Full text data of RPL19
RPL19
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
60S ribosomal protein L19
Note: presumably soluble (membrane word is not in UniProt keywords or features)
60S ribosomal protein L19
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P84098
ID RL19_HUMAN Reviewed; 196 AA.
AC P84098; B2R4K2; P14118; P22908; Q502Y6; Q7Z6E4;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-AUG-2004, sequence version 1.
DT 22-JAN-2014, entry version 97.
DE RecName: Full=60S ribosomal protein L19;
GN Name=RPL19;
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=1598220; DOI=10.1093/nar/20.10.2598;
RA Kumabe T., Schma Y., Yamamoto T.;
RT "Human cDNAs encoding elongation factor 1 gamma and the ribosomal
RT protein L19.";
RL Nucleic Acids Res. 20:2598-2598(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8095182;
RA Henry J.L., Coggin D.L., King C.R.;
RT "High-level expression of the ribosomal protein L19 in human breast
RT tumors that overexpress erbB-2.";
RL Cancer Res. 53:1403-1408(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Hypothalamus, and Muscle;
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 [6]
RP PROTEIN SEQUENCE OF 10-16; 22-38 AND 154-162, AND MASS SPECTROMETRY.
RC TISSUE=Lung carcinoma;
RA Bienvenut W.V., Vousden K.H., Lukashchuk N.;
RL Submitted (MAR-2008) to UniProtKB.
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND THR-187, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
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 [10]
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 -!- SIMILARITY: Belongs to the ribosomal protein L19e family.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD97677.1; Type=Erroneous initiation;
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; X63527; CAA45090.1; -; mRNA.
DR EMBL; S56985; AAB25672.1; -; mRNA.
DR EMBL; AK311858; BAG34799.1; -; mRNA.
DR EMBL; BX537435; CAD97677.1; ALT_INIT; mRNA.
DR EMBL; BC000530; AAH00530.1; -; mRNA.
DR EMBL; BC013016; AAH13016.1; -; mRNA.
DR EMBL; BC062709; AAH62709.1; -; mRNA.
DR EMBL; BC066315; AAH66315.1; -; mRNA.
DR EMBL; BC095445; AAH95445.1; -; mRNA.
DR PIR; A48992; A48992.
DR RefSeq; NP_000972.1; NM_000981.3.
DR UniGene; Hs.381061; -.
DR PDB; 3J3B; EM; 5.00 A; R=1-196.
DR PDBsum; 3J3B; -.
DR ProteinModelPortal; P84098; -.
DR SMR; P84098; 1-189.
DR IntAct; P84098; 18.
DR MINT; MINT-1815479; -.
DR STRING; 9606.ENSP00000225430; -.
DR PhosphoSite; P84098; -.
DR DMDM; 51338661; -.
DR PaxDb; P84098; -.
DR PRIDE; P84098; -.
DR DNASU; 6143; -.
DR Ensembl; ENST00000225430; ENSP00000225430; ENSG00000108298.
DR GeneID; 6143; -.
DR KEGG; hsa:6143; -.
DR UCSC; uc002hrq.1; human.
DR CTD; 6143; -.
DR GeneCards; GC17P037356; -.
DR HGNC; HGNC:10312; RPL19.
DR HPA; HPA043014; -.
DR MIM; 180466; gene.
DR neXtProt; NX_P84098; -.
DR PharmGKB; PA34681; -.
DR eggNOG; COG2147; -.
DR HOGENOM; HOG000231277; -.
DR HOVERGEN; HBG056059; -.
DR InParanoid; P84098; -.
DR KO; K02885; -.
DR OMA; YRDAGKI; -.
DR OrthoDB; EOG75B86V; -.
DR PhylomeDB; P84098; -.
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 GeneWiki; RPL19; -.
DR GenomeRNAi; 6143; -.
DR NextBio; 23865; -.
DR PRO; PR:P84098; -.
DR ArrayExpress; P84098; -.
DR Bgee; P84098; -.
DR CleanEx; HS_RPL19; -.
DR Genevestigator; P84098; -.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; TAS:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; NAS:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
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 Gene3D; 1.10.1200.60; -; 1.
DR Gene3D; 1.10.1650.10; -; 1.
DR InterPro; IPR027547; Ribosomal_L19/L19e.
DR InterPro; IPR023638; Ribosomal_L19/L19e_CS.
DR InterPro; IPR000196; Ribosomal_L19/L19e_dom.
DR InterPro; IPR015972; Ribosomal_L19/L19e_dom1.
DR InterPro; IPR015974; Ribosomal_L19/L19e_dom3.
DR Pfam; PF01280; Ribosomal_L19e; 1.
