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Protein

40S ribosomal protein S11-A

Gene

RPS11A

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.1 Publication

Miscellaneous

There are 2 genes for uS17 in yeast.Curated

GO - Molecular functioni

  • rRNA binding Source: UniProtKB-KW
  • 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
  • ribosomal small subunit assembly Source: SGD
  • translation Source: GO_Central

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29641-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 S11-A1 Publication
Alternative name(s):
RP41
S18
Small ribosomal subunit protein uS17-A1 Publication
YS12
Gene namesi
Name:RPS11A1 Publication
Synonyms:RPS18A
Ordered Locus Names:YDR025W
ORF Names:YD9813.03
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

SGDiS000002432 RPS11A

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 sources2 Publications
ChainiPRO_00001285232 – 15640S ribosomal protein S11-AAdd BLAST155

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources2 Publications1
Cross-linki15Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki46Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki56Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki57Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki79Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki96Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki105Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki133Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki141Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki148Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Post-translational modificationi

N-terminally acetylated by acetyltransferase NatA.2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP0CX47
PaxDbiP0CX47
PRIDEiP0CX47

PTM databases

iPTMnetiP0CX47

Expressioni

Gene expression databases

ExpressionAtlasiP0CX47 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

BioGridi32075, 208 interactors
32750, 320 interactors
IntActiP0CX47, 2 interactors
MINTiP0CX47
STRINGi4932.YDR025W

Structurei

Secondary structure

1156
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi10 – 12Combined sources3
Beta strandi23 – 25Combined sources3
Beta strandi28 – 31Combined sources4
Helixi46 – 49Combined sources4
Turni59 – 61Combined sources3
Beta strandi70 – 77Combined sources8
Beta strandi83 – 94Combined sources12
Turni95 – 98Combined sources4
Beta strandi99 – 110Combined sources12
Beta strandi122 – 127Combined sources6
Beta strandi132 – 134Combined sources3
Beta strandi137 – 143Combined sources7
Beta strandi145 – 148Combined sources4
Helixi150 – 152Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Xmodel-Q69-144[»]
3J6Xelectron microscopy6.10111-156[»]
3J6Yelectron microscopy6.10111-156[»]
3J77electron microscopy6.20111-156[»]
3J78electron microscopy6.30111-156[»]
4U3MX-ray3.00C1/c12-156[»]
4U3NX-ray3.20C1/c12-156[»]
4U3UX-ray2.90C1/c12-156[»]
4U4NX-ray3.10C1/c12-156[»]
4U4OX-ray3.60C1/c12-156[»]
4U4QX-ray3.00C1/c12-156[»]
4U4RX-ray2.80C1/c12-156[»]
4U4UX-ray3.00C1/c12-156[»]
4U4YX-ray3.20C1/c12-156[»]
4U4ZX-ray3.10C1/c12-156[»]
4U50X-ray3.20C1/c12-156[»]
4U51X-ray3.20C1/c12-156[»]
4U52X-ray3.00C1/c12-156[»]
4U53X-ray3.30C1/c12-156[»]
4U55X-ray3.20C1/c12-156[»]
4U56X-ray3.45C1/c12-156[»]
4U6FX-ray3.10C1/c12-156[»]
4V4Belectron microscopy11.70AQ69-144[»]
4V6Ielectron microscopy8.80AP1-156[»]
4V7RX-ray4.00AF/CF1-156[»]
4V88X-ray3.00AL/CL1-156[»]
4V8Yelectron microscopy4.30AL1-156[»]
4V8Zelectron microscopy6.60AL1-156[»]
4V92electron microscopy3.70L4-145[»]
5DATX-ray3.15C1/c12-156[»]
5DC3X-ray3.25C1/c12-156[»]
5DGEX-ray3.45C1/c12-156[»]
5DGVX-ray3.10C1/c12-156[»]
5FCIX-ray3.40C1/c12-147[»]
5FCJX-ray3.10C1/c12-146[»]
5I4LX-ray3.10C1/c11-156[»]
5JUOelectron microscopy4.00IB1-156[»]
5JUPelectron microscopy3.50IB1-156[»]
5JUSelectron microscopy4.20IB1-156[»]
5JUTelectron microscopy4.00IB1-156[»]
5JUUelectron microscopy4.00IB1-156[»]
5LL6electron microscopy3.90X1-156[»]
5LYBX-ray3.25C1/c12-146[»]
5M1Jelectron microscopy3.30L22-156[»]
5MC6electron microscopy3.80X1-156[»]
5MEIX-ray3.50M/c12-156[»]
5NDGX-ray3.70C1/c11-156[»]
5NDVX-ray3.30C1/c12-147[»]
5NDWX-ray3.70C1/c11-156[»]
5OBMX-ray3.40C1/c11-156[»]
5ON6X-ray3.10M/c12-156[»]
5TBWX-ray3.00M/c12-156[»]
5TGAX-ray3.30C1/c12-156[»]
5TGMX-ray3.50C1/c12-146[»]
5TZSelectron microscopy5.10D1-156[»]
5WLCelectron microscopy3.80LD1-156[»]
5WYJelectron microscopy8.70SM1-156[»]
5WYKelectron microscopy4.50SM1-156[»]
6EMLelectron microscopy3.60X1-156[»]
6FAIelectron microscopy3.40L1-156[»]
ProteinModelPortaliP0CX47
SMRiP0CX47
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0CX47

