RL18_HUMAN
ID RL18_HUMAN Reviewed; 188 AA.
AC Q07020; F8VWC5; Q8WTZ6;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=60S ribosomal protein L18;
DE AltName: Full=Large ribosomal subunit protein eL18 {ECO:0000303|PubMed:24524803};
GN Name=RPL18;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Colon;
RX PubMed=8218404; DOI=10.1016/0167-4781(93)90050-n;
RA Puder M., Barnard G.F., Staniunas R.J., Steele G.D. Jr., Chen L.B.;
RT "Nucleotide and deduced amino acid sequence of human ribosomal protein
RT L18.";
RL Biochim. Biophys. Acta 1216:134-136(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
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 GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Lung;
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 [5]
RP PROTEIN SEQUENCE OF 2-14, 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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND IDENTIFICATION BY
RP 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 the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130 AND THR-158, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
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 [15]
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 [16]
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 [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-119 AND LYS-164, AND
RP 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 [18]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS), SUBCELLULAR LOCATION,
RP SUBUNIT, AND FUNCTION.
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 [19] {ECO:0007744|PDB:5AJ0}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS).
RX PubMed=25957688; DOI=10.1016/j.cell.2015.03.052;
RA Behrmann E., Loerke J., Budkevich T.V., Yamamoto K., Schmidt A.,
RA Penczek P.A., Vos M.R., Burger J., Mielke T., Scheerer P., Spahn C.M.;
RT "Structural snapshots of actively translating human ribosomes.";
RL Cell 161:845-857(2015).
RN [20] {ECO:0007744|PDB:4UG0}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS).
RX PubMed=25901680; DOI=10.1038/nature14427;
RA Khatter H., Myasnikov A.G., Natchiar S.K., Klaholz B.P.;
RT "Structure of the human 80S ribosome.";
RL Nature 520:640-645(2015).
RN [21] {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).
RN [22]
RP VARIANT DBA18 SER-51, AND INVOLVEMENT IN DBA18.
RX PubMed=28280134; DOI=10.1136/jmedgenet-2016-104346;
RA Mirabello L., Khincha P.P., Ellis S.R., Giri N., Brodie S.,
RA Chandrasekharappa S.C., Donovan F.X., Zhou W., Hicks B.D., Boland J.F.,
RA Yeager M., Jones K., Zhu B., Wang M., Alter B.P., Savage S.A.;
RT "Novel and known ribosomal causes of Diamond-Blackfan anaemia identified
RT through comprehensive genomic characterisation.";
RL J. Med. Genet. 54:417-425(2017).
CC -!- FUNCTION: Component of the large ribosomal subunit (PubMed:12962325,
CC PubMed:23636399, PubMed:25957688, PubMed:25901680, PubMed:32669547).
CC The ribosome is a large ribonucleoprotein complex responsible for the
CC synthesis of proteins in the cell (PubMed:12962325, PubMed:23636399,
CC PubMed:25957688, PubMed:25901680, PubMed:32669547).
CC {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:25901680,
CC ECO:0000269|PubMed:25957688, ECO:0000269|PubMed:32669547,
CC ECO:0000305|PubMed:12962325}.
CC -!- SUBUNIT: Component of the large ribosomal subunit (PubMed:12962325,
CC PubMed:23636399, PubMed:25957688, PubMed:25901680, PubMed:32669547).
CC {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:25901680,
CC ECO:0000269|PubMed:25957688, ECO:0000269|PubMed:32669547,
CC ECO:0000305|PubMed:12962325}.
CC -!- INTERACTION:
CC Q07020; P54253: ATXN1; NbExp=3; IntAct=EBI-352694, EBI-930964;
CC Q07020; P42858: HTT; NbExp=12; IntAct=EBI-352694, EBI-466029;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:25957688}.
CC Cytoplasm {ECO:0000305|PubMed:23636399, ECO:0000305|PubMed:25901680}.
CC Rough endoplasmic reticulum {ECO:0000250|UniProtKB:Q95342}.
CC Note=Detected on cytosolic polysomes (PubMed:25957688). Detected in
CC ribosomes that are associated with the rough endoplasmic reticulum (By
CC similarity). {ECO:0000250|UniProtKB:Q95342,
CC ECO:0000269|PubMed:25957688}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q07020-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q07020-2; Sequence=VSP_055170;
CC -!- DISEASE: Diamond-Blackfan anemia 18 (DBA18) [MIM:618310]: A form of
CC Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic
CC anemia that usually presents early in infancy. Diamond-Blackfan anemia
CC is characterized by a moderate to severe macrocytic anemia,
CC erythroblastopenia, and an increased risk of malignancy. 30 to 40% of
CC Diamond-Blackfan anemia patients present with short stature and
CC congenital anomalies, the most frequent being craniofacial (Pierre-
CC Robin syndrome and cleft palate), thumb and urogenital anomalies. DBA18
CC inheritance is autosomal dominant. {ECO:0000269|PubMed:28280134}.
