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Protein

40S ribosomal protein S30-A

Gene

RPS30A

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 37600 molecules/cell in log phase SD medium.1 Publication
There are 2 genes for eS30 in yeast.Curated

GO - Molecular functioni

  • structural constituent of ribosome Source: SGD

GO - Biological processi

  • cytoplasmic translation Source: SGD

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciYEAST:G3O-32382-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-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-SCE-72702. Ribosomal scanning and start codon recognition.
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:
40S ribosomal protein S30-A1 Publication
Alternative name(s):
Small ribosomal subunit protein eS30-A1 Publication
Gene namesi
Name:RPS30A1 Publication
Ordered Locus Names:YLR287C-A
ORF Names:L8003.23, YLR287BC
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

SGDiS000004278. RPS30A.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic stress granule Source: SGD
  • cytosolic small ribosomal subunit Source: SGD

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001740092 – 6340S ribosomal protein S30-AAdd BLAST62

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei16PhosphoserineCombined sources1
Modified residuei48PhosphothreonineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP0CX33.
TopDownProteomicsiP0CX33.

PTM databases

iPTMnetiP0CX33.

Expressioni

Gene expression databases

ExpressionAtlasiP0CX33. 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

BioGridi31553. 209 interactors.
34577. 169 interactors.

Structurei

Secondary structure

163
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni9 – 12Combined sources4
Helixi13 – 17Combined sources5
Helixi33 – 43Combined sources11
Turni44 – 46Combined sources3
Beta strandi51 – 53Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J16electron microscopy-E1-63[»]
3J6Xelectron microscopy6.10301-63[»]
3J6Yelectron microscopy6.10301-63[»]
3J77electron microscopy6.20301-63[»]
3J78electron microscopy6.30301-63[»]
3V88X-ray3.00e1-63[»]
4U3MX-ray3.00E02-61[»]
e02-63[»]
4U3NX-ray3.20E02-61[»]
e02-63[»]
4U3UX-ray2.90E02-61[»]
e02-63[»]
4U4NX-ray3.10E02-61[»]
e02-63[»]
4U4OX-ray3.60E02-61[»]
e02-63[»]
4U4QX-ray3.00E02-61[»]
e02-63[»]
4U4RX-ray2.80E02-61[»]
e02-63[»]
4U4UX-ray3.00E02-61[»]
e02-63[»]
4U4YX-ray3.20E02-61[»]
e02-63[»]
4U4ZX-ray3.10E02-61[»]
e02-63[»]
4U50X-ray3.20E02-61[»]
e02-63[»]
4U51X-ray3.20E02-61[»]
e02-63[»]
4U52X-ray3.00E0/e02-61[»]
4U53X-ray3.30E02-61[»]
e02-63[»]
4U55X-ray3.20E02-61[»]
e02-63[»]
4U56X-ray3.45E02-61[»]
e02-63[»]
4U6FX-ray3.10E02-61[»]
e02-63[»]
4V6Ielectron microscopy8.80AZ1-63[»]
4V88X-ray3.00Ae/Ce1-63[»]
4V8Yelectron microscopy4.30A41-63[»]
4V8Zelectron microscopy6.60A41-63[»]
4V92electron microscopy3.70e7-61[»]
5DATX-ray3.15E0/e02-63[»]
5DC3X-ray3.25E0/e02-63[»]
5DGEX-ray3.45E02-61[»]
e02-63[»]
5DGFX-ray3.30E0/e02-63[»]
5DGVX-ray3.10E02-61[»]
e02-63[»]
5FCIX-ray3.40E0/e02-63[»]
5FCJX-ray3.10E0/e02-63[»]
5I4LX-ray3.10E0/e02-63[»]
5JUOelectron microscopy4.00BC1-63[»]
5JUPelectron microscopy3.50BC1-63[»]
5JUSelectron microscopy4.20BC1-63[»]
5JUTelectron microscopy4.00BC1-63[»]
5JUUelectron microscopy4.00BC1-63[»]
5LYBX-ray3.25E0/e02-63[»]
5M1Jelectron microscopy3.30e22-61[»]
5MC6electron microscopy3.80g1-63[»]
5TGAX-ray3.30E0/e02-63[»]
5TGMX-ray3.50E0/e02-63[»]
5WYJelectron microscopy8.70Sf1-63[»]
5WYKelectron microscopy4.50Sf1-63[»]
ProteinModelPortaliP0CX33.
SMRiP0CX33.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

InParanoidiP0CX33.
KOiK02983.
OMAiQPKGRAY.
OrthoDBiEOG092C5YU3.

Family and domain databases

InterProiView protein in InterPro
IPR006846. Ribosomal_S30.
PfamiView protein in Pfam
PF04758. Ribosomal_S30. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P0CX33-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKVHGSLAR AGKVKSQTPK VEKTEKPKKP KGRAYKRLLY TRRFVNVTLV
60
NGKRRMNPGP SVQ
Length:63
Mass (Da):7,118
Last modified:June 28, 2011 - v1
Checksum:i658C4C1D8D9F88CB
GO

Mass spectrometryi

Molecular mass is 6987±3.4 Da from positions 2 - 63. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U48700 Genomic DNA. Translation: AAC49317.1.
U48699 mRNA. Translation: AAC49316.1.
U17243 Genomic DNA. Translation: AAB67333.1.
BK006945 Genomic DNA. Translation: DAA09599.1.
PIRiS67074.
RefSeqiNP_013390.1. NM_001182175.1.
NP_014825.3. NM_001183601.3.

