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Protein

40S ribosomal protein S0-A

Gene

RPS0A

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

Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits.UniRule annotation2 Publications

GO - Molecular functioni

  • structural constituent of ribosome Source: SGD

GO - Biological processi

  • cytoplasmic translation Source: SGD
  • endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: SGD
  • endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: SGD
  • ribosomal small subunit assembly Source: SGD
  • rRNA export from nucleus Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Biological processi

Ribosome biogenesis, rRNA processing

Enzyme and pathway databases

BioCyciYEAST:G3O-30896-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 S0-AUniRule annotation
Alternative name(s):
Nucleic acid-binding protein NAB1A
Gene namesi
Name:RPS0AUniRule annotation
Synonyms:NAB1, NAB1A, YST1
Ordered Locus Names:YGR214W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGR214W.
SGDiS000003446. RPS0A.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Reduction in growth rate, a decrease in free 40S subunits, an increase in the amount of free 60S subunits and a decrease in polysome size.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedUniRule annotation2 Publications
ChainiPRO_00001343702 – 25240S ribosomal protein S0-AAdd BLAST251

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineUniRule annotation2 Publications1

Post-translational modificationi

N-terminally acetylated by acetyltransferase NatA.2 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP32905.
PRIDEiP32905.
TopDownProteomicsiP32905.

2D gel databases

SWISS-2DPAGEP32905.

PTM databases

iPTMnetiP32905.

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).2 Publications

Protein-protein interaction databases

BioGridi33467. 109 interactors.
DIPiDIP-5553N.
IntActiP32905. 155 interactors.
MINTiMINT-562708.

Structurei

Secondary structure

1252
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 8Combined sources4
Helixi11 – 20Combined sources10
Turni21 – 23Combined sources3
Helixi31 – 36Combined sources6
Beta strandi37 – 41Combined sources5
Turni42 – 44Combined sources3
Beta strandi45 – 48Combined sources4
Helixi50 – 64Combined sources15
Beta strandi67 – 69Combined sources3
Helixi70 – 72Combined sources3
Beta strandi73 – 77Combined sources5
Helixi80 – 92Combined sources13
Beta strandi96 – 100Combined sources5
Beta strandi106 – 108Combined sources3
Beta strandi112 – 114Combined sources3
Beta strandi119 – 124Combined sources6
Turni126 – 129Combined sources4
Helixi130 – 137Combined sources8
Turni138 – 140Combined sources3
Beta strandi143 – 147Combined sources5
Beta strandi149 – 151Combined sources3
Beta strandi157 – 161Combined sources5
Beta strandi164 – 166Combined sources3
Helixi169 – 182Combined sources14
Beta strandi183 – 187Combined sources5
Beta strandi190 – 192Combined sources3
Helixi199 – 201Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Xmodel-B14-198[»]
3J6Xelectron microscopy6.10S01-252[»]
3J6Yelectron microscopy6.10S01-252[»]
3J77electron microscopy6.20S01-252[»]
3J78electron microscopy6.30S01-252[»]
3V88X-ray3.00A1-252[»]
4U3MX-ray3.00S0/s02-252[»]
4U3NX-ray3.20S0/s02-252[»]
4U3UX-ray2.90S0/s02-252[»]
4U4NX-ray3.10S0/s02-252[»]
4U4OX-ray3.60S0/s02-252[»]
4U4QX-ray3.00S0/s02-252[»]
4U4RX-ray2.80S0/s02-252[»]
4U4UX-ray3.00S0/s02-252[»]
4U4YX-ray3.20S0/s02-252[»]
4U4ZX-ray3.10S0/s02-252[»]
4U50X-ray3.20S0/s02-252[»]
4U51X-ray3.20S0/s02-252[»]
4U52X-ray3.00S0/s02-252[»]
4U53X-ray3.30S0/s02-252[»]
4U55X-ray3.20S0/s02-252[»]
4U56X-ray3.45S0/s02-252[»]
4U6FX-ray3.10S0/s02-252[»]
4V4Belectron microscopy11.70AB14-198[»]
4V6Ielectron microscopy8.80AA1-252[»]
4V7RX-ray4.00AA/CA1-252[»]
4V88X-ray3.00AA/CA1-252[»]
4V8Yelectron microscopy4.30AA1-252[»]
4V8Zelectron microscopy6.60AA1-252[»]
4V92electron microscopy3.70A2-207[»]
5DATX-ray3.15S0/s02-252[»]
5DC3X-ray3.25S0/s02-252[»]
5FCIX-ray3.40S0/s02-252[»]
5FCJX-ray3.10S0/s02-252[»]
5I4LX-ray3.10S0/s02-207[»]
5JUOelectron microscopy4.00XA1-252[»]
5JUPelectron microscopy3.50XA1-252[»]
5JUSelectron microscopy4.20XA1-252[»]
5JUTelectron microscopy4.00XA1-252[»]
5JUUelectron microscopy4.00XA1-252[»]
ProteinModelPortaliP32905.
SMRiP32905.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32905.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S2P family.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00390000015036.
HOGENOMiHOG000232073.
InParanoidiP32905.
KOiK02998.
OMAiAPKESQW.
OrthoDBiEOG092C4HTX.

