Full text data of RPLP0
RPLP0
[Confidence: low (only semi-automatic identification from reviews)]
60S acidic ribosomal protein P0 (60S ribosomal protein L10E)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
60S acidic ribosomal protein P0 (60S ribosomal protein L10E)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P05388
ID RLA0_HUMAN Reviewed; 317 AA.
AC P05388; Q9BVK4;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1988, sequence version 1.
DT 22-JAN-2014, entry version 156.
DE RecName: Full=60S acidic ribosomal protein P0;
DE AltName: Full=60S ribosomal protein L10E;
GN Name=RPLP0;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3323886;
RA Rich B.E., Steitz J.A.;
RT "Human acidic ribosomal phosphoproteins P0, P1, and P2: analysis of
RT cDNA 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.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA 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.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA 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.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., 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].
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
RT project: 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
RP 267-297, AND 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;
RA Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N.,
RA Hudson T.J., 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, MASS SPECTROMETRY, AND 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
RT the rRNA quality control process.";
RL Mol. Cell. Biol. 29:1834-1854(2009).
RN [8]
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.,
RA Buerckstuemmer T., 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 [9]
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
CC E.coli protein L10.
CC -!- SUBUNIT: P0 forms a pentameric complex by interaction with dimers
CC of P1 and P2. Identified in a IGF2BP1-dependent mRNP granule
CC complex containing untranslated mRNAs. Interacts with Lassa virus
CC Z protein. Interacts with APEX1.
CC -!- INTERACTION:
CC O95793:STAU1; NbExp=4; IntAct=EBI-354101, EBI-358174;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Localized in
CC cytoplasmic mRNP granules containing untranslated mRNAs.
CC -!- SIMILARITY: Belongs to the ribosomal protein L10P family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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; AB007187; BAA25845.1; -; Genomic_DNA.
DR PIR; A27125; R5HUP0.
DR RefSeq; NP_000993.1; NM_001002.3.
DR RefSeq; NP_444505.1; NM_053275.3.
DR UniGene; Hs.546285; -.
DR PDB; 3J39; EM; 6.00 A; q=5-202.
DR PDB; 3J3B; EM; 5.00 A; q=1-317.
DR PDBsum; 3J39; -.
DR PDBsum; 3J3B; -.
DR ProteinModelPortal; P05388; -.
DR SMR; P05388; 5-308.
DR IntAct; P05388; 34.
DR MINT; MINT-193149; -.
DR STRING; 9606.ENSP00000339027; -.
DR PhosphoSite; P05388; -.
DR DMDM; 133041; -.
DR REPRODUCTION-2DPAGE; P05388; -.
DR PaxDb; P05388; -.
DR PRIDE; P05388; -.
DR DNASU; 6175; -.
DR Ensembl; ENST00000228306; ENSP00000339027; ENSG00000089157.
DR Ensembl; ENST00000392514; ENSP00000376299; ENSG00000089157.
DR Ensembl; ENST00000551150; ENSP00000449328; ENSG00000089157.
DR GeneID; 6175; -.
DR KEGG; hsa:6175; -.
DR UCSC; uc001txp.3; human.
DR CTD; 6175; -.
DR GeneCards; GC12M120634; -.
DR HGNC; HGNC:10371; RPLP0.
DR HPA; HPA003512; -.
DR MIM; 180510; gene.
DR neXtProt; NX_P05388; -.
DR PharmGKB; PA34772; -.
DR eggNOG; COG0244; -.
DR HOVERGEN; HBG000711; -.
DR InParanoid; P05388; -.
DR KO; K02941; -.
DR OMA; IGTNDNP; -.
DR OrthoDB; EOG71K63M; -.
DR PhylomeDB; P05388; -.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_1762; 3' -UTR-mediated translational regulation.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; RPLP0; human.
DR GeneWiki; RPLP0; -.
DR GenomeRNAi; 6175; -.
DR NextBio; 23989; -.
DR PRO; PR:P05388; -.
DR ArrayExpress; P05388; -.
DR Bgee; P05388; -.
DR CleanEx; HS_RPLP0; -.
DR Genevestigator; P05388; -.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0003735; F:structural constituent of ribosome; NAS:UniProtKB.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:InterPro.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
DR GO; GO:0006414; P:translational elongation; TAS:Reactome.
DR GO; GO:0006413; P:translational initiation; TAS:Reactome.
DR GO; GO:0006415; P:translational termination; TAS:Reactome.
DR GO; GO:0019083; P:viral transcription; TAS:Reactome.
DR InterPro; IPR001790; Ribosomal_L10/acidic_P0.
DR InterPro; IPR001813; Ribosomal_L10/L12.
