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Protein

40S ribosomal protein S28-A

Gene

RPS28A

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

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 94500 molecules/cell in log phase SD medium.1 Publication
There are 2 genes for eS28 in yeast.Curated

GO - Molecular functioni

  • RNA binding Source: GO_Central
  • structural constituent of ribosome Source: SGD

GO - Biological processi

  • cytoplasmic translation Source: SGD
  • maturation of SSU-rRNA Source: GO_Central
  • positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: SGD
  • ribosomal small subunit assembly Source: GO_Central
  • rRNA export from nucleus Source: SGD

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciYEAST:G3O-33683-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 S28-A1 Publication
Alternative name(s):
S33
Small ribosomal subunit protein eS28-A1 Publication
YS27
Gene namesi
Name:RPS28A1 Publication
Synonyms:RPS33, RPS33A
Ordered Locus Names:YOR167C
ORF Names:O3600
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR167C.
SGDiS000005693. RPS28A.

Subcellular locationi

GO - Cellular componenti

  • cytosolic small ribosomal subunit Source: SGD

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001368421 – 6740S ribosomal protein S28-AAdd BLAST67

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1 Publication1

Post-translational modificationi

N-terminally acetylated by acetyltransferase NatB.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ3E7X9.
PRIDEiQ3E7X9.
TopDownProteomicsiQ3E7X9.

PTM databases

iPTMnetiQ3E7X9.

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

BioGridi34563. 109 interactors.
DIPiDIP-29384N.
IntActiQ3E7X9. 2 interactors.
MINTiMINT-390375.

Structurei

Secondary structure

167
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 23Combined sources15
Beta strandi25 – 35Combined sources11
Beta strandi39 – 46Combined sources8
Beta strandi53 – 55Combined sources3
Beta strandi57 – 60Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J6Xelectron microscopy6.10281-67[»]
3J6Yelectron microscopy6.10281-67[»]
3J77electron microscopy6.20281-67[»]
3J78electron microscopy6.30281-67[»]
3V88X-ray3.00c1-67[»]
4U3MX-ray3.00D8/d82-67[»]
4U3NX-ray3.20D8/d82-67[»]
4U3UX-ray2.90D8/d82-67[»]
4U4NX-ray3.10D8/d82-67[»]
4U4OX-ray3.60D8/d82-67[»]
4U4QX-ray3.00D8/d82-67[»]
4U4RX-ray2.80D8/d82-67[»]
4U4UX-ray3.00D8/d82-67[»]
4U4YX-ray3.20D8/d82-67[»]
4U4ZX-ray3.10D8/d82-67[»]
4U50X-ray3.20D8/d82-67[»]
4U51X-ray3.20D8/d82-67[»]
4U52X-ray3.00D8/d82-67[»]
4U53X-ray3.30D8/d82-67[»]
4U55X-ray3.20D8/d82-67[»]
4U56X-ray3.45D8/d82-67[»]
4U6FX-ray3.10D8/d82-67[»]
4V6Ielectron microscopy8.80AY1-67[»]
4V7RX-ray4.00AR/CR1-67[»]
4V88X-ray3.00Ac/Cc1-67[»]
4V8Yelectron microscopy4.30A21-67[»]
4V8Zelectron microscopy6.60A21-67[»]
4V92electron microscopy3.70c5-67[»]
5DATX-ray3.15D8/d82-67[»]
5DC3X-ray3.25D8/d82-67[»]
5DGEX-ray3.45D8/d82-67[»]
5DGFX-ray3.30D8/d82-67[»]
5DGVX-ray3.10D8/d82-67[»]
5FCIX-ray3.40D8/d82-67[»]
5FCJX-ray3.10D8/d82-67[»]
5I4LX-ray3.10D8/d85-67[»]
5JPQelectron microscopy7.3011-67[»]
5JUOelectron microscopy4.00ZB1-67[»]
5JUPelectron microscopy3.50ZB1-67[»]
5JUSelectron microscopy4.20ZB1-67[»]
5JUTelectron microscopy4.00ZB1-67[»]
5JUUelectron microscopy4.00ZB1-67[»]
5LYBX-ray3.25D8/d85-67[»]
5TGAX-ray3.30D8/d85-67[»]
5TGMX-ray3.50D8/d85-67[»]
5TZSelectron microscopy5.10G1-67[»]
ProteinModelPortaliQ3E7X9.
SMRiQ3E7X9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000003580.
HOGENOMiHOG000224552.
InParanoidiQ3E7X9.
KOiK02979.
OMAiPVRTNDI.
OrthoDBiEOG092C5Y3A.

Family and domain databases

CDDicd04457. S1_S28E. 1 hit.
HAMAPiMF_00292. Ribosomal_S28e. 1 hit.
InterProiView protein in InterPro
IPR012340. NA-bd_OB-fold.
IPR000289. Ribosomal_S28e.
IPR028626. Ribosomal_S28e_CS.
PANTHERiPTHR10769. PTHR10769. 1 hit.
PfamiView protein in Pfam
PF01200. Ribosomal_S28e. 1 hit.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD005541. Ribosomal_S28e. 1 hit.
SUPFAMiSSF50249. SSF50249. 1 hit.
PROSITEiView protein in PROSITE
PS00961. RIBOSOMAL_S28E. 1 hit.

Sequencei

Sequence statusi: Complete.

