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Protein

60S ribosomal protein L18-A

Gene

RPL18A

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

GO - Molecular functioni

  1. structural constituent of ribosome Source: SGD

GO - Biological processi

  1. cytoplasmic translation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciYEAST:G3O-33516-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_343353. Peptide chain elongation.
REACT_346847. GTP hydrolysis and joining of the 60S ribosomal subunit.

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L18-A
Alternative name(s):
RP28
Gene namesi
Name:RPL18A
Synonyms:RP28A
Ordered Locus Names:YOL120C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XV

Organism-specific databases

CYGDiYOL120c.
SGDiS000005480. RPL18A.

Subcellular locationi

  1. Cytoplasm By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 18618560S ribosomal protein L18-APRO_0000132784Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei50 – 501N6,N6,N6-trimethyllysine1 Publication

Keywords - PTMi

Methylation

Proteomic databases

MaxQBiP0CX49.

Expressioni

Gene expression databases

ExpressionAtlasiP0CX49. differential.

Interactioni

Subunit structurei

Component of the large 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). Interacts with NAP1.2 Publications

Protein-protein interaction databases

BioGridi34281. 82 interactions.
35537. 82 interactions.
IntActiP0CX49. 1 interaction.
MINTiMINT-8285571.

Structurei

Secondary structure

1
186
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi24 – 3916Combined sources
Helixi43 – 5210Combined sources
Helixi56 – 583Combined sources
Helixi64 – 707Combined sources
Turni74 – 785Combined sources
Beta strandi79 – 8810Combined sources
Beta strandi100 – 1067Combined sources
Helixi108 – 1169Combined sources
Beta strandi120 – 1223Combined sources
Helixi124 – 1307Combined sources
Beta strandi137 – 1393Combined sources
Helixi144 – 1463Combined sources
Helixi148 – 1514Combined sources
Turni152 – 1543Combined sources
Turni157 – 1593Combined sources
Beta strandi169 – 1735Combined sources
Beta strandi177 – 1793Combined sources
Helixi180 – 1823Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-O22-141[»]
3J6Xelectron microscopy6.10581-186[»]
3J6Yelectron microscopy6.10581-186[»]
3J77electron microscopy6.20681-186[»]
3J78electron microscopy6.30681-186[»]
4U3MX-ray3.00M8/m82-186[»]
4U3NX-ray3.20M8/m82-186[»]
4U3UX-ray2.90M8/m82-186[»]
4U4NX-ray3.10M8/m82-186[»]
4U4OX-ray3.60M8/m82-186[»]
4U4QX-ray3.00M8/m82-186[»]
4U4RX-ray2.80M8/m82-186[»]
4U4UX-ray3.00M8/m82-186[»]
4U4YX-ray3.20M8/m82-186[»]
4U4ZX-ray3.10M8/m82-186[»]
4U50X-ray3.20M8/m82-186[»]
4U51X-ray3.20M8/m82-186[»]
4U52X-ray3.00M8/m82-186[»]
4U53X-ray3.30M8/m82-186[»]
4U55X-ray3.20M8/m82-186[»]
4U56X-ray3.45M8/m82-186[»]
4U6FX-ray3.10M8/m82-186[»]
4V4Belectron microscopy11.70BO22-141[»]
4V6Ielectron microscopy8.80BR1-186[»]
4V7Felectron microscopy8.70Q1-186[»]
4V7RX-ray4.00BR/DR1-186[»]
4V88X-ray3.00BQ/DQ1-186[»]
4V8Yelectron microscopy4.30BQ2-186[»]
4V8Zelectron microscopy6.60BQ2-186[»]
4V91electron microscopy3.70Q1-186[»]
ProteinModelPortaliP0CX49.
SMRiP0CX49. Positions 2-186.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0CX49.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L18e family.Curated

Phylogenomic databases

InParanoidiP0CX49.
KOiK02883.
OrthoDBiEOG790GC3.

