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Protein

40S ribosomal protein S2

Gene

RPS2

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 (PubMed:22096102). uS5 is important for the assembly and function of the 40S ribosomal subunit. Mutations in this protein affects the control of translational fidelity. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly (PubMed:15590835).1 Publication1 Publication

GO - Molecular functioni

  • small ribosomal subunit rRNA binding Source: SGD
  • structural constituent of ribosome Source: SGD

GO - Biological processi

  • positive regulation of translational fidelity Source: SGD
  • rRNA export from nucleus Source: SGD
  • rRNA methylation Source: Reactome
  • translation Source: InterPro

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein
Biological processRibosome biogenesis, rRNA processing

Enzyme and pathway databases

BioCyciYEAST:G3O-30620-MONOMER.
ReactomeiR-SCE-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-SCE-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-SCE-3214858. RMTs methylate histone arginines.
R-SCE-6790901. rRNA modification in the nucleus and cytosol.
R-SCE-6791226. Major pathway of rRNA processing in the nucleolus and cytosol.
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-8876725. Protein methylation.
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 S21 Publication
Alternative name(s):
Omnipotent suppressor protein SUP44
RP12
S4
Small ribosomal subunit protein uS51 Publication
YS5
Gene namesi
Name:RPS21 Publication
Synonyms:RPS4, SUP38, SUP44
Ordered Locus Names:YGL123W
ORF Names:G2893
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL123W.
SGDiS000003091. RPS2.

Subcellular locationi

GO - Cellular componenti

  • cytosolic small ribosomal subunit Source: SGD
  • nucleolus Source: UniProtKB-SubCell
  • nucleoplasm Source: Reactome
  • small-subunit processome Source: SGD

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources2 Publications
ChainiPRO_00001316842 – 25440S ribosomal protein S2Add BLAST253

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources2 Publications1
Modified residuei11Asymmetric dimethylarginine; by HMT1; alternate2 Publications1
Modified residuei11Omega-N-methylarginine; by HMT1; alternate2 Publications1
Cross-linki33Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Post-translational modificationi

N-terminally acetylated by acetyltransferase NatA.2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Ubl conjugation

Proteomic databases

MaxQBiP25443.
PRIDEiP25443.

PTM databases

iPTMnetiP25443.

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). Interacts with snoRNA U3. Interacts with MPP10. Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3 (PubMed:15590835).1 Publication2 Publications

Protein-protein interaction databases

BioGridi33128. 345 interactors.
IntActiP25443. 12 interactors.
MINTiMINT-4808257.
STRINGi4932.YGL123W.

Structurei

Secondary structure

1254
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi40 – 46Combined sources7
Helixi53 – 58Combined sources6
Helixi66 – 71Combined sources6
Beta strandi80 – 85Combined sources6
Beta strandi88 – 90Combined sources3
Beta strandi93 – 95Combined sources3
Beta strandi98 – 105Combined sources8
Beta strandi107 – 120Combined sources14
Helixi121 – 134Combined sources14
Beta strandi144 – 146Combined sources3
Beta strandi148 – 150Combined sources3
Beta strandi153 – 156Combined sources4
Beta strandi158 – 162Combined sources5
Beta strandi165 – 171Combined sources7
Beta strandi178 – 180Combined sources3
Helixi182 – 190Combined sources9
Beta strandi195 – 202Combined sources8
Helixi207 – 219Combined sources13
Helixi220 – 223Combined sources4
Helixi227 – 229Combined sources3
Helixi239 – 242Combined sources4
Helixi244 – 247Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Xmodel-E75-223[»]
3J6Xelectron microscopy6.10S21-254[»]
3J6Yelectron microscopy6.10S21-254[»]
3J77electron microscopy6.20S21-254[»]
3J78electron microscopy6.30S21-254[»]
3V88X-ray3.00C1-254[»]
4U3MX-ray3.00S2/s22-254[»]
4U3NX-ray3.20S2/s22-254[»]
4U3UX-ray2.90S2/s22-254[»]
4U4NX-ray3.10S2/s22-254[»]
4U4OX-ray3.60S2/s22-254[»]
4U4QX-ray3.00S2/s22-254[»]
4U4RX-ray2.80S2/s22-254[»]
4U4UX-ray3.00S2/s22-254[»]
4U4YX-ray3.20S2/s22-254[»]
4U4ZX-ray3.10S2/s22-254[»]
4U50X-ray3.20S2/s22-254[»]
4U51X-ray3.20S2/s22-254[»]
4U52X-ray3.00S2/s22-254[»]
4U53X-ray3.30S2/s22-254[»]
4U55X-ray3.20S2/s22-254[»]
4U56X-ray3.45S2/s22-254[»]
4U6FX-ray3.10S2/s22-254[»]
4V4Belectron microscopy11.70AE75-223[»]
4V6Ielectron microscopy8.80AE1-254[»]
4V7RX-ray4.00AB/CB1-254[»]
4V88X-ray3.00AC/CC1-254[»]
4V8Yelectron microscopy4.30AC1-254[»]
4V8Zelectron microscopy6.60AC1-254[»]
4V92electron microscopy3.70C34-249[»]
5DATX-ray3.15S2/s22-254[»]
5DC3X-ray3.25S2/s22-254[»]
5DGEX-ray3.45S2/s22-254[»]
5DGFX-ray3.30S2/s22-254[»]
5DGVX-ray3.10S2/s22-254[»]
5FCIX-ray3.40S2/s22-254[»]
5FCJX-ray3.10S2/s22-254[»]
5I4LX-ray3.10S2/s234-250[»]
5JUOelectron microscopy4.00ZA1-254[»]
5JUPelectron microscopy3.50ZA1-254[»]
5JUSelectron microscopy4.20ZA1-254[»]
5JUTelectron microscopy4.00ZA1-254[»]
5JUUelectron microscopy4.00ZA1-254[»]
5LL6electron microscopy3.90R1-254[»]
5LYBX-ray3.25S2/s234-250[»]
5M1Jelectron microscopy3.30C234-250[»]
5MC6electron microscopy3.80R1-254[»]
5TGAX-ray3.30S2/s234-250[»]
5TGMX-ray3.50S2/s234-250[»]
ProteinModelPortaliP25443.
SMRiP25443.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25443.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini76 – 139S5 DRBMPROSITE-ProRule annotationAdd BLAST64

