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Protein

60S ribosomal protein L15-A

Gene

RPL15A

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

There are 2 genes for eL15 in yeast.Curated

GO - Molecular functioni

  • RNA binding Source: SGD
  • structural constituent of ribosome Source: SGD

GO - Biological processi

  • cytoplasmic translation Source: SGD

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciYEAST:G3O-32188-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 L15-A1 Publication
Alternative name(s):
L13
Large ribosomal subunit protein eL15-A1 Publication
RP15R
YL10
YP18
Gene namesi
Name:RPL15A1 Publication
Synonyms:RPL10A, RPL13A, YL10A
Ordered Locus Names:YLR029C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR029C
SGDiS000004019 RPL15A

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
Initiator methionineiRemoved2 Publications
ChainiPRO_00001275662 – 20460S ribosomal protein L15-AAdd BLAST203

Proteomic databases

MaxQBiP05748
PaxDbiP05748
PRIDEiP05748

PTM databases

iPTMnetiP05748

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

BioGridi31303, 231 interactors
IntActiP05748, 23 interactors
MINTiP05748
STRINGi4932.YLR029C

Structurei

Secondary structure

1204
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 10Combined sources7
Helixi17 – 32Combined sources16
Beta strandi35 – 41Combined sources7
Helixi45 – 49Combined sources5
Turni50 – 52Combined sources3
Beta strandi59 – 67Combined sources9
Helixi98 – 109Combined sources12
Beta strandi112 – 117Combined sources6
Beta strandi120 – 123Combined sources4
Beta strandi125 – 135Combined sources11
Beta strandi137 – 139Combined sources3
Helixi140 – 144Combined sources5
Turni146 – 148Combined sources3
Helixi149 – 152Combined sources4
Helixi154 – 156Combined sources3
Helixi160 – 162Combined sources3
Helixi166 – 171Combined sources6
Beta strandi175 – 178Combined sources4
Helixi187 – 194Combined sources8
Beta strandi198 – 202Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-L3-196[»]
3J6Xelectron microscopy6.10551-204[»]
3J6Yelectron microscopy6.10551-204[»]
3J77electron microscopy6.20651-204[»]
3J78electron microscopy6.30651-204[»]
3JCTelectron microscopy3.08N1-204[»]
4U3MX-ray3.00M5/m52-204[»]
4U3NX-ray3.20M5/m52-204[»]
4U3UX-ray2.90M5/m52-204[»]
4U4NX-ray3.10M5/m52-204[»]
4U4OX-ray3.60M5/m52-204[»]
4U4QX-ray3.00M5/m52-204[»]
4U4RX-ray2.80M5/m52-204[»]
4U4UX-ray3.00M5/m52-204[»]
4U4YX-ray3.20M5/m52-204[»]
4U4ZX-ray3.10M5/m52-204[»]
4U50X-ray3.20M5/m52-204[»]
4U51X-ray3.20M5/m52-204[»]
4U52X-ray3.00M5/m52-204[»]
4U53X-ray3.30M5/m52-204[»]
4U55X-ray3.20M5/m52-204[»]
4U56X-ray3.45M5/m52-204[»]
4U6FX-ray3.10M5/m52-204[»]
4V4Belectron microscopy11.70BL2-204[»]
4V6Ielectron microscopy8.80BP1-204[»]
4V7Felectron microscopy8.70O1-204[»]
4V7RX-ray4.00BO/DO1-204[»]
4V88X-ray3.00BN/DN1-204[»]
4V8Telectron microscopy8.10N1-204[»]
4V8Yelectron microscopy4.30BN2-204[»]
4V8Zelectron microscopy6.60BN2-204[»]
4V91electron microscopy3.70N1-204[»]
5APNelectron microscopy3.91N1-204[»]
5APOelectron microscopy3.41N1-204[»]
5DATX-ray3.15M52-204[»]
m52-204[»]
5DC3X-ray3.25M5/m52-204[»]
5DGEX-ray3.45M5/m52-204[»]
5DGFX-ray3.30M5/m52-204[»]
5DGVX-ray3.10M5/m52-204[»]
5FCIX-ray3.40M5/m52-204[»]
5FCJX-ray3.10M5/m52-204[»]
5FL8electron microscopy9.50N1-204[»]
5GAKelectron microscopy3.88P1-204[»]
5H4Pelectron microscopy3.07N1-204[»]
5I4LX-ray3.10M5/m52-204[»]
5JCSelectron microscopy9.50N1-204[»]
5JUOelectron microscopy4.00S1-204[»]
5JUPelectron microscopy3.50S1-204[»]
5JUSelectron microscopy4.20S1-204[»]
5JUTelectron microscopy4.00S1-204[»]
5JUUelectron microscopy4.00S1-204[»]
5LYBX-ray3.25M5/m52-204[»]
5M1Jelectron microscopy3.30N52-204[»]
5MC6electron microscopy3.80AQ1-204[»]
5MEIX-ray3.50CP/v2-204[»]
5NDGX-ray3.70M5/m52-204[»]
5NDVX-ray3.30M5/m52-204[»]
5NDWX-ray3.70M5/m52-204[»]
5OBMX-ray3.40M5/m52-204[»]
5ON6X-ray3.10CP/v2-204[»]
5T62electron microscopy3.30a1-204[»]
5T6Relectron microscopy4.50a1-204[»]
5TBWX-ray3.00CP/v2-204[»]
5TGAX-ray3.30M5/m52-204[»]
5TGMX-ray3.50M5/m52-204[»]
5Z3Gelectron microscopy3.65R1-204[»]
6C0Felectron microscopy3.70N1-204[»]
6CB1electron microscopy4.60N1-204[»]
6ELZelectron microscopy3.30N1-204[»]
6EM1electron microscopy3.60N1-204[»]
6EM3electron microscopy3.20N1-204[»]
6EM4electron microscopy4.10N1-204[»]
6EM5electron microscopy4.30N1-204[»]
6FT6electron microscopy3.90N1-204[»]
ProteinModelPortaliP05748
SMRiP05748
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05748

