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Protein

40S ribosomal protein S24

Gene

RpS24

Organism
Drosophila melanogaster (Fruit fly)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  • nucleotide binding Source: InterPro
  • structural constituent of ribosome Source: FlyBase

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal proteinUniRule annotationImported

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 S24UniRule annotation
Gene namesi
Name:RpS24Imported
ORF Names:CG3751Imported, Dmel_CG3751Imported
OrganismiDrosophila melanogaster (Fruit fly)Imported
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0261596. RpS24.

Subcellular locationi

GO - Cellular componenti

  • ribosome Source: FlyBase
Complete GO annotation...

Interactioni

Protein-protein interaction databases

MINTiMINT-944987.
STRINGi7227.FBpp0071846.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00AY1-131[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S24e family.UniRule annotation

Phylogenomic databases

eggNOGiKOG3424. Eukaryota.
COG2004. LUCA.
GeneTreeiENSGT00390000000153.
KOiK02974.
OMAiKLHKVAD.
OrthoDBiEOG7PS1J8.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
HAMAPiMF_00545. Ribosomal_S24e.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR012678. Ribosomal_L23/L15e_core_dom.
IPR001976. Ribosomal_S24e.
IPR018098. Ribosomal_S24e_CS.
[Graphical view]
PANTHERiPTHR10496. PTHR10496. 1 hit.
PfamiPF01282. Ribosomal_S24e. 1 hit.
[Graphical view]
ProDomiPD006052. Ribosomal_S24e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF54189. SSF54189. 1 hit.
PROSITEiPS00529. RIBOSOMAL_S24E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9W229-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGTTATIRT RKFMTNRLLA RKQMVCDVLH PGLSSVNKTE IREKLAAMYK
60 70 80 90 100
VTPDVVFAFG FRTNFGGGRS TGFALIYDTL DFAKKFEPKY RLARHGLFEQ
110 120 130
KKQTRKQRKE RRNRMKKVRG TAKAKIGTGK K
Length:131
Mass (Da):15,048
Last modified:May 1, 2000 - v1
Checksum:i4D267EE9C4F45D4C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAF46871.1.
AY113512 mRNA. Translation: AAM29517.1.
RefSeqiNP_611693.1. NM_137849.4.
UniGeneiDm.19983.

Genome annotation databases

EnsemblMetazoaiFBtr0071935; FBpp0071846; FBgn0261596.
GeneIDi37589.
KEGGidme:Dmel_CG3751.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAF46871.1.
AY113512 mRNA. Translation: AAM29517.1.
RefSeqiNP_611693.1. NM_137849.4.
UniGeneiDm.19983.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00AY1-131[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-944987.
STRINGi7227.FBpp0071846.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0071935; FBpp0071846; FBgn0261596.
GeneIDi37589.
KEGGidme:Dmel_CG3751.

Organism-specific databases

CTDi6229.
FlyBaseiFBgn0261596. RpS24.

Phylogenomic databases

eggNOGiKOG3424. Eukaryota.
COG2004. LUCA.
GeneTreeiENSGT00390000000153.
KOiK02974.
OMAiKLHKVAD.
OrthoDBiEOG7PS1J8.

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

ChiTaRSiRpS24. fly.
GenomeRNAii37589.
NextBioi804437.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
HAMAPiMF_00545. Ribosomal_S24e.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR012678. Ribosomal_L23/L15e_core_dom.
IPR001976. Ribosomal_S24e.
IPR018098. Ribosomal_S24e_CS.
[Graphical view]
PANTHERiPTHR10496. PTHR10496. 1 hit.
PfamiPF01282. Ribosomal_S24e. 1 hit.
[Graphical view]
ProDomiPD006052. Ribosomal_S24e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF54189. SSF54189. 1 hit.
PROSITEiPS00529. RIBOSOMAL_S24E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Gabor G.L., 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., 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., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J., 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., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., 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., WoodageT, 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., 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: BerkeleyImported.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BerkeleyImported.
  3. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BerkeleyImported.
  4. "The transposable elements of the Drosophila melanogaster euchromatin: a genomics perspective."
    Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R., Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M., Celniker S.E.
    Genome Biol. 3:RESEARCH0084-RESEARCH0084(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BerkeleyImported.
  5. "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly."
    Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., Karpen G.H.
    Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BerkeleyImported.
  6. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BerkeleyImported.
  7. "Combined evidence annotation of transposable elements in genome sequences."
    Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D., Ashburner M., Anxolabehere D.
    PLoS Comput. Biol. 1:166-175(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BerkeleyImported.
  8. Celniker S., Carlson J., Wan K., Frise E., Hoskins R., Park S., Svirskas R., Rubin G.
    Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  9. "Drosophila melanogaster release 4 sequence."
    Berkeley Drosophila Genome Project
    Celniker S., Carlson J., Wan K., Pfeiffer B., Frise E., George R., Hoskins R., Stapleton M., Pacleb J., Park S., Svirskas R., Smith E., Yu C., Rubin G.
    Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  10. "The Release 5.1 annotation of Drosophila melanogaster heterochromatin."
    Smith C.D., Shu S., Mungall C.J., Karpen G.H.
    Science 316:1586-1591(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BerkeleyImported.
  11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BerkeleyImported.
  12. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (6.00 ANGSTROMS).
  13. FlyBase
    Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.

Entry informationi

Entry nameiQ9W229_DROME
AccessioniPrimary (citable) accession number: Q9W229
Entry historyi
Integrated into UniProtKB/TrEMBL: May 1, 2000
Last sequence update: May 1, 2000
Last modified: May 11, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

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.