Full text data of RPL8
RPL8
[Confidence: low (only semi-automatic identification from reviews)]
60S ribosomal protein L8
Note: presumably soluble (membrane word is not in UniProt keywords or features)
60S ribosomal protein L8
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P62917
ID RL8_HUMAN Reviewed; 257 AA.
AC P62917; A8K094; D3DWN2; P25120; Q567Q7; Q969V7; Q9BWQ9;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 102.
DE RecName: Full=60S ribosomal protein L8;
GN Name=RPL8;
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].
RC TISSUE=Ovary;
RX PubMed=7506540; DOI=10.1006/bbrc.1993.2607;
RA Hanes J., Klaudiny J., von der Kammer H., Scheit K.H.;
RT "Characterization by cDNA cloning of the mRNA of human ribosomal
RT protein L8.";
RL Biochem. Biophys. Res. Commun. 197:1223-1228(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11875025; DOI=10.1101/gr.214202;
RA Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S.,
RA Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.;
RT "The human ribosomal protein genes: sequencing and comparative
RT analysis of 73 genes.";
RL Genome Res. 12:379-390(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-98.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-98.
RC TISSUE=Kidney, Placenta, Skin, and Spinal cord;
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 [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-134.
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 [9]
RP PROTEIN SEQUENCE OF 2-11, AND MASS SPECTROMETRY.
RX PubMed=12962325; DOI=10.1023/A:1025068419698;
RA Odintsova T.I., Muller E.C., Ivanov A.V., Egorov T.A., Bienert R.,
RA Vladimirov S.N., Kostka S., Otto A., Wittmann-Liebold B.,
RA Karpova G.G.;
RT "Characterization and analysis of posttranslational modifications of
RT the human large cytoplasmic ribosomal subunit proteins by mass
RT spectrometry and Edman sequencing.";
RL J. Protein Chem. 22:249-258(2003).
RN [10]
RP PROTEIN REPLACEMENT STUDIES IN E.COLI, AND MUTAGENESIS.
RX PubMed=9531480;
RA Uehlein M., Wegloehner W., Urlaub H., Wittmann-Liebold B.;
RT "Functional implications of ribosomal protein L2 in protein
RT biosynthesis as shown by in vivo replacement studies.";
RL Biochem. J. 331:423-430(1998).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [12]
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 [13]
RP HYDROXYLATION AT HIS-216 BY NO66.
RX PubMed=23103944; DOI=10.1038/nchembio.1093;
RA Ge W., Wolf A., Feng T., Ho C.H., Sekirnik R., Zayer A., Granatino N.,
RA Cockman M.E., Loenarz C., Loik N.D., Hardy A.P., Claridge T.D.,
RA Hamed R.B., Chowdhury R., Gong L., Robinson C.V., Trudgian D.C.,
RA Jiang M., Mackeen M.M., McCullagh J.S., Gordiyenko Y., Thalhammer A.,
RA Yamamoto A., Yang M., Liu-Yi P., Zhang Z., Schmidt-Zachmann M.,
RA Kessler B.M., Ratcliffe P.J., Preston G.M., Coleman M.L.,
RA Schofield C.J.;
RT "Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and
RT humans.";
RL Nat. Chem. Biol. 8:960-962(2012).
RN [14]
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 -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- PTM: Hydroxylated on His-216 by NO66. The modification is impaired
CC by hypoxia.
CC -!- MISCELLANEOUS: This protein can be partially incorporated into
CC E.coli polysomes in vivo, indicating it can replace the endogenous
CC protein.
CC -!- SIMILARITY: Belongs to the ribosomal protein L2P family.
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DR EMBL; Z28407; CAA82248.1; -; mRNA.
DR EMBL; AB061821; BAB79459.1; -; Genomic_DNA.
DR EMBL; BT007379; AAP36043.1; -; mRNA.
DR EMBL; CR457046; CAG33327.1; -; mRNA.
DR EMBL; AK289459; BAF82148.1; -; mRNA.
DR EMBL; CH471162; EAW82048.1; -; Genomic_DNA.
DR EMBL; CH471162; EAW82051.1; -; Genomic_DNA.
DR EMBL; CH471162; EAW82052.1; -; Genomic_DNA.