CC Note=The disease may be caused by variants affecting the gene
CC represented in this entry.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL18 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L11566; AAA16329.1; -; mRNA.
DR EMBL; AB061825; BAB79463.1; -; Genomic_DNA.
DR EMBL; AC022154; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000374; AAH00374.1; -; mRNA.
DR EMBL; BC009708; AAH09708.1; -; mRNA.
DR EMBL; BC021743; AAH21743.1; -; mRNA.
DR CCDS; CCDS12726.1; -. [Q07020-1]
DR CCDS; CCDS58669.1; -. [Q07020-2]
DR PIR; S38352; S38352.
DR RefSeq; NP_000970.1; NM_000979.3. [Q07020-1]
DR RefSeq; NP_001257419.1; NM_001270490.1. [Q07020-2]
DR PDB; 4UG0; EM; -; LQ=1-188.
DR PDB; 4V6X; EM; 5.00 A; CQ=1-188.
DR PDB; 5AJ0; EM; 3.50 A; AQ=1-188.
DR PDB; 5LKS; EM; 3.60 A; LQ=1-188.
DR PDB; 5T2C; EM; 3.60 A; K=1-188.
DR PDB; 6IP5; EM; 3.90 A; 2K=1-188.
DR PDB; 6IP6; EM; 4.50 A; 2K=1-188.
DR PDB; 6IP8; EM; 3.90 A; 2K=1-188.
DR PDB; 6LQM; EM; 3.09 A; Z=1-188.
DR PDB; 6LSR; EM; 3.13 A; Z=1-188.
DR PDB; 6LSS; EM; 3.23 A; Z=1-188.
DR PDB; 6LU8; EM; 3.13 A; Z=1-188.
DR PDB; 6OLE; EM; 3.10 A; R=2-188.
DR PDB; 6OLF; EM; 3.90 A; R=2-188.
DR PDB; 6OLG; EM; 3.40 A; AQ=2-188.
DR PDB; 6OLI; EM; 3.50 A; R=2-188.
DR PDB; 6OLZ; EM; 3.90 A; AQ=2-188.
DR PDB; 6OM0; EM; 3.10 A; R=2-188.
DR PDB; 6OM7; EM; 3.70 A; R=2-188.
DR PDB; 6QZP; EM; 2.90 A; LQ=2-188.
DR PDB; 6W6L; EM; 3.84 A; R=1-188.
DR PDB; 6XA1; EM; 2.80 A; LQ=2-188.
DR PDB; 6Y0G; EM; 3.20 A; LQ=1-188.
DR PDB; 6Y2L; EM; 3.00 A; LQ=1-188.
DR PDB; 6Y57; EM; 3.50 A; LQ=1-188.
DR PDB; 6Y6X; EM; 2.80 A; LQ=2-188.
DR PDB; 6Z6L; EM; 3.00 A; LQ=1-188.
DR PDB; 6Z6M; EM; 3.10 A; LQ=1-188.
DR PDB; 6Z6N; EM; 2.90 A; LQ=1-188.
DR PDB; 6ZM7; EM; 2.70 A; LQ=1-188.
DR PDB; 6ZME; EM; 3.00 A; LQ=1-188.
DR PDB; 6ZMI; EM; 2.60 A; LQ=1-188.
DR PDB; 6ZMO; EM; 3.10 A; LQ=1-188.
DR PDB; 6ZVK; EM; 3.49 A; S2=2-188.
DR PDB; 7A01; EM; 3.60 A; S2=2-188.
DR PDB; 7BHP; EM; 3.30 A; LQ=1-188.
DR PDBsum; 4UG0; -.
DR PDBsum; 4V6X; -.
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; 6ZVK; -.
DR PDBsum; 7A01; -.
DR PDBsum; 7BHP; -.
DR AlphaFoldDB; Q07020; -.
DR SMR; Q07020; -.
DR BioGRID; 112061; 432.
DR ComplexPortal; CPX-5183; 60S cytosolic large ribosomal subunit.
DR CORUM; Q07020; -.
DR IntAct; Q07020; 175.
DR MINT; Q07020; -.
DR STRING; 9606.ENSP00000447001; -.
DR DrugBank; DB11638; Artenimol.
DR GlyGen; Q07020; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q07020; -.
DR PhosphoSitePlus; Q07020; -.
DR SwissPalm; Q07020; -.
DR BioMuta; RPL18; -.
DR SWISS-2DPAGE; Q07020; -.
