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Protein

60S ribosomal protein L23-A

Gene

RPL23A

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. structural constituent of ribosome Source: SGD

GO - Biological processi

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

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciYEAST:G3O-28976-MONOMER.
ReactomeiREACT_188965. SRP-dependent cotranslational protein targeting to membrane.
REACT_189050. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_189183. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_217188. Formation of a pool of free 40S subunits.
REACT_232946. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_252688. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_257951. Peptide chain elongation.

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L23-A
Alternative name(s):
L17a
YL32
Gene namesi
Name:RPL23A
Synonyms:RPL17A, RPL17AA
Ordered Locus Names:YBL087C
ORF Names:YBL0713
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome II

Organism-specific databases

CYGDiYBL087c.
SGDiS000000183. RPL23A.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. 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 – 13713660S ribosomal protein L23-APRO_0000128630Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei106 – 1061N6,N6-dimethyllysine; by RKM11 Publication
Modified residuei110 – 1101N6,N6-dimethyllysine; by RKM11 Publication

Post-translational modificationi

Methylated by RKM1 at 2 different sites, but it is unclear which are the 2 methylated residues among Lys-40, Lys-106 and/or Lys-110.1 Publication

Keywords - PTMi

Acetylation, Methylation

Proteomic databases

MaxQBiP0CX41.

Expressioni

Gene expression databases

ExpressionAtlasiP0CX41. differential.

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

BioGridi32617. 92 interactions.
36862. 27 interactions.
IntActiP0CX41. 1 interaction.
MINTiMINT-515434.

Structurei

Secondary structure

1
137
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi22 – 254Combined sources
Beta strandi27 – 315Combined sources
Beta strandi33 – 397Combined sources
Beta strandi57 – 615Combined sources
Beta strandi63 – 653Combined sources
Helixi67 – 693Combined sources
Beta strandi70 – 723Combined sources
Beta strandi74 – 807Combined sources
Beta strandi92 – 976Combined sources
Beta strandi99 – 1035Combined sources
Turni105 – 1073Combined sources
Beta strandi109 – 1124Combined sources
Helixi120 – 1234Combined sources
Helixi127 – 1315Combined sources
Beta strandi134 – 1363Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-R7-137[»]
2X7Nelectron microscopy11.80C6-137[»]
3J16electron microscopy-I1-137[»]
3J6Xelectron microscopy6.10631-137[»]
3J6Yelectron microscopy6.10631-137[»]
3J77electron microscopy6.20731-137[»]
3J78electron microscopy6.30731-137[»]
4U3MX-ray3.00N3/n32-137[»]
4U3NX-ray3.20N3/n32-137[»]
4U3UX-ray2.90N3/n32-137[»]
4U4NX-ray3.10N3/n32-137[»]
4U4OX-ray3.60N3/n32-137[»]
4U4QX-ray3.00N3/n32-137[»]
4U4RX-ray2.80N3/n32-137[»]
4U4UX-ray3.00N3/n32-137[»]
4U4YX-ray3.20N3/n32-137[»]
4U4ZX-ray3.10N3/n32-137[»]
4U50X-ray3.20N3/n32-137[»]
4U51X-ray3.20N3/n32-137[»]
4U52X-ray3.00N3/n32-137[»]
4U53X-ray3.30N3/n32-137[»]
4U55X-ray3.20N3/n32-137[»]
4U56X-ray3.45N3/n32-137[»]
4U6FX-ray3.10N3/n32-137[»]
4V4Belectron microscopy11.70BR1-137[»]
4V6Ielectron microscopy8.80BM1-137[»]
4V7Felectron microscopy8.70L1-137[»]
4V7RX-ray4.00BU/DU1-137[»]
4V88X-ray3.00BV/DV1-137[»]
4V8Telectron microscopy8.10V1-137[»]
4V8Yelectron microscopy4.30BV2-137[»]
4V8Zelectron microscopy6.60BV2-137[»]
4V91electron microscopy3.70V1-137[»]
ProteinModelPortaliP0CX41.
SMRiP0CX41. Positions 2-137.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0CX41.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L14P family.Curated

Phylogenomic databases

HOGENOMiHOG000183703.
InParanoidiP0CX41.
KOiK02894.
OrthoDBiEOG7N0CHC.

