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Protein

60S ribosomal protein L43-A

Gene

RPL43A

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

Present with 44600 molecules/cell in log phase SD medium.1 Publication
There are 2 genes for eL43 in yeast.Curated

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri39 – 60C4-typeAdd BLAST22

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • structural constituent of ribosome Source: SGD

GO - Biological processi

  • cytoplasmic translation Source: SGD

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-34199-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 L43-A1 Publication
Alternative name(s):
L37a
Large ribosomal subunit protein eL43-A1 Publication
YL35
Gene namesi
Name:RPL43A1 Publication
Ordered Locus Names:YPR043W
ORF Names:YP9499.02
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

SGDiS000006247. RPL43A.

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 methionineiRemoved1 Publication
ChainiPRO_00001398382 – 9260S ribosomal protein L43-AAdd BLAST91

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei40PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP0CX25.
PRIDEiP0CX25.

PTM databases

iPTMnetiP0CX25.

Expressioni

Gene expression databases

ExpressionAtlasiP0CX25. differential.

Interactioni

Subunit structurei

Component of the small ribosomal subunit (SSU). 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

BioGridi33849. 123 interactors.
36220. 282 interactors.
MINTiMINT-2781587.

Structurei

Secondary structure

192
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 14Combined sources6
Turni15 – 18Combined sources4
Helixi20 – 34Combined sources15
Turni40 – 42Combined sources3
Beta strandi44 – 49Combined sources6
Beta strandi54 – 57Combined sources4
Turni58 – 60Combined sources3
Beta strandi63 – 65Combined sources3
Beta strandi68 – 72Combined sources5
Helixi74 – 91Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-210-82[»]
3J6Xelectron microscopy6.10831-92[»]
3J6Yelectron microscopy6.10831-92[»]
3J77electron microscopy6.20931-92[»]
3J78electron microscopy6.30931-92[»]
3JCTelectron microscopy3.08p1-92[»]
4U3MX-ray3.00Q3/q32-92[»]
4U3NX-ray3.20Q3/q32-92[»]
4U3UX-ray2.90Q3/q32-92[»]
4U4NX-ray3.10Q3/q32-92[»]
4U4OX-ray3.60Q3/q32-92[»]
4U4QX-ray3.00Q3/q32-92[»]
4U4RX-ray2.80Q3/q32-92[»]
4U4UX-ray3.00Q3/q32-92[»]
4U4YX-ray3.20Q3/q32-92[»]
4U4ZX-ray3.10Q3/q32-92[»]
4U50X-ray3.20Q3/q32-92[»]
4U51X-ray3.20Q3/q32-92[»]
4U52X-ray3.00Q3/q32-92[»]
4U53X-ray3.30Q3/q32-92[»]
4U55X-ray3.20Q3/q32-92[»]
4U56X-ray3.45Q3/q32-92[»]
4U6FX-ray3.10Q3/q32-92[»]
4V4Belectron microscopy11.70B92-92[»]
4V6Ielectron microscopy8.80Bm1-92[»]
4V7Felectron microscopy8.70k1-92[»]
4V7RX-ray4.00Bg/Dg1-92[»]
4V88X-ray3.00Bp/Dp1-92[»]
4V8Telectron microscopy8.10p1-92[»]
4V91electron microscopy3.70p1-92[»]
5APNelectron microscopy3.91p1-92[»]
5APOelectron microscopy3.41p1-92[»]
5DATX-ray3.15Q3/q32-92[»]
5DC3X-ray3.25Q3/q32-92[»]
5DGEX-ray3.45Q3/q32-92[»]
5DGFX-ray3.30Q3/q32-92[»]
5DGVX-ray3.10Q3/q32-92[»]
5FCIX-ray3.40Q3/q32-92[»]
5FCJX-ray3.10Q3/q32-92[»]
5FL8electron microscopy9.50p1-92[»]
5GAKelectron microscopy3.88D1-92[»]
5H4Pelectron microscopy3.07p1-92[»]
5I4LX-ray3.10Q3/q32-92[»]
5JCSelectron microscopy9.50p1-92[»]
5JUOelectron microscopy4.00UA1-92[»]
5JUPelectron microscopy3.50UA1-92[»]
5JUSelectron microscopy4.20UA1-92[»]
5JUTelectron microscopy4.00UA1-92[»]
5JUUelectron microscopy4.00UA1-92[»]
5LYBX-ray3.25Q3/q32-92[»]
5MC6electron microscopy3.80AT1-92[»]
5T62electron microscopy3.30R1-92[»]
5T6Relectron microscopy4.50R1-92[»]
5TGAX-ray3.30Q3/q32-92[»]
5TGMX-ray3.50Q3/q32-92[»]
ProteinModelPortaliP0CX25.
SMRiP0CX25.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0CX25.

