RLA0_HUMAN
ID RLA0_HUMAN Reviewed; 317 AA.
AC P05388; Q3B7A4; Q9BVK4;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 233.
DE RecName: Full=60S acidic ribosomal protein P0;
DE AltName: Full=60S ribosomal protein L10E;
DE AltName: Full=Large ribosomal subunit protein uL10 {ECO:0000303|PubMed:24524803};
GN Name=RPLP0;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBUNIT.
RX PubMed=3323886; DOI=10.1128/mcb.7.11.4065-4074.1987;
RA Rich B.E., Steitz J.A.;
RT "Human acidic ribosomal phosphoproteins P0, P1, and P2: analysis of cDNA
RT clones, in vitro synthesis, and assembly.";
RL Mol. Cell. Biol. 7:4065-4074(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, Cervix, Colon, Lung, Lymph, Muscle, and Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 17-38; 84-92; 135-146; 150-162; 248-264 AND 267-297,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 218-310.
RX PubMed=9582194; DOI=10.1101/gr.8.5.509;
RA Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J.,
RA Tanaka T., Page D.C.;
RT "A map of 75 human ribosomal protein genes.";
RL Genome Res. 8:509-523(1998).
RN [6]
RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=17289661; DOI=10.1074/mcp.m600346-mcp200;
RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
RA Johnsen A.H., Christiansen J., Nielsen F.C.;
RT "Molecular composition of IMP1 ribonucleoprotein granules.";
RL Mol. Cell. Proteomics 6:798-811(2007).
RN [7]
RP INTERACTION WITH APEX1, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=19188445; DOI=10.1128/mcb.01337-08;
RA Vascotto C., Fantini D., Romanello M., Cesaratto L., Deganuto M.,
RA Leonardi A., Radicella J.P., Kelley M.R., D'Ambrosio C., Scaloni A.,
RA Quadrifoglio F., Tell G.;
RT "APE1/Ref-1 interacts with NPM1 within nucleoli and plays a role in the
RT rRNA quality control process.";
RL Mol. Cell. Biol. 29:1834-1854(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-307, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-59, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP NOMENCLATURE.
RX PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
RA Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
RA Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
RA Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
RA Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
RA Williamson J.R., Wilson D., Yonath A., Yusupov M.;
RT "A new system for naming ribosomal proteins.";
RL Curr. Opin. Struct. Biol. 24:165-169(2014).
RN [13]
RP INTERACTION WITH FMR1.
RX PubMed=24658146; DOI=10.1371/journal.pone.0091465;
RA Taha M.S., Nouri K., Milroy L.G., Moll J.M., Herrmann C., Brunsveld L.,
RA Piekorz R.P., Ahmadian M.R.;
RT "Subcellular fractionation and localization studies reveal a direct
RT interaction of the fragile X mental retardation protein (FMRP) with
RT nucleolin.";
RL PLoS ONE 9:E91465-E91465(2014).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-297, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [16]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).
RX PubMed=23636399; DOI=10.1038/nature12104;
RA Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
RA Wilson D.N., Beckmann R.;
RT "Structures of the human and Drosophila 80S ribosome.";
RL Nature 497:80-85(2013).
CC -!- FUNCTION: Ribosomal protein P0 is the functional equivalent of E.coli
CC protein L10.
CC -!- SUBUNIT: P0 forms a pentameric complex by interaction with dimers of P1
CC and P2 (PubMed:3323886). Identified in a IGF2BP1-dependent mRNP granule
CC complex containing untranslated mRNAs (PubMed:17289661). Interacts with
CC APEX1 (PubMed:19188445). Interacts with FMR1 isoform 6
CC (PubMed:24658146). {ECO:0000269|PubMed:17289661,
CC ECO:0000269|PubMed:19188445, ECO:0000269|PubMed:24658146,
CC ECO:0000269|PubMed:3323886}.
CC -!- INTERACTION:
CC P05388; O95273: CCNDBP1; NbExp=4; IntAct=EBI-354101, EBI-748961;
CC P05388; O95793: STAU1; NbExp=4; IntAct=EBI-354101, EBI-358174;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19188445}. Cytoplasm
CC {ECO:0000269|PubMed:19188445}. Note=Localized in cytoplasmic mRNP
CC granules containing untranslated mRNAs (PubMed:19188445,
CC PubMed:17289661). {ECO:0000269|PubMed:17289661,
CC ECO:0000269|PubMed:19188445}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P05388-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P05388-2; Sequence=VSP_055867;
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL10 family.
