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Protein

40S ribosomal protein S20

Gene

RPS20

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

  1. RNA binding Source: InterPro
  2. structural constituent of ribosome Source: SGD

GO - Biological processi

  1. cytoplasmic translation Source: SGD
  2. maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciYEAST:G3O-31035-MONOMER.
ReactomeiREACT_188965. SRP-dependent cotranslational protein targeting to membrane.
REACT_189050. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_189183. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_217188. Formation of a pool of free 40S subunits.
REACT_232946. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_248935. Ribosomal scanning and start codon recognition.
REACT_252688. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_257608. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_257951. Peptide chain elongation.

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S20
Gene namesi
Name:RPS20
Synonyms:URP2
Ordered Locus Names:YHL015W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VIII

Organism-specific databases

SGDiS000001007. RPS20.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 12112040S ribosomal protein S20PRO_0000146692Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine3 Publications
Cross-linki8 – 8Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications

Post-translational modificationi

N-terminally acetylated by acetyltransferase NatA. Also partially acetylated by NatC.3 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP38701.
PaxDbiP38701.
PeptideAtlasiP38701.
PRIDEiP38701.

Expressioni

Gene expression databases

GenevestigatoriP38701.

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

Protein-protein interaction databases

BioGridi36408. 62 interactions.
DIPiDIP-4060N.
IntActiP38701. 10 interactions.
MINTiMINT-539826.
STRINGi4932.YHL015W.

Structurei

Secondary structure

1
121
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi22 – 298Combined sources
Helixi31 – 4616Combined sources
Turni47 – 493Combined sources
Beta strandi51 – 577Combined sources
Beta strandi61 – 699Combined sources
Beta strandi71 – 733Combined sources
Beta strandi79 – 9416Combined sources
Helixi97 – 1059Combined sources
Beta strandi112 – 1176Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5Xmodel-J21-117[»]
3J6Xelectron microscopy6.10V1-121[»]
3J6Yelectron microscopy6.10V1-121[»]
3J77electron microscopy6.20U1-121[»]
3J78electron microscopy6.30U1-121[»]
3V88X-ray3.00U1-121[»]
4U3MX-ray3.00V/y2-121[»]
4U3NX-ray3.20V/y2-121[»]
4U3UX-ray2.90V/y2-121[»]
4U4NX-ray3.10V/y2-121[»]
4U4OX-ray3.60V/y2-121[»]
4U4QX-ray3.00V/y2-121[»]
4U4RX-ray2.80V/y2-121[»]
4U4UX-ray3.00V/y2-121[»]
4U4YX-ray3.20V/y2-121[»]
4U4ZX-ray3.10V/y2-121[»]
4U50X-ray3.20V/y2-121[»]
4U51X-ray3.20V/y2-121[»]
4U52X-ray3.00V/y2-121[»]
4U53X-ray3.30V/y2-121[»]
4U55X-ray3.20V/y2-121[»]
4U56X-ray3.45V/y2-121[»]
4U6FX-ray3.10V/y2-121[»]
4V4Belectron microscopy11.70J21-117[»]
4V6Ielectron microscopy-J1-121[»]
4V7RX-ray4.00N1-121[»]
4V88X-ray3.00U1-121[»]
4V8Yelectron microscopy4.30U1-121[»]
4V8Zelectron microscopy6.60U1-121[»]
4V92electron microscopy3.70U17-120[»]
ProteinModelPortaliP38701.
SMRiP38701. Positions 25-121.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38701.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S10P family.Curated

Phylogenomic databases

eggNOGiCOG0051.
GeneTreeiENSGT00390000003248.
HOGENOMiHOG000270245.
InParanoidiP38701.
KOiK02969.
OMAiYELKIHK.
OrthoDBiEOG751NTH.

Family and domain databases

Gene3Di3.30.70.600. 1 hit.
HAMAPiMF_00508. Ribosomal_S10.
InterProiIPR001848. Ribosomal_S10.
IPR018268. Ribosomal_S10_CS.
IPR027486. Ribosomal_S10_dom.
IPR005729. Ribosomal_S10_euk/arc.
[Graphical view]
PANTHERiPTHR11700. PTHR11700. 1 hit.
PfamiPF00338. Ribosomal_S10. 1 hit.
[Graphical view]
PRINTSiPR00971. RIBOSOMALS10.
SUPFAMiSSF54999. SSF54999. 1 hit.
TIGRFAMsiTIGR01046. S10_Arc_S20_Euk. 1 hit.
PROSITEiPS00361. RIBOSOMAL_S10. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P38701-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSDFQKEKVE EQEQQQQQII KIRITLTSTK VKQLENVSSN IVKNAEQHNL
60 70 80 90 100
VKKGPVRLPT KVLKISTRKT PNGEGSKTWE TYEMRIHKRY IDLEAPVQIV
110 120
KRITQITIEP GVDVEVVVAS N
Length:121
Mass (Da):13,907
Last modified:January 23, 2007 - v3
Checksum:i8B1607EDB63017F1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z29089 Genomic DNA. Translation: CAA82331.1.
U11582 Genomic DNA. Translation: AAB65068.1.
BK006934 Genomic DNA. Translation: DAA06671.1.
PIRiS46829.
RefSeqiNP_011848.1. NM_001179095.1.

