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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: 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.1 Publication

Miscellaneous

There are 2 genes for eL18 in yeast.Curated

GO - Molecular functioni

GO - Biological processi

  • cytoplasmic translation Source: SGD
  • translation Source: GO_Central

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciYEAST:G3O-33516-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-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:
60S ribosomal protein L18-A1 Publication
Alternative name(s):
Large ribosomal subunit protein eL18-A1 Publication
RP28
Gene namesi
Name:RPL18A1 Publication
Synonyms:RP28A
Ordered Locus Names:YOL120C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

SGDiS000005480. RPL18A.

Subcellular locationi

GO - Cellular componenti

  • cytosolic large ribosomal subunit Source: SGD

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001327842 – 18660S ribosomal protein L18-AAdd BLAST185

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei50N6,N6,N6-trimethyllysine1 Publication1
Cross-linki116Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Keywords - PTMi

Isopeptide bond, Methylation, Ubl conjugation

Proteomic databases

MaxQBiP0CX49.
PRIDEiP0CX49.

Expressioni

Gene expression databases

ExpressionAtlasiP0CX49. differential.

Interactioni

Subunit structurei

Component of the large ribosomal subunit (LSU). 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). eL18 interacts with NAP1 (PubMed:18086883).1 Publication2 Publications

Protein-protein interaction databases

BioGridi34281. 79 interactors.
35537. 117 interactors.
IntActiP0CX49. 1 interactor.
MINTiMINT-8285571.
STRINGi4932.YOL120C.

Structurei

Secondary structure

1186
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi24 – 39Combined sources16
Helixi43 – 52Combined sources10
Helixi56 – 58Combined sources3
Helixi64 – 70Combined sources7
Turni74 – 78Combined sources5
Beta strandi79 – 88Combined sources10
Beta strandi100 – 106Combined sources7
Helixi108 – 116Combined sources9
Beta strandi120 – 122Combined sources3
Helixi124 – 130Combined sources7
Beta strandi137 – 139Combined sources3
Helixi144 – 146Combined sources3
Helixi148 – 151Combined sources4
Turni152 – 154Combined sources3
Turni157 – 159Combined sources3
Beta strandi169 – 173Combined sources5
Beta strandi177 – 179Combined sources3
Helixi180 – 182Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-O22-141[»]
3J6Xelectron microscopy6.10581-186[»]
3J6Yelectron microscopy6.10581-186[»]
3J77electron microscopy6.20681-186[»]
3J78electron microscopy6.30681-186[»]
3JCTelectron microscopy3.08Q1-186[»]
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[»]
5APNelectron microscopy3.91Q1-186[»]
5APOelectron microscopy3.41Q1-186[»]
5DATX-ray3.15M8/m82-186[»]
5DC3X-ray3.25M8/m82-186[»]
5DGEX-ray3.45M8/m82-186[»]
5DGFX-ray3.30M8/m82-186[»]
5DGVX-ray3.10M8/m82-186[»]
5FCIX-ray3.40M8/m82-186[»]
5FCJX-ray3.10M8/m82-186[»]
5FL8electron microscopy9.50Q1-186[»]
5GAKelectron microscopy3.88S1-186[»]
5H4Pelectron microscopy3.07Q1-186[»]
5I4LX-ray3.10M8/m82-186[»]
5JCSelectron microscopy9.50Q1-186[»]
5JUOelectron microscopy4.00V1-186[»]
5JUPelectron microscopy3.50V1-186[»]
5JUSelectron microscopy4.20V1-186[»]
5JUTelectron microscopy4.00V1-186[»]
5JUUelectron microscopy4.00V1-186[»]
5LYBX-ray3.25M8/m82-186[»]
5M1Jelectron microscopy3.30Q52-186[»]
5MC6electron microscopy3.80BB1-186[»]
5T62electron microscopy3.30d1-186[»]
5T6Relectron microscopy4.50d1-186[»]
5TGAX-ray3.30M8/m82-186[»]
5TGMX-ray3.50M8/m82-186[»]
ProteinModelPortaliP0CX49.
SMRiP0CX49.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0CX49.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

InParanoidiP0CX49.
KOiK02883.
OMAiKHHVKKG.
OrthoDBiEOG092C592A.

Family and domain databases

InterProiView protein in InterPro
IPR000039. Ribosomal_L18e.
IPR021131. Ribosomal_L18e/L15P.
IPR021132. Ribosomal_L18e_CS.
PANTHERiPTHR10934. PTHR10934. 1 hit.
PfamiView protein in Pfam
PF17135. Ribosomal_L18. 1 hit.
SUPFAMiSSF52080. SSF52080. 1 hit.
PROSITEiView protein in PROSITE
PS01106. RIBOSOMAL_L18E. 1 hit.

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.

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 nameiRL18A_YEAST
AccessioniPrimary (citable) accession number: P0CX49
Secondary accession number(s): D6W0P3, P07279
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: June 28, 2011
Last modified: July 5, 2017
This is version 55 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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