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Protein

60S acidic ribosomal protein P0

Gene

RpLP0

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

Functioni

Ribosomal protein P0 is the functional equivalent of E.coli protein L10.

Catalytic activityi

The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.

GO - Molecular functioni

  1. DNA-(apurinic or apyrimidinic site) lyase activity Source: UniProtKB-EC
  2. structural constituent of ribosome Source: FlyBase

GO - Biological processi

  1. DNA repair Source: UniProtKB-KW
  2. ribosome biogenesis Source: InterPro
  3. translational elongation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Ribonucleoprotein, Ribosomal protein

Keywords - Biological processi

DNA damage, DNA repair

Enzyme and pathway databases

ReactomeiREACT_281936. Peptide chain elongation.
REACT_303602. Formation of a pool of free 40S subunits.
REACT_305162. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_321612. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_341839. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_342983. SRP-dependent cotranslational protein targeting to membrane.
REACT_344041. Eukaryotic Translation Termination.
REACT_351471. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).

Protein family/group databases

MoonProtiP19889.

Names & Taxonomyi

Protein namesi
Recommended name:
60S acidic ribosomal protein P0
Alternative name(s):
Apurinic-apyrimidinic endonuclease
DNA-(apurinic or apyrimidinic site) lyase (EC:4.2.99.18)
Gene namesi
Name:RpLP0
Synonyms:AP3, Ape, RpP0
ORF Names:CG7490
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0000100. RpLP0.

Subcellular locationi

GO - Cellular componenti

  1. nucleus Source: UniProtKB-SubCell
  2. ribosome Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 31731760S acidic ribosomal protein P0PRO_0000154769Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei302 – 3021Phosphoserine1 Publication
Modified residuei304 – 3041Phosphoserine; by CK1Sequence Analysis

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP19889.
PRIDEiP19889.

Expressioni

Developmental stagei

All stages of development. A larger transcript is restricted to the embryonic and early larval stages.

Gene expression databases

BgeeiP19889.

Interactioni

Subunit structurei

P0 forms a pentameric complex by interaction with dimers of P1 and P2.By similarity

Protein-protein interaction databases

BioGridi65690. 23 interactions.
DIPiDIP-21968N.
IntActiP19889. 4 interactions.
MINTiMINT-235412.

Structurei

3D structure databases

ProteinModelPortaliP19889.
SMRiP19889. Positions 5-273.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L10P family.Curated

Phylogenomic databases

eggNOGiCOG0244.
GeneTreeiENSGT00390000017839.
InParanoidiP19889.
KOiK02941.
OMAiNYVERGA.
OrthoDBiEOG71K63M.
PhylomeDBiP19889.

Family and domain databases

InterProiIPR030670. L10E_eukaryotes.
IPR001790. Ribosomal_L10P.
[Graphical view]
PfamiPF00466. Ribosomal_L10. 1 hit.
[Graphical view]
PIRSFiPIRSF039087. L10E. 1 hit.

Sequencei

Sequence statusi: Complete.

P19889-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVRENKAAWK AQYFIKVVEL FDEFPKCFIV GADNVGSKQM QNIRTSLRGL
60 70 80 90 100
AVVLMGKNTM MRKAIRGHLE NNPQLEKLLP HIKGNVGFVF TKGDLAEVRD
110 120 130 140 150
KLLESKVRAP ARPGAIAPLH VIIPAQNTGL GPEKTSFFQA LSIPTKISKG
160 170 180 190 200
TIEIINDVPI LKPGDKVGAS EATLLNMLNI SPFSYGLIVN QVYDSGSIFS
210 220 230 240 250
PEILDIKPED LRAKFQQGVA NLAAVCLSVG YPTIASAPHS IANGFKNLLA
260 270 280 290 300
IAATTEVEFK EATTIKEYIK DPSKFAAAAS ASAAPAAGGA TEKKEEAKKP
310
ESESEEEDDD MGFGLFD
Length:317
Mass (Da):34,202
Last modified:February 1, 1991 - v1
Checksum:i36E9DD5DD8CF7E1F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25772 mRNA. Translation: AAA53372.1.
AE014296 Genomic DNA. Translation: AAF51807.1.
AY075528 mRNA. Translation: AAL68335.1.
BT021447 mRNA. Translation: AAX33595.1.
PIRiA30223. R5FFP0.
RefSeqiNP_001262202.1. NM_001275273.1.
NP_524211.1. NM_079487.4.
UniGeneiDm.7933.