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

InParanoidiP0CX47
KOiK02949
OMAiKKYERYE
OrthoDBiEOG092C58OI

Family and domain databases

InterProiView protein in InterPro
IPR012340 NA-bd_OB-fold
IPR032440 Ribosomal_S11_N
IPR000266 Ribosomal_S17/S11
IPR028333 Ribosomal_S17_arc-typ
IPR019979 Ribosomal_S17_CS
PANTHERiPTHR10744 PTHR10744, 1 hit
PfamiView protein in Pfam
PF00366 Ribosomal_S17, 1 hit
PF16205 Ribosomal_S17_N, 1 hit
PRINTSiPR00973 RIBOSOMALS17
ProDomiView protein in ProDom or Entries sharing at least one domain
PD001295 Ribosomal_S17, 1 hit
SUPFAMiSSF50249 SSF50249, 1 hit
TIGRFAMsiTIGR03630 uS17_arch, 1 hit
PROSITEiView protein in PROSITE
PS00056 RIBOSOMAL_S17, 1 hit

Sequencei

Sequence statusi: Complete.

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

P0CX47-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTELTVQSE RAFQKQPHIF NNPKVKTSKR TKRWYKNAGL GFKTPKTAIE
60 70 80 90 100
GSYIDKKCPF TGLVSIRGKI LTGTVVSTKM HRTIVIRRAY LHYIPKYNRY
110 120 130 140 150
EKRHKNVPVH VSPAFRVQVG DIVTVGQCRP ISKTVRFNVV KVSAAAGKAN

KQFAKF
Length:156
Mass (Da):17,749
Last modified:June 28, 2011 - v1
Checksum:i6F7825FAE17EB084
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti12 – 13AF → FA AA sequence (PubMed:1544921).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L15408 Unassigned DNA Translation: AAC37411.1
X95966 Genomic DNA Translation: CAA65218.1
Z47814 Genomic DNA Translation: CAA87804.1
Z74321 Genomic DNA Translation: CAA98846.1
BK006938 Genomic DNA Translation: DAA11870.1
PIRiS41784
RefSeqiNP_009604.1, NM_001178396.1
NP_010308.3, NM_001180333.3

Genome annotation databases

EnsemblFungiiYBR048W; YBR048W; YBR048W
YDR025W; YDR025W; YDR025W
GeneIDi851589
852337
KEGGisce:YBR048W
sce:YDR025W

Similar proteinsi

Entry informationi

Entry nameiRS11A_YEAST
AccessioniPrimary (citable) accession number: P0CX47
Secondary accession number(s): D6VQ48, O11852, P26781
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: June 28, 2011
Last modified: April 25, 2018
This is version 64 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