DR EMBL; BC000047; AAH00047.2; -; mRNA.
DR EMBL; BC000077; AAH00077.1; -; mRNA.
DR EMBL; BC012197; AAH12197.1; -; mRNA.
DR EMBL; BC013104; AAH13104.1; -; mRNA.
DR EMBL; BC093064; AAH93064.1; -; mRNA.
DR EMBL; AB007168; BAA25829.1; -; Genomic_DNA.
DR PIR; JN0923; JN0923.
DR RefSeq; NP_000964.1; NM_000973.3.
DR RefSeq; NP_150644.1; NM_033301.1.
DR RefSeq; XP_005272389.1; XM_005272332.1.
DR UniGene; Hs.178551; -.
DR PDB; 3J3B; EM; 5.00 A; A=1-257.
DR PDBsum; 3J3B; -.
DR ProteinModelPortal; P62917; -.
DR SMR; P62917; 2-256.
DR IntAct; P62917; 33.
DR MINT; MINT-1135693; -.
DR STRING; 9606.ENSP00000262584; -.
DR PhosphoSite; P62917; -.
DR DMDM; 51702823; -.
DR PaxDb; P62917; -.
DR PRIDE; P62917; -.
DR DNASU; 6132; -.
DR Ensembl; ENST00000262584; ENSP00000262584; ENSG00000161016.
DR Ensembl; ENST00000394920; ENSP00000378378; ENSG00000161016.
DR Ensembl; ENST00000528957; ENSP00000433464; ENSG00000161016.
DR GeneID; 6132; -.
DR KEGG; hsa:6132; -.
DR UCSC; uc003zeb.3; human.
DR CTD; 6132; -.
DR GeneCards; GC08M145985; -.
DR HGNC; HGNC:10368; RPL8.
DR HPA; HPA045095; -.
DR HPA; HPA050165; -.
DR MIM; 604177; gene.
DR neXtProt; NX_P62917; -.
DR PharmGKB; PA34768; -.
DR eggNOG; COG0090; -.
DR HOVERGEN; HBG079431; -.
DR InParanoid; P62917; -.
DR KO; K02938; -.
DR OMA; AHNPDTK; -.
DR PhylomeDB; P62917; -.
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; RPL8; human.
DR GeneWiki; RPL8; -.
DR GenomeRNAi; 6132; -.
DR NextBio; 23815; -.
DR PRO; PR:P62917; -.
DR ArrayExpress; P62917; -.
DR Bgee; P62917; -.
DR CleanEx; HS_RPL8; -.
DR Genevestigator; P62917; -.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
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; 2.30.30.30; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 4.10.950.10; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR022666; Rbsml_prot_L2_RNA-bd_dom.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR002171; Ribosomal_L2.
DR InterPro; IPR023672; Ribosomal_L2_arc.
DR InterPro; IPR022669; Ribosomal_L2_C.
DR InterPro; IPR022671; Ribosomal_L2_CS.
DR InterPro; IPR014726; Ribosomal_L2_dom3.
DR InterPro; IPR008991; Translation_prot_SH3-like.
DR PANTHER; PTHR13691; PTHR13691; 1.
DR Pfam; PF00181; Ribosomal_L2; 1.
DR Pfam; PF03947; Ribosomal_L2_C; 1.
DR PIRSF; PIRSF002158; Ribosomal_L2; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR PROSITE; PS00467; RIBOSOMAL_L2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Hydroxylation; Polymorphism; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 257 60S ribosomal protein L8.
FT /FTId=PRO_0000129743.
FT MOD_RES 216 216 (3S)-3-hydroxyhistidine.
FT VARIANT 98 98 I -> V (in dbSNP:rs17850886).
FT /FTId=VAR_019658.
FT MUTAGEN 209 209 H->A,G: No incorporation into translating
FT E.coli polysomes; ribosomes assembled
FT normally. Significantly reduced
FT translational activity.
