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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

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 uL14 in yeast.Curated

GO - Molecular functioni

GO - Biological processi

  • cytoplasmic translation Source: SGD

Keywordsi

Molecular functionRibonucleoprotein, 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-A1 Publication
Alternative name(s):
L17a
Large ribosomal subunit protein uL14-A1 Publication
YL32
Gene namesi
Name:RPL23A1 Publication
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

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 methionineiRemovedCombined sources1 Publication
ChainiPRO_00001286302 – 13760S ribosomal protein L23-AAdd BLAST136

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1 Publication1
Modified residuei106N6,N6-dimethyllysine; by RKM11 Publication1
Modified residuei110N6,N6-dimethyllysine; by RKM11 Publication1

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.
PRIDEiP0CX41.
TopDownProteomicsiP0CX41.

PTM databases

iPTMnetiP0CX41.

Expressioni

Gene expression databases

ExpressionAtlasiP0CX41. differential.

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

BioGridi32617. 207 interactors.
36862. 151 interactors.
IntActiP0CX41. 2 interactors.
MINTiMINT-515434.
STRINGi4932.YER117W.

Structurei

Secondary structure

1137
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi22 – 25Combined sources4
Beta strandi27 – 31Combined sources5
Beta strandi33 – 39Combined sources7
Beta strandi57 – 61Combined sources5
Beta strandi63 – 65Combined sources3
Helixi67 – 69Combined sources3
Beta strandi70 – 72Combined sources3
Beta strandi74 – 80Combined sources7
Beta strandi92 – 97Combined sources6
Beta strandi99 – 103Combined sources5
Turni105 – 107Combined sources3
Beta strandi109 – 112Combined sources4
Helixi120 – 123Combined sources4
Helixi127 – 131Combined sources5
Beta strandi134 – 136Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5DATX-ray3.15N3/n32-137[»]
5DC3X-ray3.25N3/n32-137[»]
5DGEX-ray3.45N3/n32-137[»]
5DGFX-ray3.30N3/n32-137[»]
5DGVX-ray3.10N3/n32-137[»]
5FCIX-ray3.40N3/n32-137[»]
5FCJX-ray3.10N3/n32-137[»]
5FL8electron microscopy9.50V1-137[»]
5GAKelectron microscopy3.88X1-137[»]
5H4Pelectron microscopy3.07V1-137[»]
5I4LX-ray3.10N3/n32-137[»]
5JCSelectron microscopy9.50V1-137[»]
5JUOelectron microscopy4.00AA1-137[»]
5JUPelectron microscopy3.50AA1-137[»]
5JUSelectron microscopy4.20AA1-137[»]
5JUTelectron microscopy4.00AA1-137[»]
5JUUelectron microscopy4.00AA1-137[»]
5LYBX-ray3.25N3/n32-137[»]
5M1Jelectron microscopy3.30V52-137[»]
5MC6electron microscopy3.80AB1-137[»]
5MEIX-ray3.50CX/l22-137[»]
5T62electron microscopy3.30i1-137[»]
5T6Relectron microscopy4.50i1-137[»]
5TBWX-ray3.006/CX2-137[»]
5TGAX-ray3.30N3/n32-137[»]
5TGMX-ray3.50N3/n32-137[»]
ProteinModelPortaliP0CX41.
SMRiP0CX41.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0CX41.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000183703.
InParanoidiP0CX41.
KOiK02894.
OMAiELRKKTM.
OrthoDBiEOG092C5AG7.

Family and domain databases

Gene3Di2.40.150.20. 1 hit.
HAMAPiMF_01367. Ribosomal_L14. 1 hit.
InterProiView protein in InterPro
IPR000218. Ribosomal_L14P.
IPR019972. Ribosomal_L14P_CS.
IPR036853. Ribosomal_L14P_sf.
PANTHERiPTHR11761. PTHR11761. 1 hit.
PfamiView protein in Pfam
PF00238. Ribosomal_L14. 1 hit.
SMARTiView protein in SMART
SM01374. Ribosomal_L14. 1 hit.
SUPFAMiSSF50193. SSF50193. 1 hit.
PROSITEiView protein in PROSITE
PS00049. RIBOSOMAL_L14. 1 hit.

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.

Similar proteinsi

Entry informationi

Entry nameiRL23A_YEAST
AccessioniPrimary (citable) accession number: P0CX41
Secondary accession number(s): D3DM23, P04451
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: June 28, 2011
Last modified: November 22, 2017
This is version 61 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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