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Protein

60S ribosomal protein L11

Gene

RpL11

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

Functioni

Binds to 5S ribosomal RNA.By similarity

GO - Molecular functioni

  • rRNA binding Source: UniProtKB-KW
  • structural constituent of ribosome Source: FlyBase

GO - Biological processi

  • centrosome duplication Source: FlyBase
  • mitotic spindle elongation Source: FlyBase
  • mitotic spindle organization Source: FlyBase
  • sensory perception of pain Source: FlyBase
  • translation 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-72689. Formation of a pool of free 40S subunits.
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:
60S ribosomal protein L11
Gene namesi
Name:RpL11
Synonyms:RPL11A
ORF Names:CG7726
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0013325. RpL11.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18418460S ribosomal protein L11PRO_0000125089Add
BLAST

Proteomic databases

PaxDbiP46222.
PRIDEiP46222.

Expressioni

Gene expression databases

GenevisibleiP46222. DM.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
Fmr1Q9NFU05EBI-183104,EBI-422631

Protein-protein interaction databases

BioGridi62897. 9 interactions.
DIPiDIP-18297N.
IntActiP46222. 4 interactions.
MINTiMINT-767987.
STRINGi7227.FBpp0085717.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00CJ1-184[»]
ProteinModelPortaliP46222.
SMRiP46222. Positions 15-177.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L5P family.Curated

Phylogenomic databases

eggNOGiKOG0397. Eukaryota.
COG0094. LUCA.
GeneTreeiENSGT00390000013411.
InParanoidiP46222.
KOiK02868.
OMAiEDTMAWF.
OrthoDBiEOG7ZPNMB.
PhylomeDBiP46222.

Family and domain databases

Gene3Di3.30.1440.10. 1 hit.
InterProiIPR002132. Ribosomal_L5.
IPR031309. Ribosomal_L5_C.
IPR020929. Ribosomal_L5_CS.
IPR022803. Ribosomal_L5_domain.
IPR031310. Ribosomal_L5_N.
[Graphical view]
PfamiPF00281. Ribosomal_L5. 1 hit.
PF00673. Ribosomal_L5_C. 1 hit.
[Graphical view]
PIRSFiPIRSF002161. Ribosomal_L5. 1 hit.
SUPFAMiSSF55282. SSF55282. 1 hit.
PROSITEiPS00358. RIBOSOMAL_L5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P46222-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAVTKKIKR DPAKNPMRDL HIRKLCLNIC VGESGDRLTR AAKVLEQLTG
60 70 80 90 100
QQPVFSKARY TVRSFGIRRN EKIAVHCTVR GAKAEEILER GLKVREYELR
110 120 130 140 150
RENFSSTGNF GFGIQEHIDL GIKYDPSIGI YGLDFYVVLG RPGYNVNHRK
160 170 180
RKSGTVGFQH RLTKEDAMKW FQQKYDGIIL NTKK
Length:184
Mass (Da):21,112
Last modified:August 31, 2004 - v2
Checksum:iE64EF5568A530C09
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 185KNPMR → QEPDE in AAC46585 (PubMed:7893752).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U15643 mRNA. Translation: AAC46585.1.
AE013599 Genomic DNA. Translation: AAF57560.1.
AY094790 mRNA. Translation: AAM11143.1.
PIRiS60245.
RefSeqiNP_001286614.1. NM_001299685.1.
NP_477054.1. NM_057706.5.
UniGeneiDm.700.

Genome annotation databases

EnsemblMetazoaiFBtr0086533; FBpp0085717; FBgn0013325.
FBtr0340533; FBpp0309436; FBgn0013325.
GeneIDi37235.
KEGGidme:Dmel_CG7726.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U15643 mRNA. Translation: AAC46585.1.
AE013599 Genomic DNA. Translation: AAF57560.1.
AY094790 mRNA. Translation: AAM11143.1.
PIRiS60245.
RefSeqiNP_001286614.1. NM_001299685.1.
NP_477054.1. NM_057706.5.
UniGeneiDm.700.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00CJ1-184[»]
ProteinModelPortaliP46222.
SMRiP46222. Positions 15-177.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi62897. 9 interactions.
DIPiDIP-18297N.
IntActiP46222. 4 interactions.
MINTiMINT-767987.
STRINGi7227.FBpp0085717.

Proteomic databases

PaxDbiP46222.
PRIDEiP46222.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0086533; FBpp0085717; FBgn0013325.
FBtr0340533; FBpp0309436; FBgn0013325.
GeneIDi37235.
KEGGidme:Dmel_CG7726.

Organism-specific databases

CTDi6135.
FlyBaseiFBgn0013325. RpL11.

Phylogenomic databases

eggNOGiKOG0397. Eukaryota.
COG0094. LUCA.
GeneTreeiENSGT00390000013411.
InParanoidiP46222.
KOiK02868.
OMAiEDTMAWF.
OrthoDBiEOG7ZPNMB.
PhylomeDBiP46222.

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-72689. Formation of a pool of free 40S subunits.
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

ChiTaRSiRpL11. fly.
GenomeRNAii37235.
PROiP46222.

Gene expression databases

GenevisibleiP46222. DM.

Family and domain databases

Gene3Di3.30.1440.10. 1 hit.
InterProiIPR002132. Ribosomal_L5.
IPR031309. Ribosomal_L5_C.
IPR020929. Ribosomal_L5_CS.
IPR022803. Ribosomal_L5_domain.
IPR031310. Ribosomal_L5_N.
[Graphical view]
PfamiPF00281. Ribosomal_L5. 1 hit.
PF00673. Ribosomal_L5_C. 1 hit.
[Graphical view]
PIRSFiPIRSF002161. Ribosomal_L5. 1 hit.
SUPFAMiSSF55282. SSF55282. 1 hit.
PROSITEiPS00358. RIBOSOMAL_L5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of the Drosophila homologue of the rat ribosomal protein L11 gene."
    Larochelle S., Suter B.
    Biochim. Biophys. Acta 1261:147-150(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Oregon-R.
  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. "A Drosophila full-length cDNA resource."
    Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  5. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (6.0 ANGSTROMS) OF THE 80S RIBOSOME.

Entry informationi

Entry nameiRL11_DROME
AccessioniPrimary (citable) accession number: P46222
Secondary accession number(s): Q9V8U9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: August 31, 2004
Last modified: June 8, 2016
This is version 124 of the entry and version 2 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.