SQ SEQUENCE 257 AA; 28025 MW; CE1610449749318B CRC64;
MGRVIRGQRK GAGSVFRAHV KHRKGAARLR AVDFAERHGY IKGIVKDIIH DPGRGAPLAK
VVFRDPYRFK KRTELFIAAE GIHTGQFVYC GKKAQLNIGN VLPVGTMPEG TIVCCLEEKP
GDRGKLARAS GNYATVISHN PETKKTRVKL PSGSKKVISS ANRAVVGVVA GGGRIDKPIL
KAGRAYHKYK AKRNCWPRVR GVAMNPVEHP FGGGNHQHIG KPSTIRRDAP AGRKVGLIAA
RRTGRLRGTK TVQEKEN
//
ID RL8_HUMAN Reviewed; 257 AA.
AC P62917; A8K094; D3DWN2; P25120; Q567Q7; Q969V7; Q9BWQ9;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 102.
DE RecName: Full=60S ribosomal protein L8;
GN Name=RPL8;
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].
RC TISSUE=Ovary;
RX PubMed=7506540; DOI=10.1006/bbrc.1993.2607;
RA Hanes J., Klaudiny J., von der Kammer H., Scheit K.H.;
RT "Characterization by cDNA cloning of the mRNA of human ribosomal
RT protein L8.";
RL Biochem. Biophys. Res. Commun. 197:1223-1228(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11875025; DOI=10.1101/gr.214202;
RA Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S.,
RA Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.;
RT "The human ribosomal protein genes: sequencing and comparative
RT analysis of 73 genes.";
RL Genome Res. 12:379-390(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-98.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-98.
RC TISSUE=Kidney, Placenta, Skin, and Spinal cord;
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 [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-134.
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 [9]
RP PROTEIN SEQUENCE OF 2-11, AND MASS SPECTROMETRY.
RX PubMed=12962325; DOI=10.1023/A:1025068419698;
RA Odintsova T.I., Muller E.C., Ivanov A.V., Egorov T.A., Bienert R.,
RA Vladimirov S.N., Kostka S., Otto A., Wittmann-Liebold B.,
RA Karpova G.G.;
RT "Characterization and analysis of posttranslational modifications of
RT the human large cytoplasmic ribosomal subunit proteins by mass
RT spectrometry and Edman sequencing.";
RL J. Protein Chem. 22:249-258(2003).
RN [10]
RP PROTEIN REPLACEMENT STUDIES IN E.COLI, AND MUTAGENESIS.
RX PubMed=9531480;
RA Uehlein M., Wegloehner W., Urlaub H., Wittmann-Liebold B.;
RT "Functional implications of ribosomal protein L2 in protein
RT biosynthesis as shown by in vivo replacement studies.";
RL Biochem. J. 331:423-430(1998).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [12]
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 [13]
RP HYDROXYLATION AT HIS-216 BY NO66.
RX PubMed=23103944; DOI=10.1038/nchembio.1093;
RA Ge W., Wolf A., Feng T., Ho C.H., Sekirnik R., Zayer A., Granatino N.,
RA Cockman M.E., Loenarz C., Loik N.D., Hardy A.P., Claridge T.D.,
RA Hamed R.B., Chowdhury R., Gong L., Robinson C.V., Trudgian D.C.,
RA Jiang M., Mackeen M.M., McCullagh J.S., Gordiyenko Y., Thalhammer A.,
RA Yamamoto A., Yang M., Liu-Yi P., Zhang Z., Schmidt-Zachmann M.,
RA Kessler B.M., Ratcliffe P.J., Preston G.M., Coleman M.L.,
RA Schofield C.J.;
RT "Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and
RT humans.";
RL Nat. Chem. Biol. 8:960-962(2012).
RN [14]
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 -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- PTM: Hydroxylated on His-216 by NO66. The modification is impaired
CC by hypoxia.
CC -!- MISCELLANEOUS: This protein can be partially incorporated into
CC E.coli polysomes in vivo, indicating it can replace the endogenous
CC protein.
CC -!- SIMILARITY: Belongs to the ribosomal protein L2P family.
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DR EMBL; Z28407; CAA82248.1; -; mRNA.
DR EMBL; AB061821; BAB79459.1; -; Genomic_DNA.
DR EMBL; BT007379; AAP36043.1; -; mRNA.
DR EMBL; CR457046; CAG33327.1; -; mRNA.
DR EMBL; AK289459; BAF82148.1; -; mRNA.
DR EMBL; CH471162; EAW82048.1; -; Genomic_DNA.
