Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

60S ribosomal protein L13

Gene

RpL13

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 3 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
  • mitotic spindle elongation Source: FlyBase
  • mitotic spindle organization 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 L13
Alternative name(s):
BBC1 protein homolog
Gene namesi
Name:RpL13
Synonyms:bbc1
ORF Names:CG4651
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0011272. RpL13.

Subcellular locationi

GO - Cellular componenti

  • ribosome Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 21821860S ribosomal protein L13PRO_0000192925Add
BLAST

Proteomic databases

PaxDbiP41126.
PRIDEiP41126.

Expressioni

Gene expression databases

BgeeiP41126.
ExpressionAtlasiP41126. differential.
GenevisibleiP41126. DM.

Interactioni

Protein-protein interaction databases

BioGridi60423. 14 interactions.
DIPiDIP-19420N.
IntActiP41126. 2 interactions.
MINTiMINT-752357.
STRINGi7227.FBpp0079484.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00CL1-218[»]
ProteinModelPortaliP41126.
SMRiP41126. Positions 2-211.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L13e family.Curated

Phylogenomic databases

eggNOGiKOG3295. Eukaryota.
COG4352. LUCA.
GeneTreeiENSGT00390000007818.
InParanoidiP41126.
KOiK02873.
OMAiHCPTFRY.
OrthoDBiEOG74TX1G.
PhylomeDBiP41126.

Family and domain databases

InterProiIPR001380. Ribosomal_L13e.
IPR018256. Ribosomal_L13e_CS.
[Graphical view]
PANTHERiPTHR11722. PTHR11722. 1 hit.
PfamiPF01294. Ribosomal_L13e. 1 hit.
[Graphical view]
PROSITEiPS01104. RIBOSOMAL_L13E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P41126-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKGNNMIPN QHYHKWWQRH VKTWFNQPAR KVRRHANRVK KAKAVFPRPA
60 70 80 90 100
SGALRPVVRC PTIRYHTKLR AGRGFTLEEL KGAGIGANFA KTIGIAVDRR
110 120 130 140 150
RKNKSLESRQ RNIQRLKEYR SKLILFPINE KKIRAGESSL EECKLATQLK
160 170 180 190 200
GPVLPIKNEQ PAVVEFREVT KDEKKFKAFA TLRKARTDAR LVGIRAKRAK
210
EAAESEDAAK GDPKKAKK
Length:218
Mass (Da):24,951
Last modified:February 1, 1995 - v1
Checksum:i2DBCF34B2E650A63
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X77926 Genomic DNA. Translation: CAA54898.1.
AE014134 Genomic DNA. Translation: AAF52842.1.
AE014134 Genomic DNA. Translation: ABC65888.1.
BT053725 mRNA. Translation: ACK77643.1.
BT128812 mRNA. Translation: AEM72508.1.
PIRiJC4260.
S42877.
RefSeqiNP_001033891.1. NM_001038802.2.
NP_001260312.1. NM_001273383.2.
NP_523530.1. NM_078806.4.
UniGeneiDm.21541.

Genome annotation databases

EnsemblMetazoaiFBtr0079888; FBpp0079484; FBgn0011272.
FBtr0100164; FBpp0099517; FBgn0011272.
FBtr0310482; FBpp0302626; FBgn0011272.
GeneIDi34329.
KEGGidme:Dmel_CG4651.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X77926 Genomic DNA. Translation: CAA54898.1.
AE014134 Genomic DNA. Translation: AAF52842.1.
AE014134 Genomic DNA. Translation: ABC65888.1.
BT053725 mRNA. Translation: ACK77643.1.
BT128812 mRNA. Translation: AEM72508.1.
PIRiJC4260.
S42877.
RefSeqiNP_001033891.1. NM_001038802.2.
NP_001260312.1. NM_001273383.2.
NP_523530.1. NM_078806.4.
UniGeneiDm.21541.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00CL1-218[»]
ProteinModelPortaliP41126.
SMRiP41126. Positions 2-211.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi60423. 14 interactions.
DIPiDIP-19420N.
IntActiP41126. 2 interactions.
MINTiMINT-752357.
STRINGi7227.FBpp0079484.

Proteomic databases

PaxDbiP41126.
PRIDEiP41126.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0079888; FBpp0079484; FBgn0011272.
FBtr0100164; FBpp0099517; FBgn0011272.
FBtr0310482; FBpp0302626; FBgn0011272.
GeneIDi34329.
KEGGidme:Dmel_CG4651.

Organism-specific databases

CTDi6137.
FlyBaseiFBgn0011272. RpL13.

Phylogenomic databases

eggNOGiKOG3295. Eukaryota.
COG4352. LUCA.
GeneTreeiENSGT00390000007818.
InParanoidiP41126.
KOiK02873.
OMAiHCPTFRY.
OrthoDBiEOG74TX1G.
PhylomeDBiP41126.

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

ChiTaRSiRpL13. fly.
GenomeRNAii34329.
NextBioi787975.
PROiP41126.

Gene expression databases

BgeeiP41126.
ExpressionAtlasiP41126. differential.
GenevisibleiP41126. DM.

Family and domain databases

InterProiIPR001380. Ribosomal_L13e.
IPR018256. Ribosomal_L13e_CS.
[Graphical view]
PANTHERiPTHR11722. PTHR11722. 1 hit.
PfamiPF01294. Ribosomal_L13e. 1 hit.
[Graphical view]
PROSITEiPS01104. RIBOSOMAL_L13E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Drosophila melanogaster homologue of the human BBC1 gene is highly expressed during embryogenesis."
    Helps N.R., Adams S.M., Brammar W.J., Varley J.M.
    Gene 162:245-248(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Brighton.
    Tissue: Embryo.
  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. Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.
    Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
    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 nameiRL13_DROME
AccessioniPrimary (citable) accession number: P41126
Secondary accession number(s): A4V0I6, B7FNN5, Q9VL55
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 11, 2016
This is version 117 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.