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Protein

40S ribosomal protein S18-A

Gene

RPS18A

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Located at the top of the head of the 40S subunit, it contacts several helices of the 18S rRNA.By similarity

GO - Molecular functioni

  • rRNA binding Source: UniProtKB-KW
  • 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
  • rRNA export from nucleus Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29981-MONOMER.
ReactomeiREACT_290856. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_302067. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_307259. Formation of a pool of free 40S subunits.
REACT_314339. SRP-dependent cotranslational protein targeting to membrane.
REACT_332565. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_335938. Ribosomal scanning and start codon recognition.
REACT_343353. Peptide chain elongation.
REACT_346847. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_351622. Formation of the ternary complex, and subsequently, the 43S complex.

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S18-A
Gene namesi
Name:RPS18A
Ordered Locus Names:YDR450W
ORF Names:D9461.35
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome IV

Organism-specific databases

SGDiS000002858. RPS18A.

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
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 14614540S ribosomal protein S18-APRO_0000132227Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine3 Publications
Modified residuei48 – 481N6-methyllysine; by RKM11 Publication

Post-translational modificationi

N-terminally acetylated by acetyltransferase NatA.2 Publications

Keywords - PTMi

Acetylation, Methylation

Proteomic databases

MaxQBiP0CX55.

Expressioni

Gene expression databases

ExpressionAtlasiP0CX55. differential.

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

BioGridi32505. 76 interactions.
35143. 67 interactions.
IntActiP0CX55. 1 interaction.
MINTiMINT-572872.
STRINGi4932.YML026C.

Structurei

Secondary structure

1
146
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi13 – 175Combined sources
Beta strandi20 – 223Combined sources
Beta strandi24 – 274Combined sources
Helixi28 – 314Combined sources
Helixi32 – 343Combined sources
Helixi40 – 4910Combined sources
Turni58 – 603Combined sources
Helixi63 – 7311Combined sources
Turni76 – 805Combined sources
Helixi83 – 853Combined sources
Beta strandi86 – 883Combined sources
Beta strandi92 – 943Combined sources
Helixi103 – 11917Combined sources
Helixi122 – 1287Combined sources
Beta strandi133 – 1353Combined sources
Beta strandi139 – 1413Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5Xmodel-M15-145[»]
3J6Xelectron microscopy6.10181-146[»]
3J6Yelectron microscopy6.10181-146[»]
3J77electron microscopy6.20181-146[»]
3J78electron microscopy6.30181-146[»]
3V88X-ray3.00S1-146[»]
4U3MX-ray3.00C8/c82-146[»]
4U3NX-ray3.20C8/c82-146[»]
4U3UX-ray2.90C8/c82-146[»]
4U4NX-ray3.10C8/c82-146[»]
4U4OX-ray3.60C8/c82-146[»]
4U4QX-ray3.00C8/c82-146[»]
4U4RX-ray2.80C8/c82-146[»]
4U4UX-ray3.00C8/c82-146[»]
4U4YX-ray3.20C8/c82-146[»]
4U4ZX-ray3.10C8/c82-146[»]
4U50X-ray3.20C8/c82-146[»]
4U51X-ray3.20C8/c82-146[»]
4U52X-ray3.00C8/c82-146[»]
4U53X-ray3.30C8/c82-146[»]
4U55X-ray3.20C8/c82-146[»]
4U56X-ray3.45C8/c82-146[»]
4U6FX-ray3.10C8/c82-146[»]
4V4Belectron microscopy11.70AM15-146[»]
4V6Ielectron microscopy8.80AM1-146[»]
4V7RX-ray4.00AL/CL1-146[»]
4V88X-ray3.00AS/CS1-146[»]
4V8Yelectron microscopy4.30AS1-146[»]
4V8Zelectron microscopy6.60AS1-146[»]
4V92electron microscopy3.70S2-141[»]
ProteinModelPortaliP0CX55.
SMRiP0CX55. Positions 2-146.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0CX55.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S13P family.Curated

Phylogenomic databases

InParanoidiP0CX55.
KOiK02964.
OrthoDBiEOG7966V3.

Family and domain databases

Gene3Di4.10.910.10. 1 hit.
HAMAPiMF_01315. Ribosomal_S13_S18.
InterProiIPR027437. 30s_Rbsml_prot_S13_C.
IPR001892. Ribosomal_S13.
IPR010979. Ribosomal_S13-like_H2TH.
IPR018269. Ribosomal_S13_CS.
[Graphical view]
PfamiPF00416. Ribosomal_S13. 1 hit.
[Graphical view]
PIRSFiPIRSF002134. Ribosomal_S13. 1 hit.
SUPFAMiSSF46946. SSF46946. 1 hit.
PROSITEiPS00646. RIBOSOMAL_S13_1. 1 hit.
PS50159. RIBOSOMAL_S13_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0CX55-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLVVQEQGS FQHILRLLNT NVDGNIKIVY ALTTIKGVGR RYSNLVCKKA
60 70 80 90 100
DVDLHKRAGE LTQEELERIV QIMQNPTHYK IPAWFLNRQN DITDGKDYHT
110 120 130 140
LANNVESKLR DDLERLKKIR AHRGIRHFWG LRVRGQHTKT TGRRRA
Length:146
Mass (Da):17,038
Last modified:June 28, 2011 - v1
Checksum:i1F50BF9ADD20CA19
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33007 Genomic DNA. Translation: AAB64891.1.
BK006938 Genomic DNA. Translation: DAA12285.1.
PIRiS50886.
RefSeqiNP_010738.1. NM_001180758.1.
NP_013686.1. NM_001182384.1.

