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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

  • large ribosomal subunit rRNA binding Source: GO_Central
  • 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-28976-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 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
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

SGDiS000000183. RPL23A.

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 methionineiRemovedCombined sources1 Publication
Chaini2 – 13713660S ribosomal protein L23-APRO_0000128630Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources1 Publication
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.
TopDownProteomicsiP0CX41.

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. 89 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[»]
3JCTelectron microscopy3.08V1-137[»]
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[»]
5APNelectron microscopy3.91V1-137[»]
5APOelectron microscopy3.41V1-137[»]
5DC3X-ray3.25N3/n32-137[»]
5FCIX-ray3.40N3/n32-137[»]
5FCJX-ray3.10N3/n32-137[»]
5FL8electron microscopy9.50V1-137[»]
5GAKelectron microscopy3.88X1-137[»]
5I4LX-ray3.10N3/n32-137[»]
ProteinModelPortaliP0CX41.
SMRiP0CX41. Positions 6-137.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0CX41.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L14P family.Curated

Phylogenomic databases

HOGENOMiHOG000183703.
InParanoidiP0CX41.
KOiK02894.
OrthoDBiEOG092C5AG7.

Family and domain databases

Gene3Di2.40.150.20. 1 hit.
HAMAPiMF_01367. Ribosomal_L14. 1 hit.
InterProiIPR000218. Ribosomal_L14P.
IPR019972. Ribosomal_L14P_CS.
[Graphical view]
PANTHERiPTHR11761. PTHR11761. 1 hit.
PfamiPF00238. Ribosomal_L14. 1 hit.
[Graphical view]
SMARTiSM01374. 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[»]
3JCTelectron microscopy3.08V1-137[»]
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[»]
5APNelectron microscopy3.91V1-137[»]
5APOelectron microscopy3.41V1-137[»]
5DC3X-ray3.25N3/n32-137[»]
5FCIX-ray3.40N3/n32-137[»]
5FCJX-ray3.10N3/n32-137[»]
5FL8electron microscopy9.50V1-137[»]
5GAKelectron microscopy3.88X1-137[»]
5I4LX-ray3.10N3/n32-137[»]
ProteinModelPortaliP0CX41.
SMRiP0CX41. Positions 6-137.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32617. 89 interactions.
36862. 27 interactions.
IntActiP0CX41. 1 interaction.
MINTiMINT-515434.

Proteomic databases

MaxQBiP0CX41.
TopDownProteomicsiP0CX41.

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

SGDiS000000183. RPL23A.

Phylogenomic databases

HOGENOMiHOG000183703.
InParanoidiP0CX41.
KOiK02894.
OrthoDBiEOG092C5AG7.

Enzyme and pathway databases

BioCyciYEAST:G3O-28976-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).

Miscellaneous databases

EvolutionaryTraceiP0CX41.
PROiP0CX41.

Gene expression databases

ExpressionAtlasiP0CX41. differential.

Family and domain databases

Gene3Di2.40.150.20. 1 hit.
HAMAPiMF_01367. Ribosomal_L14. 1 hit.
InterProiIPR000218. Ribosomal_L14P.
IPR019972. Ribosomal_L14P_CS.
[Graphical view]
PANTHERiPTHR11761. PTHR11761. 1 hit.
PfamiPF00238. Ribosomal_L14. 1 hit.
[Graphical view]
SMARTiSM01374. Ribosomal_L14. 1 hit.
[Graphical view]
SUPFAMiSSF50193. SSF50193. 1 hit.
PROSITEiPS00049. RIBOSOMAL_L14. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: September 7, 2016
This is version 48 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

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.