Genome annotation databases

EnsemblMetazoaiFBtr0078481; FBpp0078134; FBgn0000100.
FBtr0334113; FBpp0306232; FBgn0000100.
GeneIDi40451.
KEGGidme:Dmel_CG7490.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25772 mRNA. Translation: AAA53372.1.
AE014296 Genomic DNA. Translation: AAF51807.1.
AY075528 mRNA. Translation: AAL68335.1.
BT021447 mRNA. Translation: AAX33595.1.
PIRiA30223. R5FFP0.
RefSeqiNP_001262202.1. NM_001275273.1.
NP_524211.1. NM_079487.4.
UniGeneiDm.7933.

3D structure databases

ProteinModelPortaliP19889.
SMRiP19889. Positions 5-273.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi65690. 23 interactions.
DIPiDIP-21968N.
IntActiP19889. 4 interactions.
MINTiMINT-235412.

Protein family/group databases

MoonProtiP19889.

Proteomic databases

PaxDbiP19889.
PRIDEiP19889.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0078481; FBpp0078134; FBgn0000100.
FBtr0334113; FBpp0306232; FBgn0000100.
GeneIDi40451.
KEGGidme:Dmel_CG7490.

Organism-specific databases

CTDi6175.
FlyBaseiFBgn0000100. RpLP0.

Phylogenomic databases

eggNOGiCOG0244.
GeneTreeiENSGT00390000017839.
InParanoidiP19889.
KOiK02941.
OMAiNYVERGA.
OrthoDBiEOG71K63M.
PhylomeDBiP19889.

Enzyme and pathway databases

ReactomeiREACT_281936. Peptide chain elongation.
REACT_303602. Formation of a pool of free 40S subunits.
REACT_305162. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_321612. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_341839. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_342983. SRP-dependent cotranslational protein targeting to membrane.
REACT_344041. Eukaryotic Translation Termination.
REACT_351471. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).

Miscellaneous databases

GenomeRNAii40451.
NextBioi818852.
PROiP19889.

Gene expression databases

BgeeiP19889.

Family and domain databases

InterProiIPR030670. L10E_eukaryotes.
IPR001790. Ribosomal_L10P.
[Graphical view]
PfamiPF00466. Ribosomal_L10. 1 hit.
[Graphical view]
PIRSFiPIRSF039087. L10E. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Antibody to a human DNA repair protein allows for cloning of a Drosophila cDNA that encodes an apurinic endonuclease."
    Kelley M.R., Venugopal S., Harless J., Deutsch W.A.
    Mol. Cell. Biol. 9:965-973(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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.
  5. 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 (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.
  6. "Drosophila AP3, a presumptive DNA repair protein, is homologous to human ribosomal associated protein P0."
    Grabowski D.T., Deutsch W.A., Derda D., Kelley M.R.
    Nucleic Acids Res. 19:4297-4297(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: SIMILARITY TO RIBOSOMAL PROTEIN P0.
  7. "Drosophila ribosomal protein PO contains apurinic/apyrimidinic endonuclease activity."
    Yacoub A., Kelley M.R., Deutsch W.A.
    Nucleic Acids Res. 24:4298-4303(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA REPAIR ACTIVITY.
  8. "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-302 AND SER-304, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiRLA0_DROME
AccessioniPrimary (citable) accession number: P19889
Secondary accession number(s): Q5BHX7, Q9VNV9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: April 1, 2015
This is version 144 of the entry and version 1 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

External Data

Dasty 3

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 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.