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Protein

40S ribosomal protein S6-A

Gene

RPS6A

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -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 (PubMed:22096102). eS6 is involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly (PubMed:15590835).1 Publication1 Publication

Miscellaneous

Present with 66000 molecules/cell in log phase SD medium.1 Publication
There are 2 genes for eS6 in yeast.Curated

GO - Molecular functioni

  • structural constituent of ribosome Source: SGD

GO - Biological processi

  • cytoplasmic translation Source: SGD
  • maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: SGD
  • rRNA methylation Source: Reactome

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein
Biological processRibosome biogenesis, rRNA processing

Enzyme and pathway databases

BioCyciYEAST:G3O-33995-MONOMER
ReactomeiR-SCE-156827 L13a-mediated translational silencing of Ceruloplasmin expression
R-SCE-166208 mTORC1-mediated signalling
R-SCE-1799339 SRP-dependent cotranslational protein targeting to membrane
R-SCE-6791226 Major pathway of rRNA processing in the nucleolus and cytosol
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 S6-A1 Publication
Alternative name(s):
RP9
S10
Small ribosomal subunit protein eS6-A1 Publication
YS4
Gene namesi
Name:RPS6A1 Publication
Synonyms:RPS101, RPS10B
Ordered Locus Names:YPL090C
ORF Names:LPG18C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

SGDiS000006011 RPS6A

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, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001373421 – 23640S ribosomal protein S6-AAdd BLAST236

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki116Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki131Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki149Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei163PhosphothreonineCombined sources1
Cross-linki214Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP0CX37
PaxDbiP0CX37
PRIDEiP0CX37

PTM databases

iPTMnetiP0CX37

Expressioni

Gene expression databases

ExpressionAtlasiP0CX37 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). Interacts with snoRNA U3. uS11 interacts with MPP10. Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3 (PubMed:15590835).1 Publication2 Publications

Protein-protein interaction databases

BioGridi32879, 336 interactors
36091, 303 interactors
IntActiP0CX37, 3 interactors
MINTiP0CX37
STRINGi4932.YPL090C

Structurei

Secondary structure

1236
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 7Combined sources6
Turni8 – 11Combined sources4
Beta strandi12 – 17Combined sources6
Helixi21 – 24Combined sources4
Helixi25 – 27Combined sources3
Beta strandi31 – 33Combined sources3
Beta strandi35 – 38Combined sources4
Turni39 – 41Combined sources3
Beta strandi43 – 45Combined sources3
Beta strandi49 – 57Combined sources9
Helixi58 – 60Combined sources3
Beta strandi69 – 77Combined sources9
Beta strandi81 – 83Combined sources3
Beta strandi87 – 90Combined sources4
Beta strandi93 – 98Combined sources6
Beta strandi106 – 115Combined sources10
Helixi122 – 125Combined sources4
Helixi138 – 143Combined sources6
Turni144 – 146Combined sources3
Helixi148 – 150Combined sources3
Helixi153 – 155Combined sources3
Beta strandi160 – 163Combined sources4
Beta strandi168 – 171Combined sources4
Helixi181 – 216Combined sources36
Beta strandi219 – 222Combined sources4
Turni223 – 225Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J16electron microscopy-C1-236[»]
3J6Xelectron microscopy6.10S61-236[»]
3J6Yelectron microscopy6.10S61-236[»]
3J77electron microscopy6.20S61-236[»]
3J78electron microscopy6.30S61-236[»]
4U3MX-ray3.00S6/s61-236[»]
4U3NX-ray3.20S6/s61-236[»]
4U3UX-ray2.90S6/s61-236[»]
4U4NX-ray3.10S6/s61-236[»]
4U4OX-ray3.60S6/s61-236[»]
4U4QX-ray3.00S6/s61-236[»]
4U4RX-ray2.80S6/s61-236[»]
4U4UX-ray3.00S6/s61-236[»]
4U4YX-ray3.20S6/s61-236[»]
4U4ZX-ray3.10S6/s61-236[»]
4U50X-ray3.20S6/s61-236[»]
4U51X-ray3.20S6/s61-236[»]
4U52X-ray3.00S6/s61-236[»]
4U53X-ray3.30S6/s61-236[»]
4U55X-ray3.20S6/s61-236[»]
4U56X-ray3.45S6/s61-236[»]
4U6FX-ray3.10S6/s61-236[»]
4V88X-ray3.00AG/CG1-236[»]
4V8Yelectron microscopy4.30AG1-236[»]
4V8Zelectron microscopy6.60AG1-236[»]
4V92electron microscopy3.70G1-226[»]
5DATX-ray3.15S6/s61-236[»]
5DC3X-ray3.25S6/s61-236[»]
5DGEX-ray3.45S6/s61-236[»]
5DGFX-ray3.30S6/s61-236[»]
5DGVX-ray3.10S6/s61-236[»]
5FCIX-ray3.40S6/s61-236[»]
5FCJX-ray3.10S6/s61-236[»]
5I4LX-ray3.10S6/s61-226[»]
5JUOelectron microscopy4.00DB1-236[»]
5JUPelectron microscopy3.50DB1-236[»]
5JUSelectron microscopy4.20DB1-236[»]
5JUTelectron microscopy4.00DB1-236[»]
5JUUelectron microscopy4.00DB1-236[»]
5LL6electron microscopy3.90T1-236[»]
5LYBX-ray3.25S6/s61-226[»]
5M1Jelectron microscopy3.30G21-226[»]
5MC6electron microscopy3.80T1-236[»]
5MEIX-ray3.50H/s61-226[»]
5NDGX-ray3.70S6/s61-236[»]
5NDVX-ray3.30S61-236[»]
s61-218[»]
5NDWX-ray3.70S6/s61-236[»]
5OBMX-ray3.40S6/s61-236[»]
5ON6X-ray3.10H/s61-226[»]
5TBWX-ray3.00H/s61-226[»]
5TGAX-ray3.30S6/s61-226[»]
5TGMX-ray3.50S6/s61-226[»]
5TZSelectron microscopy5.1031-236[»]
5WLCelectron microscopy3.80L61-236[»]
5WYJelectron microscopy8.70SH1-236[»]
6EMLelectron microscopy3.60T1-236[»]
6FAIelectron microscopy3.40G1-236[»]
ProteinModelPortaliP0CX37
SMRiP0CX37
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

