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Protein

60S ribosomal protein L9-A

Gene

RPL9A

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -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

Present with 52400 molecules/cell in log phase SD medium.1 Publication
There are 2 genes for uL6 in yeast.Curated

GO - Molecular functioni

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

GO - Biological processi

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciYEAST:G3O-30641-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 L9-A1 Publication
Alternative name(s):
L8
RP24
YL11
Gene namesi
Name:RPL9A1 Publication
Synonyms:RPL8A, RPL9
Ordered Locus Names:YGL147C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL147C
SGDiS000003115 RPL9A

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001311111 – 19160S ribosomal protein L9-AAdd BLAST191

Proteomic databases

MaxQBiP05738
PaxDbiP05738
PRIDEiP05738

PTM databases

iPTMnetiP05738

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). uL6 lines the binding pocket for eukaryotic elongation factor 2 (eEF2) (PubMed:9559554, PubMed:22096102).1 Publication1 Publication

Protein-protein interaction databases

BioGridi33105, 215 interactors
DIPiDIP-4826N
IntActiP05738, 10 interactors
MINTiP05738
STRINGi4932.YGL147C

Structurei

Secondary structure

1191
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP05738
SMRiP05738
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05738

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000015224
HOGENOMiHOG000039905
InParanoidiP05738
KOiK02940
OMAiKIDAWFS
OrthoDBiEOG092C4TE3

Family and domain databases

Gene3Di3.90.930.12, 2 hits
InterProiView protein in InterPro
IPR000702 Ribosomal_L6
IPR020040 Ribosomal_L6_a/b-dom
IPR036789 Ribosomal_L6_a/b-dom_sf
IPR002359 Ribosomal_L6_CS2
PANTHERiPTHR11655 PTHR11655, 1 hit
PfamiView protein in Pfam
PF00347 Ribosomal_L6, 2 hits
PIRSFiPIRSF002162 Ribosomal_L6, 1 hit
SUPFAMiSSF56053 SSF56053, 2 hits
PROSITEiView protein in PROSITE
PS00700 RIBOSOMAL_L6_2, 1 hit

Sequencei

Sequence statusi: Complete.

P05738-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKYIQTEQQI EVPEGVTVSI KSRIVKVVGP RGTLTKNLKH IDVTFTKVNN
60 70 80 90 100
QLIKVAVHNG GRKHVAALRT VKSLVDNMIT GVTKGYKYKM RYVYAHFPIN
110 120 130 140 150
VNIVEKDGAK FIEVRNFLGD KKIRNVPVRD GVTIEFSTNV KDEIVLSGNS
160 170 180 190
VEDVSQNAAD LQQICRVRNK DIRKFLDGIY VSHKGFITED L
Length:191
Mass (Da):21,569
Last modified:December 1, 1992 - v2
Checksum:iCAA342FCDD061175
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60190 Genomic DNA Translation: CAA42746.1
X99960 Genomic DNA Translation: CAA68215.1
Z72669 Genomic DNA Translation: CAA96859.1
BK006941 Genomic DNA Translation: DAA07963.1
PIRiS19077 R5BYL9
RefSeqiNP_011368.3, NM_001181012.3

Genome annotation databases

EnsemblFungiiYGL147C; YGL147C; YGL147C
GeneIDi852730
KEGGisce:YGL147C

Similar proteinsi

Entry informationi

Entry nameiRL9A_YEAST
AccessioniPrimary (citable) accession number: P05738
Secondary accession number(s): D6VU02
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: December 1, 1992
Last modified: September 12, 2018
This is version 178 of the entry and version 2 of the sequence. See 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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