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P46769 (RSSA_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
40S ribosomal protein SA
Gene names
Name:rps-0
ORF Names:B0393.1
OrganismCaenorhabditis elegans
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length276 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits By similarity.

Subunit structure

Component of the small 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). Interacts with rps-21 By similarity.

Subcellular location

Cytoplasm.

Developmental stage

Expressed at a stable level throughout development. Ref.3

Sequence similarities

Belongs to the ribosomal protein S2P family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionRibonucleoprotein
Ribosomal protein
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processapoptotic process

Inferred from mutant phenotype. Source: WormBase

embryo development ending in birth or egg hatching

Inferred from mutant phenotype. Source: WormBase

endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)

Inferred from Biological aspect of Ancestor. Source: RefGenome

endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA)

Inferred from Biological aspect of Ancestor. Source: RefGenome

growth

Inferred from mutant phenotype. Source: WormBase

hermaphrodite genitalia development

Inferred from mutant phenotype. Source: WormBase

molting cycle, collagen and cuticulin-based cuticle

Inferred from mutant phenotype. Source: WormBase

nematode larval development

Inferred from mutant phenotype. Source: WormBase

rRNA export from nucleus

Inferred from Biological aspect of Ancestor. Source: RefGenome

ribosomal small subunit assembly

Inferred from Biological aspect of Ancestor. Source: RefGenome

translation

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular component90S preribosome

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytosolic small ribosomal subunit

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular functionprotein binding

Inferred from physical interaction. Source: IntAct

structural constituent of ribosome

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

rps-21P491974EBI-313262,EBI-313268

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 27627540S ribosomal protein SA
PRO_0000134352

Amino acid modifications

Modified residue21N-acetylserine Ref.2

Sequences

Sequence LengthMass (Da)Tools
P46769 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 51CB51C5C1B923DE

FASTA27630,703
        10         20         30         40         50         60 
MSGGAAHSAL TEEDVMKLLA TQAHLGSTNL NFQMQQYVYK RRFDGPNIIN VKKTWEKLLL 

        70         80         90        100        110        120 
AARAIAAVEN PADVVVVSAR PYAQRALLKF AAHTGATAIF GRFSPGCLTN QIQKTFKEPR 

       130        140        150        160        170        180 
LLVISDPRID HQAVTEASYV GVPVISFVNT ESPLKLIDIG VPCNNKGERS IGLMWWMLAR 

       190        200        210        220        230        240 
EILILRGKIS RQTGFVLEGK EIMPDLYFYR DPTETEKEET GAHADVAEAQ EYQQPTDIDF 

       250        260        270 
TTQGGKVDDW AAETATWTAE TKTTEEWANA PTQSNW 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
[2]Bienvenut W.V.
Submitted (AUG-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-17; 42-52; 64-80; 129-155; 170-180 AND 192-200, MASS SPECTROMETRY, ACETYLATION AT SER-2.
[3]"Proteomic analysis of protein expression profiles during Caenorhabditis elegans development using two-dimensional difference gel electrophoresis."
Tabuse Y., Nabetani T., Tsugita A.
Proteomics 5:2876-2891(2005) [PubMed: 15996007] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z37983 Genomic DNA. Translation: CAA86061.1.
PIRT18742.
RefSeqNP_497978.1. NM_065577.4.
UniGeneCel.10142.

3D structure databases

ProteinModelPortalP46769.
SMRP46769. Positions 10-210.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-26217N.
IntActP46769. 4 interactions.
MINTMINT-1037948.
STRINGP46769.

2D gel databases

World-2DPAGE0020:P46769.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaB0393.1.1; B0393.1.1; B0393.1.
B0393.1.2; B0393.1.2; B0393.1.
GeneID175628.
KEGGcel:B0393.1.
UCSCB0393.1.1. c. elegans.

Organism-specific databases

CTD175628.
WormBaseB0393.1; CE00854; WBGene00004469; rps-0.

Phylogenomic databases

eggNOGmeNOG04038.
GeneTreeEMGT00050000005297.
HOGENOMHBG736296.
InParanoidP46769.
OMALAANCHI.
PhylomeDBP46769.

Family and domain databases

InterProIPR001865. Ribosomal_S2.
IPR018130. Ribosomal_S2_CS.
IPR005707. Ribosomal_S2_euk/arc.
IPR023591. Ribosomal_S2_flav_dom.
[Graphical view]
KOK02998.
PANTHERPTHR11489. Ribosomal_S2_e/a. 1 hit.
PfamPF00318. Ribosomal_S2. 2 hits.
[Graphical view]
PRINTSPR00395. RIBOSOMALS2.
SUPFAMSSF52313. Ribosomal_S2. 1 hit.
TIGRFAMsTIGR01012. Sa_S2_E_A. 1 hit.
PROSITEPS00962. RIBOSOMAL_S2_1. 1 hit.
PS00963. RIBOSOMAL_S2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio888964.

Entry information

Entry nameRSSA_CAEEL
AccessionPrimary (citable) accession number: P46769
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 82 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

Ribosomal proteins

Ribosomal proteins families and list of entries

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormPep

SIMILARITY comments

Index of protein domains and families