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Protein

40S ribosomal protein S3

Gene

RpS3

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

Functioni

Has DNA repair activity directed towards the mutagenic lesions 8-oxoguanine and abasic sites in DNA. It can cleave DNA containing 8-oxoguanine residues efficiently. Also acts as an ap lyase, cleaving phosphodiester bonds via a beta,delta elimination reaction.

GO - Molecular functioni

  • damaged DNA binding Source: UniProtKB
  • DNA-(apurinic or apyrimidinic site) lyase activity Source: FlyBase
  • oxidized purine DNA binding Source: UniProtKB
  • oxidized purine nucleobase lesion DNA N-glycosylase activity Source: FlyBase
  • RNA binding Source: UniProtKB-KW
  • structural constituent of ribosome Source: FlyBase

GO - Biological processi

  • cellular response to DNA damage stimulus Source: FlyBase
  • DNA repair Source: FlyBase
  • mitotic nuclear division Source: FlyBase
  • negative regulation of neuron apoptotic process Source: FlyBase
  • translation Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease, Ribonucleoprotein, Ribosomal protein

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

RNA-binding

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 S3
Gene namesi
Name:RpS3
Synonyms:M(3)95A
ORF Names:CG6779
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0002622. RpS3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: FlyBase
  • cytosolic small ribosomal subunit Source: FlyBase
  • microtubule associated complex Source: FlyBase
  • nuclear matrix Source: FlyBase
  • nucleus Source: FlyBase
  • ribosome Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 24624640S ribosomal protein S3PRO_0000130328Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei223 – 2231Phosphothreonine1 Publication
Modified residuei226 – 2261Phosphothreonine1 Publication
Modified residuei241 – 2411Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ06559.
PRIDEiQ06559.

PTM databases

iPTMnetiQ06559.

Expressioni

Gene expression databases

BgeeiQ06559.
ExpressionAtlasiQ06559. differential.
GenevisibleiQ06559. DM.

Interactioni

Protein-protein interaction databases

BioGridi67703. 86 interactions.
DIPiDIP-17168N.
IntActiQ06559. 3 interactions.
MINTiMINT-812597.
STRINGi7227.FBpp0083802.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00AD1-246[»]
ProteinModelPortaliQ06559.
SMRiQ06559. Positions 7-215.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 9472KH type-2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ribosomal protein S3P family.Curated
Contains 1 KH type-2 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3181. Eukaryota.
COG0092. LUCA.
GeneTreeiENSGT00390000008610.
InParanoidiQ06559.
KOiK02985.
OMAiQKFTEGY.
OrthoDBiEOG7F7W9M.
PhylomeDBiQ06559.

Family and domain databases

Gene3Di3.30.1140.32. 1 hit.
3.30.300.20. 1 hit.
InterProiIPR015946. KH_dom-like_a/b.
IPR004044. KH_dom_type_2.
IPR009019. KH_prok-type.
IPR001351. Ribosomal_S3_C.
IPR018280. Ribosomal_S3_CS.
IPR005703. Ribosomal_S3_euk/arc.
[Graphical view]
PfamiPF07650. KH_2. 1 hit.
[Graphical view]
SUPFAMiSSF54814. SSF54814. 1 hit.
SSF54821. SSF54821. 1 hit.
TIGRFAMsiTIGR01008. uS3_euk_arch. 1 hit.
PROSITEiPS50823. KH_TYPE_2. 1 hit.
PS00548. RIBOSOMAL_S3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q06559-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNANLPISKK RKFVSDGIFK AELNEFLTRE LAEDGYSGVE VRVTPSRTEI
60 70 80 90 100
IIMATKTQQV LGEKGRRIRE LTAMVQKRFN FETGRIELYA EKVAARGLCA
110 120 130 140 150
IAQAESLRYK LTGGLAVRRA CYGVLRYIME SGAKGCEVVV SGKLRGQRAK
160 170 180 190 200
SMKFVDGLMI HSGDPCNDYV ETATRHVLLR QGVLGIKVKV MLPYDPKNKI
210 220 230 240
GPKKPLPDNV SVVEPKEEKI YETPETEYKI PPPSKPLDDL SEAKVL
Length:246
Mass (Da):27,471
Last modified:June 1, 1994 - v1
Checksum:i122A6E775339E673
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti46 – 472SR → FG in CAA51425 (PubMed:8070662).Curated
Sequence conflicti62 – 621G → A in CAA51425 (PubMed:8070662).Curated
Sequence conflicti114 – 1141G → E in CAA51425 (PubMed:8070662).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13690 mRNA. Translation: AAA28875.1.
X72921 Genomic DNA. Translation: CAA51425.1.
AE014297 Genomic DNA. Translation: AAF56129.1.
AY118971 mRNA. Translation: AAM50831.1.
PIRiS35620.
RefSeqiNP_001287481.1. NM_001300552.1.
NP_476632.1. NM_057284.6.
UniGeneiDm.20234.

