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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: -Experimental evidence at protein leveli

Functioni

Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. 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.1 Publication

Miscellaneous

Present with 10600 molecules/cell in log phase SD medium.1 Publication
There are 2 genes for uS12 in yeast.Curated

GO - Molecular functioni

  • structural constituent of ribosome Source: SGD

GO - Biological processi

  • maintenance of translational fidelity Source: UniProtKB
  • maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: SGD
  • regulation of translational fidelity Source: SGD

Keywordsi

Molecular functionRibonucleoprotein, 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-A1 Publication
Alternative name(s):
RP37
S28
Small ribosomal subunit protein uS12-A1 Publication
YS14
Gene namesi
Name:RPS23A1 Publication
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

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

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
PaxDbiP0CX29
PRIDEiP0CX29

PTM databases

iPTMnetiP0CX29

Expressioni

Gene expression databases

ExpressionAtlasiP0CX29 differential

Interactioni

Subunit structurei

Component of the small ribosomal subunit (SSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102).1 Publication1 Publication

Protein-protein interaction databases

BioGridi33363, 195 interactors
36298, 73 interactors
STRINGi4932.YPR132W

Structurei

Secondary structure

1145
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi12 – 22Combined sources11
Helixi23 – 25Combined sources3
Helixi27 – 33Combined sources7
Helixi36 – 39Combined sources4
Beta strandi45 – 47Combined sources3
Beta strandi49 – 58Combined sources10
Beta strandi63 – 65Combined sources3
Beta strandi70 – 76Combined sources7
Turni77 – 80Combined sources4
Beta strandi81 – 86Combined sources6
Beta strandi101 – 106Combined sources6
Turni113 – 116Combined sources4
Beta strandi122 – 127Combined sources6
Helixi132 – 136Combined sources5

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[»]
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[»]
5DGEX-ray3.45D3/d32-145[»]
5DGFX-ray3.30D3/d32-145[»]
5DGVX-ray3.10D3/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[»]
5LL6electron microscopy3.90c1-145[»]
5M1Jelectron microscopy3.30X22-145[»]
5MC6electron microscopy3.80c1-145[»]
5MEIX-ray3.50Y/d32-145[»]
5NDGX-ray3.70D3/d32-145[»]
5NDVX-ray3.30D3/d32-145[»]
5NDWX-ray3.70D3/d32-145[»]
5OBMX-ray3.40D3/d32-145[»]
5ON6X-ray3.10Y/d32-145[»]
5TBWX-ray3.00Y/d32-145[»]
5TGAX-ray3.30D3/d32-145[»]
5TZSelectron microscopy5.10r1-145[»]
5WYJelectron microscopy8.70SY1-145[»]
5WYKelectron microscopy4.50SY1-145[»]
6EMLelectron microscopy3.60c1-145[»]
6FAIelectron microscopy3.40X1-145[»]
ProteinModelPortaliP0CX29
SMRiP0CX29
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0CX29

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

InParanoidiP0CX29
KOiK02973
OMAiKFRWSQR
OrthoDBiEOG092C58LL

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.

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

Similar proteinsi

Entry informationi

Entry nameiRS23A_YEAST
AccessioniPrimary (citable) accession number: P0CX29
Secondary accession number(s): D6VUP9, P32827
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: June 28, 2011
Last modified: May 23, 2018
This is version 63 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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