Genome annotation databases

EnsemblFungiiYDR450W; YDR450W; YDR450W.
YML026C; YML026C; YML026C.
GeneIDi852061.
854982.
KEGGisce:YDR450W.
sce:YML026C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33007 Genomic DNA. Translation: AAB64891.1.
BK006938 Genomic DNA. Translation: DAA12285.1.
PIRiS50886.
RefSeqiNP_010738.1. NM_001180758.1.
NP_013686.1. NM_001182384.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5Xmodel-M15-145[»]
3J6Xelectron microscopy6.10181-146[»]
3J6Yelectron microscopy6.10181-146[»]
3J77electron microscopy6.20181-146[»]
3J78electron microscopy6.30181-146[»]
3V88X-ray3.00S1-146[»]
4U3MX-ray3.00C8/c82-146[»]
4U3NX-ray3.20C8/c82-146[»]
4U3UX-ray2.90C8/c82-146[»]
4U4NX-ray3.10C8/c82-146[»]
4U4OX-ray3.60C8/c82-146[»]
4U4QX-ray3.00C8/c82-146[»]
4U4RX-ray2.80C8/c82-146[»]
4U4UX-ray3.00C8/c82-146[»]
4U4YX-ray3.20C8/c82-146[»]
4U4ZX-ray3.10C8/c82-146[»]
4U50X-ray3.20C8/c82-146[»]
4U51X-ray3.20C8/c82-146[»]
4U52X-ray3.00C8/c82-146[»]
4U53X-ray3.30C8/c82-146[»]
4U55X-ray3.20C8/c82-146[»]
4U56X-ray3.45C8/c82-146[»]
4U6FX-ray3.10C8/c82-146[»]
4V4Belectron microscopy11.70AM15-146[»]
4V6Ielectron microscopy8.80AM1-146[»]
4V7RX-ray4.00AL/CL1-146[»]
4V88X-ray3.00AS/CS1-146[»]
4V8Yelectron microscopy4.30AS1-146[»]
4V8Zelectron microscopy6.60AS1-146[»]
4V92electron microscopy3.70S2-141[»]
ProteinModelPortaliP0CX55.
SMRiP0CX55. Positions 2-146.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32505. 76 interactions.
35143. 67 interactions.
IntActiP0CX55. 1 interaction.
MINTiMINT-572872.
STRINGi4932.YML026C.

Proteomic databases

MaxQBiP0CX55.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR450W; YDR450W; YDR450W.
YML026C; YML026C; YML026C.
GeneIDi852061.
854982.
KEGGisce:YDR450W.
sce:YML026C.

Organism-specific databases

SGDiS000002858. RPS18A.

Phylogenomic databases

InParanoidiP0CX55.
KOiK02964.
OrthoDBiEOG7966V3.

Enzyme and pathway databases

BioCyciYEAST:G3O-29981-MONOMER.
ReactomeiREACT_290856. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_302067. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_307259. Formation of a pool of free 40S subunits.
REACT_314339. SRP-dependent cotranslational protein targeting to membrane.
REACT_332565. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_335938. Ribosomal scanning and start codon recognition.
REACT_343353. Peptide chain elongation.
REACT_346847. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_351622. Formation of the ternary complex, and subsequently, the 43S complex.

Miscellaneous databases

EvolutionaryTraceiP0CX55.
NextBioi970337.
PROiP0CX55.

Gene expression databases

ExpressionAtlasiP0CX55. differential.

Family and domain databases

Gene3Di4.10.910.10. 1 hit.
HAMAPiMF_01315. Ribosomal_S13_S18.
InterProiIPR027437. 30s_Rbsml_prot_S13_C.
IPR001892. Ribosomal_S13.
IPR010979. Ribosomal_S13-like_H2TH.
IPR018269. Ribosomal_S13_CS.
[Graphical view]
PfamiPF00416. Ribosomal_S13. 1 hit.
[Graphical view]
PIRSFiPIRSF002134. Ribosomal_S13. 1 hit.
SUPFAMiSSF46946. SSF46946. 1 hit.
PROSITEiPS00646. RIBOSOMAL_S13_1. 1 hit.
PS50159. RIBOSOMAL_S13_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(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. Bienvenut W.V., Peters C.
    Submitted (MAY-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-36; 58-68 AND 81-88, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
  4. "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.
  5. "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.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  9. "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].
  10. "Methylation of translation-associated proteins in Saccharomyces cerevisiae: Identification of methylated lysines and their methyltransferases."
    Couttas T.A., Raftery M.J., Padula M.P., Herbert B.R., Wilkins M.R.
    Proteomics 12:960-972(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT LYS-48 BY RKM1.
  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 15-145, 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 15-146, ELECTRON MICROSCOPY.

Entry informationi

Entry nameiRS18A_YEAST
AccessioniPrimary (citable) accession number: P0CX55
Secondary accession number(s): D6VT75, P35271
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: June 28, 2011
Last modified: June 24, 2015
This is version 33 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 48100 molecules/cell in log phase SD medium.1 Publication
There are 2 genes for S18 in yeast.

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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: 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.