Genome annotation databases

EnsemblMetazoaiFBtr0084410; FBpp0083802; FBgn0002622.
FBtr0346349; FBpp0312066; FBgn0002622.
GeneIDi42761.
KEGGidme:Dmel_CG6779.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13690 mRNA. Translation: AAA28875.1.
X72921 Genomic DNA. Translation: CAA51425.1.
AE014297 Genomic DNA. Translation: AAF56129.1.
AY118971 mRNA. Translation: AAM50831.1.
PIRiS35620.
RefSeqiNP_001287481.1. NM_001300552.1.
NP_476632.1. NM_057284.6.
UniGeneiDm.20234.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00AD1-246[»]
ProteinModelPortaliQ06559.
SMRiQ06559. Positions 7-215.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi67703. 86 interactions.
DIPiDIP-17168N.
IntActiQ06559. 3 interactions.
MINTiMINT-812597.
STRINGi7227.FBpp0083802.

PTM databases

iPTMnetiQ06559.

Proteomic databases

PaxDbiQ06559.
PRIDEiQ06559.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0084410; FBpp0083802; FBgn0002622.
FBtr0346349; FBpp0312066; FBgn0002622.
GeneIDi42761.
KEGGidme:Dmel_CG6779.

Organism-specific databases

CTDi6188.
FlyBaseiFBgn0002622. RpS3.

Phylogenomic databases

eggNOGiKOG3181. Eukaryota.
COG0092. LUCA.
GeneTreeiENSGT00390000008610.
InParanoidiQ06559.
KOiK02985.
OMAiQKFTEGY.
OrthoDBiEOG7F7W9M.
PhylomeDBiQ06559.

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

ChiTaRSiRpS3. fly.
GenomeRNAii42761.
PROiQ06559.

Gene expression databases

BgeeiQ06559.
ExpressionAtlasiQ06559. differential.
GenevisibleiQ06559. DM.

Family and domain databases

Gene3Di3.30.1140.32. 1 hit.
3.30.300.20. 1 hit.
InterProiIPR015946. KH_dom-like_a/b.
IPR004044. KH_dom_type_2.
IPR009019. KH_prok-type.
IPR001351. Ribosomal_S3_C.
IPR018280. Ribosomal_S3_CS.
IPR005703. Ribosomal_S3_euk/arc.
[Graphical view]
PfamiPF07650. KH_2. 1 hit.
[Graphical view]
SUPFAMiSSF54814. SSF54814. 1 hit.
SSF54821. SSF54821. 1 hit.
TIGRFAMsiTIGR01008. uS3_euk_arch. 1 hit.
PROSITEiPS50823. KH_TYPE_2. 1 hit.
PS00548. RIBOSOMAL_S3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of the Drosophila ribosomal protein S3: another multifunctional ribosomal protein with AP endonuclease DNA repair activity."
    Wilson D.M. III, Deutsch W.A., Kelley M.R.
    Nucleic Acids Res. 21:2516-2516(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "A Drosophila third chromosome Minute locus encodes a ribosomal protein."
    Andersson S., Saeboe-Larssen S., Lambertsson A., Meriam J., Jacobs-Lorena M.
    Genetics 137:513-520(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Shahrinau / Wild-type.
  3. "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.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. "A Drosophila full-length cDNA resource."
    Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  6. "A Drosophila ribosomal protein contains 8-oxoguanine and abasic site DNA repair activities."
    Yacoub A., Augeri L., Kelley M.R., Doetsch P.W., Deutsch W.A.
    EMBO J. 15:2306-2312(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA REPAIR ACTIVITY.
  7. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-223; THR-226 AND SER-241, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  8. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (6.0 ANGSTROMS) OF THE 80S RIBOSOME.

Entry informationi

Entry nameiRS3_DROME
AccessioniPrimary (citable) accession number: Q06559
Secondary accession number(s): Q9VCM9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: June 8, 2016
This is version 154 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.