CC {ECO:0000305}.
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DR EMBL; M17885; AAA36470.1; -; mRNA.
DR EMBL; AC004263; AAC05176.1; -; Genomic_DNA.
DR EMBL; BC000087; AAH00087.1; -; mRNA.
DR EMBL; BC000345; AAH00345.1; -; mRNA.
DR EMBL; BC000752; AAH00752.1; -; mRNA.
DR EMBL; BC001127; AAH01127.1; -; mRNA.
DR EMBL; BC001834; AAH01834.1; -; mRNA.
DR EMBL; BC003655; AAH03655.1; -; mRNA.
DR EMBL; BC005863; AAH05863.1; -; mRNA.
DR EMBL; BC008092; AAH08092.1; -; mRNA.
DR EMBL; BC008594; AAH08594.1; -; mRNA.
DR EMBL; BC009867; AAH09867.1; -; mRNA.
DR EMBL; BC015173; AAH15173.1; -; mRNA.
DR EMBL; BC015690; AAH15690.1; -; mRNA.
DR EMBL; BC107717; AAI07718.1; -; mRNA.
DR EMBL; AB007187; BAA25845.1; -; Genomic_DNA.
DR CCDS; CCDS9193.1; -. [P05388-1]
DR PIR; A27125; R5HUP0.
DR RefSeq; NP_000993.1; NM_001002.3. [P05388-1]
DR RefSeq; NP_444505.1; NM_053275.3. [P05388-1]
DR PDB; 4V6W; EM; 6.00 A; q=5-227.
DR PDB; 4V6X; EM; 5.00 A; Cq=1-317.
DR PDB; 5AJ0; EM; 3.50 A; AK=1-317.
DR PDB; 6OLG; EM; 3.40 A; AK=1-109.
DR PDB; 6ZM7; EM; 2.70 A; Ls=1-317.
DR PDB; 6ZME; EM; 3.00 A; Ls=1-317.
DR PDB; 6ZMI; EM; 2.60 A; Ls=1-317.
DR PDB; 6ZMO; EM; 3.10 A; Ls=1-317.
DR PDBsum; 4V6W; -.
DR PDBsum; 4V6X; -.
DR PDBsum; 5AJ0; -.
DR PDBsum; 6OLG; -.
DR PDBsum; 6ZM7; -.
DR PDBsum; 6ZME; -.
DR PDBsum; 6ZMI; -.
DR PDBsum; 6ZMO; -.
DR AlphaFoldDB; P05388; -.
DR SMR; P05388; -.
DR BioGRID; 112094; 566.
DR ComplexPortal; CPX-5183; 60S cytosolic large ribosomal subunit.
DR CORUM; P05388; -.
DR IntAct; P05388; 105.
DR MINT; P05388; -.
DR STRING; 9606.ENSP00000449328; -.
DR GlyGen; P05388; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P05388; -.
DR MetOSite; P05388; -.
DR PhosphoSitePlus; P05388; -.
DR SwissPalm; P05388; -.
DR BioMuta; RPLP0; -.
DR DMDM; 133041; -.
DR REPRODUCTION-2DPAGE; P05388; -.
DR EPD; P05388; -.
DR jPOST; P05388; -.
DR MassIVE; P05388; -.
DR MaxQB; P05388; -.
DR PaxDb; P05388; -.
DR PeptideAtlas; P05388; -.
DR PRIDE; P05388; -.
DR ProteomicsDB; 51833; -. [P05388-1]
DR ProteomicsDB; 61651; -.
DR TopDownProteomics; P05388-1; -. [P05388-1]
DR Antibodypedia; 1255; 307 antibodies from 29 providers.
DR DNASU; 6175; -.
DR Ensembl; ENST00000228306.8; ENSP00000339027.3; ENSG00000089157.16. [P05388-1]
DR Ensembl; ENST00000313104.9; ENSP00000366471.4; ENSG00000089157.16. [P05388-2]
DR Ensembl; ENST00000392514.9; ENSP00000376299.4; ENSG00000089157.16. [P05388-1]
DR Ensembl; ENST00000551150.5; ENSP00000449328.1; ENSG00000089157.16. [P05388-1]
DR GeneID; 6175; -.
DR KEGG; hsa:6175; -.
