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Protein

40S ribosomal protein S21

Gene

RpS21

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May be an associated component of the ribosome rather than a core structural subunit. May act as a translation initiation factor. Has a role in regulation of cell proliferation in the hematopoietic organs and the imaginal disks of larva.1 Publication

GO - Molecular functioni

  • ribosome binding Source: UniProtKB
  • structural constituent of ribosome Source: FlyBase

GO - Biological processi

  • lymph gland development Source: FlyBase
  • regulation of cell proliferation Source: UniProtKB
  • regulation of translation Source: UniProtKB-KW
  • rRNA processing Source: UniProtKB-KW
  • translation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Ribonucleoprotein, Ribosomal protein

Keywords - Biological processi

rRNA processing, Translation regulation

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-6791226. Major pathway of rRNA processing in the nucleolus.
R-DME-72649. Translation initiation complex formation.
R-DME-72689. Formation of a pool of free 40S subunits.
R-DME-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-DME-72702. Ribosomal scanning and start codon recognition.
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:
40S ribosomal protein S211 PublicationImported
Alternative name(s):
Overgrown hematopoietic organs at 23BImported
Gene namesi
Name:RpS21
Synonyms:oho23B
ORF Names:CG2986
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0015521. RpS21.

Subcellular locationi

  • Cytoplasm 1 Publication

  • Note: Associates with the 40S subunit of ribosomes, sta.1 Publication

GO - Cellular componenti

  • cytoplasm Source: FlyBase
  • ribosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 838340S ribosomal protein S21PRO_0000395418Add
BLAST

Proteomic databases

PaxDbiO76927.
PRIDEiO76927.

Expressioni

Developmental stagei

Uniformly expressed at all developmental stages.1 Publication

Gene expression databases

BgeeiO76927.
ExpressionAtlasiO76927. differential.
GenevisibleiO76927. DM.

Interactioni

Subunit structurei

Interacts with sta.1 Publication

Protein-protein interaction databases

BioGridi59710. 49 interactions.
IntActiO76927. 1 interaction.
MINTiMINT-1624415.
STRINGi7227.FBpp0077309.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00AV1-83[»]
ProteinModelPortaliO76927.
SMRiO76927. Positions 1-82.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S21e family.Sequence analysis

Phylogenomic databases

eggNOGiKOG3486. Eukaryota.
ENOG4112266. LUCA.
GeneTreeiENSGT00390000017515.
HOGENOMiHOG000236508.
InParanoidiO76927.
KOiK02971.
OMAiTRYAICG.
OrthoDBiEOG7HQNBQ.
PhylomeDBiO76927.

Family and domain databases

InterProiIPR001931. Ribosomal_S21e.
IPR018279. Ribosomal_S21e_CS.
[Graphical view]
PANTHERiPTHR10442. PTHR10442. 1 hit.
PfamiPF01249. Ribosomal_S21e. 1 hit.
[Graphical view]
PIRSFiPIRSF002148. Ribosomal_S21e. 1 hit.
ProDomiPD006584. Ribosomal_S21e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEiPS00996. RIBOSOMAL_S21E. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A1 Publication (identifier: O76927-1) [UniParc]FASTAAdd to basket

Also known as: B1 Publication

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MENDAGENVD LYVPRKCSAS NRIIHAKDHA SVQLSIVDVD PETGRQTDGS
60 70 80
KTYAICGEIR RMGESDDCIV RLAKKDGIIT KNF
Length:83
Mass (Da):9,167
Last modified:November 1, 1998 - v1
Checksum:iDDFB9D498B3E1E05
GO
Isoform E1 Publication (identifier: O76927-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     82-83: Missing.

Note: No experimental confirmation available.Curated
Show »
Length:81
Mass (Da):8,906
Checksum:i2D498B3E1E05C02F
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei82 – 832Missing in isoform E. 1 PublicationVSP_039463

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ009557 Genomic DNA. Translation: CAA08751.1.
AE014134 Genomic DNA. Translation: AAF51191.1.
AE014134 Genomic DNA. Translation: AAN10392.1.
AE014134 Genomic DNA. Translation: AAN10393.2.
BT015189 mRNA. Translation: AAT94418.1.
RefSeqiNP_001259970.1. NM_001273041.1. [O76927-1]
NP_523462.2. NM_078738.5. [O76927-2]
NP_722853.1. NM_164506.4. [O76927-1]
NP_722854.1. NM_164507.4. [O76927-1]
NP_722855.1. NM_164508.3. [O76927-1]
UniGeneiDm.2727.