Genome annotation databases

EnsemblFungiiYHL015W; YHL015W; YHL015W.
GeneIDi856371.
KEGGisce:YHL015W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z29089 Genomic DNA. Translation: CAA82331.1.
U11582 Genomic DNA. Translation: AAB65068.1.
BK006934 Genomic DNA. Translation: DAA06671.1.
PIRiS46829.
RefSeqiNP_011848.1. NM_001179095.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5Xmodel-J21-117[»]
3J6Xelectron microscopy6.10V1-121[»]
3J6Yelectron microscopy6.10V1-121[»]
3J77electron microscopy6.20U1-121[»]
3J78electron microscopy6.30U1-121[»]
3V88X-ray3.00U1-121[»]
4U3MX-ray3.00V/y2-121[»]
4U3NX-ray3.20V/y2-121[»]
4U3UX-ray2.90V/y2-121[»]
4U4NX-ray3.10V/y2-121[»]
4U4OX-ray3.60V/y2-121[»]
4U4QX-ray3.00V/y2-121[»]
4U4RX-ray2.80V/y2-121[»]
4U4UX-ray3.00V/y2-121[»]
4U4YX-ray3.20V/y2-121[»]
4U4ZX-ray3.10V/y2-121[»]
4U50X-ray3.20V/y2-121[»]
4U51X-ray3.20V/y2-121[»]
4U52X-ray3.00V/y2-121[»]
4U53X-ray3.30V/y2-121[»]
4U55X-ray3.20V/y2-121[»]
4U56X-ray3.45V/y2-121[»]
4U6FX-ray3.10V/y2-121[»]
4V4Belectron microscopy11.70J21-117[»]
4V6Ielectron microscopy-J1-121[»]
4V7RX-ray4.00N1-121[»]
4V88X-ray3.00U1-121[»]
4V8Yelectron microscopy4.30U1-121[»]
4V8Zelectron microscopy6.60U1-121[»]
4V92electron microscopy3.70U17-120[»]
ProteinModelPortaliP38701.
SMRiP38701. Positions 25-121.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36408. 62 interactions.
DIPiDIP-4060N.
IntActiP38701. 10 interactions.
MINTiMINT-539826.
STRINGi4932.YHL015W.

Proteomic databases

MaxQBiP38701.
PaxDbiP38701.
PeptideAtlasiP38701.
PRIDEiP38701.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYHL015W; YHL015W; YHL015W.
GeneIDi856371.
KEGGisce:YHL015W.

Organism-specific databases

SGDiS000001007. RPS20.

Phylogenomic databases

eggNOGiCOG0051.
GeneTreeiENSGT00390000003248.
HOGENOMiHOG000270245.
InParanoidiP38701.
KOiK02969.
OMAiYELKIHK.
OrthoDBiEOG751NTH.

Enzyme and pathway databases

BioCyciYEAST:G3O-31035-MONOMER.
ReactomeiREACT_188965. SRP-dependent cotranslational protein targeting to membrane.
REACT_189050. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_189183. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_217188. Formation of a pool of free 40S subunits.
REACT_232946. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_248935. Ribosomal scanning and start codon recognition.
REACT_252688. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_257608. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_257951. Peptide chain elongation.

Miscellaneous databases

EvolutionaryTraceiP38701.
NextBioi981849.
PROiP38701.

Gene expression databases

GenevestigatoriP38701.

Family and domain databases

Gene3Di3.30.70.600. 1 hit.
HAMAPiMF_00508. Ribosomal_S10.
InterProiIPR001848. Ribosomal_S10.
IPR018268. Ribosomal_S10_CS.
IPR027486. Ribosomal_S10_dom.
IPR005729. Ribosomal_S10_euk/arc.
[Graphical view]
PANTHERiPTHR11700. PTHR11700. 1 hit.
PfamiPF00338. Ribosomal_S10. 1 hit.
[Graphical view]
PRINTSiPR00971. RIBOSOMALS10.
SUPFAMiSSF54999. SSF54999. 1 hit.
TIGRFAMsiTIGR01046. S10_Arc_S20_Euk. 1 hit.
PROSITEiPS00361. RIBOSOMAL_S10. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Suppression of yeast RNA polymerase III mutations by the URP2 gene encoding a protein homologous to the mammalian ribosomal protein S20."
    Hermann-Le Denmat S., Sipickzki M., Thuriaux P.
    J. Mol. Biol. 240:1-7(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 28383 / FL100 / VTT C-80102.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Bienvenut W.V., Peters C.
    Submitted (MAY-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-21; 33-43; 78-85 AND 90-102, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
  5. "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.
  6. "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: CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2 BY NATA.
  7. Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-8.
    Strain: SUB592.
  8. "A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery."
    Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.
    Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-8.
  9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Structure of the 80S ribosome from Saccharomyces cerevisiae -- tRNA-ribosome and subunit-subunit interactions."
    Spahn C.M.T., Beckmann R., Eswar N., Penczek P.A., Sali A., Blobel G., Frank J.
    Cell 107:373-386(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING OF 21-117, ELECTRON MICROSCOPY.
  12. "Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation."
    Spahn C.M.T., Gomez-Lorenzo M.G., Grassucci R.A., Joergensen R., Andersen G.R., Beckmann R., Penczek P.A., Ballesta J.P.G., Frank J.
    EMBO J. 23:1008-1019(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING OF 21-121, ELECTRON MICROSCOPY.

Entry informationi

Entry nameiRS20_YEAST
AccessioniPrimary (citable) accession number: P38701
Secondary accession number(s): D3DKP7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: February 4, 2015
This is version 134 of the entry and version 3 of the sequence. [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 VIII
    Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

External Data

Dasty 3

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 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.