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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

  • structural constituent of ribosome Source: SGD

GO - Biological processi

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

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciYEAST:G3O-30825-MONOMER.
ReactomeiR-SCE-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-SCE-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-SCE-72689. Formation of a pool of free 40S subunits.
R-SCE-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-SCE-72702. Ribosomal scanning and start codon recognition.
R-SCE-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-SCE-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-SCE-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

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
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

SGDiS000003350. RPS23A.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi64P → A: Lethal mutation. 1 Publication1
Mutagenesisi65N → A: Lethal mutation. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001464821 – 14540S ribosomal protein S23-AAdd BLAST145

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki56Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei643,4-dihydroxyproline1 Publication1

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, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP0CX29.
PRIDEiP0CX29.

Expressioni

Gene expression databases

ExpressionAtlasiP0CX29. baseline.

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. 79 interactors.
36298. 24 interactors.

Structurei

Secondary structure

1145
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni9 – 11Combined sources3
Helixi12 – 23Combined sources12
Helixi27 – 34Combined sources8
Helixi36 – 39Combined sources4
Beta strandi40 – 43Combined sources4
Beta strandi45 – 60Combined sources16
Beta strandi68 – 76Combined sources9
Turni77 – 79Combined sources3
Beta strandi82 – 86Combined sources5
Beta strandi89 – 91Combined sources3
Turni93 – 95Combined sources3
Beta strandi101 – 106Combined sources6
Beta strandi108 – 112Combined sources5
Beta strandi115 – 117Combined sources3
Beta strandi122 – 127Combined sources6
Turni128 – 130Combined sources3
Helixi132 – 136Combined sources5
Beta strandi137 – 140Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5DATX-ray3.15D3/d32-145[»]
5DC3X-ray3.25D3/d32-145[»]
5FCIX-ray3.40D3/d32-145[»]
5FCJX-ray3.10D3/d32-145[»]
5I4LX-ray3.10D3/d32-145[»]
5JUOelectron microscopy4.00UB1-145[»]
5JUPelectron microscopy3.50UB1-145[»]
5JUSelectron microscopy4.20UB1-145[»]
5JUTelectron microscopy4.00UB1-145[»]
5JUUelectron microscopy4.00UB1-145[»]
ProteinModelPortaliP0CX29.
SMRiP0CX29.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0CX29.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S12P family.Curated

Phylogenomic databases

InParanoidiP0CX29.
KOiK02973.
OrthoDBiEOG092C58LL.

Family and domain databases

CDDicd03367. Ribosomal_S23. 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.

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
PDB 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[»]
5DATX-ray3.15D3/d32-145[»]
5DC3X-ray3.25D3/d32-145[»]
5FCIX-ray3.40D3/d32-145[»]
5FCJX-ray3.10D3/d32-145[»]
5I4LX-ray3.10D3/d32-145[»]
5JUOelectron microscopy4.00UB1-145[»]
5JUPelectron microscopy3.50UB1-145[»]
5JUSelectron microscopy4.20UB1-145[»]
5JUTelectron microscopy4.00UB1-145[»]
5JUUelectron microscopy4.00UB1-145[»]
ProteinModelPortaliP0CX29.
SMRiP0CX29.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33363. 79 interactors.
36298. 24 interactors.

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

SGDiS000003350. RPS23A.

Phylogenomic databases

InParanoidiP0CX29.
KOiK02973.
OrthoDBiEOG092C58LL.

Enzyme and pathway databases

BioCyciYEAST:G3O-30825-MONOMER.
ReactomeiR-SCE-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-SCE-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-SCE-72689. Formation of a pool of free 40S subunits.
R-SCE-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-SCE-72702. Ribosomal scanning and start codon recognition.
R-SCE-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-SCE-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-SCE-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

EvolutionaryTraceiP0CX29.
PROiP0CX29.

Gene expression databases

ExpressionAtlasiP0CX29. baseline.

Family and domain databases

CDDicd03367. Ribosomal_S23. 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...

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: November 30, 2016
This is version 49 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

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 one 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.