DR MANE-Select; ENST00000392514.9; ENSP00000376299.4; NM_001002.4; NP_000993.1.
DR UCSC; uc001txp.4; human. [P05388-1]
DR CTD; 6175; -.
DR DisGeNET; 6175; -.
DR GeneCards; RPLP0; -.
DR HGNC; HGNC:10371; RPLP0.
DR HPA; ENSG00000089157; Low tissue specificity.
DR MIM; 180510; gene.
DR neXtProt; NX_P05388; -.
DR OpenTargets; ENSG00000089157; -.
DR PharmGKB; PA34772; -.
DR VEuPathDB; HostDB:ENSG00000089157; -.
DR eggNOG; KOG0815; Eukaryota.
DR GeneTree; ENSGT00390000017839; -.
DR InParanoid; P05388; -.
DR OMA; MAHVAEW; -.
DR PhylomeDB; P05388; -.
DR TreeFam; TF300849; -.
DR PathwayCommons; P05388; -.
DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-HSA-156902; Peptide chain elongation.
DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-HSA-192823; Viral mRNA Translation.
DR Reactome; R-HSA-2408557; Selenocysteine synthesis.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-HSA-72764; Eukaryotic Translation Termination.
DR Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9633012; Response of EIF2AK4 (GCN2) to amino acid deficiency.
DR Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; P05388; -.
DR SIGNOR; P05388; -.
DR BioGRID-ORCS; 6175; 801 hits in 1080 CRISPR screens.
DR ChiTaRS; RPLP0; human.
DR GeneWiki; RPLP0; -.
DR GenomeRNAi; 6175; -.
DR Pharos; P05388; Tbio.
DR PRO; PR:P05388; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P05388; protein.
DR Bgee; ENSG00000089157; Expressed in stromal cell of endometrium and 107 other tissues.
DR ExpressionAtlas; P05388; baseline and differential.
DR Genevisible; P05388; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:GO_Central.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IBA:GO_Central.
DR GO; GO:0042277; F:peptide binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
DR GO; GO:0071353; P:cellular response to interleukin-4; IEA:Ensembl.
DR GO; GO:1904628; P:cellular response to phorbol 13-acetate 12-myristate; IEA:Ensembl.
DR GO; GO:1904401; P:cellular response to Thyroid stimulating hormone; IEA:Ensembl.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR GO; GO:0007595; P:lactation; IEA:Ensembl.
DR GO; GO:0010269; P:response to selenium ion; IEA:Ensembl.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR GO; GO:0006412; P:translation; NAS:UniProtKB.
DR Gene3D; 3.30.70.1730; -; 1.
DR Gene3D; 3.90.105.20; -; 1.
DR InterPro; IPR030670; L10E_eukaryotes.
DR InterPro; IPR043141; Ribosomal_L10-like_sf.
DR InterPro; IPR001790; Ribosomal_L10P.
DR InterPro; IPR043164; RL10_insert_sf.
DR InterPro; IPR040637; RL10P_insert.
DR Pfam; PF00466; Ribosomal_L10; 1.
DR Pfam; PF17777; RL10P_insert; 1.
DR PIRSF; PIRSF039087; L10E; 1.
DR SUPFAM; SSF160369; SSF160369; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT CHAIN 1..317
FT /note="60S acidic ribosomal protein P0"
FT /id="PRO_0000154758"
FT REGION 294..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..317
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P14869"
FT MOD_RES 59
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT CROSSLNK 297
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 297
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT VAR_SEQ 156..217
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055867"
FT CONFLICT 246
FT /note="K -> E (in Ref. 3; AAH01127)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 317 AA; 34274 MW; 255AD25571C51199 CRC64;
MPREDRATWK SNYFLKIIQL LDDYPKCFIV GADNVGSKQM QQIRMSLRGK AVVLMGKNTM
MRKAIRGHLE NNPALEKLLP HIRGNVGFVF TKEDLTEIRD MLLANKVPAA ARAGAIAPCE
VTVPAQNTGL GPEKTSFFQA LGITTKISRG TIEILSDVQL IKTGDKVGAS EATLLNMLNI
SPFSFGLVIQ QVFDNGSIYN PEVLDITEET LHSRFLEGVR NVASVCLQIG YPTVASVPHS
IINGYKRVLA LSVETDYTFP LAEKVKAFLA DPSAFVAAAP VAAATTAAPA AAAAPAKVEA
KEESEESDED MGFGLFD