InParanoidiP0CX37
KOiK02991
OMAiKGYIFRI
OrthoDBiEOG092C4QCP

Family and domain databases

InterProiView protein in InterPro
IPR014401 Ribosomal_S6_euk
IPR001377 Ribosomal_S6e
IPR018282 Ribosomal_S6e_CS
PANTHERiPTHR11502 PTHR11502, 1 hit
PfamiView protein in Pfam
PF01092 Ribosomal_S6e, 1 hit
PIRSFiPIRSF002129 Ribosom_S6_euk, 1 hit
SMARTiView protein in SMART
SM01405 Ribosomal_S6e, 1 hit
PROSITEiView protein in PROSITE
PS00578 RIBOSOMAL_S6E, 1 hit

Sequencei

Sequence statusi: Complete.

P0CX37-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLNISYPVN GSQKTFEIDD EHRIRVFFDK RIGQEVDGEA VGDEFKGYVF
60 70 80 90 100
KISGGNDKQG FPMKQGVLLP TRIKLLLTKN VSCYRPRRDG ERKRKSVRGA
110 120 130 140 150
IVGPDLAVLA LVIVKKGEQE LEGLTDTTVP KRLGPKRANN IRKFFGLSKE
160 170 180 190 200
DDVRDFVIRR EVTKGEKTYT KAPKIQRLVT PQRLQRKRHQ RALKVRNAQA
210 220 230
QREAAAEYAQ LLAKRLSERK AEKAEIRKRR ASSLKA
Length:236
Mass (Da):26,996
Last modified:June 28, 2011 - v1
Checksum:i78B523BB7FDABEE0
GO

Sequence cautioni

The sequence AAB68209 differs from that shown. Reason: Erroneous gene model prediction.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02746 Genomic DNA Translation: CAA26525.1
U43281 Genomic DNA Translation: AAB68209.1 Sequence problems.
BK006949 Genomic DNA Translation: DAA11343.1
PIRiA23787 R3BY10
RefSeqiNP_009740.3, NM_001178529.3
NP_015235.1, NM_001183904.1

Genome annotation databases

EnsemblFungiiYBR181C; YBR181C; YBR181C
YPL090C; YPL090C; YPL090C
GeneIDi852479
856015
KEGGisce:YBR181C
sce:YPL090C

Similar proteinsi

Entry informationi

Entry nameiRS6A_YEAST
AccessioniPrimary (citable) accession number: P0CX37
Secondary accession number(s): D6VQH5
, P02365, P05751, Q02894
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: June 28, 2011
Last modified: April 25, 2018
This is version 66 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
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Main funding by: National Institutes of Health