Family & Domainsi

Sequence similaritiesi

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri39 – 60C4-typeAdd BLAST22

Keywords - Domaini

Zinc-finger

Phylogenomic databases

InParanoidiP0CX25.
KOiK02921.
OrthoDBiEOG092C5X8P.

Family and domain databases

Gene3Di2.20.25.30. 1 hit.
HAMAPiMF_00327. Ribosomal_L37Ae. 1 hit.
InterProiView protein in InterPro
IPR002674. Ribosomal_L37ae.
IPR011331. Ribosomal_L37ae/L37e.
IPR011332. Ribosomal_zn-bd.
PfamiView protein in Pfam
PF01780. Ribosomal_L37ae. 1 hit.
SUPFAMiSSF57829. SSF57829. 1 hit.
TIGRFAMsiTIGR00280. eL43_euk_arch. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P0CX25-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKRTKKVGI TGKYGVRYGS SLRRQVKKLE IQQHARYDCS FCGKKTVKRG
60 70 80 90
AAGIWTCSCC KKTVAGGAYT VSTAAAATVR STIRRLREMV EA
Length:92
Mass (Da):10,091
Last modified:June 28, 2011 - v1
Checksum:iE2057BF56B131730
GO

Mass spectrometryi

Molecular mass is 9953.311 Da from positions 2 - 92. Determined by ESI. Monoisotopic mass.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z73616 Genomic DNA. Translation: CAA97993.1.
Z71255 Genomic DNA. Translation: CAA94991.1.
Z49219 Genomic DNA. Translation: CAA89164.1.
BK006949 Genomic DNA. Translation: DAA11468.1.
PIRiS54068.
RefSeqiNP_012628.3. NM_001181752.3.
NP_015368.1. NM_001184140.1.