DR SUPFAM; SSF48140; SSF48140; 1.
DR PROSITE; PS00526; RIBOSOMAL_L19E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Direct protein sequencing;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT CHAIN 1 196 60S ribosomal protein L19.
FT /FTId=PRO_0000131169.
FT MOD_RES 13 13 Phosphoserine.
FT MOD_RES 187 187 Phosphothreonine.
SQ SEQUENCE 196 AA; 23466 MW; 4AF506393E526216 CRC64;
MSMLRLQKRL ASSVLRCGKK KVWLDPNETN EIANANSRQQ IRKLIKDGLI IRKPVTVHSR
ARCRKNTLAR RKGRHMGIGK RKGTANARMP EKVTWMRRMR ILRRLLRRYR ESKKIDRHMY
HSLYLKVKGN VFKNKRILME HIHKLKADKA RKKLLADQAE ARRSKTKEAR KRREERLQAK
KEEIIKTLSK EEETKK
//
ID RL19_HUMAN Reviewed; 196 AA.
AC P84098; B2R4K2; P14118; P22908; Q502Y6; Q7Z6E4;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-AUG-2004, sequence version 1.
DT 22-JAN-2014, entry version 97.
DE RecName: Full=60S ribosomal protein L19;
GN Name=RPL19;
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=1598220; DOI=10.1093/nar/20.10.2598;
RA Kumabe T., Schma Y., Yamamoto T.;
RT "Human cDNAs encoding elongation factor 1 gamma and the ribosomal
RT protein L19.";
RL Nucleic Acids Res. 20:2598-2598(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8095182;
RA Henry J.L., Coggin D.L., King C.R.;
RT "High-level expression of the ribosomal protein L19 in human breast
RT tumors that overexpress erbB-2.";
RL Cancer Res. 53:1403-1408(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Hypothalamus, and Muscle;
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 [6]
RP PROTEIN SEQUENCE OF 10-16; 22-38 AND 154-162, AND MASS SPECTROMETRY.
RC TISSUE=Lung carcinoma;
RA Bienvenut W.V., Vousden K.H., Lukashchuk N.;
RL Submitted (MAR-2008) to UniProtKB.
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND THR-187, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
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 [10]
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 -!- SIMILARITY: Belongs to the ribosomal protein L19e family.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD97677.1; Type=Erroneous initiation;
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; X63527; CAA45090.1; -; mRNA.
DR EMBL; S56985; AAB25672.1; -; mRNA.
DR EMBL; AK311858; BAG34799.1; -; mRNA.
DR EMBL; BX537435; CAD97677.1; ALT_INIT; mRNA.
DR EMBL; BC000530; AAH00530.1; -; mRNA.
DR EMBL; BC013016; AAH13016.1; -; mRNA.
DR EMBL; BC062709; AAH62709.1; -; mRNA.
DR EMBL; BC066315; AAH66315.1; -; mRNA.
DR EMBL; BC095445; AAH95445.1; -; mRNA.
DR PIR; A48992; A48992.
DR RefSeq; NP_000972.1; NM_000981.3.
DR UniGene; Hs.381061; -.
DR PDB; 3J3B; EM; 5.00 A; R=1-196.
DR PDBsum; 3J3B; -.
DR ProteinModelPortal; P84098; -.
DR SMR; P84098; 1-189.
DR IntAct; P84098; 18.
DR MINT; MINT-1815479; -.
DR STRING; 9606.ENSP00000225430; -.
DR PhosphoSite; P84098; -.
DR DMDM; 51338661; -.
DR PaxDb; P84098; -.
DR PRIDE; P84098; -.
DR DNASU; 6143; -.
DR Ensembl; ENST00000225430; ENSP00000225430; ENSG00000108298.
DR GeneID; 6143; -.
DR KEGG; hsa:6143; -.
DR UCSC; uc002hrq.1; human.
DR CTD; 6143; -.
DR GeneCards; GC17P037356; -.
DR HGNC; HGNC:10312; RPL19.
DR HPA; HPA043014; -.
DR MIM; 180466; gene.
DR neXtProt; NX_P84098; -.
DR PharmGKB; PA34681; -.
DR eggNOG; COG2147; -.
DR HOGENOM; HOG000231277; -.
DR HOVERGEN; HBG056059; -.
DR InParanoid; P84098; -.
DR KO; K02885; -.
DR OMA; YRDAGKI; -.
DR OrthoDB; EOG75B86V; -.
DR PhylomeDB; P84098; -.
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 GeneWiki; RPL19; -.
DR GenomeRNAi; 6143; -.
DR NextBio; 23865; -.
DR PRO; PR:P84098; -.
DR ArrayExpress; P84098; -.
