Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

40S ribosomal protein S13

Gene

RPS13

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

GO - Molecular functioni

  • small ribosomal subunit rRNA binding Source: SGD
  • 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
  • translation Source: GO_Central

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciYEAST:G3O-29671-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 S131 Publication
Alternative name(s):
S27a
Small ribosomal subunit protein uS151 Publication
YS15
Gene namesi
Name:RPS131 Publication
Synonyms:RPS13C
Ordered Locus Names:YDR064W
ORF Names:D4252, YD9609.18
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR064W
SGDiS000002471 RPS13

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 methionineiRemoved2 Publications
ChainiPRO_00001156892 – 15140S ribosomal protein S13Add BLAST150

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei32PhosphoserineCombined sources1
Cross-linki39Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki43Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP05756
PaxDbiP05756
PRIDEiP05756
TopDownProteomicsiP05756

PTM databases

iPTMnetiP05756

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

BioGridi32119, 168 interactors
IntActiP05756, 55 interactors
MINTiP05756
STRINGi4932.YDR064W

Structurei

Secondary structure

1151
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi30 – 42Combined sources13
Helixi47 – 56Combined sources10
Helixi63 – 66Combined sources4
Beta strandi67 – 69Combined sources3
Helixi71 – 77Combined sources7
Helixi86 – 104Combined sources19
Helixi109 – 131Combined sources23
Helixi143 – 150Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Xmodel-O66-130[»]
3J6Xelectron microscopy6.10131-151[»]
3J6Yelectron microscopy6.10131-151[»]
3J77electron microscopy6.20131-151[»]
3J78electron microscopy6.30131-151[»]
4U3MX-ray3.00C3/c32-151[»]
4U3NX-ray3.20C3/c32-151[»]
4U3UX-ray2.90C3/c32-151[»]
4U4NX-ray3.10C3/c32-151[»]
4U4OX-ray3.60C3/c32-151[»]
4U4QX-ray3.00C3/c32-151[»]
4U4RX-ray2.80C3/c32-151[»]
4U4UX-ray3.00C3/c32-151[»]
4U4YX-ray3.20C3/c32-151[»]
4U4ZX-ray3.10C3/c32-151[»]
4U50X-ray3.20C3/c32-151[»]
4U51X-ray3.20C3/c32-151[»]
4U52X-ray3.00C3/c32-151[»]
4U53X-ray3.30C3/c32-151[»]
4U55X-ray3.20C3/c32-151[»]
4U56X-ray3.45C3/c32-151[»]
4U6FX-ray3.10C3/c32-151[»]
4V4Belectron microscopy11.70AO66-130[»]
4V6Ielectron microscopy8.80AO1-151[»]
4V7RX-ray4.00AG/CG1-151[»]
4V88X-ray3.00AN/CN1-151[»]
4V8Yelectron microscopy4.30AN1-151[»]
4V8Zelectron microscopy6.60AN1-151[»]
4V92electron microscopy3.70N2-151[»]
5DATX-ray3.15C3/c32-151[»]
5DC3X-ray3.25C3/c32-151[»]
5DGEX-ray3.45C3/c32-151[»]
5DGFX-ray3.30C3/c32-151[»]
5DGVX-ray3.10C3/c32-151[»]
5FCIX-ray3.40C3/c32-151[»]
5FCJX-ray3.10C3/c32-151[»]
5I4LX-ray3.10C3/c32-151[»]
5JPQelectron microscopy7.30v1-151[»]
5JUOelectron microscopy4.00KB1-151[»]
5JUPelectron microscopy3.50KB1-151[»]
5JUSelectron microscopy4.20KB1-151[»]
5JUTelectron microscopy4.00KB1-151[»]
5JUUelectron microscopy4.00KB1-151[»]
5LL6electron microscopy3.90Y1-151[»]
5LYBX-ray3.25C3/c32-151[»]
5M1Jelectron microscopy3.30N22-151[»]
5MC6electron microscopy3.80Y1-151[»]
5MEIX-ray3.50O/c32-151[»]
5NDGX-ray3.70C3/c32-151[»]
5NDVX-ray3.30C3/c32-151[»]
5NDWX-ray3.70C3/c32-151[»]
5OBMX-ray3.40C3/c32-151[»]
5ON6X-ray3.10O/c32-151[»]
5TBWX-ray3.00O/c32-151[»]
5TGAX-ray3.30C3/c32-151[»]
5TGMX-ray3.50C3/c32-151[»]
5WLCelectron microscopy3.80NF1-151[»]
5WYJelectron microscopy8.70SO1-151[»]
5WYKelectron microscopy4.50SO1-151[»]
6EMLelectron microscopy3.60Y1-151[»]
6FAIelectron microscopy3.40N1-151[»]
ProteinModelPortaliP05756
SMRiP05756
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05756

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000017491
HOGENOMiHOG000180723
InParanoidiP05756
KOiK02953
OMAiWHLVKKA
OrthoDBiEOG092C5Q82

Family and domain databases

CDDicd00353 Ribosomal_S15p_S13e, 1 hit
HAMAPiMF_01343_A Ribosomal_S15_A, 1 hit
InterProiView protein in InterPro
IPR012606 Ribosomal_S13/S15_N
IPR000589 Ribosomal_S15
IPR023029 Ribosomal_S15P
IPR009068 S15_NS1_RNA-bd
PANTHERiPTHR11885 PTHR11885, 1 hit
PfamiView protein in Pfam
PF08069 Ribosomal_S13_N, 1 hit
PF00312 Ribosomal_S15, 1 hit
SMARTiView protein in SMART
SM01386 Ribosomal_S13_N, 1 hit
SM01387 Ribosomal_S15, 1 hit
SUPFAMiSSF47060 SSF47060, 1 hit
PROSITEiView protein in PROSITE
PS00362 RIBOSOMAL_S15, 1 hit

Sequencei

Sequence statusi: Complete.

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

P05756-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRMHSAGKG ISSSAIPYSR NAPAWFKLSS ESVIEQIVKY ARKGLTPSQI
60 70 80 90 100
GVLLRDAHGV TQARVITGNK IMRILKSNGL APEIPEDLYY LIKKAVSVRK
110 120 130 140 150
HLERNRKDKD AKFRLILIES RIHRLARYYR TVAVLPPNWK YESATASALV

N
Length:151
Mass (Da):17,029
Last modified:January 23, 2007 - v3
Checksum:i9AA9EFBEC837053D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti25W → G AA sequence (PubMed:6814480).Curated1
Sequence conflicti32S → C AA sequence (PubMed:6814480).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X84162 Genomic DNA Translation: CAA58980.1
Z49209 Genomic DNA Translation: CAA89093.1
Z74360 Genomic DNA Translation: CAA98882.1
BK006938 Genomic DNA Translation: DAA11910.1
PIRiS54048
RefSeqiNP_010349.3, NM_001180372.3

Genome annotation databases

EnsemblFungiiYDR064W; YDR064W; YDR064W
GeneIDi851636
KEGGisce:YDR064W

Similar proteinsi

Entry informationi

Entry nameiRS13_YEAST
AccessioniPrimary (citable) accession number: P05756
Secondary accession number(s): D6VS50
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 178 of the entry and version 3 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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health