Family and domain databases

Gene3Di2.40.150.20. 1 hit.
HAMAPiMF_01367. Ribosomal_L14.
InterProiIPR019972. Ribosomal_L14_CS.
IPR023571. Ribosomal_L14_dom.
IPR000218. Ribosomal_L14b/L23e.
[Graphical view]
PANTHERiPTHR11761. PTHR11761. 1 hit.
PfamiPF00238. Ribosomal_L14. 1 hit.
[Graphical view]
SUPFAMiSSF50193. SSF50193. 1 hit.
PROSITEiPS00049. RIBOSOMAL_L14. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0CX41-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGNGAQGTK FRISLGLPVG AIMNCADNSG ARNLYIIAVK GSGSRLNRLP
60 70 80 90 100
AASLGDMVMA TVKKGKPELR KKVMPAIVVR QAKSWRRRDG VFLYFEDNAG
110 120 130
VIANPKGEMK GSAITGPVGK ECADLWPRVA SNSGVVV
Length:137
Mass (Da):14,473
Last modified:June 28, 2011 - v1
Checksum:iDEB983B3CB1DFAB1
GO

Mass spectrometryi

Molecular mass is 14430.702 Da from positions 2 - 137. Determined by ESI. Monoisotopic mass with either 7 methylation modifications or 1 acetylation and 4 methylation modifications.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01694 Genomic DNA. Translation: CAA25841.1.
X79489 Genomic DNA. Translation: CAA56018.1.
Z35848 Genomic DNA. Translation: CAA84908.1.
BK006936 Genomic DNA. Translation: DAA07037.1.
PIRiA02792. R5BY17.
RefSeqiNP_009466.1. NM_001178327.1.
NP_011042.3. NM_001179007.3.

Genome annotation databases

EnsemblFungiiYBL087C; YBL087C; YBL087C.
YER117W; YER117W; YER117W.
GeneIDi852191.
856853.
KEGGisce:YBL087C.
sce:YER117W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01694 Genomic DNA. Translation: CAA25841.1.
X79489 Genomic DNA. Translation: CAA56018.1.
Z35848 Genomic DNA. Translation: CAA84908.1.
BK006936 Genomic DNA. Translation: DAA07037.1.
PIRiA02792. R5BY17.
RefSeqiNP_009466.1. NM_001178327.1.
NP_011042.3. NM_001179007.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-R7-137[»]
2X7Nelectron microscopy11.80C6-137[»]
3J16electron microscopy-I1-137[»]
3J6Xelectron microscopy6.10631-137[»]
3J6Yelectron microscopy6.10631-137[»]
3J77electron microscopy6.20731-137[»]
3J78electron microscopy6.30731-137[»]
4U3MX-ray3.00N3/n32-137[»]
4U3NX-ray3.20N3/n32-137[»]
4U3UX-ray2.90N3/n32-137[»]
4U4NX-ray3.10N3/n32-137[»]
4U4OX-ray3.60N3/n32-137[»]
4U4QX-ray3.00N3/n32-137[»]
4U4RX-ray2.80N3/n32-137[»]
4U4UX-ray3.00N3/n32-137[»]
4U4YX-ray3.20N3/n32-137[»]
4U4ZX-ray3.10N3/n32-137[»]
4U50X-ray3.20N3/n32-137[»]
4U51X-ray3.20N3/n32-137[»]
4U52X-ray3.00N3/n32-137[»]
4U53X-ray3.30N3/n32-137[»]
4U55X-ray3.20N3/n32-137[»]
4U56X-ray3.45N3/n32-137[»]
4U6FX-ray3.10N3/n32-137[»]
4V4Belectron microscopy11.70BR1-137[»]
4V6Ielectron microscopy8.80BM1-137[»]
4V7Felectron microscopy8.70L1-137[»]
4V7RX-ray4.00BU/DU1-137[»]
4V88X-ray3.00BV/DV1-137[»]
4V8Telectron microscopy8.10V1-137[»]
4V8Yelectron microscopy4.30BV2-137[»]
4V8Zelectron microscopy6.60BV2-137[»]
4V91electron microscopy3.70V1-137[»]
ProteinModelPortaliP0CX41.
SMRiP0CX41. Positions 2-137.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32617. 92 interactions.
36862. 27 interactions.
IntActiP0CX41. 1 interaction.
MINTiMINT-515434.