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000001433.
HOGENOMiHOG000072596.
InParanoidiP25443.
KOiK02981.
OMAiPHTVPMK.
OrthoDBiEOG092C4FYC.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
InterProiView protein in InterPro
IPR000851. Ribosomal_S5.
IPR005324. Ribosomal_S5_C.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR005711. Ribosomal_S5_euk/arc.
IPR013810. Ribosomal_S5_N.
IPR018192. Ribosomal_S5_N_CS.
PANTHERiPTHR13718. PTHR13718. 1 hit.
PfamiView protein in Pfam
PF00333. Ribosomal_S5. 1 hit.
PF03719. Ribosomal_S5_C. 1 hit.
SUPFAMiSSF54211. SSF54211. 1 hit.
TIGRFAMsiTIGR01020. uS5_euk_arch. 1 hit.
PROSITEiView protein in PROSITE
PS00585. RIBOSOMAL_S5. 1 hit.
PS50881. S5_DSRBD. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P25443-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAPEAQQQK RGGFGGRNRG RPNRRGPRNT EEKGWVPVTK LGRLVKAGKI
60 70 80 90 100
TTIEEIFLHS LPVKEFQIID TLLPGLQDEV MNIKPVQKQT RAGQRTRFKA
110 120 130 140 150
VVVVGDSNGH VGLGIKTAKE VAGAIRAGII IAKLSVIPIR RGYWGTNLGQ
160 170 180 190 200
PHSLATKTTG KCGSVTVRLI PAPRGSGIVA SPAVKKLLQL AGVEDVYTQS
210 220 230 240 250
NGKTRTLENT LKAAFVAIGN TYGFLTPNLW AEQPLPVSPL DIYSDEASAQ

KKRF
Length:254
Mass (Da):27,450
Last modified:January 23, 2007 - v3
Checksum:i5EFDA4C7DE7BDFFB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59375 Genomic DNA. Translation: AAA63576.1.
X94106 Genomic DNA. Translation: CAA63835.1.
Z72645 Genomic DNA. Translation: CAA96831.1.
AY557815 Genomic DNA. Translation: AAS56141.1.
BK006941 Genomic DNA. Translation: DAA07986.1.
PIRiA36363. R3BYS2.
RefSeqiNP_011392.1. NM_001180988.1.

Genome annotation databases

EnsemblFungiiYGL123W; YGL123W; YGL123W.
GeneIDi852754.
KEGGisce:YGL123W.

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.

Entry informationi

Entry nameiRS2_YEAST
AccessioniPrimary (citable) accession number: P25443
Secondary accession number(s): D6VU25
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: July 5, 2017
This is version 163 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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