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Protein

40S ribosomal protein S18

Gene

RpS18

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

Functioni

Located at the top of the head of the 40S subunit, it contacts several helices of the 18S rRNA.By similarity

GO - Molecular functioni

GO - Biological processi

  • mitotic spindle elongation Source: FlyBase
  • mitotic spindle organization Source: FlyBase
  • translation Source: FlyBase
  • translational initiation Source: FlyBase
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-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 S18
Gene namesi
Name:RpS18
ORF Names:CG8900
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0010411. RpS18.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15215240S ribosomal protein S18PRO_0000132220Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei41 – 411Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP41094.
PRIDEiP41094.

PTM databases

iPTMnetiP41094.

Expressioni

Gene expression databases

BgeeiP41094.
ExpressionAtlasiP41094. differential.
GenevisibleiP41094. DM.

Interactioni

Protein-protein interaction databases

BioGridi62947. 13 interactions.
DIPiDIP-21027N.
STRINGi7227.FBpp0085585.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00AS1-152[»]
ProteinModelPortaliP41094.
SMRiP41094. Positions 3-145.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S13P family.Curated

Phylogenomic databases

eggNOGiKOG3311. Eukaryota.
COG0099. LUCA.
GeneTreeiENSGT00390000012691.
InParanoidiP41094.
KOiK02964.
OMAiRIMNTDL.
OrthoDBiEOG7Q5HG2.
PhylomeDBiP41094.

Family and domain databases

Gene3Di4.10.910.10. 1 hit.
HAMAPiMF_01315. Ribosomal_S13_S18.
InterProiIPR027437. 30s_Rbsml_prot_S13_C.
IPR001892. Ribosomal_S13.
IPR010979. Ribosomal_S13-like_H2TH.
IPR018269. Ribosomal_S13_CS.
[Graphical view]
PfamiPF00416. Ribosomal_S13. 1 hit.
[Graphical view]
PIRSFiPIRSF002134. Ribosomal_S13. 1 hit.
SUPFAMiSSF46946. SSF46946. 1 hit.
PROSITEiPS00646. RIBOSOMAL_S13_1. 1 hit.
PS50159. RIBOSOMAL_S13_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P41094-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLVIPEKFQ HILRIMNTNI DGKRKVGIAM TAIKGVGRRY SNIVLKKADV
60 70 80 90 100
DLTKRAGECT EEEVDKVVTI ISNPLQYKVP NWFLNRQKDI IDGKYWQLTS
110 120 130 140 150
SNLDSKLRDD LERLKKIRSH RGLRHYWGLR VRGQHTKTTG RRGRTVGVSK

KK
Length:152
Mass (Da):17,612
Last modified:February 1, 1995 - v1
Checksum:iF52F9E8665B880EF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111H → R in AAM48463 (PubMed:12537569).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L22959 mRNA. Translation: AAA28870.1.
AE013599 Genomic DNA. Translation: AAF57491.1.
AY118434 mRNA. Translation: AAM48463.1.
BT024929 mRNA. Translation: ABE01159.1.
RefSeqiNP_476964.1. NM_057616.6.
NP_725943.1. NM_166383.4.
UniGeneiDm.20558.

Genome annotation databases

EnsemblMetazoaiFBtr0086273; FBpp0085585; FBgn0010411.
FBtr0086274; FBpp0085586; FBgn0010411.
GeneIDi37292.
KEGGidme:Dmel_CG8900.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L22959 mRNA. Translation: AAA28870.1.
AE013599 Genomic DNA. Translation: AAF57491.1.
AY118434 mRNA. Translation: AAM48463.1.
BT024929 mRNA. Translation: ABE01159.1.
RefSeqiNP_476964.1. NM_057616.6.
NP_725943.1. NM_166383.4.
UniGeneiDm.20558.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00AS1-152[»]
ProteinModelPortaliP41094.
SMRiP41094. Positions 3-145.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi62947. 13 interactions.
DIPiDIP-21027N.
STRINGi7227.FBpp0085585.

PTM databases

iPTMnetiP41094.

Proteomic databases

PaxDbiP41094.
PRIDEiP41094.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0086273; FBpp0085585; FBgn0010411.
FBtr0086274; FBpp0085586; FBgn0010411.
GeneIDi37292.
KEGGidme:Dmel_CG8900.

Organism-specific databases

CTDi6222.
FlyBaseiFBgn0010411. RpS18.

Phylogenomic databases

eggNOGiKOG3311. Eukaryota.
COG0099. LUCA.
GeneTreeiENSGT00390000012691.
InParanoidiP41094.
KOiK02964.
OMAiRIMNTDL.
OrthoDBiEOG7Q5HG2.
PhylomeDBiP41094.

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-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

ChiTaRSiRpS18. fly.
GenomeRNAii37292.
NextBioi802956.
PROiP41094.

Gene expression databases

BgeeiP41094.
ExpressionAtlasiP41094. differential.
GenevisibleiP41094. DM.

Family and domain databases

Gene3Di4.10.910.10. 1 hit.
HAMAPiMF_01315. Ribosomal_S13_S18.
InterProiIPR027437. 30s_Rbsml_prot_S13_C.
IPR001892. Ribosomal_S13.
IPR010979. Ribosomal_S13-like_H2TH.
IPR018269. Ribosomal_S13_CS.
[Graphical view]
PfamiPF00416. Ribosomal_S13. 1 hit.
[Graphical view]
PIRSFiPIRSF002134. Ribosomal_S13. 1 hit.
SUPFAMiSSF46946. SSF46946. 1 hit.
PROSITEiPS00646. RIBOSOMAL_S13_1. 1 hit.
PS50159. RIBOSOMAL_S13_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Drosophila melanogaster homolog of ribosomal protein S18."
    Garwood J., Lepesant J.-A.
    Gene 141:231-235(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Canton-S.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.
  5. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.
    Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
  6. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  7. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (6.0 ANGSTROMS) OF THE 80S RIBOSOME.

Entry informationi

Entry nameiRS18_DROME
AccessioniPrimary (citable) accession number: P41094
Secondary accession number(s): Q1WWH7, Q8MT19, Q9V911
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 11, 2016
This is version 131 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.