RL8_HUMAN
ID RL8_HUMAN Reviewed; 257 AA.
AC P62917; A8K094; D3DWN2; P25120; Q567Q7; Q969V7; Q9BWQ9;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=60S ribosomal protein L8;
DE AltName: Full=Large ribosomal subunit protein uL2 {ECO:0000303|PubMed:24524803};
GN Name=RPL8;
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].
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 protein
RT 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 analysis of
RT 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 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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; 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 [9]
RP PROTEIN SEQUENCE OF 2-11, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP AND SUBUNIT.
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., Karpova G.G.;
RT "Characterization and analysis of posttranslational modifications of the
RT human large cytoplasmic ribosomal subunit proteins by mass spectrometry and
RT Edman sequencing.";
RL J. Protein Chem. 22:249-258(2003).
RN [10]
RP PROTEIN REPLACEMENT STUDIES IN E.COLI, AND MUTAGENESIS.
RX PubMed=9531480; DOI=10.1042/bj3310423;
RA Uehlein M., Wegloehner W., Urlaub H., Wittmann-Liebold B.;
RT "Functional implications of ribosomal protein L2 in protein biosynthesis as
RT shown by in vivo replacement studies.";
RL Biochem. J. 331:423-430(1998).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [12]
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 cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [13]
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 [14]
RP HYDROXYLATION AT HIS-216 BY RIOX1.
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., Hamed R.B.,
RA Chowdhury R., Gong L., Robinson C.V., Trudgian D.C., Jiang M.,
RA Mackeen M.M., McCullagh J.S., Gordiyenko Y., Thalhammer A., Yamamoto A.,
RA Yang M., Liu-Yi P., Zhang Z., Schmidt-Zachmann M., Kessler B.M.,
RA Ratcliffe P.J., Preston G.M., Coleman M.L., Schofield C.J.;
RT "Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and
RT humans.";
RL Nat. Chem. Biol. 8:960-962(2012).
RN [15]
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 [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
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 [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-42; LYS-149; LYS-234 AND LYS-250,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [19]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
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).
RN [20] {ECO:0007744|PDB:6LQM, ECO:0007744|PDB:6LSR, ECO:0007744|PDB:6LSS, ECO:0007744|PDB:6LU8}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.09 ANGSTROMS), FUNCTION, AND SUBUNIT.
RX PubMed=32669547; DOI=10.1038/s41467-020-17237-x;
RA Liang X., Zuo M.Q., Zhang Y., Li N., Ma C., Dong M.Q., Gao N.;
RT "Structural snapshots of human pre-60S ribosomal particles before and after
RT nuclear export.";
RL Nat. Commun. 11:3542-3542(2020).
CC -!- FUNCTION: Component of the large ribosomal subunit. The ribosome is a
CC large ribonucleoprotein complex responsible for the synthesis of
CC proteins in the cell. {ECO:0000269|PubMed:23636399,
CC ECO:0000269|PubMed:32669547, ECO:0000305|PubMed:12962325}.
CC -!- SUBUNIT: Component of the large ribosomal subunit (PubMed:23636399,
CC PubMed:32669547). Interacts with CRY1 (By similarity).
CC {ECO:0000250|UniProtKB:P62918, ECO:0000269|PubMed:23636399,
CC ECO:0000269|PubMed:32669547, ECO:0000305|PubMed:12962325}.
CC -!- INTERACTION:
CC P62917; Q99558: MAP3K14; NbExp=3; IntAct=EBI-438527, EBI-358011;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399}.
CC -!- PTM: Hydroxylated on His-216 by RIOX1. The modification is impaired by
CC hypoxia. {ECO:0000269|PubMed:23103944}.
CC -!- MISCELLANEOUS: This protein can be partially incorporated into E.coli
CC polysomes in vivo, indicating it can replace the endogenous protein.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL2 family.
CC {ECO:0000305}.
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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 CCDS; CCDS6433.1; -.
DR PIR; JN0923; JN0923.
DR RefSeq; NP_000964.1; NM_000973.4.
DR RefSeq; NP_001304700.1; NM_001317771.1.
DR RefSeq; NP_001304711.1; NM_001317782.1.
DR RefSeq; NP_150644.1; NM_033301.2.
DR PDB; 4CCM; X-ray; 2.51 A; C/D=205-239.
DR PDB; 4CCN; X-ray; 2.23 A; C/D=205-239.
DR PDB; 4CCO; X-ray; 2.30 A; C/D=205-224.
