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Protein

60S ribosomal protein L11-2

Gene

rpl-11.2

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Binds to 5S ribosomal RNA (By similarity).By similarity

Miscellaneous

There's a functional difference between the two L11-encoding proteins in C.elegans. rpl-11.1 plays a role in the germline whereas rpl-11.2 has a somatic function.1 Publication

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding

Enzyme and pathway databases

ReactomeiR-CEL-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-CEL-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-CEL-72689. Formation of a pool of free 40S subunits.
R-CEL-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-CEL-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-CEL-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L11-2Curated
Gene namesi
Name:rpl-11.2Imported
ORF Names:F07D10.1Imported
OrganismiCaenorhabditis elegansImported
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome X

Organism-specific databases

WormBaseiF07D10.1; CE07033; WBGene00004423; rpl-11.2.

Subcellular locationi

GO - Cellular componenti

Pathology & Biotechi

Disruption phenotypei

RNAi-mediated knockdown results in a growth defect.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004369031 – 19660S ribosomal protein L11-2CuratedAdd BLAST196

Proteomic databases

EPDiQ19162.
PaxDbiQ19162.
PeptideAtlasiQ19162.

Expressioni

Gene expression databases

BgeeiWBGene00004423.

Interactioni

Subunit structurei

Component of the large ribosomal subunit.By similarity

Protein-protein interaction databases

DIPiDIP-26065N.
MINTiMINT-1118628.
STRINGi6239.F07D10.1.2.

Structurei

3D structure databases

ProteinModelPortaliQ19162.
SMRiQ19162.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the universal ribosomal protein uL5 family.UniRule annotation

Phylogenomic databases

eggNOGiKOG0397. Eukaryota.
COG0094. LUCA.
GeneTreeiENSGT00390000013411.
HOGENOMiHOG000231312.
InParanoidiQ19162.
KOiK02868.
OMAiEDTMAWF.
OrthoDBiEOG091G0LSV.
PhylomeDBiQ19162.

Family and domain databases

Gene3Di3.30.1440.10. 1 hit.
InterProiView protein in InterPro
IPR002132. Ribosomal_L5.
IPR031309. Ribosomal_L5_C.
IPR020929. Ribosomal_L5_CS.
IPR022803. Ribosomal_L5_domain.
IPR031310. Ribosomal_L5_N.
PfamiView protein in Pfam
PF00281. Ribosomal_L5. 1 hit.
PF00673. Ribosomal_L5_C. 1 hit.
PIRSFiPIRSF002161. Ribosomal_L5. 1 hit.
SUPFAMiSSF55282. SSF55282. 1 hit.
PROSITEiView protein in PROSITE
PS00358. RIBOSOMAL_L5. 1 hit.

Sequencei

Sequence statusi: Complete.

Q19162-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGDIEKQTEI REKKARNVMR ELKIQKLCLN ICVGESGDRL TRAAKVLEQL
60 70 80 90 100
TGQTPVFSKA RYTVRTFGIR RNEKIAVHCT VRGPKAEEIL EKGLKVKEYE
110 120 130 140 150
LYKENFSDTG NFGFGVQEHI DLGIKYDPSI GIYGMDFYVV LDRAGRRIAK
160 170 180 190
RRRAPGRVGP SHRVEREESI KWFQQKYDGI ILPPKPKVKR TFHRRR
Length:196
Mass (Da):22,776
Last modified:November 1, 1996 - v1
Checksum:iA5B397B6254FBD92
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX284606 Genomic DNA. Translation: CCD61193.1.
PIRiT29860.
RefSeqiNP_508413.1. NM_076012.5.
UniGeneiCel.38559.

Genome annotation databases

EnsemblMetazoaiF07D10.1; F07D10.1; WBGene00004423.
GeneIDi180535.
KEGGicel:CELE_F07D10.1.
UCSCiF07D10.1.1. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX284606 Genomic DNA. Translation: CCD61193.1.
PIRiT29860.
RefSeqiNP_508413.1. NM_076012.5.
UniGeneiCel.38559.

3D structure databases

ProteinModelPortaliQ19162.
SMRiQ19162.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-26065N.
MINTiMINT-1118628.
STRINGi6239.F07D10.1.2.

Proteomic databases

EPDiQ19162.
PaxDbiQ19162.
PeptideAtlasiQ19162.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiF07D10.1; F07D10.1; WBGene00004423.
GeneIDi180535.
KEGGicel:CELE_F07D10.1.
UCSCiF07D10.1.1. c. elegans.

Organism-specific databases

CTDi180535.
WormBaseiF07D10.1; CE07033; WBGene00004423; rpl-11.2.

Phylogenomic databases

eggNOGiKOG0397. Eukaryota.
COG0094. LUCA.
GeneTreeiENSGT00390000013411.
HOGENOMiHOG000231312.
InParanoidiQ19162.
KOiK02868.
OMAiEDTMAWF.
OrthoDBiEOG091G0LSV.
PhylomeDBiQ19162.

Enzyme and pathway databases

ReactomeiR-CEL-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-CEL-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-CEL-72689. Formation of a pool of free 40S subunits.
R-CEL-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-CEL-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-CEL-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

PROiPR:Q19162.

Gene expression databases

BgeeiWBGene00004423.

Family and domain databases

Gene3Di3.30.1440.10. 1 hit.
InterProiView protein in InterPro
IPR002132. Ribosomal_L5.
IPR031309. Ribosomal_L5_C.
IPR020929. Ribosomal_L5_CS.
IPR022803. Ribosomal_L5_domain.
IPR031310. Ribosomal_L5_N.
PfamiView protein in Pfam
PF00281. Ribosomal_L5. 1 hit.
PF00673. Ribosomal_L5_C. 1 hit.
PIRSFiPIRSF002161. Ribosomal_L5. 1 hit.
SUPFAMiSSF55282. SSF55282. 1 hit.
PROSITEiView protein in PROSITE
PS00358. RIBOSOMAL_L5. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRL112_CAEEL
AccessioniPrimary (citable) accession number: Q19162
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 6, 2016
Last sequence update: November 1, 1996
Last modified: June 7, 2017
This is version 120 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. Ribosomal proteins
    Ribosomal proteins families and list of entries
  3. 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.