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Protein

60S ribosomal protein L15

Gene

RpL15

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-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 L15
Gene namesi
Name:RpL15
Synonyms:ZITI
ORF Names:CG17420
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0028697. RpL15.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 20420460S ribosomal protein L15PRO_0000127555Add
BLAST

Proteomic databases

PaxDbiO17445.
PRIDEiO17445.

Expressioni

Gene expression databases

BgeeiO17445.
ExpressionAtlasiO17445. differential.
GenevisibleiO17445. DM.

Interactioni

Protein-protein interaction databases

BioGridi78043. 27 interactions.
DIPiDIP-17499N.
IntActiO17445. 1 interaction.
MINTiMINT-1548325.
STRINGi7227.FBpp0300652.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00CN1-204[»]
ProteinModelPortaliO17445.
SMRiO17445. Positions 3-177.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L15e family.Curated

Phylogenomic databases

eggNOGiKOG1678. Eukaryota.
COG1632. LUCA.
GeneTreeiENSGT00390000005092.
InParanoidiO17445.
KOiK02877.
OMAiQRKKQSD.
OrthoDBiEOG7M3J1R.
PhylomeDBiO17445.

Family and domain databases

Gene3Di3.40.1120.10. 1 hit.
InterProiIPR024794. Rbsml_L15e_core_dom.
IPR000439. Ribosomal_L15e.
IPR020925. Ribosomal_L15e_CS.
IPR012678. Ribosomal_L23/L15e_core_dom.
[Graphical view]
PANTHERiPTHR11847. PTHR11847. 1 hit.
PfamiPF00827. Ribosomal_L15e. 1 hit.
[Graphical view]
SMARTiSM01384. Ribosomal_L15e. 1 hit.
[Graphical view]
SUPFAMiSSF54189. SSF54189. 1 hit.
PROSITEiPS01194. RIBOSOMAL_L15E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O17445-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGAYRYMQEL YRKKQSDVMR YLLRIRVWQY RQLTKLHRSP RPTRPDKARR
60 70 80 90 100
LGYRAKQGFV IYRIRVRRGG RKRPVPKGCT YGKPKSHGVN QLKPYRGLQS
110 120 130 140 150
IAEERVGRRL GGLRVLNSYW IAQDASYKYF EVILIDTHHS AIRRDPKINW
160 170 180 190 200
ICKHVHKHRE LRGLTSAGKS SRGIGKGYRY SQTIGGSRRA AWKRKNREHM

HRKR
Length:204
Mass (Da):24,325
Last modified:January 1, 1998 - v1
Checksum:iBEB765555EB80EAC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF030251 mRNA. Translation: AAB84223.1.
AE014296 Genomic DNA. Translation: EAA46270.1.
AE014296 Genomic DNA. Translation: EAA46271.1.
AE014296 Genomic DNA. Translation: EDP28095.1.
AY094841 mRNA. Translation: AAM11194.1.
RefSeqiNP_001015155.1. NM_001015155.3.
NP_001015156.1. NM_001015156.2.
NP_001104429.2. NM_001110959.3.
NP_001104430.1. NM_001110960.2.
NP_001245395.1. NM_001258466.1.
NP_001245396.1. NM_001258467.1.
NP_001245397.1. NM_001258468.1.
NP_001245398.1. NM_001258469.1.
UniGeneiDm.6828.

Genome annotation databases

EnsemblMetazoaiFBtr0113742; FBpp0112465; FBgn0028697.
FBtr0113743; FBpp0112466; FBgn0028697.
FBtr0113744; FBpp0112467; FBgn0028697.
FBtr0301801; FBpp0291015; FBgn0028697.
FBtr0308333; FBpp0300652; FBgn0028697.
FBtr0308334; FBpp0300653; FBgn0028697.
FBtr0308335; FBpp0300654; FBgn0028697.
FBtr0308336; FBpp0300655; FBgn0028697.
GeneIDi3354918.
KEGGidme:Dmel_CG17420.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF030251 mRNA. Translation: AAB84223.1.
AE014296 Genomic DNA. Translation: EAA46270.1.
AE014296 Genomic DNA. Translation: EAA46271.1.
AE014296 Genomic DNA. Translation: EDP28095.1.
AY094841 mRNA. Translation: AAM11194.1.
RefSeqiNP_001015155.1. NM_001015155.3.
NP_001015156.1. NM_001015156.2.
NP_001104429.2. NM_001110959.3.
NP_001104430.1. NM_001110960.2.
NP_001245395.1. NM_001258466.1.
NP_001245396.1. NM_001258467.1.
NP_001245397.1. NM_001258468.1.
NP_001245398.1. NM_001258469.1.
UniGeneiDm.6828.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00CN1-204[»]
ProteinModelPortaliO17445.
SMRiO17445. Positions 3-177.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi78043. 27 interactions.
DIPiDIP-17499N.
IntActiO17445. 1 interaction.
MINTiMINT-1548325.
STRINGi7227.FBpp0300652.

Proteomic databases

PaxDbiO17445.
PRIDEiO17445.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0113742; FBpp0112465; FBgn0028697.
FBtr0113743; FBpp0112466; FBgn0028697.
FBtr0113744; FBpp0112467; FBgn0028697.
FBtr0301801; FBpp0291015; FBgn0028697.
FBtr0308333; FBpp0300652; FBgn0028697.
FBtr0308334; FBpp0300653; FBgn0028697.
FBtr0308335; FBpp0300654; FBgn0028697.
FBtr0308336; FBpp0300655; FBgn0028697.
GeneIDi3354918.
KEGGidme:Dmel_CG17420.

Organism-specific databases

CTDi6138.
FlyBaseiFBgn0028697. RpL15.

Phylogenomic databases

eggNOGiKOG1678. Eukaryota.
COG1632. LUCA.
GeneTreeiENSGT00390000005092.
InParanoidiO17445.
KOiK02877.
OMAiQRKKQSD.
OrthoDBiEOG7M3J1R.
PhylomeDBiO17445.

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

ChiTaRSiRpL15. fly.
GenomeRNAii3354918.
PROiO17445.

Gene expression databases

BgeeiO17445.
ExpressionAtlasiO17445. differential.
GenevisibleiO17445. DM.

Family and domain databases

Gene3Di3.40.1120.10. 1 hit.
InterProiIPR024794. Rbsml_L15e_core_dom.
IPR000439. Ribosomal_L15e.
IPR020925. Ribosomal_L15e_CS.
IPR012678. Ribosomal_L23/L15e_core_dom.
[Graphical view]
PANTHERiPTHR11847. PTHR11847. 1 hit.
PfamiPF00827. Ribosomal_L15e. 1 hit.
[Graphical view]
SMARTiSM01384. Ribosomal_L15e. 1 hit.
[Graphical view]
SUPFAMiSSF54189. SSF54189. 1 hit.
PROSITEiPS01194. RIBOSOMAL_L15E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Inaguma Y., Joanisse D.R., Tanguay R.M.
    Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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: STRUCTURE BY ELECTRON MICROSCOPY (6.0 ANGSTROMS) OF THE 80S RIBOSOME.

Entry informationi

Entry nameiRL15_DROME
AccessioniPrimary (citable) accession number: O17445
Secondary accession number(s): A8Y561, Q7PL86, Q9W5N1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: July 6, 2016
This is version 109 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.