DR PDB; 4UG0; EM; -; LA=1-257.
DR PDB; 4V6X; EM; 5.00 A; CA=1-257.
DR PDB; 4Y3O; X-ray; 2.20 A; C/D=212-222.
DR PDB; 5AJ0; EM; 3.50 A; AA=1-257.
DR PDB; 5LKS; EM; 3.60 A; LA=1-257.
DR PDB; 5T2C; EM; 3.60 A; D=1-257.
DR PDB; 6IP5; EM; 3.90 A; 1D=1-257.
DR PDB; 6IP6; EM; 4.50 A; 1D=1-257.
DR PDB; 6IP8; EM; 3.90 A; 1D=1-257.
DR PDB; 6LQM; EM; 3.09 A; m=1-257.
DR PDB; 6LSR; EM; 3.13 A; m=1-257.
DR PDB; 6LSS; EM; 3.23 A; m=1-257.
DR PDB; 6LU8; EM; 3.13 A; m=1-257.
DR PDB; 6OLE; EM; 3.10 A; A=2-253.
DR PDB; 6OLF; EM; 3.90 A; A=2-253.
DR PDB; 6OLG; EM; 3.40 A; AA=1-257.
DR PDB; 6OLI; EM; 3.50 A; A=2-253.
DR PDB; 6OLZ; EM; 3.90 A; AA=2-249.
DR PDB; 6OM0; EM; 3.10 A; A=2-253.
DR PDB; 6OM7; EM; 3.70 A; A=2-253.
DR PDB; 6QZP; EM; 2.90 A; LA=2-249.
DR PDB; 6W6L; EM; 3.84 A; A=1-257.
DR PDB; 6XA1; EM; 2.80 A; LA=2-249.
DR PDB; 6Y0G; EM; 3.20 A; LA=1-257.
DR PDB; 6Y2L; EM; 3.00 A; LA=1-257.
DR PDB; 6Y57; EM; 3.50 A; LA=1-257.
DR PDB; 6Y6X; EM; 2.80 A; LA=2-249.
DR PDB; 6Z6L; EM; 3.00 A; LA=1-257.
DR PDB; 6Z6M; EM; 3.10 A; LA=1-257.
DR PDB; 6Z6N; EM; 2.90 A; LA=1-257.
DR PDB; 6ZM7; EM; 2.70 A; LA=1-257.
DR PDB; 6ZME; EM; 3.00 A; LA=1-257.
DR PDB; 6ZMI; EM; 2.60 A; LA=1-257.
DR PDB; 6ZMO; EM; 3.10 A; LA=1-257.
DR PDB; 7BHP; EM; 3.30 A; LA=1-257.
DR PDBsum; 4CCM; -.
DR PDBsum; 4CCN; -.
DR PDBsum; 4CCO; -.
DR PDBsum; 4UG0; -.
DR PDBsum; 4V6X; -.
DR PDBsum; 4Y3O; -.
DR PDBsum; 5AJ0; -.
DR PDBsum; 5LKS; -.
DR PDBsum; 5T2C; -.
DR PDBsum; 6IP5; -.
DR PDBsum; 6IP6; -.
DR PDBsum; 6IP8; -.
DR PDBsum; 6LQM; -.
DR PDBsum; 6LSR; -.
DR PDBsum; 6LSS; -.
DR PDBsum; 6LU8; -.
DR PDBsum; 6OLE; -.
DR PDBsum; 6OLF; -.
DR PDBsum; 6OLG; -.
DR PDBsum; 6OLI; -.
DR PDBsum; 6OLZ; -.
DR PDBsum; 6OM0; -.
DR PDBsum; 6OM7; -.
DR PDBsum; 6QZP; -.
DR PDBsum; 6W6L; -.
DR PDBsum; 6XA1; -.
DR PDBsum; 6Y0G; -.
DR PDBsum; 6Y2L; -.
DR PDBsum; 6Y57; -.
DR PDBsum; 6Y6X; -.
DR PDBsum; 6Z6L; -.
DR PDBsum; 6Z6M; -.
DR PDBsum; 6Z6N; -.
DR PDBsum; 6ZM7; -.
DR PDBsum; 6ZME; -.
DR PDBsum; 6ZMI; -.
DR PDBsum; 6ZMO; -.
DR PDBsum; 7BHP; -.
DR AlphaFoldDB; P62917; -.
DR SMR; P62917; -.
DR BioGRID; 112052; 454.