DR Bgee; P84098; -.
DR CleanEx; HS_RPL19; -.
DR Genevestigator; P84098; -.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; TAS:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; NAS:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
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 Gene3D; 1.10.1200.60; -; 1.
DR Gene3D; 1.10.1650.10; -; 1.
DR InterPro; IPR027547; Ribosomal_L19/L19e.
DR InterPro; IPR023638; Ribosomal_L19/L19e_CS.
DR InterPro; IPR000196; Ribosomal_L19/L19e_dom.
DR InterPro; IPR015972; Ribosomal_L19/L19e_dom1.
DR InterPro; IPR015974; Ribosomal_L19/L19e_dom3.
DR Pfam; PF01280; Ribosomal_L19e; 1.
DR SUPFAM; SSF48140; SSF48140; 1.
DR PROSITE; PS00526; RIBOSOMAL_L19E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Direct protein sequencing;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT CHAIN 1 196 60S ribosomal protein L19.
FT /FTId=PRO_0000131169.
FT MOD_RES 13 13 Phosphoserine.
FT MOD_RES 187 187 Phosphothreonine.
SQ SEQUENCE 196 AA; 23466 MW; 4AF506393E526216 CRC64;
MSMLRLQKRL ASSVLRCGKK KVWLDPNETN EIANANSRQQ IRKLIKDGLI IRKPVTVHSR
ARCRKNTLAR RKGRHMGIGK RKGTANARMP EKVTWMRRMR ILRRLLRRYR ESKKIDRHMY
HSLYLKVKGN VFKNKRILME HIHKLKADKA RKKLLADQAE ARRSKTKEAR KRREERLQAK
KEEIIKTLSK EEETKK
//
MIM
180466
*RECORD*
*FIELD* NO
180466
*FIELD* TI
*180466 RIBOSOMAL PROTEIN L19; RPL19
*FIELD* TX
The ribosome is the only organelle conserved between prokaryotes and
read moreeukaryotes. In eukaryotes, this organelle consists of a 60S large
subunit and a 40S small subunit. The mammalian ribosome contains 4
species of RNA (see 180450) and approximately 80 different ribosomal
proteins, most of which appear to be present in equimolar amounts. In
mammalian cells, ribosomal proteins can account for up to 15% of the
total cellular protein, and the expression of the different ribosomal
protein genes, which can account for up to 7 to 9% of the total cellular
mRNAs, is coordinately regulated to meet the cell's varying requirements
for protein synthesis. The mammalian ribosomal protein genes are members
of multigene families, most of which are composed of multiple processed
pseudogenes and a single functional intron-containing gene. The presence
of multiple pseudogenes hampered the isolation and study of the
functional ribosomal protein genes. By study of somatic cell hybrids,
Nakamichi et al. (1986) had found that DNA sequences complementary to 6
mammalian ribosomal protein cDNAs could be assigned to chromosomes 5, 8,
and 17. Ten fragments mapped to 3 chromosomes. These are probably a
mixture of functional (expressed) genes and pseudogenes. One that maps
to 5q23-q33 rescues Chinese hamster emetine-resistance mutations in
interspecies hybrids and is therefore the transcriptionally active RPS14
gene (130620). Davies et al. (1989) described a PCR-based strategy for
the detection of intron-containing genes in the presence of multiple
pseudogenes. Feo et al. (1992) used this technique to identify the
intron-containing PCR products of 7 human ribosomal protein genes and to
map their chromosomal locations by hybridization to human/rodent somatic
cell hybrids. All 7 ribosomal protein genes were found to be on
different chromosomes: RPL19 on 17p12-q11; RPL30 (180467) on 8; RPL35A
(180468) on 18; RPL36A (180469) on 14; RPS6 (180460) on 9pter-p13; RPS11
(180471) on 19cen-qter; and RPS17 (180472) on 11pter-p13. These are also
different sites from the chromosomal location of previously mapped
ribosomal protein genes S14 on chromosome 5 (130620), S4 on Xq and Yp
(312760), and RPL7A on 9q3-q34 (185640). Davies and Fried (1995) used
fluorescence in situ hybridization to position the RPL19 gene to 17q11.
The wide distribution of the ribosomal protein genes throughout the
human genome suggests that coordinate regulation of their expression in
response to a cell's varying requirements for protein synthesis is not a
result of cis-activation of chromosomal regions but is mediated by
trans-acting factors.
*FIELD* RF
1. Davies, B.; Feo, S.; Heard, E.; Fried, M.: A strategy to detect
and isolate an intron-containing gene in the presence of multiple
processed pseudogenes. Proc. Nat. Acad. Sci. 86: 6691-6695, 1989.