Family and domain databases

InterProiIPR000039. Ribosomal_L18e.
IPR021131. Ribosomal_L18e/L15P.
IPR021132. Ribosomal_L18e_CS.
[Graphical view]
PANTHERiPTHR10934. PTHR10934. 1 hit.
PfamiPF00828. Ribosomal_L18e. 1 hit.
[Graphical view]
SUPFAMiSSF52080. SSF52080. 1 hit.
PROSITEiPS01106. RIBOSOMAL_L18E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0CX49-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGIDHTSKQH KRSGHRTAPK SDNVYLKLLV KLYTFLARRT DAPFNKVVLK
60 70 80 90 100
ALFLSKINRP PVSVSRIARA LKQEGAANKT VVVVGTVTDD ARIFEFPKTT
110 120 130 140 150
VAALRFTAGA RAKIVKAGGE CITLDQLAVR APKGQNTLIL RGPRNSREAV
160 170 180
RHFGMGPHKG KAPRILSTGR KFERARGRRR SKGFKV
Length:186
Mass (Da):20,563
Last modified:June 28, 2011 - v1
Checksum:iD097B187F369EACD
GO

Mass spectrometryi

Molecular mass is 20419.431 Da from positions 2 - 186. Determined by ESI. Monoisotopic mass.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01099 Genomic DNA. Translation: CAA25573.1.
X02635 Genomic DNA. Translation: CAA26481.1.
X95258 Genomic DNA. Translation: CAA64550.1.
Z74862 Genomic DNA. Translation: CAA99139.1.
BK006948 Genomic DNA. Translation: DAA10664.1.
PIRiS05867. R5BY8E.
RefSeqiNP_014098.1. NM_001183139.1.
NP_014521.1. NM_001183374.1.

Genome annotation databases

EnsemblFungiiYNL301C; YNL301C; YNL301C.
YOL120C; YOL120C; YOL120C.
GeneIDi854029.
855415.
KEGGisce:YNL301C.
sce:YOL120C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01099 Genomic DNA. Translation: CAA25573.1.
X02635 Genomic DNA. Translation: CAA26481.1.
X95258 Genomic DNA. Translation: CAA64550.1.
Z74862 Genomic DNA. Translation: CAA99139.1.
BK006948 Genomic DNA. Translation: DAA10664.1.
PIRiS05867. R5BY8E.
RefSeqiNP_014098.1. NM_001183139.1.
NP_014521.1. NM_001183374.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-O22-141[»]
3J6Xelectron microscopy6.10581-186[»]
3J6Yelectron microscopy6.10581-186[»]
3J77electron microscopy6.20681-186[»]
3J78electron microscopy6.30681-186[»]
4U3MX-ray3.00M8/m82-186[»]
4U3NX-ray3.20M8/m82-186[»]
4U3UX-ray2.90M8/m82-186[»]
4U4NX-ray3.10M8/m82-186[»]
4U4OX-ray3.60M8/m82-186[»]
4U4QX-ray3.00M8/m82-186[»]
4U4RX-ray2.80M8/m82-186[»]
4U4UX-ray3.00M8/m82-186[»]
4U4YX-ray3.20M8/m82-186[»]
4U4ZX-ray3.10M8/m82-186[»]
4U50X-ray3.20M8/m82-186[»]
4U51X-ray3.20M8/m82-186[»]
4U52X-ray3.00M8/m82-186[»]
4U53X-ray3.30M8/m82-186[»]
4U55X-ray3.20M8/m82-186[»]
4U56X-ray3.45M8/m82-186[»]
4U6FX-ray3.10M8/m82-186[»]
4V4Belectron microscopy11.70BO22-141[»]
4V6Ielectron microscopy8.80BR1-186[»]
4V7Felectron microscopy8.70Q1-186[»]
4V7RX-ray4.00BR/DR1-186[»]
4V88X-ray3.00BQ/DQ1-186[»]
4V8Yelectron microscopy4.30BQ2-186[»]
4V8Zelectron microscopy6.60BQ2-186[»]
4V91electron microscopy3.70Q1-186[»]
ProteinModelPortaliP0CX49.
SMRiP0CX49. Positions 2-186.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34281. 82 interactions.
35537. 82 interactions.
IntActiP0CX49. 1 interaction.
MINTiMINT-8285571.

