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Protein

40S ribosomal protein S14

Gene

RpS14a

more
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  • structural constituent of ribosome Source: FlyBase

GO - Biological processi

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-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 S14
Gene namesi
Name:RpS14a
ORF Names:CG1524
AND
Name:RpS14b
ORF Names:CG1527
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0004403. RpS14a.
FBgn0004404. RpS14b.

Subcellular locationi

GO - Cellular componenti

  • ribosome Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15115140S ribosomal protein S14PRO_0000123342Add
BLAST

Proteomic databases

PaxDbiP14130.
PRIDEiP14130.

Expressioni

Gene expression databases

BgeeiP14130.
GenevisibleiP14130. DM.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
maskQ9VCA82EBI-114906,EBI-89853

Protein-protein interaction databases

BioGridi70690. 20 interactions.
70691. 10 interactions.
DIPiDIP-18685N.
IntActiP14130. 14 interactions.
MINTiMINT-905007.
STRINGi7227.FBpp0071052.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00AO1-151[»]
ProteinModelPortaliP14130.
SMRiP14130. Positions 17-140.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S11P family.Curated

Phylogenomic databases

eggNOGiKOG0407. Eukaryota.
COG0100. LUCA.
InParanoidiP14130.
KOiK02955.
OMAiKWGVAHI.
OrthoDBiEOG77DJ81.
PhylomeDBiP14130.

Family and domain databases

Gene3Di3.30.420.80. 1 hit.
HAMAPiMF_01310. Ribosomal_S11.
InterProiIPR001971. Ribosomal_S11.
IPR018102. Ribosomal_S11_CS.
[Graphical view]
PANTHERiPTHR11759. PTHR11759. 1 hit.
PfamiPF00411. Ribosomal_S11. 1 hit.
[Graphical view]
PIRSFiPIRSF002131. Ribosomal_S11. 1 hit.
PROSITEiPS00054. RIBOSOMAL_S11. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P14130-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPRKAKVQK EEVQVQLGPQ VRDGEIVFGV AHIYASFNDT FVHVTDLSGR
60 70 80 90 100
ETIARVTGGM KVKADRDEAS PYAAMLAAQD VAEKCKTLGI TALHIKLRAT
110 120 130 140 150
GGNKTKTPGP GAQSALRALA RSSMKIGRIE DVTPIPSDST RRKGGRRGRR

L
Length:151
Mass (Da):16,265
Last modified:January 1, 1990 - v1
Checksum:i7FD3C0E7A32C4216
GO

Sequence cautioni

The sequence AAL48136.1 differs from that shown. Reason: Frameshift at position 76. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21045 Genomic DNA. Translation: AAA28853.1.
M21045 Genomic DNA. Translation: AAA28852.1.
AE014298 Genomic DNA. Translation: AAF46298.1.
AE014298 Genomic DNA. Translation: AAF46299.1.
AY070665 mRNA. Translation: AAL48136.1. Frameshift.
AY071321 mRNA. Translation: AAL48943.1.
PIRiA30815.
RefSeqiNP_001284995.1. NM_001298066.1.
NP_524884.1. NM_080145.5.
NP_536352.1. NM_080427.4.
NP_727218.1. NM_167137.2.
UniGeneiDm.38448.

Genome annotation databases

EnsemblMetazoaiFBtr0071094; FBpp0071050; FBgn0004403.
FBtr0071095; FBpp0071051; FBgn0004403.
FBtr0071096; FBpp0071052; FBgn0004404.
FBtr0345291; FBpp0311458; FBgn0004404.
GeneIDi47218.
47219.
KEGGidme:Dmel_CG1524.
dme:Dmel_CG1527.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21045 Genomic DNA. Translation: AAA28853.1.
M21045 Genomic DNA. Translation: AAA28852.1.
AE014298 Genomic DNA. Translation: AAF46298.1.
AE014298 Genomic DNA. Translation: AAF46299.1.
AY070665 mRNA. Translation: AAL48136.1. Frameshift.
AY071321 mRNA. Translation: AAL48943.1.
PIRiA30815.
RefSeqiNP_001284995.1. NM_001298066.1.
NP_524884.1. NM_080145.5.
NP_536352.1. NM_080427.4.
NP_727218.1. NM_167137.2.
UniGeneiDm.38448.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00AO1-151[»]
ProteinModelPortaliP14130.
SMRiP14130. Positions 17-140.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi70690. 20 interactions.
70691. 10 interactions.
DIPiDIP-18685N.
IntActiP14130. 14 interactions.
MINTiMINT-905007.
STRINGi7227.FBpp0071052.

Proteomic databases

PaxDbiP14130.
PRIDEiP14130.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0071094; FBpp0071050; FBgn0004403.
FBtr0071095; FBpp0071051; FBgn0004403.
FBtr0071096; FBpp0071052; FBgn0004404.
FBtr0345291; FBpp0311458; FBgn0004404.
GeneIDi47218.
47219.
KEGGidme:Dmel_CG1524.
dme:Dmel_CG1527.

Organism-specific databases

CTDi47218.
47219.
FlyBaseiFBgn0004403. RpS14a.
FBgn0004404. RpS14b.

Phylogenomic databases

eggNOGiKOG0407. Eukaryota.
COG0100. LUCA.
InParanoidiP14130.
KOiK02955.
OMAiKWGVAHI.
OrthoDBiEOG77DJ81.
PhylomeDBiP14130.

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-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

ChiTaRSiRpS14a. fly.
NextBioi838951.
PROiP14130.

Gene expression databases

BgeeiP14130.
GenevisibleiP14130. DM.

Family and domain databases

Gene3Di3.30.420.80. 1 hit.
HAMAPiMF_01310. Ribosomal_S11.
InterProiIPR001971. Ribosomal_S11.
IPR018102. Ribosomal_S11_CS.
[Graphical view]
PANTHERiPTHR11759. PTHR11759. 1 hit.
PfamiPF00411. Ribosomal_S11. 1 hit.
[Graphical view]
PIRSFiPIRSF002131. Ribosomal_S11. 1 hit.
PROSITEiPS00054. RIBOSOMAL_S11. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Ribosomal protein S14 is encoded by a pair of highly conserved, adjacent genes on the X chromosome of Drosophila melanogaster."
    Brown S.J., Rhoads D.D., Stewart M.J., van Slyke B., Chen I.-T., Johnson T.K., Denell R.E., Roufa D.J.
    Mol. Cell. Biol. 8:4314-4321(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (RPS14A AND RPS14B).
  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] (RPS14A AND RPS14B).
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (RPS14A AND RPS14B).
    Strain: Berkeley.
    Tissue: Embryo and Head.
  5. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (6.0 ANGSTROMS) OF THE 80S RIBOSOME.

Entry informationi

Entry nameiRS14_DROME
AccessioniPrimary (citable) accession number: P14130
Secondary accession number(s): Q0KHV1, Q8SZL7, Q9V3R5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: May 11, 2016
This is version 119 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.