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Protein

60S acidic ribosomal protein P0

Gene

rpa-0

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Ribosomal protein P0 is the functional equivalent of E.coli protein L10.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

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 acidic ribosomal protein P0
Gene namesi
Name:rpa-0
ORF Names:F25H2.10
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome I

Organism-specific databases

WormBaseiF25H2.10; CE09655; WBGene00004408; rla-0.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 31231160S acidic ribosomal protein P0PRO_0000154766Add
BLAST

Post-translational modificationi

Phosphorylated.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ93572.
PaxDbiQ93572.

2D gel databases

World-2DPAGE0011:Q93572.
0020:Q93572.

Interactioni

Subunit structurei

P0 forms a pentameric complex by interaction with dimers of P1 and P2.

Protein-protein interaction databases

BioGridi38357. 7 interactions.
DIPiDIP-26018N.
IntActiQ93572. 4 interactions.
MINTiMINT-1046682.
STRINGi6239.F25H2.10.2.

Structurei

3D structure databases

ProteinModelPortaliQ93572.
SMRiQ93572. Positions 7-211.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L10P family.Curated

Phylogenomic databases

eggNOGiKOG0815. Eukaryota.
COG0244. LUCA.
GeneTreeiENSGT00390000017839.
HOGENOMiHOG000210987.
InParanoidiQ93572.
KOiK02941.
OMAiIGTNDNP.
PhylomeDBiQ93572.

Family and domain databases

InterProiIPR030670. L10E_eukaryotes.
IPR001790. Ribosomal_L10P.
[Graphical view]
PfamiPF00466. Ribosomal_L10. 1 hit.
[Graphical view]
PIRSFiPIRSF039087. L10E. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q93572-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVREDRSTWK ANYFTKLVEL FEEYPKCLLV GVDNVGSKQM QEIRQAMRGH
60 70 80 90 100
AEILMGKNTM IRKALRGHLG KNPSLEKLLP HIVENVGFVF TKEDLGEIRS
110 120 130 140 150
KLLENRKGAP AKAGAIAPCD VKLPPQNTGM GPEKTSFFQA LQIPTKIARG
160 170 180 190 200
TIEILNDVHL IKEGDKVGAS ESALLNMLGV TPFSYGLVVR QVYDDGTLYT
210 220 230 240 250
PEVLDMTTEE LRKRFLSGVR NVASVSLAVN YPTLASVAHS LANGLQNMLG
260 270 280 290 300
VAAVTDVSFK EAETIKAFIA DPSKFAAAAP AAAAAPAAAA PAAKKEEPKE
310
ESDDDMGFGL FD
Length:312
Mass (Da):33,774
Last modified:January 23, 2007 - v3
Checksum:i0D90B15C30BDCB30
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z79754 Genomic DNA. Translation: CAB02098.1.
PIRiT21351.
RefSeqiNP_492766.1. NM_060365.7.
UniGeneiCel.20069.

Genome annotation databases

EnsemblMetazoaiF25H2.10; F25H2.10; WBGene00004408.
GeneIDi172943.
KEGGicel:CELE_F25H2.10.
UCSCiF25H2.10.1. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z79754 Genomic DNA. Translation: CAB02098.1.
PIRiT21351.
RefSeqiNP_492766.1. NM_060365.7.
UniGeneiCel.20069.

3D structure databases

ProteinModelPortaliQ93572.
SMRiQ93572. Positions 7-211.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi38357. 7 interactions.
DIPiDIP-26018N.
IntActiQ93572. 4 interactions.
MINTiMINT-1046682.
STRINGi6239.F25H2.10.2.

2D gel databases

World-2DPAGE0011:Q93572.
0020:Q93572.

Proteomic databases

EPDiQ93572.
PaxDbiQ93572.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiF25H2.10; F25H2.10; WBGene00004408.
GeneIDi172943.
KEGGicel:CELE_F25H2.10.
UCSCiF25H2.10.1. c. elegans.

Organism-specific databases

CTDi172943.
WormBaseiF25H2.10; CE09655; WBGene00004408; rla-0.

Phylogenomic databases

eggNOGiKOG0815. Eukaryota.
COG0244. LUCA.
GeneTreeiENSGT00390000017839.
HOGENOMiHOG000210987.
InParanoidiQ93572.
KOiK02941.
OMAiIGTNDNP.
PhylomeDBiQ93572.

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

PROiQ93572.

Family and domain databases

InterProiIPR030670. L10E_eukaryotes.
IPR001790. Ribosomal_L10P.
[Graphical view]
PfamiPF00466. Ribosomal_L10. 1 hit.
[Graphical view]
PIRSFiPIRSF039087. L10E. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.
  2. "Two-dimensional gel electrophoresis of Caenorhabditis elegans homogenates and identification of protein spots by microsequencing."
    Bini L., Heid H., Liberatori S., Geier G., Pallini V., Zwilling R.
    Electrophoresis 18:557-562(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-16.
    Strain: Bristol N2.

Entry informationi

Entry nameiRLA0_CAEEL
AccessioniPrimary (citable) accession number: Q93572
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 110 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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.