DR EMBL; CH471162; EAW82051.1; -; Genomic_DNA.
DR EMBL; CH471162; EAW82052.1; -; Genomic_DNA.
DR EMBL; BC000047; AAH00047.2; -; mRNA.
DR EMBL; BC000077; AAH00077.1; -; mRNA.
DR EMBL; BC012197; AAH12197.1; -; mRNA.
DR EMBL; BC013104; AAH13104.1; -; mRNA.
DR EMBL; BC093064; AAH93064.1; -; mRNA.
DR EMBL; AB007168; BAA25829.1; -; Genomic_DNA.
DR PIR; JN0923; JN0923.
DR RefSeq; NP_000964.1; NM_000973.3.
DR RefSeq; NP_150644.1; NM_033301.1.
DR RefSeq; XP_005272389.1; XM_005272332.1.
DR UniGene; Hs.178551; -.
DR PDB; 3J3B; EM; 5.00 A; A=1-257.
DR PDBsum; 3J3B; -.
DR ProteinModelPortal; P62917; -.
DR SMR; P62917; 2-256.
DR IntAct; P62917; 33.
DR MINT; MINT-1135693; -.
DR STRING; 9606.ENSP00000262584; -.
DR PhosphoSite; P62917; -.
DR DMDM; 51702823; -.
DR PaxDb; P62917; -.
DR PRIDE; P62917; -.
DR DNASU; 6132; -.
DR Ensembl; ENST00000262584; ENSP00000262584; ENSG00000161016.
DR Ensembl; ENST00000394920; ENSP00000378378; ENSG00000161016.
DR Ensembl; ENST00000528957; ENSP00000433464; ENSG00000161016.
DR GeneID; 6132; -.
DR KEGG; hsa:6132; -.
DR UCSC; uc003zeb.3; human.
DR CTD; 6132; -.
DR GeneCards; GC08M145985; -.
DR HGNC; HGNC:10368; RPL8.
DR HPA; HPA045095; -.
DR HPA; HPA050165; -.
DR MIM; 604177; gene.
DR neXtProt; NX_P62917; -.
DR PharmGKB; PA34768; -.
DR eggNOG; COG0090; -.
DR HOVERGEN; HBG079431; -.
DR InParanoid; P62917; -.
DR KO; K02938; -.
DR OMA; AHNPDTK; -.
DR PhylomeDB; P62917; -.
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; RPL8; human.
DR GeneWiki; RPL8; -.
DR GenomeRNAi; 6132; -.
DR NextBio; 23815; -.
DR PRO; PR:P62917; -.
DR ArrayExpress; P62917; -.
DR Bgee; P62917; -.
DR CleanEx; HS_RPL8; -.
DR Genevestigator; P62917; -.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
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; 2.30.30.30; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 4.10.950.10; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR022666; Rbsml_prot_L2_RNA-bd_dom.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR002171; Ribosomal_L2.
DR InterPro; IPR023672; Ribosomal_L2_arc.
DR InterPro; IPR022669; Ribosomal_L2_C.
DR InterPro; IPR022671; Ribosomal_L2_CS.
DR InterPro; IPR014726; Ribosomal_L2_dom3.
DR InterPro; IPR008991; Translation_prot_SH3-like.
DR PANTHER; PTHR13691; PTHR13691; 1.
DR Pfam; PF00181; Ribosomal_L2; 1.
DR Pfam; PF03947; Ribosomal_L2_C; 1.
DR PIRSF; PIRSF002158; Ribosomal_L2; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR PROSITE; PS00467; RIBOSOMAL_L2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Hydroxylation; Polymorphism; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 257 60S ribosomal protein L8.
FT /FTId=PRO_0000129743.
FT MOD_RES 216 216 (3S)-3-hydroxyhistidine.
FT VARIANT 98 98 I -> V (in dbSNP:rs17850886).
FT /FTId=VAR_019658.
FT MUTAGEN 209 209 H->A,G: No incorporation into translating
FT E.coli polysomes; ribosomes assembled
FT normally. Significantly reduced
FT translational activity.