DR ComplexPortal; CPX-5183; 60S cytosolic large ribosomal subunit.
DR CORUM; P62917; -.
DR DIP; DIP-37967N; -.
DR IntAct; P62917; 134.
DR MINT; P62917; -.
DR STRING; 9606.ENSP00000262584; -.
DR DrugBank; DB02494; (S)-3-phenyllactic acid.
DR DrugBank; DB07374; Anisomycin.
DR DrugBank; DB08437; Puromycin.
DR GlyGen; P62917; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P62917; -.
DR MetOSite; P62917; -.
DR PhosphoSitePlus; P62917; -.
DR SwissPalm; P62917; -.
DR BioMuta; RPL8; -.
DR DMDM; 51702823; -.
DR EPD; P62917; -.
DR jPOST; P62917; -.
DR MassIVE; P62917; -.
DR MaxQB; P62917; -.
DR PaxDb; P62917; -.
DR PeptideAtlas; P62917; -.
DR PRIDE; P62917; -.
DR ProteomicsDB; 57454; -.
DR TopDownProteomics; P62917; -.
DR Antibodypedia; 14991; 300 antibodies from 32 providers.
DR DNASU; 6132; -.
DR Ensembl; ENST00000262584.7; ENSP00000262584.3; ENSG00000161016.18.
DR Ensembl; ENST00000394920.6; ENSP00000378378.2; ENSG00000161016.18.
DR Ensembl; ENST00000528957.6; ENSP00000433464.2; ENSG00000161016.18.
DR GeneID; 6132; -.
DR KEGG; hsa:6132; -.
DR MANE-Select; ENST00000528957.6; ENSP00000433464.2; NM_001317782.2; NP_001304711.1.
DR UCSC; uc003zeb.4; human.
DR CTD; 6132; -.
DR DisGeNET; 6132; -.
DR GeneCards; RPL8; -.
DR HGNC; HGNC:10368; RPL8.
DR HPA; ENSG00000161016; Low tissue specificity.
DR MIM; 604177; gene.
DR neXtProt; NX_P62917; -.
DR OpenTargets; ENSG00000161016; -.
DR PharmGKB; PA34768; -.
DR VEuPathDB; HostDB:ENSG00000161016; -.
DR eggNOG; KOG2309; Eukaryota.
DR GeneTree; ENSGT00940000153244; -.
DR InParanoid; P62917; -.
DR OMA; SCIELRP; -.
DR OrthoDB; 1156335at2759; -.
DR PhylomeDB; P62917; -.
DR TreeFam; TF300748; -.
DR PathwayCommons; P62917; -.
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-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; P62917; -.
DR SIGNOR; P62917; -.
DR BioGRID-ORCS; 6132; 828 hits in 1073 CRISPR screens.
DR ChiTaRS; RPL8; human.
DR GeneWiki; RPL8; -.
DR GenomeRNAi; 6132; -.
DR Pharos; P62917; Tbio.
DR PRO; PR:P62917; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P62917; protein.
DR Bgee; ENSG00000161016; Expressed in oviduct epithelium and 114 other tissues.
DR ExpressionAtlas; P62917; baseline and differential.
DR Genevisible; P62917; HS.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0042788; C:polysomal ribosome; IDA:UniProtKB.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0002181; P:cytoplasmic translation; IDA:UniProtKB.
DR GO; GO:0006412; P:translation; TAS:ProtInc.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 4.10.950.10; -; 1.
DR HAMAP; MF_01320_A; Ribosomal_L2_A; 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_sf.
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 SMART; SM01383; Ribosomal_L2; 1.
DR SMART; SM01382; Ribosomal_L2_C; 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; Cytoplasm; Direct protein sequencing; Hydroxylation;
KW Isopeptide bond; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12962325"
FT CHAIN 2..257
FT /note="60S ribosomal protein L8"
FT /id="PRO_0000129743"
FT REGION 207..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 216
FT /note="(3S)-3-hydroxyhistidine"
FT /evidence="ECO:0000269|PubMed:23103944"
FT CROSSLNK 42
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 149
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 234
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 250
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 98
FT /note="I -> V (in dbSNP:rs11539893)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3"
FT /id="VAR_019658"
FT MUTAGEN 209
FT /note="H->A,G: No incorporation into translating E.coli
FT polysomes; ribosomes assembled normally. Significantly
FT reduced translational activity."
FT /evidence="ECO:0000269|PubMed:9531480"
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
