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Protein

40S ribosomal protein S11

Gene

RpS11

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

  • mitotic spindle elongation Source: FlyBase
  • mitotic spindle organization Source: FlyBase
  • neurogenesis Source: FlyBase
  • translation Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

ReactomeiR-DME-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-DME-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-DME-6791226. Major pathway of rRNA processing in the nucleolus.
R-DME-72649. Translation initiation complex formation.
R-DME-72689. Formation of a pool of free 40S subunits.
R-DME-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-DME-72702. Ribosomal scanning and start codon recognition.
R-DME-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-DME-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-DME-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S11
Gene namesi
Name:RpS11
ORF Names:CG8857
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0033699. RpS11.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: FlyBase
  • cytosolic small ribosomal subunit Source: GO_Central
  • nuclear chromosome Source: FlyBase
  • nucleolus Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 15515440S ribosomal protein S11By similarityPRO_0000282944Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ0E9B6.
PRIDEiQ0E9B6.

Expressioni

Gene expression databases

BgeeiFBgn0033699.
ExpressionAtlasiQ0E9B6. differential.
GenevisibleiQ0E9B6. DM.

Interactioni

Protein-protein interaction databases

BioGridi62099. 16 interactions.
IntActiQ0E9B6. 3 interactions.
STRINGi7227.FBpp0087115.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00AL1-155[»]
ProteinModelPortaliQ0E9B6.
SMRiQ0E9B6. Positions 4-144.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S17P family.Sequence analysis

Phylogenomic databases

eggNOGiKOG1728. Eukaryota.
COG0186. LUCA.
GeneTreeiENSGT00390000002732.
InParanoidiQ0E9B6.
KOiK02949.
OMAiLVTIGEC.
OrthoDBiEOG091G0QVV.
PhylomeDBiQ0E9B6.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
HAMAPiMF_01345_B. Ribosomal_S17_B. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR032440. Ribosomal_S11_N.
IPR000266. Ribosomal_S17/S11.
IPR028333. Ribosomal_S17_arc-typ.
IPR019979. Ribosomal_S17_CS.
[Graphical view]
PANTHERiPTHR10744. PTHR10744. 1 hit.
PfamiPF00366. Ribosomal_S17. 1 hit.
PF16205. Ribosomal_S17_N. 1 hit.
[Graphical view]
PRINTSiPR00973. RIBOSOMALS17.
ProDomiPD001295. Ribosomal_S17. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR03630. uS17_arch. 1 hit.
PROSITEiPS00056. RIBOSOMAL_S17. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q0E9B6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADQNERAFQ KQFGVNLNRK VKPGITKKKL LRRSRDVGLG FKTPREAIDG
60 70 80 90 100
TYIDKKCPWT GDVRIRGRIL TGVVRKAKMQ RTIVIRRDYL HFVRKYSRFE
110 120 130 140 150
KRHRNMSVHC SPVFRDVEHG DIVTIGECRP LSKTVRFNVL KVSKGQGAKK

SFKKY
Length:155
Mass (Da):18,105
Last modified:October 17, 2006 - v1
Checksum:iC766CB496B78C2D2
GO

Sequence cautioni

The sequence ACR53996 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence ACR53998 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAM71028.1.
BT088759 mRNA. Translation: ACR53996.1. Different initiation.
BT088761 mRNA. Translation: ACR53998.1. Different initiation.
RefSeqiNP_725114.1. NM_165868.2.

Genome annotation databases

EnsemblMetazoaiFBtr0088007; FBpp0087115; FBgn0033699.
GeneIDi36321.
KEGGidme:Dmel_CG8857.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAM71028.1.
BT088759 mRNA. Translation: ACR53996.1. Different initiation.
BT088761 mRNA. Translation: ACR53998.1. Different initiation.
RefSeqiNP_725114.1. NM_165868.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00AL1-155[»]
ProteinModelPortaliQ0E9B6.
SMRiQ0E9B6. Positions 4-144.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi62099. 16 interactions.
IntActiQ0E9B6. 3 interactions.
STRINGi7227.FBpp0087115.

Proteomic databases

PaxDbiQ0E9B6.
PRIDEiQ0E9B6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0088007; FBpp0087115; FBgn0033699.
GeneIDi36321.
KEGGidme:Dmel_CG8857.

Organism-specific databases

CTDi6205.
FlyBaseiFBgn0033699. RpS11.

Phylogenomic databases

eggNOGiKOG1728. Eukaryota.
COG0186. LUCA.
GeneTreeiENSGT00390000002732.
InParanoidiQ0E9B6.
KOiK02949.
OMAiLVTIGEC.
OrthoDBiEOG091G0QVV.
PhylomeDBiQ0E9B6.

Enzyme and pathway databases

ReactomeiR-DME-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-DME-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-DME-6791226. Major pathway of rRNA processing in the nucleolus.
R-DME-72649. Translation initiation complex formation.
R-DME-72689. Formation of a pool of free 40S subunits.
R-DME-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-DME-72702. Ribosomal scanning and start codon recognition.
R-DME-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-DME-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-DME-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

ChiTaRSiRpS11. fly.
GenomeRNAii36321.
PROiQ0E9B6.

Gene expression databases

BgeeiFBgn0033699.
ExpressionAtlasiQ0E9B6. differential.
GenevisibleiQ0E9B6. DM.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
HAMAPiMF_01345_B. Ribosomal_S17_B. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR032440. Ribosomal_S11_N.
IPR000266. Ribosomal_S17/S11.
IPR028333. Ribosomal_S17_arc-typ.
IPR019979. Ribosomal_S17_CS.
[Graphical view]
PANTHERiPTHR10744. PTHR10744. 1 hit.
PfamiPF00366. Ribosomal_S17. 1 hit.
PF16205. Ribosomal_S17_N. 1 hit.
[Graphical view]
PRINTSiPR00973. RIBOSOMALS17.
ProDomiPD001295. Ribosomal_S17. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR03630. uS17_arch. 1 hit.
PROSITEiPS00056. RIBOSOMAL_S17. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRS11_DROME
AccessioniPrimary (citable) accession number: Q0E9B6
Secondary accession number(s): C4JD62, E2QC50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: October 17, 2006
Last modified: September 7, 2016
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Ribosomal proteins
    Ribosomal proteins families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

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.