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Description:
60S acidic ribosomal protein P0 (DNA-(apurinic or apyrimidinic site)lyase) (EC 4.2.99.18) (Apurinic-apyrimidinic endonuclease).
Molecular weight: 34202
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 )
Important dates:
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 1.
07-FEB-2006, entry version 63.
Phylogenetic order:
Eukaryota Metazoa Arthropoda Hexapoda Insecta Pterygota Neoptera Endopterygota Diptera Brachycera Muscomorpha Ephydroidea Drosophilidae Drosophila.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein RLA0_DROME:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | M25772 | AAA53372.1 | - |
| EMBL | AE003596 | AAF51807.1 | - |
| EMBL | AY075528 | AAL68335.1 | - |
| EMBL | BT021447 | AAX33595.1 | - |
| PIR | A30223 | R5FFP0. | |
| IntAct | P19889 | -.1 | |
| Ensembl | CG7490 | Drosophila melanogaster.1 | |
| FlyBase | FBgn0000100 | RpLP0. | |
| BioCyc | DMEL-XXX-02:DMEL-XXX-02-017821-MONOMER | -.1 | |
| GO | GO:0005830 | C:cytosolic ribosome (sensu Eukaryota) | NAS. |
| GO | GO:0003906 | F:DNA-(apurinic or apyrimidinic site) lyase a... | NAS. |
| GO | GO:0005515 | F:protein binding | IPI. |
| GO | GO:0003735 | F:structural constituent of ribosome | NAS. |
| GO | GO:0006412 | P:protein biosynthesis | NAS. |
| InterPro | IPR001813 | Ribosomal_60S. | |
| InterPro | IPR001790 | Ribosomal_L10. | |
| Pfam | PF00428 | Ribosomal_60s | 1. |
| Pfam | PF00466 | Ribosomal_L10 | 1. |
Keywords:
Complete proteome; DNA damage; DNA repair; Lyase; Nuclear protein; Phosphorylation; Ribonucleoprotein; Ribosomal protein.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX MEDLINE=89261760; PubMed=2471063;
RA Kelley M.R., Venugopal S., Harless J., Deutsch W.A.;
RT "Antibody to a human DNA repair protein allows for cloning of a
RT Drosophila cDNA that encodes an apurinic endonuclease.";
RL Mol. Cell. Biol. 9:965-973(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z.,
RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O.,
RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RX MEDLINE=22426069; PubMed=12537572;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a
RT systematic review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX MEDLINE=22426066; PubMed=12537569;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA Rubin G.M., Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A.,
RA Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SIMILARITY TO RIBOSOMAL PROTEIN P0.
RX MEDLINE=91334151; PubMed=1870984;
RA Grabowski D.T., Deutsch W.A., Derda D., Kelley M.R.;
RT "Drosophila AP3, a presumptive DNA repair protein, is homologous to
RT human ribosomal associated protein P0.";
RL Nucleic Acids Res. 19:4297-4297(1991).
RN [7]
RP DNA REPAIR ACTIVITY.
RX MEDLINE=97086697; PubMed=8932386; DOI=10.1093/nar/24.21.4298;
RA Yacoub A., Kelley M.R., Deutsch W.A.;
RT "Drosophila ribosomal protein PO contains apurinic/apyrimidinic
RT endonuclease activity.";
RL Nucleic Acids Res. 24:4298-4303(1996).
Feature:
CHAIN 1 317 60S acidic ribosomal protein P0.
/FTId=PRO_0000154769.
MOD_RES 304 304 Phosphoserine (by CK1) (Potential).
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: P0 forms a pentameric complex by interaction with dimers
of P1 and P2 (By similarity).
-!- INTERACTION:
P42325:Nca; NbExp=1; IntAct=EBI-195497, EBI-149848;
P08570:RpLP1; NbExp=1; IntAct=EBI-195497, EBI-125901;
-!- SUBCELLULAR LOCATION: Nuclear and cytoplasmic.
-!- DEVELOPMENTAL STAGE: All stages of development. A larger
transcript is restricted to the embryonic and early larval stages.
-!- PTM: Phosphorylated (By similarity).
-!- SIMILARITY: Belongs to the ribosomal protein L10P family.
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Sequence length: 317
MVRENKAAWK AQYFIKVVEL FDEFPKCFIV GADNVGSKQM QNIRTSLRGL AVVLMGKNTM
MRKAIRGHLE NNPQLEKLLP HIKGNVGFVF TKGDLAEVRD KLLESKVRAP ARPGAIAPLH
VIIPAQNTGL GPEKTSFFQA LSIPTKISKG TIEIINDVPI LKPGDKVGAS EATLLNMLNI
SPFSYGLIVN QVYDSGSIFS PEILDIKPED LRAKFQQGVA NLAAVCLSVG YPTIASAPHS
IANGFKNLLA IAATTEVEFK EATTIKEYIK DPSKFAAAAS ASAAPAAGGA TEKKEEAKKP
ESESEEEDDD MGFGLFD