Genome annotation databases

EnsemblMetazoaiFBtr0077621; FBpp0077307; FBgn0015521. [O76927-1]
FBtr0077622; FBpp0077308; FBgn0015521. [O76927-1]
FBtr0077623; FBpp0077309; FBgn0015521. [O76927-1]
FBtr0335131; FBpp0307130; FBgn0015521. [O76927-1]
GeneIDi33487.
KEGGidme:Dmel_CG2986.
UCSCiCG2986-RA. d. melanogaster. [O76927-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ009557 Genomic DNA. Translation: CAA08751.1.
AE014134 Genomic DNA. Translation: AAF51191.1.
AE014134 Genomic DNA. Translation: AAN10392.1.
AE014134 Genomic DNA. Translation: AAN10393.2.
BT015189 mRNA. Translation: AAT94418.1.
RefSeqiNP_001259970.1. NM_001273041.1. [O76927-1]
NP_523462.2. NM_078738.5. [O76927-2]
NP_722853.1. NM_164506.4. [O76927-1]
NP_722854.1. NM_164507.4. [O76927-1]
NP_722855.1. NM_164508.3. [O76927-1]
UniGeneiDm.2727.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00AV1-83[»]
ProteinModelPortaliO76927.
SMRiO76927. Positions 1-82.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi59710. 49 interactions.
IntActiO76927. 1 interaction.
MINTiMINT-1624415.
STRINGi7227.FBpp0077309.

Proteomic databases

PaxDbiO76927.
PRIDEiO76927.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0077621; FBpp0077307; FBgn0015521. [O76927-1]
FBtr0077622; FBpp0077308; FBgn0015521. [O76927-1]
FBtr0077623; FBpp0077309; FBgn0015521. [O76927-1]
FBtr0335131; FBpp0307130; FBgn0015521. [O76927-1]
GeneIDi33487.
KEGGidme:Dmel_CG2986.
UCSCiCG2986-RA. d. melanogaster. [O76927-1]

Organism-specific databases

CTDi6227.
FlyBaseiFBgn0015521. RpS21.

Phylogenomic databases

eggNOGiKOG3486. Eukaryota.
ENOG4112266. LUCA.
GeneTreeiENSGT00390000017515.
HOGENOMiHOG000236508.
InParanoidiO76927.
KOiK02971.
OMAiTRYAICG.
OrthoDBiEOG7HQNBQ.
PhylomeDBiO76927.

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-6791226. Major pathway of rRNA processing in the nucleolus.
R-DME-72649. Translation initiation complex formation.
R-DME-72689. Formation of a pool of free 40S subunits.
R-DME-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-DME-72702. Ribosomal scanning and start codon recognition.
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

ChiTaRSiRpS21. fly.
GenomeRNAii33487.
PROiO76927.

Gene expression databases

BgeeiO76927.
ExpressionAtlasiO76927. differential.
GenevisibleiO76927. DM.

Family and domain databases

InterProiIPR001931. Ribosomal_S21e.
IPR018279. Ribosomal_S21e_CS.
[Graphical view]
PANTHERiPTHR10442. PTHR10442. 1 hit.
PfamiPF01249. Ribosomal_S21e. 1 hit.
[Graphical view]
PIRSFiPIRSF002148. Ribosomal_S21e. 1 hit.
ProDomiPD006584. Ribosomal_S21e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEiPS00996. RIBOSOMAL_S21E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Down-regulation of RpS21, a putative translation initiation factor interacting with P40, produces viable minute imagos and larval lethality with overgrown hematopoietic organs and imaginal discs."
    Toeroek I., Herrmann-Horle D., Kiss I., Tick G., Speer G., Schmitt R., Mechler B.M.
    Mol. Cell. Biol. 19:2308-2321(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH STA, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
  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, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  4. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
    Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
    Strain: BerkeleyImported.
    Tissue: Head.
  5. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (6.0 ANGSTROMS) OF THE 80S RIBOSOME.

Entry informationi

Entry nameiRS21_DROME
AccessioniPrimary (citable) accession number: O76927
Secondary accession number(s): A4V027
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: November 1, 1998
Last modified: June 8, 2016
This is version 130 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.