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 L15-A

Gene

RPL15A

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

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.

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

GO - Cellular componenti

  • cytosolic large ribosomal subunit Source: SGD

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.
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. 227 interactors.
IntActiP05748. 23 interactors.
MINTiMINT-8285329.
STRINGi4932.YLR029C.

Structurei

Secondary structure

1204
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 10Combined sources8
Helixi17 – 32Combined sources16
Beta strandi35 – 38Combined sources4
Helixi45 – 50Combined sources6
Beta strandi59 – 67Combined sources9
Helixi76 – 78Combined sources3
Helixi84 – 86Combined sources3
Beta strandi89 – 91Combined sources3
Helixi98 – 109Combined sources12
Turni110 – 112Combined sources3
Beta strandi113 – 123Combined sources11
Beta strandi125 – 135Combined sources11
Beta strandi137 – 139Combined sources3
Helixi140 – 143Combined sources4
Turni146 – 148Combined sources3
Helixi149 – 152Combined sources4
Helixi154 – 156Combined sources3
Turni157 – 159Combined sources3
Helixi160 – 162Combined sources3
Helixi166 – 171Combined sources6
Helixi178 – 180Combined sources3
Beta strandi183 – 185Combined sources3
Helixi187 – 194Combined sources8
Beta strandi197 – 199Combined sources3

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[»]
5T62electron microscopy3.30a1-204[»]
5T6Relectron microscopy4.50a1-204[»]
5TGAX-ray3.30M5/m52-204[»]
5TGMX-ray3.50M5/m52-204[»]
ProteinModelPortaliP05748.
SMRiP05748.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05748.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000229584.
InParanoidiP05748.
KOiK02877.
OMAiERVGHNC.
OrthoDBiEOG092C4JEJ.

Family and domain databases

Gene3Di3.40.1120.10. 1 hit.
InterProiView protein in InterPro
IPR024794. Rbsml_L15e_core_dom.
IPR000439. Ribosomal_L15e.
IPR020925. Ribosomal_L15e_CS.
IPR012678. Ribosomal_L23/L15e_core_dom.
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

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 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: July 5, 2017
This is version 154 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