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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

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

GO - Biological processi

  • cytoplasmic translation Source: SGD
  • 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.
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 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
Proteomesi
  • UP000002311 Componenti: Chromosome VIII

Organism-specific databases

EuPathDBiFungiDB:YHL015W.
SGDiS000001007. RPS20.

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)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources2 Publications
ChainiPRO_00001466922 – 12140S ribosomal protein S20Add BLAST120

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources2 Publications1
Cross-linki6Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki8Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources2 Publications
Cross-linki21Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki32Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki101Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Post-translational modificationi

N-terminally acetylated by acetyltransferase NatA. Also partially acetylated by NatC.2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP38701.
PRIDEiP38701.
TopDownProteomicsiP38701.

PTM databases

iPTMnetiP38701.

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. 47 interactors.
DIPiDIP-4060N.
IntActiP38701. 11 interactors.
MINTiMINT-539826.

Structurei

Secondary structure

1121
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi22 – 29Combined sources8
Helixi31 – 46Combined sources16
Turni47 – 49Combined sources3
Beta strandi51 – 57Combined sources7
Beta strandi61 – 69Combined sources9
Beta strandi71 – 73Combined sources3
Beta strandi79 – 94Combined sources16
Helixi97 – 105Combined sources9
Beta strandi112 – 117Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Xmodel-J21-117[»]
3J6Xelectron microscopy6.10201-121[»]
3J6Yelectron microscopy6.10201-121[»]
3J77electron microscopy6.20201-121[»]
3J78electron microscopy6.30201-121[»]
3V88X-ray3.00U1-121[»]
4U3MX-ray3.00D0/d02-121[»]
4U3NX-ray3.20D0/d02-121[»]
4U3UX-ray2.90D0/d02-121[»]
4U4NX-ray3.10D0/d02-121[»]
4U4OX-ray3.60D0/d02-121[»]
4U4QX-ray3.00D0/d02-121[»]
4U4RX-ray2.80D0/d02-121[»]
4U4UX-ray3.00D0/d02-121[»]
4U4YX-ray3.20D0/d02-121[»]
4U4ZX-ray3.10D0/d02-121[»]
4U50X-ray3.20D0/d02-121[»]
4U51X-ray3.20D0/d02-121[»]
4U52X-ray3.00D0/d02-121[»]
4U53X-ray3.30D0/d02-121[»]
4U55X-ray3.20D0/d02-121[»]
4U56X-ray3.45D0/d02-121[»]
4U6FX-ray3.10D0/d02-121[»]
4V4Belectron microscopy11.70AJ21-117[»]
4V6Ielectron microscopy8.80AJ1-121[»]
4V7RX-ray4.00AN/CN1-121[»]
4V88X-ray3.00AU/CU1-121[»]
4V8Yelectron microscopy4.30AU1-121[»]
4V8Zelectron microscopy6.60AU1-121[»]
4V92electron microscopy3.70U17-120[»]
5DATX-ray3.15D0/d02-121[»]
5DC3X-ray3.25D0/d02-121[»]
5FCIX-ray3.40D0/d02-121[»]
5FCJX-ray3.10D0/d02-121[»]
5I4LX-ray3.10D0/d012-121[»]
5JUOelectron microscopy4.00RB1-121[»]
5JUPelectron microscopy3.50RB1-121[»]
5JUSelectron microscopy4.20RB1-121[»]
5JUTelectron microscopy4.00RB1-121[»]
5JUUelectron microscopy4.00RB1-121[»]
ProteinModelPortaliP38701.
SMRiP38701.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38701.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S10P family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000003248.
HOGENOMiHOG000270245.
InParanoidiP38701.
KOiK02969.
OMAiNRSTHID.
OrthoDBiEOG092C5OAL.

Family and domain databases

Gene3Di3.30.70.600. 1 hit.
HAMAPiMF_00508. Ribosomal_S10. 1 hit.
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.
SMARTiSM01403. Ribosomal_S10. 1 hit.
[Graphical view]
SUPFAMiSSF54999. SSF54999. 1 hit.
TIGRFAMsiTIGR01046. uS10_euk_arch. 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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Xmodel-J21-117[»]
3J6Xelectron microscopy6.10201-121[»]
3J6Yelectron microscopy6.10201-121[»]
3J77electron microscopy6.20201-121[»]
3J78electron microscopy6.30201-121[»]
3V88X-ray3.00U1-121[»]
4U3MX-ray3.00D0/d02-121[»]
4U3NX-ray3.20D0/d02-121[»]
4U3UX-ray2.90D0/d02-121[»]
4U4NX-ray3.10D0/d02-121[»]
4U4OX-ray3.60D0/d02-121[»]
4U4QX-ray3.00D0/d02-121[»]
4U4RX-ray2.80D0/d02-121[»]
4U4UX-ray3.00D0/d02-121[»]
4U4YX-ray3.20D0/d02-121[»]
4U4ZX-ray3.10D0/d02-121[»]
4U50X-ray3.20D0/d02-121[»]
4U51X-ray3.20D0/d02-121[»]
4U52X-ray3.00D0/d02-121[»]
4U53X-ray3.30D0/d02-121[»]
4U55X-ray3.20D0/d02-121[»]
4U56X-ray3.45D0/d02-121[»]
4U6FX-ray3.10D0/d02-121[»]
4V4Belectron microscopy11.70AJ21-117[»]
4V6Ielectron microscopy8.80AJ1-121[»]
4V7RX-ray4.00AN/CN1-121[»]
4V88X-ray3.00AU/CU1-121[»]
4V8Yelectron microscopy4.30AU1-121[»]
4V8Zelectron microscopy6.60AU1-121[»]
4V92electron microscopy3.70U17-120[»]
5DATX-ray3.15D0/d02-121[»]
5DC3X-ray3.25D0/d02-121[»]
5FCIX-ray3.40D0/d02-121[»]
5FCJX-ray3.10D0/d02-121[»]
5I4LX-ray3.10D0/d012-121[»]
5JUOelectron microscopy4.00RB1-121[»]
5JUPelectron microscopy3.50RB1-121[»]
5JUSelectron microscopy4.20RB1-121[»]
5JUTelectron microscopy4.00RB1-121[»]
5JUUelectron microscopy4.00RB1-121[»]
ProteinModelPortaliP38701.
SMRiP38701.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36408. 47 interactors.
DIPiDIP-4060N.
IntActiP38701. 11 interactors.
MINTiMINT-539826.

PTM databases

iPTMnetiP38701.

Proteomic databases

MaxQBiP38701.
PRIDEiP38701.
TopDownProteomicsiP38701.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YHL015W.
SGDiS000001007. RPS20.

Phylogenomic databases

GeneTreeiENSGT00390000003248.
HOGENOMiHOG000270245.
InParanoidiP38701.
KOiK02969.
OMAiNRSTHID.
OrthoDBiEOG092C5OAL.

Enzyme and pathway databases

BioCyciYEAST:G3O-31035-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

EvolutionaryTraceiP38701.
PROiP38701.

Family and domain databases

Gene3Di3.30.70.600. 1 hit.
HAMAPiMF_00508. Ribosomal_S10. 1 hit.
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.
SMARTiSM01403. Ribosomal_S10. 1 hit.
[Graphical view]
SUPFAMiSSF54999. SSF54999. 1 hit.
TIGRFAMsiTIGR01046. uS10_euk_arch. 1 hit.
PROSITEiPS00361. RIBOSOMAL_S10. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 154 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

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.