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P19889 (RLA0_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
60S acidic ribosomal protein P0
Alternative name(s):
Apurinic-apyrimidinic endonuclease
DNA-(apurinic or apyrimidinic site) lyase
EC=4.2.99.18
Gene names
Name:RpLP0
Synonyms:AP3, Ape, RpP0
ORF Names:CG7490
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length317 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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.

Subunit structure

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

Subcellular location

Cytoplasm. Nucleus.

Developmental stage

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

Sequence similarities

Belongs to the ribosomal protein L10P family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 31731760S acidic ribosomal protein P0
PRO_0000154769

Amino acid modifications

Modified residue3021Phosphoserine Ref.8
Modified residue3041Phosphoserine; by CK1 Potential

Sequences

Sequence LengthMass (Da)Tools
P19889 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 36E9DD5DD8CF7E1F

FASTA31734,202
        10         20         30         40         50         60 
MVRENKAAWK AQYFIKVVEL FDEFPKCFIV GADNVGSKQM QNIRTSLRGL AVVLMGKNTM 

        70         80         90        100        110        120 
MRKAIRGHLE NNPQLEKLLP HIKGNVGFVF TKGDLAEVRD KLLESKVRAP ARPGAIAPLH 

       130        140        150        160        170        180 
VIIPAQNTGL GPEKTSFFQA LSIPTKISKG TIEIINDVPI LKPGDKVGAS EATLLNMLNI 

       190        200        210        220        230        240 
SPFSYGLIVN QVYDSGSIFS PEILDIKPED LRAKFQQGVA NLAAVCLSVG YPTIASAPHS 

       250        260        270        280        290        300 
IANGFKNLLA IAATTEVEFK EATTIKEYIK DPSKFAAAAS ASAAPAAGGA TEKKEEAKKP 

       310 
ESESEEEDDD MGFGLFD 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]"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.
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M25772 mRNA. Translation: AAA53372.1.
AE014296 Genomic DNA. Translation: AAF51807.1.
AY075528 mRNA. Translation: AAL68335.1.
BT021447 mRNA. Translation: AAX33595.1.
PIRR5FFP0. A30223.
RefSeqNP_001262202.1. NM_001275273.1.
NP_524211.1. NM_079487.4.
UniGeneDm.7933.

3D structure databases

ProteinModelPortalP19889.
SMRP19889. Positions 5-273.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid65690. 23 interactions.
DIPDIP-21968N.
IntActP19889. 4 interactions.
MINTMINT-235412.

Proteomic databases

PaxDbP19889.
PRIDEP19889.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0078481; FBpp0078134; FBgn0000100.
FBtr0334113; FBpp0306232; FBgn0000100.
GeneID40451.
KEGGdme:Dmel_CG7490.

Organism-specific databases

CTD6175.
FlyBaseFBgn0000100. RpLP0.

Phylogenomic databases

eggNOGCOG0244.
GeneTreeENSGT00390000017839.
InParanoidP19889.
KOK02941.
OMAWKKDEIE.
OrthoDBEOG71K63M.
PhylomeDBP19889.

Gene expression databases

BgeeP19889.

Family and domain databases

InterProIPR001790. Ribosomal_L10/acidic_P0.
IPR001813. Ribosomal_L10/L12.
[Graphical view]
PfamPF00428. Ribosomal_60s. 1 hit.
PF00466. Ribosomal_L10. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi40451.
NextBio818852.
PROP19889.

Entry information

Entry nameRLA0_DROME
AccessionPrimary (citable) accession number: P19889
Secondary accession number(s): Q5BHX7, Q9VNV9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: July 9, 2014
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

Drosophila

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