2. Davies, B.; Fried, M.: The L19 ribosomal protein gene (RPL19):
gene organization, chromosomal mapping, and novel promoter region. Genomics 25:
372-380, 1995.
3. Feo, S.; Davies, B.; Fried, M.: The mapping of seven intron-containing
ribosomal protein genes shows they are unlinked in the human genome. Genomics 13:
201-207, 1992.
4. Nakamichi, N. N.; Kao, F.-T.; Wasmuth, J.; Roufa, D. J.: Ribosomal
protein gene sequences map to human chromosomes 5, 8, and 17. Somat.
Cell Molec. Genet. 12: 225-236, 1986.
*FIELD* CD
Victor A. McKusick: 6/6/1992
*FIELD* ED
alopez: 06/21/2007
psherman: 9/9/1999
terry: 3/7/1995
carol: 6/6/1992
*RECORD*
*FIELD* NO
180466
*FIELD* TI
*180466 RIBOSOMAL PROTEIN L19; RPL19
*FIELD* TX
The ribosome is the only organelle conserved between prokaryotes and
read moreeukaryotes. In eukaryotes, this organelle consists of a 60S large
subunit and a 40S small subunit. The mammalian ribosome contains 4
species of RNA (see 180450) and approximately 80 different ribosomal
proteins, most of which appear to be present in equimolar amounts. In
mammalian cells, ribosomal proteins can account for up to 15% of the
total cellular protein, and the expression of the different ribosomal
protein genes, which can account for up to 7 to 9% of the total cellular
mRNAs, is coordinately regulated to meet the cell's varying requirements
for protein synthesis. The mammalian ribosomal protein genes are members
of multigene families, most of which are composed of multiple processed
pseudogenes and a single functional intron-containing gene. The presence
of multiple pseudogenes hampered the isolation and study of the
functional ribosomal protein genes. By study of somatic cell hybrids,
Nakamichi et al. (1986) had found that DNA sequences complementary to 6
mammalian ribosomal protein cDNAs could be assigned to chromosomes 5, 8,
and 17. Ten fragments mapped to 3 chromosomes. These are probably a
mixture of functional (expressed) genes and pseudogenes. One that maps
to 5q23-q33 rescues Chinese hamster emetine-resistance mutations in
interspecies hybrids and is therefore the transcriptionally active RPS14
gene (130620). Davies et al. (1989) described a PCR-based strategy for
the detection of intron-containing genes in the presence of multiple
pseudogenes. Feo et al. (1992) used this technique to identify the
intron-containing PCR products of 7 human ribosomal protein genes and to
map their chromosomal locations by hybridization to human/rodent somatic
cell hybrids. All 7 ribosomal protein genes were found to be on
different chromosomes: RPL19 on 17p12-q11; RPL30 (180467) on 8; RPL35A
(180468) on 18; RPL36A (180469) on 14; RPS6 (180460) on 9pter-p13; RPS11
(180471) on 19cen-qter; and RPS17 (180472) on 11pter-p13. These are also
different sites from the chromosomal location of previously mapped
ribosomal protein genes S14 on chromosome 5 (130620), S4 on Xq and Yp
(312760), and RPL7A on 9q3-q34 (185640). Davies and Fried (1995) used
fluorescence in situ hybridization to position the RPL19 gene to 17q11.
The wide distribution of the ribosomal protein genes throughout the
human genome suggests that coordinate regulation of their expression in
response to a cell's varying requirements for protein synthesis is not a
result of cis-activation of chromosomal regions but is mediated by
trans-acting factors.
*FIELD* RF
1. Davies, B.; Feo, S.; Heard, E.; Fried, M.: A strategy to detect
and isolate an intron-containing gene in the presence of multiple
processed pseudogenes. Proc. Nat. Acad. Sci. 86: 6691-6695, 1989.
2. Davies, B.; Fried, M.: The L19 ribosomal protein gene (RPL19):
gene organization, chromosomal mapping, and novel promoter region. Genomics 25:
372-380, 1995.
3. Feo, S.; Davies, B.; Fried, M.: The mapping of seven intron-containing
ribosomal protein genes shows they are unlinked in the human genome. Genomics 13:
201-207, 1992.
4. Nakamichi, N. N.; Kao, F.-T.; Wasmuth, J.; Roufa, D. J.: Ribosomal
protein gene sequences map to human chromosomes 5, 8, and 17. Somat.
Cell Molec. Genet. 12: 225-236, 1986.
*FIELD* CD
Victor A. McKusick: 6/6/1992
*FIELD* ED
alopez: 06/21/2007
psherman: 9/9/1999
terry: 3/7/1995
carol: 6/6/1992