Family and domain databases

CDDicd01425. RPS2. 1 hit.
HAMAPiMF_03015. Ribosomal_S2_euk. 1 hit.
InterProiIPR001865. Ribosomal_S2.
IPR018130. Ribosomal_S2_CS.
IPR027498. Ribosomal_S2_euk.
IPR005707. Ribosomal_S2_euk/arc.
IPR023591. Ribosomal_S2_flav_dom.
[Graphical view]
PANTHERiPTHR11489. PTHR11489. 1 hit.
PfamiPF00318. Ribosomal_S2. 2 hits.
[Graphical view]
PRINTSiPR00395. RIBOSOMALS2.
SUPFAMiSSF52313. SSF52313. 1 hit.
TIGRFAMsiTIGR01012. uS2_euk_arch. 1 hit.
PROSITEiPS00962. RIBOSOMAL_S2_1. 1 hit.
PS00963. RIBOSOMAL_S2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P32905-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLPATFDLT PEDAQLLLAA NTHLGARNVQ VHQEPYVFNA RPDGVHVINV
60 70 80 90 100
GKTWEKLVLA ARIIAAIPNP EDVVAISSRT FGQRAVLKFA AHTGATPIAG
110 120 130 140 150
RFTPGSFTNY ITRSFKEPRL VIVTDPRSDA QAIKEASYVN IPVIALTDLD
160 170 180 190 200
SPSEFVDVAI PCNNRGKHSI GLIWYLLARE VLRLRGALVD RTQPWSIMPD
210 220 230 240 250
LYFYRDPEEV EQQVAEEATT EEAGEEEAKE EVTEEQAEAT EWAEENADNV

EW
Length:252
Mass (Da):28,024
Last modified:January 23, 2007 - v3
Checksum:iD6F263456282C771
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M88277 Genomic DNA. Translation: AAB05643.1.
Z72999 Genomic DNA. Translation: CAA97241.1.
BK006941 Genomic DNA. Translation: DAA08308.1.
PIRiS42143.
RefSeqiNP_011730.1. NM_001181343.1.

