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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: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

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

GO - Biological processi

  • cytoplasmic translation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciYEAST:G3O-32188-MONOMER.
ReactomeiREACT_290856. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_302067. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_307259. Formation of a pool of free 40S subunits.
REACT_314339. SRP-dependent cotranslational protein targeting to membrane.
REACT_332565. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_343353. Peptide chain elongation.
REACT_346847. GTP hydrolysis and joining of the 60S ribosomal subunit.

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L15-A
Alternative name(s):
L13
RP15R
YL10
YP18
Gene namesi
Name:RPL15A
Synonyms:RPL10A, RPL13A, YL10A
Ordered Locus Names:YLR029C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR029C.
SGDiS000004019. RPL15A.

Subcellular locationi

GO - Cellular componenti

  • cytosolic large ribosomal subunit Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 20420360S ribosomal protein L15-APRO_0000127566Add
BLAST

Proteomic databases

MaxQBiP05748.
PeptideAtlasiP05748.

Expressioni

Gene expression databases

GenevestigatoriP05748.

Interactioni

Subunit structurei

Component of the large ribosomal subunit. Mature ribosomes consist of a small (40S) and a large (60S) subunit. The 40S subunit contains 32 different proteins (encoded by 56 genes) and 1 molecule of RNA (18S). The 60S subunit contains 46 different proteins (encoded by 81 genes) and 3 molecules of RNA (25S, 5.8S and 5S).1 Publication

Protein-protein interaction databases

BioGridi31303. 119 interactions.
IntActiP05748. 21 interactions.
MINTiMINT-8285329.
STRINGi4932.YLR029C.

Structurei

Secondary structure

1
204
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 108Combined sources
Helixi17 – 3216Combined sources
Beta strandi35 – 384Combined sources
Helixi45 – 506Combined sources
Beta strandi59 – 679Combined sources
Helixi76 – 783Combined sources
Helixi84 – 863Combined sources
Beta strandi89 – 913Combined sources
Helixi98 – 10912Combined sources
Turni110 – 1123Combined sources
Beta strandi113 – 12311Combined sources
Beta strandi125 – 13511Combined sources
Beta strandi137 – 1393Combined sources
Helixi140 – 1434Combined sources
Turni146 – 1483Combined sources
Helixi149 – 1524Combined sources
Helixi154 – 1563Combined sources
Turni157 – 1593Combined sources
Helixi160 – 1623Combined sources
Helixi166 – 1716Combined sources
Helixi178 – 1803Combined sources
Beta strandi183 – 1853Combined sources
Helixi187 – 1948Combined sources
Beta strandi197 – 1993Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-L3-196[»]
3J6Xelectron microscopy6.10551-204[»]
3J6Yelectron microscopy6.10551-204[»]
3J77electron microscopy6.20651-204[»]
3J78electron microscopy6.30651-204[»]
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[»]
ProteinModelPortaliP05748.
SMRiP05748. Positions 3-175.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05748.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L15e family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000005092.
HOGENOMiHOG000229584.
InParanoidiP05748.
KOiK02877.
OMAiSKMGQVK.
OrthoDBiEOG7S4XJ3.

Family and domain databases

Gene3Di3.40.1120.10. 1 hit.
InterProiIPR024794. Rbsml_L15e_core_dom.
IPR000439. Ribosomal_L15e.
IPR020925. Ribosomal_L15e_CS.
IPR012678. Ribosomal_L23/L15e_core_dom.
[Graphical view]
PANTHERiPTHR11847. PTHR11847. 1 hit.
PfamiPF00827. Ribosomal_L15e. 1 hit.
[Graphical view]
SUPFAMiSSF54189. SSF54189. 1 hit.
PROSITEiPS01194. RIBOSOMAL_L15E. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti28 – 281W → G AA sequence (PubMed:6814480).Curated

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.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-L3-196[»]
3J6Xelectron microscopy6.10551-204[»]
3J6Yelectron microscopy6.10551-204[»]
3J77electron microscopy6.20651-204[»]
3J78electron microscopy6.30651-204[»]
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[»]
ProteinModelPortaliP05748.
SMRiP05748. Positions 3-175.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31303. 119 interactions.
IntActiP05748. 21 interactions.
MINTiMINT-8285329.
STRINGi4932.YLR029C.