SQ SEQUENCE 257 AA; 28025 MW; CE1610449749318B CRC64;
MGRVIRGQRK GAGSVFRAHV KHRKGAARLR AVDFAERHGY IKGIVKDIIH DPGRGAPLAK
VVFRDPYRFK KRTELFIAAE GIHTGQFVYC GKKAQLNIGN VLPVGTMPEG TIVCCLEEKP
GDRGKLARAS GNYATVISHN PETKKTRVKL PSGSKKVISS ANRAVVGVVA GGGRIDKPIL
KAGRAYHKYK AKRNCWPRVR GVAMNPVEHP FGGGNHQHIG KPSTIRRDAP AGRKVGLIAA
RRTGRLRGTK TVQEKEN
//
MIM
604177
*RECORD*
*FIELD* NO
604177
*FIELD* TI
*604177 RIBOSOMAL PROTEIN L8; RPL8
*FIELD* TX
The mammalian ribosome is composed of 4 RNA species (see 180450) and
read moreapproximately 80 different proteins (see 180466).
The rat ribosomal protein L8 (Rpl8) associates with 5.8S rRNA, very
likely participates in the binding of aminoacyl-tRNA, and has been
identified as a constituent of the EF2 (130610)-binding site at the
ribosomal subunit interface. By screening a human ovarian granulosa cell
cDNA expression library with antibodies against human follicular fluid
glycoproteins, Hanes et al. (1993) isolated a partial RPL8 cDNA. They
completed the full-length cDNA sequence using PCR. The deduced 257-amino
acid human RPL8 protein is identical to rat Rpl8. Northern blot analysis
detected a 900-bp RPL8 transcript in human granulosa cells and white
blood cells.
By somatic cell hybrid and radiation hybrid mapping analyses, Kenmochi
et al. (1998) mapped the human RPL8 gene to 8q.
*FIELD* RF
1. Hanes, J.; Klaudiny, J.; von der Kammer, H.; Scheit, K. H.: Characterization
by cDNA cloning of the mRNA of human ribosomal protein L8. Biochem.
Biophys. Res. Commun. 197: 1223-1228, 1993.
2. Kenmochi, N.; Kawaguchi, T.; Rozen, S.; Davis, E.; Goodman, N.;
Hudson, T. J.; Tanaka, T.; Page, D. C.: A map of 75 human ribosomal
protein genes. Genome Res. 8: 509-523, 1998.
*FIELD* CD
Patti M. Sherman: 9/21/1999
*FIELD* ED
mgross: 09/23/1999
psherman: 9/22/1999
*RECORD*
*FIELD* NO
604177
*FIELD* TI
*604177 RIBOSOMAL PROTEIN L8; RPL8
*FIELD* TX
The mammalian ribosome is composed of 4 RNA species (see 180450) and
read moreapproximately 80 different proteins (see 180466).
The rat ribosomal protein L8 (Rpl8) associates with 5.8S rRNA, very
likely participates in the binding of aminoacyl-tRNA, and has been
identified as a constituent of the EF2 (130610)-binding site at the
ribosomal subunit interface. By screening a human ovarian granulosa cell
cDNA expression library with antibodies against human follicular fluid
glycoproteins, Hanes et al. (1993) isolated a partial RPL8 cDNA. They
completed the full-length cDNA sequence using PCR. The deduced 257-amino
acid human RPL8 protein is identical to rat Rpl8. Northern blot analysis
detected a 900-bp RPL8 transcript in human granulosa cells and white
blood cells.
By somatic cell hybrid and radiation hybrid mapping analyses, Kenmochi
et al. (1998) mapped the human RPL8 gene to 8q.
*FIELD* RF
1. Hanes, J.; Klaudiny, J.; von der Kammer, H.; Scheit, K. H.: Characterization
by cDNA cloning of the mRNA of human ribosomal protein L8. Biochem.
Biophys. Res. Commun. 197: 1223-1228, 1993.
2. Kenmochi, N.; Kawaguchi, T.; Rozen, S.; Davis, E.; Goodman, N.;
Hudson, T. J.; Tanaka, T.; Page, D. C.: A map of 75 human ribosomal
protein genes. Genome Res. 8: 509-523, 1998.
*FIELD* CD
Patti M. Sherman: 9/21/1999
*FIELD* ED
mgross: 09/23/1999
psherman: 9/22/1999