Q3E7X9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDNKTPVTLA KVIKVLGRTG SRGGVTQVRV EFLEDTSRTI VRNVKGPVRE
60
NDILVLMESE REARRLR
Length:67
Mass (Da):7,592
Last modified:November 8, 2005 - v1
Checksum:iBA145824DEE8A641
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00128 Genomic DNA. Translation: CAA24958.1.
U55021 Genomic DNA. Translation: AAB47414.1.
Z75075 Genomic DNA. Translation: CAA99373.1.
AY692746 Genomic DNA. Translation: AAT92765.1.
BK006948 Genomic DNA. Translation: DAA10941.1.
PIRiA02750. R3BY33.
RefSeqiNP_014810.1. NM_001183586.1.

Genome annotation databases

EnsemblFungiiYOR167C; YOR167C; YOR167C.
GeneIDi854338.
KEGGisce:YOR167C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00128 Genomic DNA. Translation: CAA24958.1.
U55021 Genomic DNA. Translation: AAB47414.1.
Z75075 Genomic DNA. Translation: CAA99373.1.
AY692746 Genomic DNA. Translation: AAT92765.1.
BK006948 Genomic DNA. Translation: DAA10941.1.
PIRiA02750. R3BY33.
RefSeqiNP_014810.1. NM_001183586.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J6Xelectron microscopy6.10281-67[»]
3J6Yelectron microscopy6.10281-67[»]
3J77electron microscopy6.20281-67[»]
3J78electron microscopy6.30281-67[»]
3V88X-ray3.00c1-67[»]
4U3MX-ray3.00D8/d82-67[»]
4U3NX-ray3.20D8/d82-67[»]
4U3UX-ray2.90D8/d82-67[»]
4U4NX-ray3.10D8/d82-67[»]
4U4OX-ray3.60D8/d82-67[»]
4U4QX-ray3.00D8/d82-67[»]
4U4RX-ray2.80D8/d82-67[»]
4U4UX-ray3.00D8/d82-67[»]
4U4YX-ray3.20D8/d82-67[»]
4U4ZX-ray3.10D8/d82-67[»]
4U50X-ray3.20D8/d82-67[»]
4U51X-ray3.20D8/d82-67[»]
4U52X-ray3.00D8/d82-67[»]
4U53X-ray3.30D8/d82-67[»]
4U55X-ray3.20D8/d82-67[»]
4U56X-ray3.45D8/d82-67[»]
4U6FX-ray3.10D8/d82-67[»]
4V6Ielectron microscopy8.80AY1-67[»]
4V7RX-ray4.00AR/CR1-67[»]
4V88X-ray3.00Ac/Cc1-67[»]
4V8Yelectron microscopy4.30A21-67[»]
4V8Zelectron microscopy6.60A21-67[»]
4V92electron microscopy3.70c5-67[»]
5DATX-ray3.15D8/d82-67[»]
5DC3X-ray3.25D8/d82-67[»]
5DGEX-ray3.45D8/d82-67[»]
5DGFX-ray3.30D8/d82-67[»]
5DGVX-ray3.10D8/d82-67[»]
5FCIX-ray3.40D8/d82-67[»]
5FCJX-ray3.10D8/d82-67[»]
5I4LX-ray3.10D8/d85-67[»]
5JPQelectron microscopy7.3011-67[»]
5JUOelectron microscopy4.00ZB1-67[»]
5JUPelectron microscopy3.50ZB1-67[»]
5JUSelectron microscopy4.20ZB1-67[»]
5JUTelectron microscopy4.00ZB1-67[»]
5JUUelectron microscopy4.00ZB1-67[»]
5LYBX-ray3.25D8/d85-67[»]
5TGAX-ray3.30D8/d85-67[»]
5TGMX-ray3.50D8/d85-67[»]
5TZSelectron microscopy5.10G1-67[»]
ProteinModelPortaliQ3E7X9.
SMRiQ3E7X9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34563. 109 interactors.
DIPiDIP-29384N.
IntActiQ3E7X9. 2 interactors.
MINTiMINT-390375.

PTM databases

iPTMnetiQ3E7X9.

Proteomic databases

MaxQBiQ3E7X9.
PRIDEiQ3E7X9.
TopDownProteomicsiQ3E7X9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR167C; YOR167C; YOR167C.
GeneIDi854338.
KEGGisce:YOR167C.

Organism-specific databases

EuPathDBiFungiDB:YOR167C.
SGDiS000005693. RPS28A.

Phylogenomic databases

GeneTreeiENSGT00390000003580.
HOGENOMiHOG000224552.
InParanoidiQ3E7X9.
KOiK02979.
OMAiPVRTNDI.
OrthoDBiEOG092C5Y3A.

Enzyme and pathway databases

BioCyciYEAST:G3O-33683-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

PROiPR:Q3E7X9.

Family and domain databases

CDDicd04457. S1_S28E. 1 hit.
HAMAPiMF_00292. Ribosomal_S28e. 1 hit.
InterProiView protein in InterPro
IPR012340. NA-bd_OB-fold.
IPR000289. Ribosomal_S28e.
IPR028626. Ribosomal_S28e_CS.
PANTHERiPTHR10769. PTHR10769. 1 hit.
PfamiView protein in Pfam
PF01200. Ribosomal_S28e. 1 hit.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD005541. Ribosomal_S28e. 1 hit.
SUPFAMiSSF50249. SSF50249. 1 hit.
PROSITEiView protein in PROSITE
PS00961. RIBOSOMAL_S28E. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRS28A_YEAST
AccessioniPrimary (citable) accession number: Q3E7X9
Secondary accession number(s): D6W2M5, P02380
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 8, 2005
Last modified: April 12, 2017
This is version 102 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

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 XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: 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.