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00910000144184
HOGENOMiHOG000229584
InParanoidiP05748
KOiK02877
OMAiERVGHNC
OrthoDBiEOG092C4JEJ

Family and domain databases

Gene3Di3.40.1120.10, 1 hit
InterProiView protein in InterPro
IPR024794 Rbsml_L15e_core_dom_sf
IPR000439 Ribosomal_L15e
IPR020925 Ribosomal_L15e_CS
IPR012678 Ribosomal_L23/L15e_core_dom_sf
PANTHERiPTHR11847 PTHR11847, 1 hit
PfamiView protein in Pfam
PF00827 Ribosomal_L15e, 1 hit
SMARTiView protein in SMART
SM01384 Ribosomal_L15e, 1 hit
SUPFAMiSSF54189 SSF54189, 1 hit
PROSITEiView protein in PROSITE
PS01194 RIBOSOMAL_L15E, 1 hit

Sequencei

Sequence statusi: Complete.

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

P05748-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGAYKYLEEL QRKKQSDVLR FLQRVRVWEY RQKNVIHRAA RPTRPDKARR
60 70 80 90 100
LGYKAKQGFV IYRVRVRRGN RKRPVPKGAT YGKPTNQGVN ELKYQRSLRA
110 120 130 140 150
TAEERVGRRA ANLRVLNSYW VNQDSTYKYF EVILVDPQHK AIRRDARYNW
160 170 180 190 200
ICDPVHKHRE ARGLTATGKK SRGINKGHKF NNTKAGRRKT WKRQNTLSLW

RYRK
Length:204
Mass (Da):24,422
Last modified:January 23, 2007 - v3
Checksum:i3913F9E4AB9ECA2C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti28W → G AA sequence (PubMed:6814480).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14675 Genomic DNA Translation: BAA03506.1
Z73201 Genomic DNA Translation: CAA97553.1
BK006945 Genomic DNA Translation: DAA09347.1
PIRiS48502
RefSeqiNP_013129.1, NM_001181916.1

Genome annotation databases

EnsemblFungiiYLR029C; YLR029C; YLR029C
GeneIDi850716
KEGGisce:YLR029C

Similar proteinsi

Entry informationi

Entry nameiRL15A_YEAST
AccessioniPrimary (citable) accession number: P05748
Secondary accession number(s): D6VY31
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 163 of the entry and version 3 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

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 XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

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