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Protein

40S ribosomal protein S15Ab

Gene

RpS15Ab

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

Functioni

GO - Molecular functioni

GO - Biological processi

  • mitotic spindle elongation Source: FlyBase
  • mitotic spindle organization Source: FlyBase
  • translation Source: InterPro
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-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 S15Ab
Gene namesi
Name:RpS15Ab
Synonyms:RpS15A
ORF Names:CG12324
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0033555. RpS15Ab.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 13012940S ribosomal protein S15AbPRO_0000126611Add
BLAST

Proteomic databases

PaxDbiQ7KR04.
PRIDEiQ7KR04.

Expressioni

Gene expression databases

GenevisibleiQ7KR04. DM.

Interactioni

Protein-protein interaction databases

BioGridi61949. 20 interactions.
IntActiQ7KR04. 2 interactions.
STRINGi7227.FBpp0087321.

Structurei

3D structure databases

ProteinModelPortaliQ7KR04.
SMRiQ7KR04. Positions 2-130.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S8P family.Curated

Phylogenomic databases

eggNOGiKOG1754. Eukaryota.
COG0096. LUCA.
GeneTreeiENSGT00390000003021.
InParanoidiQ7KR04.
KOiK02957.
OMAiQKHGYIN.
OrthoDBiEOG77Q4ZM.
PhylomeDBiQ7KR04.

Family and domain databases

InterProiIPR000630. Ribosomal_S8.
[Graphical view]
PANTHERiPTHR11758. PTHR11758. 1 hit.
PfamiPF00410. Ribosomal_S8. 1 hit.
[Graphical view]
SUPFAMiSSF56047. SSF56047. 1 hit.
PROSITEiPS00053. RIBOSOMAL_S8. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q7KR04-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVRMNVLADA LKCINNAEKR GKRQVLLRPC SKVIIKFLTV MMKHGYIGEF
60 70 80 90 100
EIVEDHRAGK IVVNLTGRLN KCGVISPRFD APINDIEKWT NNLLPSRQFG
110 120 130
YVVLTTSGGI MDHEEARRKH LGGKILGFFF
Length:130
Mass (Da):14,741
Last modified:January 23, 2007 - v3
Checksum:i3D47B82F5F93A808
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti6 – 61V → I in strain: LA79.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAM68752.1.
AY061830 mRNA. Translation: AAL27641.1.
AY150713 Genomic DNA. Translation: AAN78363.1.
AY150714 Genomic DNA. Translation: AAN78364.1.
AY150715 Genomic DNA. Translation: AAN78365.1.
AY150716 Genomic DNA. Translation: AAN78366.1.
AY150717 Genomic DNA. Translation: AAN78367.1.
AY150718 Genomic DNA. Translation: AAN78368.1.
AY150719 Genomic DNA. Translation: AAN78369.1.
AY150720 Genomic DNA. Translation: AAN78370.1.
AY150721 Genomic DNA. Translation: AAN78371.1.
AY150722 Genomic DNA. Translation: AAN78372.1.
AY150723 Genomic DNA. Translation: AAN78373.1.
AY150724 Genomic DNA. Translation: AAN78374.1.
AY150725 Genomic DNA. Translation: AAN78375.1.
AY150726 Genomic DNA. Translation: AAN78376.1.
AY150727 Genomic DNA. Translation: AAN78377.1.
AY150728 Genomic DNA. Translation: AAN78378.1.
RefSeqiNP_610616.1. NM_136772.3.
UniGeneiDm.19904.

Genome annotation databases

EnsemblMetazoaiFBtr0088226; FBpp0087321; FBgn0033555.
GeneIDi36142.
KEGGidme:Dmel_CG12324.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAM68752.1.
AY061830 mRNA. Translation: AAL27641.1.
AY150713 Genomic DNA. Translation: AAN78363.1.
AY150714 Genomic DNA. Translation: AAN78364.1.
AY150715 Genomic DNA. Translation: AAN78365.1.
AY150716 Genomic DNA. Translation: AAN78366.1.
AY150717 Genomic DNA. Translation: AAN78367.1.
AY150718 Genomic DNA. Translation: AAN78368.1.
AY150719 Genomic DNA. Translation: AAN78369.1.
AY150720 Genomic DNA. Translation: AAN78370.1.
AY150721 Genomic DNA. Translation: AAN78371.1.
AY150722 Genomic DNA. Translation: AAN78372.1.
AY150723 Genomic DNA. Translation: AAN78373.1.
AY150724 Genomic DNA. Translation: AAN78374.1.
AY150725 Genomic DNA. Translation: AAN78375.1.
AY150726 Genomic DNA. Translation: AAN78376.1.
AY150727 Genomic DNA. Translation: AAN78377.1.
AY150728 Genomic DNA. Translation: AAN78378.1.
RefSeqiNP_610616.1. NM_136772.3.
UniGeneiDm.19904.

3D structure databases

ProteinModelPortaliQ7KR04.
SMRiQ7KR04. Positions 2-130.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi61949. 20 interactions.
IntActiQ7KR04. 2 interactions.
STRINGi7227.FBpp0087321.

Proteomic databases

PaxDbiQ7KR04.
PRIDEiQ7KR04.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0088226; FBpp0087321; FBgn0033555.
GeneIDi36142.
KEGGidme:Dmel_CG12324.

Organism-specific databases

CTDi36142.
FlyBaseiFBgn0033555. RpS15Ab.

Phylogenomic databases

eggNOGiKOG1754. Eukaryota.
COG0096. LUCA.
GeneTreeiENSGT00390000003021.
InParanoidiQ7KR04.
KOiK02957.
OMAiQKHGYIN.
OrthoDBiEOG77Q4ZM.
PhylomeDBiQ7KR04.

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

GenomeRNAii36142.
PROiQ7KR04.

Gene expression databases

GenevisibleiQ7KR04. DM.

Family and domain databases

InterProiIPR000630. Ribosomal_S8.
[Graphical view]
PANTHERiPTHR11758. PTHR11758. 1 hit.
PfamiPF00410. Ribosomal_S8. 1 hit.
[Graphical view]
SUPFAMiSSF56047. SSF56047. 1 hit.
PROSITEiPS00053. RIBOSOMAL_S8. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Retroposed new genes out of the X in Drosophila."
    Betran E., Thornton K., Long M.
    Genome Res. 12:1854-1859(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 253.27, Closs19, Closs3, HG84, LA79, north34, north7_13, OK17, yep10, yep25, yep7 and Z.
  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.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.

Entry informationi

Entry nameiRS15B_DROME
AccessioniPrimary (citable) accession number: Q7KR04
Secondary accession number(s): Q8I8H7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2004
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 85 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  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.