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Protein

40S ribosomal protein S28-B

Gene

RPS28B

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

  • cytoplasmic translation Source: SGD
  • positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: SGD
  • rRNA export from nucleus Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciYEAST:G3O-32364-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-B
Alternative name(s):
S33
YS27
Gene namesi
Name:RPS28B
Synonyms:RPS33B
Ordered Locus Names:YLR264W
ORF Names:L8479.5
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR264W.
SGDiS000004254. RPS28B.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 676740S ribosomal protein S28-BPRO_0000136843Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources1 Publication

Post-translational modificationi

N-terminally acetylated by acetyltransferase NatB.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

TopDownProteomicsiP0C0X0.

PTM databases

iPTMnetiP0C0X0.

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

Binary interactionsi

WithEntry#Exp.IntActNotes
DCP1Q125173EBI-16112,EBI-38519
EDC3P399983EBI-16112,EBI-22300

Protein-protein interaction databases

BioGridi31532. 65 interactions.
DIPiDIP-1389N.
IntActiP0C0X0. 16 interactions.
MINTiMINT-390389.

Structurei

3D structure databases

ProteinModelPortaliP0C0X0.
SMRiP0C0X0. Positions 5-67.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S28e family.Curated

Phylogenomic databases

HOGENOMiHOG000224552.
InParanoidiP0C0X0.
KOiK02979.
OMAiILCLLET.
OrthoDBiEOG7NCVH3.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
HAMAPiMF_00292. Ribosomal_S28e.
InterProiIPR012340. NA-bd_OB-fold.
IPR000289. Ribosomal_S28e.
IPR028626. Ribosomal_S28e_CS.
[Graphical view]
PANTHERiPTHR10769. PTHR10769. 1 hit.
PfamiPF01200. Ribosomal_S28e. 1 hit.
[Graphical view]
ProDomiPD005541. Ribosomal_S28e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF50249. SSF50249. 1 hit.
PROSITEiPS00961. RIBOSOMAL_S28E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0C0X0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSKTPVTLA KVIKVLGRTG SRGGVTQVRV EFLEDTSRTI VRNVKGPVRE
60
NDILVLMESE REARRLR
Length:67
Mass (Da):7,565
Last modified:January 10, 2006 - v1
Checksum:iABF5A8353F18A641
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U17244 Genomic DNA. Translation: AAB67375.1.
BK006945 Genomic DNA. Translation: DAA09577.1.
PIRiS51401.
RefSeqiNP_013366.1. NM_001182151.1.

Genome annotation databases

EnsemblFungiiYLR264W; YLR264W; YLR264W.
GeneIDi850969.
KEGGisce:YLR264W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U17244 Genomic DNA. Translation: AAB67375.1.
BK006945 Genomic DNA. Translation: DAA09577.1.
PIRiS51401.
RefSeqiNP_013366.1. NM_001182151.1.

3D structure databases

ProteinModelPortaliP0C0X0.
SMRiP0C0X0. Positions 5-67.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31532. 65 interactions.
DIPiDIP-1389N.
IntActiP0C0X0. 16 interactions.
MINTiMINT-390389.

PTM databases

iPTMnetiP0C0X0.

Proteomic databases

TopDownProteomicsiP0C0X0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR264W; YLR264W; YLR264W.
GeneIDi850969.
KEGGisce:YLR264W.

Organism-specific databases

EuPathDBiFungiDB:YLR264W.
SGDiS000004254. RPS28B.

Phylogenomic databases

HOGENOMiHOG000224552.
InParanoidiP0C0X0.
KOiK02979.
OMAiILCLLET.
OrthoDBiEOG7NCVH3.

Enzyme and pathway databases

BioCyciYEAST:G3O-32364-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

NextBioi967463.
PROiP0C0X0.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
HAMAPiMF_00292. Ribosomal_S28e.
InterProiIPR012340. NA-bd_OB-fold.
IPR000289. Ribosomal_S28e.
IPR028626. Ribosomal_S28e_CS.
[Graphical view]
PANTHERiPTHR10769. PTHR10769. 1 hit.
PfamiPF01200. Ribosomal_S28e. 1 hit.
[Graphical view]
ProDomiPD005541. Ribosomal_S28e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF50249. SSF50249. 1 hit.
PROSITEiPS00961. RIBOSOMAL_S28E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae."
    Planta R.J., Mager W.H.
    Yeast 14:471-477(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NOMENCLATURE, SUBUNIT.
  4. "The action of N-terminal acetyltransferases on yeast ribosomal proteins."
    Arnold R.J., Polevoda B., Reilly J.P., Sherman F.
    J. Biol. Chem. 274:37035-37040(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT MET-1 BY NATB.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRS28B_YEAST
AccessioniPrimary (citable) accession number: P0C0X0
Secondary accession number(s): D6VYR1, P02380
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 10, 2006
Last modified: May 11, 2016
This is version 91 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 8600 molecules/cell in log phase SD medium.1 Publication
There are 2 genes for S28 in yeast.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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