Proteomic databases

MaxQBiP0CX49.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL301C; YNL301C; YNL301C.
YOL120C; YOL120C; YOL120C.
GeneIDi854029.
855415.
KEGGisce:YNL301C.
sce:YOL120C.

Organism-specific databases

CYGDiYOL120c.
SGDiS000005480. RPL18A.

Phylogenomic databases

InParanoidiP0CX49.
KOiK02883.
OrthoDBiEOG790GC3.

Enzyme and pathway databases

BioCyciYEAST:G3O-33516-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_343353. Peptide chain elongation.
REACT_346847. GTP hydrolysis and joining of the 60S ribosomal subunit.

Miscellaneous databases

EvolutionaryTraceiP0CX49.
NextBioi975577.
PROiP0CX49.

Gene expression databases

ExpressionAtlasiP0CX49. differential.

Family and domain databases

InterProiIPR000039. Ribosomal_L18e.
IPR021131. Ribosomal_L18e/L15P.
IPR021132. Ribosomal_L18e_CS.
[Graphical view]
PANTHERiPTHR10934. PTHR10934. 1 hit.
PfamiPF00828. Ribosomal_L18e. 1 hit.
[Graphical view]
SUPFAMiSSF52080. SSF52080. 1 hit.
PROSITEiPS01106. RIBOSOMAL_L18E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and organization of two linked ribosomal protein genes in yeast."
    Molenaar C.M.T., Woudt L.P., Jansen A.E.M., Mager W.H., Planta R.J., Donovan D.M., Pearson N.J.
    Nucleic Acids Res. 12:7345-7358(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "DNA sequence analysis of a 10 624 bp fragment of the left arm of chromosome XV from Saccharomyces cerevisiae reveals a RNA binding protein, a mitochondrial protein, two ribosomal proteins and two new open reading frames."
    Lafuente M.J., Gamo F.-J., Gancedo C.
    Yeast 12:1041-1045(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  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. "Direct mass spectrometric analysis of intact proteins of the yeast large ribosomal subunit using capillary LC/FTICR."
    Lee S.-W., Berger S.J., Martinovic S., Pasa-Tolic L., Anderson G.A., Shen Y., Zhao R., Smith R.D.
    Proc. Natl. Acad. Sci. U.S.A. 99:5942-5947(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE.
  7. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Phosphorylation by casein kinase 2 regulates Nap1 localization and function."
    Calvert M.E.K., Keck K.M., Ptak C., Shabanowitz J., Hunt D.F., Pemberton L.F.
    Mol. Cell. Biol. 28:1313-1325(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NAP1, IDENTIFICATION BY MASS SPECTROMETRY.
  9. Cited for: 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. "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-50.
  12. "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 22-141, ELECTRON MICROSCOPY.
  13. "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 22-141, ELECTRON MICROSCOPY.
  14. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (8.80 ANGSTROMS).
  15. "Crystal structure of the eukaryotic ribosome."
    Ben-Shem A., Jenner L., Yusupova G., Yusupov M.
    Science 330:1203-1209(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS).
  16. Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).

Entry informationi

Entry nameiRL18A_YEAST
AccessioniPrimary (citable) accession number: P0CX49
Secondary accession number(s): D6W0P3, P07279
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: June 28, 2011
Last modified: April 29, 2015
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

There are 2 genes for L18 in yeast.

Keywords - Technical termi

3D-structure, Complete proteome, 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 XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: 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.