Genome annotation databases

EnsemblFungiiYGR214W; YGR214W; YGR214W.
GeneIDi853128.
KEGGisce:YGR214W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M88277 Genomic DNA. Translation: AAB05643.1.
Z72999 Genomic DNA. Translation: CAA97241.1.
BK006941 Genomic DNA. Translation: DAA08308.1.
PIRiS42143.
RefSeqiNP_011730.1. NM_001181343.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Xmodel-B14-198[»]
3J6Xelectron microscopy6.10S01-252[»]
3J6Yelectron microscopy6.10S01-252[»]
3J77electron microscopy6.20S01-252[»]
3J78electron microscopy6.30S01-252[»]
3V88X-ray3.00A1-252[»]
4U3MX-ray3.00S0/s02-252[»]
4U3NX-ray3.20S0/s02-252[»]
4U3UX-ray2.90S0/s02-252[»]
4U4NX-ray3.10S0/s02-252[»]
4U4OX-ray3.60S0/s02-252[»]
4U4QX-ray3.00S0/s02-252[»]
4U4RX-ray2.80S0/s02-252[»]
4U4UX-ray3.00S0/s02-252[»]
4U4YX-ray3.20S0/s02-252[»]
4U4ZX-ray3.10S0/s02-252[»]
4U50X-ray3.20S0/s02-252[»]
4U51X-ray3.20S0/s02-252[»]
4U52X-ray3.00S0/s02-252[»]
4U53X-ray3.30S0/s02-252[»]
4U55X-ray3.20S0/s02-252[»]
4U56X-ray3.45S0/s02-252[»]
4U6FX-ray3.10S0/s02-252[»]
4V4Belectron microscopy11.70AB14-198[»]
4V6Ielectron microscopy8.80AA1-252[»]
4V7RX-ray4.00AA/CA1-252[»]
4V88X-ray3.00AA/CA1-252[»]
4V8Yelectron microscopy4.30AA1-252[»]
4V8Zelectron microscopy6.60AA1-252[»]
4V92electron microscopy3.70A2-207[»]
5DATX-ray3.15S0/s02-252[»]
5DC3X-ray3.25S0/s02-252[»]
5FCIX-ray3.40S0/s02-252[»]
5FCJX-ray3.10S0/s02-252[»]
5I4LX-ray3.10S0/s02-207[»]
5JUOelectron microscopy4.00XA1-252[»]
5JUPelectron microscopy3.50XA1-252[»]
5JUSelectron microscopy4.20XA1-252[»]
5JUTelectron microscopy4.00XA1-252[»]
5JUUelectron microscopy4.00XA1-252[»]
ProteinModelPortaliP32905.
SMRiP32905.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33467. 109 interactors.
DIPiDIP-5553N.
IntActiP32905. 155 interactors.
MINTiMINT-562708.

PTM databases

iPTMnetiP32905.

2D gel databases

SWISS-2DPAGEP32905.

Proteomic databases

MaxQBiP32905.
PRIDEiP32905.
TopDownProteomicsiP32905.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR214W; YGR214W; YGR214W.
GeneIDi853128.
KEGGisce:YGR214W.

Organism-specific databases

EuPathDBiFungiDB:YGR214W.
SGDiS000003446. RPS0A.

Phylogenomic databases

GeneTreeiENSGT00390000015036.
HOGENOMiHOG000232073.
InParanoidiP32905.
KOiK02998.
OMAiAPKESQW.
OrthoDBiEOG092C4HTX.

Enzyme and pathway databases

BioCyciYEAST:G3O-30896-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

EvolutionaryTraceiP32905.
PROiP32905.

Family and domain databases

CDDicd01425. RPS2. 1 hit.
HAMAPiMF_03015. Ribosomal_S2_euk. 1 hit.
InterProiIPR001865. Ribosomal_S2.
IPR018130. Ribosomal_S2_CS.
IPR027498. Ribosomal_S2_euk.
IPR005707. Ribosomal_S2_euk/arc.
IPR023591. Ribosomal_S2_flav_dom.
[Graphical view]
PANTHERiPTHR11489. PTHR11489. 1 hit.
PfamiPF00318. Ribosomal_S2. 2 hits.
[Graphical view]
PRINTSiPR00395. RIBOSOMALS2.
SUPFAMiSSF52313. SSF52313. 1 hit.
TIGRFAMsiTIGR01012. uS2_euk_arch. 1 hit.
PROSITEiPS00962. RIBOSOMAL_S2_1. 1 hit.
PS00963. RIBOSOMAL_S2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRSSA1_YEAST
AccessioniPrimary (citable) accession number: P32905
Secondary accession number(s): D6VUZ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 157 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 93700 molecules/cell in log phase SD medium.1 Publication
There are 2 genes for S0 in yeast.
This protein appears to have acquired a second function as a laminin receptor specifically in the vertebrate lineage. This protein does not bind laminin.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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.