Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

60S ribosomal protein L34-A

Gene

RPL34A

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 23600 molecules/cell in log phase SD medium.1 Publication
There are 2 genes for eL34 in yeast.Curated

GO - Molecular functioni

GO - Biological processi

  • cytoplasmic translation Source: SGD
  • ribosome biogenesis Source: SGD
  • translation Source: GO_Central

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciYEAST:G3O-30350-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 L34-A1 Publication
Alternative name(s):
Large ribosomal subunit protein eL34-A1 Publication
Gene namesi
Name:RPL34A1 Publication
Ordered Locus Names:YER056C-A
ORF Names:YER056BC
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome V

Organism-specific databases

EuPathDBiFungiDB:YER056C-A
SGDiS000002135 RPL34A

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_00001318451 – 12160S ribosomal protein L34-AAdd BLAST121

Proteomic databases

MaxQBiP87262
PaxDbiP87262
PRIDEiP87262

PTM databases

iPTMnetiP87262

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).1 Publication1 Publication

Protein-protein interaction databases

BioGridi36797, 104 interactors
IntActiP87262, 13 interactors
MINTiP87262
STRINGi4932.YER056C-A

Structurei

Secondary structure

1121
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 10Combined sources3
Helixi16 – 18Combined sources3
Beta strandi19 – 24Combined sources6
Turni26 – 28Combined sources3
Beta strandi30 – 35Combined sources6
Turni45 – 47Combined sources3
Beta strandi52 – 54Combined sources3
Helixi59 – 64Combined sources6
Helixi67 – 70Combined sources4
Turni75 – 79Combined sources5
Helixi83 – 111Combined sources29

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J6Xelectron microscopy6.10741-121[»]
3J6Yelectron microscopy6.10741-121[»]
3J77electron microscopy6.20841-121[»]
3J78electron microscopy6.30841-121[»]
3JCTelectron microscopy3.08g1-121[»]
4U3MX-ray3.00O4/o42-121[»]
4U3NX-ray3.20O4/o42-121[»]
4U3UX-ray2.90O4/o42-121[»]
4U4NX-ray3.10O4/o42-121[»]
4U4OX-ray3.60O4/o42-109[»]
4U4QX-ray3.00O4/o42-120[»]
4U4RX-ray2.80O4/o42-121[»]
4U4UX-ray3.00O4/o42-121[»]
4U4YX-ray3.20O4/o42-120[»]
4U4ZX-ray3.10O4/o42-109[»]
4U50X-ray3.20O4/o42-120[»]
4U51X-ray3.20O4/o42-120[»]
4U52X-ray3.00O4/o42-109[»]
4U53X-ray3.30O4/o42-121[»]
4U55X-ray3.20O4/o42-120[»]
4U56X-ray3.45O4/o42-120[»]
4U6FX-ray3.10O4/o42-120[»]
4V6Ielectron microscopy8.80Bi1-118[»]
4V7Felectron microscopy8.70f1-121[»]
4V88X-ray3.00Bg/Dg1-121[»]
4V8Telectron microscopy8.10g1-121[»]
4V8Yelectron microscopy4.30Bg2-121[»]
4V8Zelectron microscopy6.60Bg2-121[»]
4V91electron microscopy3.70g1-121[»]
5APNelectron microscopy3.91g1-121[»]
5APOelectron microscopy3.41g1-121[»]
5DATX-ray3.15O4/o42-121[»]
5DC3X-ray3.25O4/o42-121[»]
5DGEX-ray3.45O4/o42-109[»]
5DGFX-ray3.30O4/o42-121[»]
5DGVX-ray3.10O4/o42-121[»]
5FCIX-ray3.40O4/o42-121[»]
5FCJX-ray3.10O4/o42-121[»]
5FL8electron microscopy9.50g1-121[»]
5GAKelectron microscopy3.88i1-121[»]
5H4Pelectron microscopy3.07g1-121[»]
5I4LX-ray3.10O4/o42-113[»]
5JCSelectron microscopy9.50g1-121[»]
5JUOelectron microscopy4.00LA1-121[»]
5JUPelectron microscopy3.50LA1-121[»]
5JUSelectron microscopy4.20LA1-121[»]
5JUTelectron microscopy4.00LA1-121[»]
5JUUelectron microscopy4.00LA1-121[»]
5LYBX-ray3.25O4/o42-113[»]
5M1Jelectron microscopy3.30g52-113[»]
5MC6electron microscopy3.80BN1-121[»]
5MEIX-ray3.50AH/DI2-113[»]
5NDGX-ray3.70O4/o42-113[»]
5NDVX-ray3.30O4/o42-113[»]
5NDWX-ray3.70O4/o42-113[»]
5OBMX-ray3.40O4/o42-113[»]
5ON6X-ray3.10AH/DI2-113[»]
5T62electron microscopy3.30t1-121[»]
5T6Relectron microscopy4.50t1-121[»]
5TBWX-ray3.00AH/DI2-113[»]
5TGAX-ray3.30O4/o42-113[»]
5TGMX-ray3.50O4/o42-113[»]
6ELZelectron microscopy3.30g1-121[»]
6EM5electron microscopy4.30g1-121[»]
ProteinModelPortaliP87262
SMRiP87262
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000008294
HOGENOMiHOG000216922
InParanoidiP87262
KOiK02915
OMAiKTHAFAK
OrthoDBiEOG092C5L2Y

Family and domain databases

Gene3Di3.40.1800.40, 1 hit
InterProiView protein in InterPro
IPR008195 Ribosomal_L34Ae
IPR038562 Ribosomal_L34Ae_sf
IPR018065 Ribosomal_L34e_CS
PANTHERiPTHR10759 PTHR10759, 1 hit
PfamiView protein in Pfam
PF01199 Ribosomal_L34e, 1 hit
PRINTSiPR01250 RIBOSOMALL34
PROSITEiView protein in PROSITE
PS01145 RIBOSOMAL_L34E, 1 hit

Sequencei

Sequence statusi: Complete.

P87262-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQRVTFRRR NPYNTRSNKI KVVKTPGGIL RAQHVKKLAT RPKCGDCGSA
60 70 80 90 100
LQGISTLRPR QYATVSKTHK TVSRAYGGSR CANCVKERII RAFLIEEQKI
110 120
VKKVVKEQTE AAKKSEKKAK K
Length:121
Mass (Da):13,639
Last modified:July 1, 1997 - v1
Checksum:iF3315816CD85ACEA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18813 Genomic DNA Translation: AAB64609.1
BK006939 Genomic DNA Translation: DAA07714.1
PIRiS53549
RefSeqiNP_010977.2, NM_001180036.1

Genome annotation databases

EnsemblFungiiYER056C-A; YER056C-A; YER056C-A
GeneIDi856784
KEGGisce:YER056C-A

Similar proteinsi

Entry informationi

Entry nameiRL34A_YEAST
AccessioniPrimary (citable) accession number: P87262
Secondary accession number(s): D3DLW0, Q03189
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 1, 1997
Last modified: April 25, 2018
This is version 137 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health