Genome annotation databases

EnsemblFungiiYLR287C-A; YLR287C-A; YLR287C-A.
YOR182C; YOR182C; YOR182C.
GeneIDi850994.
854354.
KEGGisce:YLR287C-A.
sce:YOR182C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U48700 Genomic DNA. Translation: AAC49317.1.
U48699 mRNA. Translation: AAC49316.1.
U17243 Genomic DNA. Translation: AAB67333.1.
BK006945 Genomic DNA. Translation: DAA09599.1.
PIRiS67074.
RefSeqiNP_013390.1. NM_001182175.1.
NP_014825.3. NM_001183601.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J16electron microscopy-E1-63[»]
3J6Xelectron microscopy6.10301-63[»]
3J6Yelectron microscopy6.10301-63[»]
3J77electron microscopy6.20301-63[»]
3J78electron microscopy6.30301-63[»]
3V88X-ray3.00e1-63[»]
4U3MX-ray3.00E02-61[»]
e02-63[»]
4U3NX-ray3.20E02-61[»]
e02-63[»]
4U3UX-ray2.90E02-61[»]
e02-63[»]
4U4NX-ray3.10E02-61[»]
e02-63[»]
4U4OX-ray3.60E02-61[»]
e02-63[»]
4U4QX-ray3.00E02-61[»]
e02-63[»]
4U4RX-ray2.80E02-61[»]
e02-63[»]
4U4UX-ray3.00E02-61[»]
e02-63[»]
4U4YX-ray3.20E02-61[»]
e02-63[»]
4U4ZX-ray3.10E02-61[»]
e02-63[»]
4U50X-ray3.20E02-61[»]
e02-63[»]
4U51X-ray3.20E02-61[»]
e02-63[»]
4U52X-ray3.00E0/e02-61[»]
4U53X-ray3.30E02-61[»]
e02-63[»]
4U55X-ray3.20E02-61[»]
e02-63[»]
4U56X-ray3.45E02-61[»]
e02-63[»]
4U6FX-ray3.10E02-61[»]
e02-63[»]
4V6Ielectron microscopy8.80AZ1-63[»]
4V88X-ray3.00Ae/Ce1-63[»]
4V8Yelectron microscopy4.30A41-63[»]
4V8Zelectron microscopy6.60A41-63[»]
4V92electron microscopy3.70e7-61[»]
5DATX-ray3.15E0/e02-63[»]
5DC3X-ray3.25E0/e02-63[»]
5DGEX-ray3.45E02-61[»]
e02-63[»]
5DGFX-ray3.30E0/e02-63[»]
5DGVX-ray3.10E02-61[»]
e02-63[»]
5FCIX-ray3.40E0/e02-63[»]
5FCJX-ray3.10E0/e02-63[»]
5I4LX-ray3.10E0/e02-63[»]
5JUOelectron microscopy4.00BC1-63[»]
5JUPelectron microscopy3.50BC1-63[»]
5JUSelectron microscopy4.20BC1-63[»]
5JUTelectron microscopy4.00BC1-63[»]
5JUUelectron microscopy4.00BC1-63[»]
5LYBX-ray3.25E0/e02-63[»]
5M1Jelectron microscopy3.30e22-61[»]
5MC6electron microscopy3.80g1-63[»]
5TGAX-ray3.30E0/e02-63[»]
5TGMX-ray3.50E0/e02-63[»]
5WYJelectron microscopy8.70Sf1-63[»]
5WYKelectron microscopy4.50Sf1-63[»]
ProteinModelPortaliP0CX33.
SMRiP0CX33.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31553. 209 interactors.
34577. 169 interactors.

PTM databases

iPTMnetiP0CX33.

Proteomic databases

PRIDEiP0CX33.
TopDownProteomicsiP0CX33.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR287C-A; YLR287C-A; YLR287C-A.
YOR182C; YOR182C; YOR182C.
GeneIDi850994.
854354.
KEGGisce:YLR287C-A.
sce:YOR182C.

Organism-specific databases

SGDiS000004278. RPS30A.

Phylogenomic databases

InParanoidiP0CX33.
KOiK02983.
OMAiQPKGRAY.
OrthoDBiEOG092C5YU3.

Enzyme and pathway databases

BioCyciYEAST:G3O-32382-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-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-SCE-72702. Ribosomal scanning and start codon recognition.
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

PROiPR:P0CX33.

Gene expression databases

ExpressionAtlasiP0CX33. differential.

Family and domain databases

InterProiView protein in InterPro
IPR006846. Ribosomal_S30.
PfamiView protein in Pfam
PF04758. Ribosomal_S30. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRS30A_YEAST
AccessioniPrimary (citable) accession number: P0CX33
Secondary accession number(s): D6VYT3, Q12087
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: June 28, 2011
Last modified: June 7, 2017
This is version 53 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, 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

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.