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Protein

60S acidic ribosomal protein P1

Gene

RpLP1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Plays an important role in the elongation step of protein synthesis.

GO - Molecular functioni

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-72689. Formation of a pool of free 40S subunits.
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:
60S acidic ribosomal protein P1
Alternative name(s):
Acidic ribosomal protein RPA2
RP21C
Gene namesi
Name:RpLP1
Synonyms:M(2)21C, rp21C, RPA2, RpP2
ORF Names:CG4087
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0002593. RpLP1.

Subcellular locationi

GO - Cellular componenti

  • cytosolic large ribosomal subunit Source: GO_Central
  • preribosome, large subunit precursor Source: GO_Central
  • ribosome Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11211260S acidic ribosomal protein P1PRO_0000157692Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei99 – 991Phosphoserine1 Publication
Modified residuei102 – 1021Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP08570.
PRIDEiP08570.

PTM databases

iPTMnetiP08570.

Expressioni

Gene expression databases

BgeeiP08570.
ExpressionAtlasiP08570. differential.
GenevisibleiP08570. DM.

Interactioni

Subunit structurei

P1 and P2 exist as dimers at the large ribosomal subunit.

Protein-protein interaction databases

BioGridi59470. 45 interactions.
DIPiDIP-18310N.
IntActiP08570. 11 interactions.
MINTiMINT-332892.
STRINGi7227.FBpp0304265.

Structurei

3D structure databases

ProteinModelPortaliP08570.
SMRiP08570. Positions 1-112.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L12P family.Curated

Phylogenomic databases

eggNOGiKOG1762. Eukaryota.
COG2058. LUCA.
GeneTreeiENSGT00550000074698.
InParanoidiP08570.
KOiK02942.
OMAiANQELAC.
OrthoDBiEOG7M0NVC.
PhylomeDBiP08570.

Family and domain databases

HAMAPiMF_01478. Ribosomal_L12_arch.
InterProiIPR027534. Ribosomal_L12.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P08570-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTKAELACV YASLILVDDD VAVTGEKINT ILKAANVEVE PYWPGLFAKA
60 70 80 90 100
LEGINVKDLI TNIGSGVGAA PAGGAAPAAA AAAPAAESKK EEKKKEEESD
110
QSDDDMGFGL FD
Length:112
Mass (Da):11,513
Last modified:February 1, 1996 - v2
Checksum:i2EA9CA3E884A7CCF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91C → S in CAA68557 (PubMed:3122177).Curated
Sequence conflicti53 – 531G → A in CAA68557 (PubMed:3122177).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00504 mRNA. Translation: CAA68557.1.
S62170 mRNA. Translation: AAB26902.1.
AE014134 Genomic DNA. Translation: AAF51499.1.
AY069125 mRNA. Translation: AAL39270.1.
PIRiS00659. R5FF2E.
RefSeqiNP_001259822.1. NM_001272893.1.
NP_476630.1. NM_057282.4.
UniGeneiDm.2270.

Genome annotation databases

EnsemblMetazoaiFBtr0078056; FBpp0077716; FBgn0002593.
FBtr0331932; FBpp0304265; FBgn0002593.
GeneIDi33214.
KEGGidme:Dmel_CG4087.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00504 mRNA. Translation: CAA68557.1.
S62170 mRNA. Translation: AAB26902.1.
AE014134 Genomic DNA. Translation: AAF51499.1.
AY069125 mRNA. Translation: AAL39270.1.
PIRiS00659. R5FF2E.
RefSeqiNP_001259822.1. NM_001272893.1.
NP_476630.1. NM_057282.4.
UniGeneiDm.2270.

3D structure databases

ProteinModelPortaliP08570.
SMRiP08570. Positions 1-112.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi59470. 45 interactions.
DIPiDIP-18310N.
IntActiP08570. 11 interactions.
MINTiMINT-332892.
STRINGi7227.FBpp0304265.

PTM databases

iPTMnetiP08570.

Proteomic databases

PaxDbiP08570.
PRIDEiP08570.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0078056; FBpp0077716; FBgn0002593.
FBtr0331932; FBpp0304265; FBgn0002593.
GeneIDi33214.
KEGGidme:Dmel_CG4087.

Organism-specific databases

CTDi6176.
FlyBaseiFBgn0002593. RpLP1.

Phylogenomic databases

eggNOGiKOG1762. Eukaryota.
COG2058. LUCA.
GeneTreeiENSGT00550000074698.
InParanoidiP08570.
KOiK02942.
OMAiANQELAC.
OrthoDBiEOG7M0NVC.
PhylomeDBiP08570.

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-72689. Formation of a pool of free 40S subunits.
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

ChiTaRSiRpLP1. fly.
GenomeRNAii33214.
PROiP08570.

Gene expression databases

BgeeiP08570.
ExpressionAtlasiP08570. differential.
GenevisibleiP08570. DM.

Family and domain databases

HAMAPiMF_01478. Ribosomal_L12_arch.
InterProiIPR027534. Ribosomal_L12.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA and deduced amino acid sequence of Drosophila rp21C, another 'A'-type ribosomal protein."
    Wigboldus J.D.
    Nucleic Acids Res. 15:10064-10064(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Drosophila acidic ribosomal protein rpA2: sequence and characterization."
    Olson P.F., Salo T., Garrison K., Fessler J.H.
    J. Cell. Biochem. 51:353-359(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.
  6. "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 SER-99 AND SER-102, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiRLA1_DROME
AccessioniPrimary (citable) accession number: P08570
Secondary accession number(s): Q9VPP6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: February 1, 1996
Last modified: July 6, 2016
This is version 140 of the entry and version 2 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.