DR CPTAC; CPTAC-432; -.
DR CPTAC; CPTAC-433; -.
DR EPD; Q07020; -.
DR jPOST; Q07020; -.
DR MassIVE; Q07020; -.
DR MaxQB; Q07020; -.
DR PaxDb; Q07020; -.
DR PeptideAtlas; Q07020; -.
DR PRIDE; Q07020; -.
DR ProteomicsDB; 28967; -.
DR ProteomicsDB; 58499; -. [Q07020-1]
DR TopDownProteomics; Q07020-1; -. [Q07020-1]
DR Antibodypedia; 31739; 194 antibodies from 27 providers.
DR DNASU; 6141; -.
DR Ensembl; ENST00000549920.6; ENSP00000447001.1; ENSG00000063177.13. [Q07020-1]
DR Ensembl; ENST00000552588.5; ENSP00000449204.1; ENSG00000063177.13. [Q07020-2]
DR GeneID; 6141; -.
DR KEGG; hsa:6141; -.
DR MANE-Select; ENST00000549920.6; ENSP00000447001.1; NM_000979.4; NP_000970.1.
DR UCSC; uc002pjq.3; human. [Q07020-1]
DR CTD; 6141; -.
DR DisGeNET; 6141; -.
DR GeneCards; RPL18; -.
DR GeneReviews; RPL18; -.
DR HGNC; HGNC:10310; RPL18.
DR HPA; ENSG00000063177; Low tissue specificity.
DR MalaCards; RPL18; -.
DR MIM; 604179; gene.
DR MIM; 618310; phenotype.
DR neXtProt; NX_Q07020; -.
DR OpenTargets; ENSG00000063177; -.
DR Orphanet; 124; Blackfan-Diamond anemia.
DR PharmGKB; PA34679; -.
DR VEuPathDB; HostDB:ENSG00000063177; -.
DR eggNOG; KOG1714; Eukaryota.
DR GeneTree; ENSGT00390000012976; -.
DR InParanoid; Q07020; -.
DR OMA; MSKIHRP; -.
DR PhylomeDB; Q07020; -.
DR TreeFam; TF300202; -.
DR PathwayCommons; Q07020; -.
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; Q07020; -.
DR SIGNOR; Q07020; -.
DR BioGRID-ORCS; 6141; 807 hits in 1079 CRISPR screens.
DR ChiTaRS; RPL18; human.
DR GeneWiki; RPL18; -.
DR GenomeRNAi; 6141; -.
DR Pharos; Q07020; Tbio.
DR PRO; PR:Q07020; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q07020; protein.
DR Bgee; ENSG00000063177; Expressed in nipple and 215 other tissues.
DR ExpressionAtlas; Q07020; baseline and differential.
DR Genevisible; Q07020; HS.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0042788; C:polysomal ribosome; IDA:UniProtKB.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
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 InterPro; IPR036227; L18e/L15P_sf.
DR InterPro; IPR021132; Ribosomal_L18/L18-A/B/e_CS.
DR InterPro; IPR000039; Ribosomal_L18e.
DR InterPro; IPR021131; Ribosomal_L18e/L15P.
DR PANTHER; PTHR10934; PTHR10934; 1.
DR Pfam; PF17135; Ribosomal_L18; 1.
DR SUPFAM; SSF52080; SSF52080; 1.
DR PROSITE; PS01106; RIBOSOMAL_L18E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Diamond-Blackfan anemia;
KW Direct protein sequencing; Disease variant; Endoplasmic reticulum;
KW Isopeptide bond; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12962325"
FT CHAIN 2..188
FT /note="60S ribosomal protein L18"
FT /id="PRO_0000132769"
FT REGION 151..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..188
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 158
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CROSSLNK 119
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 164
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..30
FT /note="MGVDIRHNKDRKVRRKEPKSQDIYLRLLVK -> M (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_055170"
FT VARIANT 51
FT /note="L -> S (in DBA18; unknown pathological significance;
FT dbSNP:rs1568425218)"
FT /evidence="ECO:0000269|PubMed:28280134"
FT /id="VAR_081935"
FT CONFLICT 62
FT /note="S -> C (in Ref. 4; AAH21743)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 188 AA; 21634 MW; C4E416E7A5329B7C CRC64;
MGVDIRHNKD RKVRRKEPKS QDIYLRLLVK LYRFLARRTN STFNQVVLKR LFMSRTNRPP
LSLSRMIRKM KLPGRENKTA VVVGTITDDV RVQEVPKLKV CALRVTSRAR SRILRAGGKI
LTFDQLALDS PKGCGTVLLS GPRKGREVYR HFGKAPGTPH SHTKPYVRSK GRKFERARGR
RASRGYKN