DR Pfam; PF00428; Ribosomal_60s; 1.
DR Pfam; PF00466; Ribosomal_L10; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Host-virus interaction; Nucleus; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1 317 60S acidic ribosomal protein P0.
FT /FTId=PRO_0000154758.
FT CONFLICT 246 246 K -> E (in Ref. 3; AAH01127).
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
//
ID RLA0_HUMAN Reviewed; 317 AA.
AC P05388; Q9BVK4;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1988, sequence version 1.
DT 22-JAN-2014, entry version 156.
DE RecName: Full=60S acidic ribosomal protein P0;
DE AltName: Full=60S ribosomal protein L10E;
GN Name=RPLP0;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3323886;
RA Rich B.E., Steitz J.A.;
RT "Human acidic ribosomal phosphoproteins P0, P1, and P2: analysis of
RT cDNA 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.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA 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.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA 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.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., 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].
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
RT project: 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
RP 267-297, AND 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;
RA Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N.,
RA Hudson T.J., 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, MASS SPECTROMETRY, AND 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
RT the rRNA quality control process.";
RL Mol. Cell. Biol. 29:1834-1854(2009).
RN [8]
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.,
RA Buerckstuemmer T., 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 [9]
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
CC E.coli protein L10.
CC -!- SUBUNIT: P0 forms a pentameric complex by interaction with dimers
CC of P1 and P2. Identified in a IGF2BP1-dependent mRNP granule
CC complex containing untranslated mRNAs. Interacts with Lassa virus
CC Z protein. Interacts with APEX1.
CC -!- INTERACTION:
CC O95793:STAU1; NbExp=4; IntAct=EBI-354101, EBI-358174;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Localized in
CC cytoplasmic mRNP granules containing untranslated mRNAs.
CC -!- SIMILARITY: Belongs to the ribosomal protein L10P family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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; AB007187; BAA25845.1; -; Genomic_DNA.
DR PIR; A27125; R5HUP0.
DR RefSeq; NP_000993.1; NM_001002.3.
DR RefSeq; NP_444505.1; NM_053275.3.
DR UniGene; Hs.546285; -.
DR PDB; 3J39; EM; 6.00 A; q=5-202.
DR PDB; 3J3B; EM; 5.00 A; q=1-317.
DR PDBsum; 3J39; -.
DR PDBsum; 3J3B; -.
DR ProteinModelPortal; P05388; -.
DR SMR; P05388; 5-308.
DR IntAct; P05388; 34.
DR MINT; MINT-193149; -.
DR STRING; 9606.ENSP00000339027; -.
DR PhosphoSite; P05388; -.
DR DMDM; 133041; -.
DR REPRODUCTION-2DPAGE; P05388; -.
DR PaxDb; P05388; -.
DR PRIDE; P05388; -.
DR DNASU; 6175; -.
DR Ensembl; ENST00000228306; ENSP00000339027; ENSG00000089157.
DR Ensembl; ENST00000392514; ENSP00000376299; ENSG00000089157.
DR Ensembl; ENST00000551150; ENSP00000449328; ENSG00000089157.
DR GeneID; 6175; -.
DR KEGG; hsa:6175; -.
DR UCSC; uc001txp.3; human.
DR CTD; 6175; -.
DR GeneCards; GC12M120634; -.
DR HGNC; HGNC:10371; RPLP0.
DR HPA; HPA003512; -.
DR MIM; 180510; gene.
DR neXtProt; NX_P05388; -.
DR PharmGKB; PA34772; -.
DR eggNOG; COG0244; -.
DR HOVERGEN; HBG000711; -.
DR InParanoid; P05388; -.
DR KO; K02941; -.
DR OMA; IGTNDNP; -.
DR OrthoDB; EOG71K63M; -.
DR PhylomeDB; P05388; -.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_1762; 3' -UTR-mediated translational regulation.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; RPLP0; human.
DR GeneWiki; RPLP0; -.
DR GenomeRNAi; 6175; -.
DR NextBio; 23989; -.
DR PRO; PR:P05388; -.
DR ArrayExpress; P05388; -.
DR Bgee; P05388; -.
DR CleanEx; HS_RPLP0; -.
DR Genevestigator; P05388; -.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0003735; F:structural constituent of ribosome; NAS:UniProtKB.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:InterPro.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
DR GO; GO:0006414; P:translational elongation; TAS:Reactome.
DR GO; GO:0006413; P:translational initiation; TAS:Reactome.
DR GO; GO:0006415; P:translational termination; TAS:Reactome.
DR GO; GO:0019083; P:viral transcription; TAS:Reactome.
DR InterPro; IPR001790; Ribosomal_L10/acidic_P0.
