microscopy6.60AX1-145[»]
4V92electron microscopy3.70X2-143[»]
ProteinModelPortaliP0CX29.
SMRiP0CX29. Positions 2-145.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33363. 94 interactions.
36298. 23 interactions.

Proteomic databases

MaxQBiP0CX29.
PRIDEiP0CX29.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR118W; YGR118W; YGR118W.
YPR132W; YPR132W; YPR132W.
GeneIDi853015.
856250.
KEGGisce:YGR118W.
sce:YPR132W.

Organism-specific databases

CYGDiYGR118w.
SGDiS000003350. RPS23A.

Phylogenomic databases

InParanoidiP0CX29.
KOiK02973.
OrthoDBiEOG7SN8R7.

Enzyme and pathway databases

BioCyciYEAST:G3O-30825-MONOMER.
ReactomeiREACT_290856. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_302067. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_307259. Formation of a pool of free 40S subunits.
REACT_314339. SRP-dependent cotranslational protein targeting to membrane.
REACT_332565. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_335938. Ribosomal scanning and start codon recognition.
REACT_343353. Peptide chain elongation.
REACT_346847. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_351622. Formation of the ternary complex, and subsequently, the 43S complex.

Miscellaneous databases

EvolutionaryTraceiP0CX29.
NextBioi972878.

Gene expression databases

ExpressionAtlasiP0CX29. differential.

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. S23_S12_E_A. 1 hit.
PROSITEiPS00055. RIBOSOMAL_S12. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel cloning strategy reveals the gene for the yeast homologue to Escherichia coli ribosomal protein S12."
    Alksne L.E., Warner J.R.
    J. Biol. Chem. 268:10813-10819(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The sequence of a 23.4 kb segment on the right arm of chromosome VII from Saccharomyces cerevisiae reveals CLB6, SPT6, RP28A and NUP57 genes, a Ty3 element and 11 new open reading frames."
    Hansen M., Albers M., Backes U., Coblenz A., Leuther H., Neu R., Schreer A., Schaefer B., Zimmermann M., Wolf K.
    Yeast 12:1273-1277(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae."
    Planta R.J., Mager W.H.
    Yeast 14:471-477(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NOMENCLATURE, SUBUNIT.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: HYDROXYLATION AT PRO-64, MUTAGENESIS OF PRO-64 AND ASN-65.
  10. "Structure of the 80S ribosome from Saccharomyces cerevisiae -- tRNA-ribosome and subunit-subunit interactions."
    Spahn C.M.T., Beckmann R., Eswar N., Penczek P.A., Sali A., Blobel G., Frank J.
    Cell 107:373-386(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING OF 28-145, ELECTRON MICROSCOPY.
  11. "Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation."
    Spahn C.M.T., Gomez-Lorenzo M.G., Grassucci R.A., Joergensen R., Andersen G.R., Beckmann R., Penczek P.A., Ballesta J.P.G., Frank J.
    EMBO J. 23:1008-1019(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING OF 28-145, ELECTRON MICROSCOPY.

Entry informationi

Entry nameiRS23A_YEAST
AccessioniPrimary (citable) accession number: P0CX29
Secondary accession number(s): D6VUP9, P32827
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: June 28, 2011
Last modified: April 1, 2015
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 10600 molecules/cell in log phase SD medium.1 Publication
There are 2 genes for S23 in yeast.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Ribosomal proteins
    Ribosomal proteins families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

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.