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Protein

60S ribosomal protein L10

Gene

RpL10

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

Functioni

GO - Molecular functioni

  • structural constituent of ribosome Source: FlyBase

GO - Biological processi

  • centrosome duplication Source: FlyBase
  • centrosome organization Source: FlyBase
  • mitotic spindle elongation Source: FlyBase
  • mitotic spindle organization Source: FlyBase
  • sensory perception of pain Source: FlyBase
  • translation Source: InterPro
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-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 L10
Alternative name(s):
QM protein homolog
dQM
Gene namesi
Name:RpL10
Synonyms:Qm
ORF Names:CG17521
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0024733. RpL10.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: FlyBase
  • neuronal cell body Source: FlyBase
  • ribosome Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 21821860S ribosomal protein L10PRO_0000147114Add
BLAST

Proteomic databases

PaxDbiO61231.
PRIDEiO61231.

Expressioni

Gene expression databases

BgeeiO61231.
ExpressionAtlasiO61231. differential.
GenevisibleiO61231. DM.

Interactioni

Subunit structurei

Component of the large ribosomal subunit. Mature ribosomes consist of a small (40S) and a large (60S) subunit. The 40S subunit contains about 33 different proteins and 1 molecule of RNA (18S). The 60S subunit contains about 49 different proteins and 3 molecules of RNA (28S, 5.8S and 5S) (By similarity).By similarity

Protein-protein interaction databases

BioGridi68678. 13 interactions.
DIPiDIP-18809N.
IntActiO61231. 3 interactions.
MINTiMINT-888527.
STRINGi7227.FBpp0306039.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00CI1-218[»]
ProteinModelPortaliO61231.
SMRiO61231. Positions 3-206.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L10e family.Curated

Phylogenomic databases

eggNOGiKOG0857. Eukaryota.
COG0197. LUCA.
GeneTreeiENSGT00390000003897.
InParanoidiO61231.
KOiK02866.
OMAiEHKMATG.
OrthoDBiEOG76MK97.
PhylomeDBiO61231.

Family and domain databases

Gene3Di3.90.1170.10. 1 hit.
InterProiIPR001197. Ribosomal_L10e.
IPR016180. Ribosomal_L10e/L16.
IPR018255. Ribosomal_L10e_CS.
[Graphical view]
PfamiPF00252. Ribosomal_L16. 1 hit.
[Graphical view]
PIRSFiPIRSF005590. Ribosomal_L10. 1 hit.
SUPFAMiSSF54686. SSF54686. 1 hit.
TIGRFAMsiTIGR00279. uL16_euk_arch. 1 hit.
PROSITEiPS01257. RIBOSOMAL_L10E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O61231-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRRPARCYR YCKNKPYPKS RFCRGVPDPK IRIFDLGRKK ATVEDFPLCV
60 70 80 90 100
HLVSDEYEQL SSEALEAGRI CCNKYLVKYC GKDQFHIRMR LHPFHVIRIN
110 120 130 140 150
KMLSCAGADR LQTGMRGAFG KPQGTVARVR IGQPIMSVRS SDRYKAQVIE
160 170 180 190 200
ALRRAKFKFP GRQKIYVSKK WGFTKYERER YEELRDDNRL EPDGCNVKYR
210
PEHGPIAAWE KAQRDVYA
Length:218
Mass (Da):25,528
Last modified:August 1, 1998 - v1
Checksum:i2EFC207CEB832BE4
GO

Sequence cautioni

The sequence AAO39584.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti73 – 9927Missing in AAO39584 (Ref. 5) CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49721 mRNA. Translation: AAC16108.1.
AE014296 Genomic DNA. Translation: AAF45440.3.
AE014296 Genomic DNA. Translation: AAG22453.4.
AY070910 mRNA. Translation: AAL48532.1.
BT003580 mRNA. Translation: AAO39584.1. Different initiation.
RefSeqiNP_001262233.1. NM_001275304.1.
NP_651954.3. NM_143697.5.
NP_730773.4. NM_168984.5.
UniGeneiDm.1411.

Genome annotation databases

EnsemblMetazoaiFBtr0299869; FBpp0289147; FBgn0024733.
FBtr0299870; FBpp0289148; FBgn0024733.
FBtr0333910; FBpp0306039; FBgn0024733.
GeneIDi43864.
KEGGidme:Dmel_CG17521.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49721 mRNA. Translation: AAC16108.1.
AE014296 Genomic DNA. Translation: AAF45440.3.
AE014296 Genomic DNA. Translation: AAG22453.4.
AY070910 mRNA. Translation: AAL48532.1.
BT003580 mRNA. Translation: AAO39584.1. Different initiation.
RefSeqiNP_001262233.1. NM_001275304.1.
NP_651954.3. NM_143697.5.
NP_730773.4. NM_168984.5.
UniGeneiDm.1411.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00CI1-218[»]
ProteinModelPortaliO61231.
SMRiO61231. Positions 3-206.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi68678. 13 interactions.
DIPiDIP-18809N.
IntActiO61231. 3 interactions.
MINTiMINT-888527.
STRINGi7227.FBpp0306039.

Proteomic databases

PaxDbiO61231.
PRIDEiO61231.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0299869; FBpp0289147; FBgn0024733.
FBtr0299870; FBpp0289148; FBgn0024733.
FBtr0333910; FBpp0306039; FBgn0024733.
GeneIDi43864.
KEGGidme:Dmel_CG17521.

Organism-specific databases

CTDi6134.
FlyBaseiFBgn0024733. RpL10.

Phylogenomic databases

eggNOGiKOG0857. Eukaryota.
COG0197. LUCA.
GeneTreeiENSGT00390000003897.
InParanoidiO61231.
KOiK02866.
OMAiEHKMATG.
OrthoDBiEOG76MK97.
PhylomeDBiO61231.

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

ChiTaRSiRpL10. fly.
GenomeRNAii43864.
NextBioi836242.
PROiO61231.

Gene expression databases

BgeeiO61231.
ExpressionAtlasiO61231. differential.
GenevisibleiO61231. DM.

Family and domain databases

Gene3Di3.90.1170.10. 1 hit.
InterProiIPR001197. Ribosomal_L10e.
IPR016180. Ribosomal_L10e/L16.
IPR018255. Ribosomal_L10e_CS.
[Graphical view]
PfamiPF00252. Ribosomal_L16. 1 hit.
[Graphical view]
PIRSFiPIRSF005590. Ribosomal_L10. 1 hit.
SUPFAMiSSF54686. SSF54686. 1 hit.
TIGRFAMsiTIGR00279. uL16_euk_arch. 1 hit.
PROSITEiPS01257. RIBOSOMAL_L10E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The isolation, localization and characterization of the QM homolog in Drosophila melanogaster."
    Nguyen-Yue Y.H., Loftus T.M., Torok T., Bryant P., Stanbridge E.J.
    DNA Seq. 7:337-347(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: CNS.
  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: Embryo.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  6. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (6.0 ANGSTROMS) OF THE 80S RIBOSOME.

Entry informationi

Entry nameiRL10_DROME
AccessioniPrimary (citable) accession number: O61231
Secondary accession number(s): Q0E8B5
, Q86NY2, Q9I813, Q9W5T1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: May 11, 2016
This is version 132 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.