DR InterPro; IPR001813; Ribosomal_L10/L12.
DR Pfam; PF00428; Ribosomal_60s; 1.
DR Pfam; PF00466; Ribosomal_L10; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Host-virus interaction; Nucleus; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1 317 60S acidic ribosomal protein P0.
FT /FTId=PRO_0000154758.
FT CONFLICT 246 246 K -> E (in Ref. 3; AAH01127).
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
//
MIM
180510
*RECORD*
*FIELD* NO
180510
*FIELD* TI
*180510 RIBOSOMAL PHOSPHOPROTEIN, LARGE, P0; RPLP0
;;RIBOSOMAL PHOSPHOPROTEIN, ACIDIC, P0
read more*FIELD* TX
DESCRIPTION
Acidic ribosomal proteins, called A-proteins or P-proteins, are
generally present in multiple copies on the ribosome and have
isoelectric points in the range of pH 3 to 5, in contrast to most
ribosomal proteins, which are single copy and basic. A-proteins have
hydrophobic amino acid compositions, notably about 20% alanine.
CLONING
Rich and Steitz (1987) described the isolation and analysis of 3 cDNA
molecules that encode the human P-proteins, P2 (180530), P1 (180520),
and P0. The human P1 and P2 cDNA nucleotide sequences and deduced amino
acid sequences of the proteins are very similar to the sequences that
have been determined for the corresponding rat, shrimp, and yeast
proteins and cDNAs. P0 sequences had not previously been described. To
demonstrate that the coding sequences are full length, Rich and Steitz
(1987) transcribed the P0, P1, and P2 cDNAs in vitro. The P0, P1, and P2
proteins produced were serologically and electrophoretically identical
to P-proteins extracted from HeLa cells. The deduced P0 protein contains
317 amino acids and is the largest of the 3 proteins. Northern blot
analysis revealed expression of a 1.2-kb transcript in HeLa cells.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the RPLP0
gene to chromosome 12 (TMAP D12S1979).
*FIELD* RF
1. Rich, B. E.; Steitz, J. A.: Human acidic ribosomal phosphoproteins
P0, P1, and P2: analysis of cDNA clones, in vitro synthesis, and assembly. Molec.
Cell. Biol. 7: 4065-4074, 1987.
*FIELD* CN
Paul J. Converse - updated: 4/11/2002
*FIELD* CD
Victor A. McKusick: 12/3/1987
*FIELD* ED
mgross: 04/12/2002
mgross: 4/11/2002
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/27/1989
marie: 3/25/1988
root: 12/3/1987
*RECORD*
*FIELD* NO
180510
*FIELD* TI
*180510 RIBOSOMAL PHOSPHOPROTEIN, LARGE, P0; RPLP0
;;RIBOSOMAL PHOSPHOPROTEIN, ACIDIC, P0
read more*FIELD* TX
DESCRIPTION
Acidic ribosomal proteins, called A-proteins or P-proteins, are
generally present in multiple copies on the ribosome and have
isoelectric points in the range of pH 3 to 5, in contrast to most
ribosomal proteins, which are single copy and basic. A-proteins have
hydrophobic amino acid compositions, notably about 20% alanine.
CLONING
Rich and Steitz (1987) described the isolation and analysis of 3 cDNA
molecules that encode the human P-proteins, P2 (180530), P1 (180520),
and P0. The human P1 and P2 cDNA nucleotide sequences and deduced amino
acid sequences of the proteins are very similar to the sequences that
have been determined for the corresponding rat, shrimp, and yeast
proteins and cDNAs. P0 sequences had not previously been described. To
demonstrate that the coding sequences are full length, Rich and Steitz
(1987) transcribed the P0, P1, and P2 cDNAs in vitro. The P0, P1, and P2
proteins produced were serologically and electrophoretically identical
to P-proteins extracted from HeLa cells. The deduced P0 protein contains
317 amino acids and is the largest of the 3 proteins. Northern blot
analysis revealed expression of a 1.2-kb transcript in HeLa cells.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the RPLP0
gene to chromosome 12 (TMAP D12S1979).
*FIELD* RF
1. Rich, B. E.; Steitz, J. A.: Human acidic ribosomal phosphoproteins
P0, P1, and P2: analysis of cDNA clones, in vitro synthesis, and assembly. Molec.
Cell. Biol. 7: 4065-4074, 1987.
*FIELD* CN
Paul J. Converse - updated: 4/11/2002
*FIELD* CD
Victor A. McKusick: 12/3/1987
*FIELD* ED
mgross: 04/12/2002
mgross: 4/11/2002
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/27/1989
marie: 3/25/1988
root: 12/3/1987