Proteomic databases

MaxQBiP0CX41.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBL087C; YBL087C; YBL087C.
YER117W; YER117W; YER117W.
GeneIDi852191.
856853.
KEGGisce:YBL087C.
sce:YER117W.

Organism-specific databases

CYGDiYBL087c.
SGDiS000000183. RPL23A.

Phylogenomic databases

HOGENOMiHOG000183703.
InParanoidiP0CX41.
KOiK02894.
OrthoDBiEOG7N0CHC.

Enzyme and pathway databases

BioCyciYEAST:G3O-28976-MONOMER.
ReactomeiREACT_188965. SRP-dependent cotranslational protein targeting to membrane.
REACT_189050. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_189183. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_217188. Formation of a pool of free 40S subunits.
REACT_232946. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_252688. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_257951. Peptide chain elongation.

Miscellaneous databases

EvolutionaryTraceiP0CX41.
NextBioi970670.

Gene expression databases

ExpressionAtlasiP0CX41. differential.

Family and domain databases

Gene3Di2.40.150.20. 1 hit.
HAMAPiMF_01367. Ribosomal_L14.
InterProiIPR019972. Ribosomal_L14_CS.
IPR023571. Ribosomal_L14_dom.
IPR000218. Ribosomal_L14b/L23e.
[Graphical view]
PANTHERiPTHR11761. PTHR11761. 1 hit.
PfamiPF00238. Ribosomal_L14. 1 hit.
[Graphical view]
SUPFAMiSSF50193. SSF50193. 1 hit.
PROSITEiPS00049. RIBOSOMAL_L14. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces cerevisiae chromosome II."
    Obermaier B., Gassenhuber J., Piravandi E., Domdey H.
    Yeast 11:1103-1112(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "Complete DNA sequence of yeast chromosome II."
    Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
    , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
    EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "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.
  6. "Direct mass spectrometric analysis of intact proteins of the yeast large ribosomal subunit using capillary LC/FTICR."
    Lee S.-W., Berger S.J., Martinovic S., Pasa-Tolic L., Anderson G.A., Shen Y., Zhao R., Smith R.D.
    Proc. Natl. Acad. Sci. U.S.A. 99:5942-5947(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
  7. "A novel SET domain methyltransferase modifies ribosomal protein Rpl23ab in yeast."
    Porras-Yakushi T.R., Whitelegge J.P., Miranda T.B., Clarke S.
    J. Biol. Chem. 280:34590-34598(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT SER-2, METHYLATION.
  8. "Yeast ribosomal/cytochrome c SET domain methyltransferase subfamily: identification of Rpl23ab methylation sites and recognition motifs."
    Porras-Yakushi T.R., Whitelegge J.P., Clarke S.
    J. Biol. Chem. 282:12368-12376(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT LYS-106 AND LYS-110.
  9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  10. "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 7-137, ELECTRON MICROSCOPY.
  11. "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.
  12. "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.
  13. Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 80S RIBOSOME.

Entry informationi

Entry nameiRL23A_YEAST
AccessioniPrimary (citable) accession number: P0CX41
Secondary accession number(s): D3DM23, P04451
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: June 28, 2011
Last modified: March 4, 2015
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

There are 2 genes for L23 in yeast.

Keywords - Technical termi

3D-structure, Complete proteome, 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 II
    Yeast (Saccharomyces cerevisiae) chromosome II: 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.