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Protein

40S ribosomal protein S26

Gene

RpS26

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

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

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 S26
Short name:
DS31
Gene namesi
Name:RpS26
ORF Names:CG10305
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0261597. RpS26.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11411440S ribosomal protein S26PRO_0000204520Add
BLAST

Proteomic databases

PaxDbiP13008.
PRIDEiP13008.

Expressioni

Gene expression databases

BgeeiP13008.
ExpressionAtlasiP13008. differential.
GenevisibleiP13008. DM.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
Dmel_CG14543Q9VBI04EBI-171405,EBI-170896

Protein-protein interaction databases

BioGridi61093. 34 interactions.
DIPiDIP-17487N.
IntActiP13008. 7 interactions.
MINTiMINT-297533.
STRINGi7227.FBpp0080641.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00Aa1-114[»]
ProteinModelPortaliP13008.
SMRiP13008. Positions 2-97.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S26e family.Curated

Phylogenomic databases

eggNOGiKOG1768. Eukaryota.
COG4830. LUCA.
GeneTreeiENSGT00390000002517.
InParanoidiP13008.
KOiK02976.
OMAiCSRCVGK.
OrthoDBiEOG7B31Q7.
PhylomeDBiP13008.

Family and domain databases

InterProiIPR000892. Ribosomal_S26e.
[Graphical view]
PfamiPF01283. Ribosomal_S26e. 1 hit.
[Graphical view]
PROSITEiPS00733. RIBOSOMAL_S26E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P13008-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKKRRNGGR NKHNRGHVKP VRCTNCARCV PKDKAIKKFV IRNIVEAAAV
60 70 80 90 100
RDITEASIWD SYVLPKLYAK LHYCVSCAIH SKVVRNRSRE ARRIRTPPLR
110
SFPKDMARNN QNRK
Length:114
Mass (Da):13,267
Last modified:January 1, 1990 - v1
Checksum:i0F0A6D8A8C6A8D7F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13625 mRNA. Translation: CAB38441.1.
X14247 Genomic DNA. Translation: CAA32463.1.
AE014134 Genomic DNA. Translation: AAN11004.1.
AE014134 Genomic DNA. Translation: AAN11005.1.
AY069761 mRNA. Translation: AAL39906.1.
BT072894 mRNA. Translation: ACN71213.1.
PIRiS03724. R3FF26.
RefSeqiNP_001260537.1. NM_001273608.1.
NP_001286042.1. NM_001299113.1.
NP_523595.1. NM_078871.6.
NP_724109.1. NM_165252.2.
NP_724110.1. NM_165253.2.
UniGeneiDm.6957.

Genome annotation databases

EnsemblMetazoaiFBtr0081089; FBpp0080639; FBgn0261597.
FBtr0081090; FBpp0080640; FBgn0261597.
FBtr0081091; FBpp0080641; FBgn0261597.
FBtr0331455; FBpp0303872; FBgn0261597.
FBtr0346591; FBpp0312181; FBgn0261597.
GeneIDi35098.
KEGGidme:Dmel_CG10305.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13625 mRNA. Translation: CAB38441.1.
X14247 Genomic DNA. Translation: CAA32463.1.
AE014134 Genomic DNA. Translation: AAN11004.1.
AE014134 Genomic DNA. Translation: AAN11005.1.
AY069761 mRNA. Translation: AAL39906.1.
BT072894 mRNA. Translation: ACN71213.1.
PIRiS03724. R3FF26.
RefSeqiNP_001260537.1. NM_001273608.1.
NP_001286042.1. NM_001299113.1.
NP_523595.1. NM_078871.6.
NP_724109.1. NM_165252.2.
NP_724110.1. NM_165253.2.
UniGeneiDm.6957.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00Aa1-114[»]
ProteinModelPortaliP13008.
SMRiP13008. Positions 2-97.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi61093. 34 interactions.
DIPiDIP-17487N.
IntActiP13008. 7 interactions.
MINTiMINT-297533.
STRINGi7227.FBpp0080641.

Proteomic databases

PaxDbiP13008.
PRIDEiP13008.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0081089; FBpp0080639; FBgn0261597.
FBtr0081090; FBpp0080640; FBgn0261597.
FBtr0081091; FBpp0080641; FBgn0261597.
FBtr0331455; FBpp0303872; FBgn0261597.
FBtr0346591; FBpp0312181; FBgn0261597.
GeneIDi35098.
KEGGidme:Dmel_CG10305.

Organism-specific databases

CTDi6231.
FlyBaseiFBgn0261597. RpS26.

Phylogenomic databases

eggNOGiKOG1768. Eukaryota.
COG4830. LUCA.
GeneTreeiENSGT00390000002517.
InParanoidiP13008.
KOiK02976.
OMAiCSRCVGK.
OrthoDBiEOG7B31Q7.
PhylomeDBiP13008.

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

ChiTaRSiRpS26. fly.
GenomeRNAii35098.
PROiP13008.

Gene expression databases

BgeeiP13008.
ExpressionAtlasiP13008. differential.
GenevisibleiP13008. DM.

Family and domain databases

InterProiIPR000892. Ribosomal_S26e.
[Graphical view]
PfamiPF01283. Ribosomal_S26e. 1 hit.
[Graphical view]
PROSITEiPS00733. RIBOSOMAL_S26E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of cDNA for a Drosophila ribosomal protein with homology to rat ribosomal protein S26."
    Itoh N., Ohta K., Ohta M., Kawasaki T., Yamashina I.
    Nucleic Acids Res. 17:441-441(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Canton-S.
  2. "The nucleotide sequence of a gene for a putative ribosomal protein S31 of Drosophila."
    Itoh N., Ohta K., Ohta M., Kawasaki T., Yamashina I.
    Nucleic Acids Res. 17:2121-2121(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION.
    Strain: Canton-S.
  3. "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.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  6. Carlson J.W., Booth B., Frise E., Sandler J., Wan K.H., Yu C., Celniker S.E.
    Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
  7. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (6.0 ANGSTROMS) OF THE 80S RIBOSOME.

Entry informationi

Entry nameiRS26_DROME
AccessioniPrimary (citable) accession number: P13008
Secondary accession number(s): A4V0T7
, C0PV38, P10380, Q0E8P4, Q9VJ88
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: July 6, 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.