Proteomic databases

MaxQBiP05748.
PeptideAtlasiP05748.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR029C; YLR029C; YLR029C.
GeneIDi850716.
KEGGisce:YLR029C.

Organism-specific databases

EuPathDBiFungiDB:YLR029C.
SGDiS000004019. RPL15A.

Phylogenomic databases

GeneTreeiENSGT00390000005092.
HOGENOMiHOG000229584.
InParanoidiP05748.
KOiK02877.
OMAiSKMGQVK.
OrthoDBiEOG7S4XJ3.

Enzyme and pathway databases

BioCyciYEAST:G3O-32188-MONOMER.
ReactomeiREACT_290856. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_302067. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_307259. Formation of a pool of free 40S subunits.
REACT_314339. SRP-dependent cotranslational protein targeting to membrane.
REACT_332565. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_343353. Peptide chain elongation.
REACT_346847. GTP hydrolysis and joining of the 60S ribosomal subunit.

Miscellaneous databases

EvolutionaryTraceiP05748.
NextBioi966784.
PROiP05748.

Gene expression databases

GenevestigatoriP05748.

Family and domain databases

Gene3Di3.40.1120.10. 1 hit.
InterProiIPR024794. Rbsml_L15e_core_dom.
IPR000439. Ribosomal_L15e.
IPR020925. Ribosomal_L15e_CS.
IPR012678. Ribosomal_L23/L15e_core_dom.
[Graphical view]
PANTHERiPTHR11847. PTHR11847. 1 hit.
PfamiPF00827. Ribosomal_L15e. 1 hit.
[Graphical view]
SUPFAMiSSF54189. SSF54189. 1 hit.
PROSITEiPS01194. RIBOSOMAL_L15E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Tomiyoshi A., Suzuki K., Otaka E.
    Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Isolation of seventeen proteins and amino-terminal amino acid sequences of eight proteins from cytoplasmic ribosomes of yeast."
    Otaka E., Higo K., Osawa S.
    Biochemistry 21:4545-4550(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-44.
  5. "NH2-terminal acetylation of ribosomal proteins of Saccharomyces cerevisiae."
    Takakura H., Tsunasawa S., Miyagi M., Warner J.R.
    J. Biol. Chem. 267:5442-5445(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-9.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Structure of the 80S ribosome from Saccharomyces cerevisiae -- tRNA-ribosome and subunit-subunit interactions."
    Spahn C.M.T., Beckmann R., Eswar N., Penczek P.A., Sali A., Blobel G., Frank J.
    Cell 107:373-386(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING OF 3-196, ELECTRON MICROSCOPY.
  8. "Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation."
    Spahn C.M.T., Gomez-Lorenzo M.G., Grassucci R.A., Joergensen R., Andersen G.R., Beckmann R., Penczek P.A., Ballesta J.P.G., Frank J.
    EMBO J. 23:1008-1019(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING, ELECTRON MICROSCOPY.
  9. "The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae."
    Planta R.J., Mager W.H.
    Yeast 14:471-477(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NOMENCLATURE, SUBUNIT.
  10. "Crystal structure of the eukaryotic ribosome."
    Ben-Shem A., Jenner L., Yusupova G., Yusupov M.
    Science 330:1203-1209(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 80S RIBOSOME.
  11. Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 80S RIBOSOME.

Entry informationi

Entry nameiRL15A_YEAST
AccessioniPrimary (citable) accession number: P05748
Secondary accession number(s): D6VY31
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: May 27, 2015
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

There are 2 genes for L15 in yeast.

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

External Data

Dasty 3

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 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.