Genome annotation databases

EnsemblFungiiYJR094W-A; YJR094W-A; YJR094W-A.
YPR043W; YPR043W; YPR043W.
GeneIDi853557.
856156.
KEGGisce:YJR094W-A.
sce:YPR043W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z73616 Genomic DNA. Translation: CAA97993.1.
Z71255 Genomic DNA. Translation: CAA94991.1.
Z49219 Genomic DNA. Translation: CAA89164.1.
BK006949 Genomic DNA. Translation: DAA11468.1.
PIRiS54068.
RefSeqiNP_012628.3. NM_001181752.3.
NP_015368.1. NM_001184140.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-210-82[»]
3J6Xelectron microscopy6.10831-92[»]
3J6Yelectron microscopy6.10831-92[»]
3J77electron microscopy6.20931-92[»]
3J78electron microscopy6.30931-92[»]
3JCTelectron microscopy3.08p1-92[»]
4U3MX-ray3.00Q3/q32-92[»]
4U3NX-ray3.20Q3/q32-92[»]
4U3UX-ray2.90Q3/q32-92[»]
4U4NX-ray3.10Q3/q32-92[»]
4U4OX-ray3.60Q3/q32-92[»]
4U4QX-ray3.00Q3/q32-92[»]
4U4RX-ray2.80Q3/q32-92[»]
4U4UX-ray3.00Q3/q32-92[»]
4U4YX-ray3.20Q3/q32-92[»]
4U4ZX-ray3.10Q3/q32-92[»]
4U50X-ray3.20Q3/q32-92[»]
4U51X-ray3.20Q3/q32-92[»]
4U52X-ray3.00Q3/q32-92[»]
4U53X-ray3.30Q3/q32-92[»]
4U55X-ray3.20Q3/q32-92[»]
4U56X-ray3.45Q3/q32-92[»]
4U6FX-ray3.10Q3/q32-92[»]
4V4Belectron microscopy11.70B92-92[»]
4V6Ielectron microscopy8.80Bm1-92[»]
4V7Felectron microscopy8.70k1-92[»]
4V7RX-ray4.00Bg/Dg1-92[»]
4V88X-ray3.00Bp/Dp1-92[»]
4V8Telectron microscopy8.10p1-92[»]
4V91electron microscopy3.70p1-92[»]
5APNelectron microscopy3.91p1-92[»]
5APOelectron microscopy3.41p1-92[»]
5DATX-ray3.15Q3/q32-92[»]
5DC3X-ray3.25Q3/q32-92[»]
5DGEX-ray3.45Q3/q32-92[»]
5DGFX-ray3.30Q3/q32-92[»]
5DGVX-ray3.10Q3/q32-92[»]
5FCIX-ray3.40Q3/q32-92[»]
5FCJX-ray3.10Q3/q32-92[»]
5FL8electron microscopy9.50p1-92[»]
5GAKelectron microscopy3.88D1-92[»]
5H4Pelectron microscopy3.07p1-92[»]
5I4LX-ray3.10Q3/q32-92[»]
5JCSelectron microscopy9.50p1-92[»]
5JUOelectron microscopy4.00UA1-92[»]
5JUPelectron microscopy3.50UA1-92[»]
5JUSelectron microscopy4.20UA1-92[»]
5JUTelectron microscopy4.00UA1-92[»]
5JUUelectron microscopy4.00UA1-92[»]
5LYBX-ray3.25Q3/q32-92[»]
5MC6electron microscopy3.80AT1-92[»]
5T62electron microscopy3.30R1-92[»]
5T6Relectron microscopy4.50R1-92[»]
5TGAX-ray3.30Q3/q32-92[»]
5TGMX-ray3.50Q3/q32-92[»]
ProteinModelPortaliP0CX25.
SMRiP0CX25.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33849. 123 interactors.
36220. 282 interactors.
MINTiMINT-2781587.

PTM databases

iPTMnetiP0CX25.

Proteomic databases

MaxQBiP0CX25.
PRIDEiP0CX25.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJR094W-A; YJR094W-A; YJR094W-A.
YPR043W; YPR043W; YPR043W.
GeneIDi853557.
856156.
KEGGisce:YJR094W-A.
sce:YPR043W.

Organism-specific databases

SGDiS000006247. RPL43A.

Phylogenomic databases

InParanoidiP0CX25.
KOiK02921.
OrthoDBiEOG092C5X8P.

Enzyme and pathway databases

BioCyciYEAST:G3O-34199-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

EvolutionaryTraceiP0CX25.
PROiPR:P0CX25.

Gene expression databases

ExpressionAtlasiP0CX25. differential.

Family and domain databases

Gene3Di2.20.25.30. 1 hit.
HAMAPiMF_00327. Ribosomal_L37Ae. 1 hit.
InterProiView protein in InterPro
IPR002674. Ribosomal_L37ae.
IPR011331. Ribosomal_L37ae/L37e.
IPR011332. Ribosomal_zn-bd.
PfamiView protein in Pfam
PF01780. Ribosomal_L37ae. 1 hit.
SUPFAMiSSF57829. SSF57829. 1 hit.
TIGRFAMsiTIGR00280. eL43_euk_arch. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRL43A_YEAST
AccessioniPrimary (citable) accession number: P0CX25
Secondary accession number(s): D6VWR3, P49631
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: June 28, 2011
Last modified: April 12, 2017
This is version 56 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 XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: 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.