ID   RL5_HUMAN               Reviewed;         297 AA.
AC   P46777; Q32LZ3; Q53HH6; Q9H3F4;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 217.
DE   RecName: Full=Large ribosomal subunit protein uL18 {ECO:0000303|PubMed:24524803};
DE   AltName: Full=60S ribosomal protein L5;
GN   Name=RPL5; ORFNames=MSTP030;
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=Colon;
RX   PubMed=7772601; DOI=10.1016/0167-4781(95)00045-i;
RA   Frigerio J.-M., Dagorn J.-C., Iovanna J.L.;
RT   "Cloning, sequencing and expression of the L5, L21, L27a, L28, S5, S9, S10
RT   and S29 human ribosomal protein mRNAs.";
RL   Biochim. Biophys. Acta 1262:64-68(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Aorta;
RA   Liu B., Liu Y.Q., Wang X.Y., Zhao B., Sheng H., Zhao X.W., Liu S., Xu Y.Y.,
RA   Ye J., Song L., Gao Y., Zhang C.L., Zhang J., Wei Y.J., Cao H.Q., Zhao Y.,
RA   Liu L.S., Ding J.F., Gao R.L., Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C.,
RA   Zhao M.S., Hui R.T.;
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Coronary arterial endothelium;
RA   Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA   Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT CYS-210.
RC   TISSUE=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   [6]
RP   PROTEIN SEQUENCE OF 2-12, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   FUNCTION.
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   [7]
RP   PROTEIN SEQUENCE OF 69-85; 159-188 AND 222-228, SUBCELLULAR LOCATION, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RA   Bienvenut W.V.;
RL   Submitted (AUG-2005) to UniProtKB.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 153-297.
RX   PubMed=8806611; DOI=10.1006/bbrc.1996.1330;
RA   Kim J.-M., Cha J.-Y., Marshak D.R., Bae Y.-S.;
RT   "Interaction of the beta subunit of casein kinase II with the ribosomal
RT   protein L5.";
RL   Biochem. Biophys. Res. Commun. 226:180-186(1996).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 162-176.
RX   PubMed=7937132; DOI=10.1093/nar/22.20.4073;
RA   Qu L.H., Nicoloso M., Michot B., Azum M.C., Caizergues-Ferrer M.,
RA   Renalier M.H., Bachellerie J.-P.;
RT   "U21, a novel small nucleolar RNA with a 13 nt. complementarity to 28S
RT   rRNA, is encoded in an intron of ribosomal protein L5 gene in chicken and
RT   mammals.";
RL   Nucleic Acids Res. 22:4073-4081(1994).
RN   [10]
RP   INTERACTION WITH IPO5; IPO7 AND KPNB1, AND SUBCELLULAR LOCATION.
RX   PubMed=9687515; DOI=10.1093/emboj/17.15.4491;
RA   Jaekel S., Goerlich D.;
RT   "Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear import of
RT   ribosomal proteins in mammalian cells.";
RL   EMBO J. 17:4491-4502(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   SUBCELLULAR LOCATION, AND INTERACTION WITH NVL.
RX   PubMed=15469983; DOI=10.1091/mbc.e04-08-0692;
RA   Nagahama M., Hara Y., Seki A., Yamazoe T., Kawate Y., Shinohara T.,
RA   Hatsuzawa K., Tani K., Tagaya M.;
RT   "NVL2 is a nucleolar AAA-ATPase that interacts with ribosomal protein L5
RT   through its nucleolar localization sequence.";
RL   Mol. Biol. Cell 15:5712-5723(2004).
RN   [13]
RP   FUNCTION, AND VARIANT DBA6 SER-140.
RX   PubMed=19061985; DOI=10.1016/j.ajhg.2008.11.004;
RA   Gazda H.T., Sheen M.R., Vlachos A., Choesmel V., O'Donohue M.-F.,
RA   Schneider H., Darras N., Hasman C., Sieff C.A., Newburger P.E., Ball S.E.,
RA   Niewiadomska E., Matysiak M., Zaucha J.M., Glader B., Niemeyer C.,
RA   Meerpohl J.J., Atsidaftos E., Lipton J.M., Gleizes P.-E., Beggs A.H.;
RT   "Ribosomal protein L5 and L11 mutations are associated with cleft palate
RT   and abnormal thumbs in Diamond-Blackfan anemia patients.";
RL   Am. J. Hum. Genet. 83:769-780(2008).
RN   [14]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-5 AND LYS-48, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [15]
RP   INTERACTION WITH RRP1B.
RX   PubMed=20926688; DOI=10.1091/mbc.e10-04-0287;
RA   Chamousset D., De Wever V., Moorhead G.B., Chen Y., Boisvert F.M.,
RA   Lamond A.I., Trinkle-Mulcahy L.;
RT   "RRP1B targets PP1 to mammalian cell nucleoli and is associated with pre-
RT   60S ribosomal subunits.";
RL   Mol. Biol. Cell 21:4212-4226(2010).
RN   [16]
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   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272, 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   [18]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [19]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=24120868; DOI=10.1016/j.celrep.2013.08.049;
RA   Sloan K.E., Bohnsack M.T., Watkins N.J.;
RT   "The 5S RNP couples p53 homeostasis to ribosome biogenesis and nucleolar
RT   stress.";
RL   Cell Rep. 5:237-247(2013).
RN   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185 AND THR-232, AND
RP   IDENTIFICATION BY 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   [21]
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   [22]
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   [23]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Colon carcinoma;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
RN   [24]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-220, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA   Impens F., Radoshevich L., Cossart P., Ribet D.;
RT   "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT   external stimuli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN   [25]
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   [26]
RP   STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME, FUNCTION,
RP   SUBUNIT, AND 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   [27] {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   [28]
RP   VARIANT DBA6 VAL-285.
RX   PubMed=19191325; DOI=10.1002/humu.20874;
RA   Cmejla R., Cmejlova J., Handrkova H., Petrak J., Petrtylova K., Mihal V.,
RA   Stary J., Cerna Z., Jabali Y., Pospisilova D.;
RT   "Identification of mutations in the ribosomal protein L5 (RPL5) and
RT   ribosomal protein L11 (RPL11) genes in Czech patients with Diamond-Blackfan
RT   anemia.";
RL   Hum. Mutat. 30:321-327(2009).
CC   -!- FUNCTION: Component of the ribosome, a large ribonucleoprotein complex
CC       responsible for the synthesis of proteins in the cell. The small
CC       ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the
CC       encoded message by selecting cognate aminoacyl-transfer RNA (tRNA)
CC       molecules. The large subunit (LSU) contains the ribosomal catalytic
CC       site termed the peptidyl transferase center (PTC), which catalyzes the
CC       formation of peptide bonds, thereby polymerizing the amino acids
CC       delivered by tRNAs into a polypeptide chain. The nascent polypeptides
CC       leave the ribosome through a tunnel in the LSU and interact with
CC       protein factors that function in enzymatic processing, targeting, and
CC       the membrane insertion of nascent chains at the exit of the ribosomal
CC       tunnel. As part of the 5S RNP/5S ribonucleoprotein particle it is an
CC       essential component of the LSU, required for its formation and the
CC       maturation of rRNAs (PubMed:12962325, PubMed:19061985, PubMed:24120868,
CC       PubMed:23636399). It also couples ribosome biogenesis to p53/TP53
CC       activation. As part of the 5S RNP it accumulates in the nucleoplasm and
CC       inhibits MDM2, when ribosome biogenesis is perturbed, mediating the
CC       stabilization and the activation of TP53 (PubMed:24120868).
CC       {ECO:0000269|PubMed:12962325, ECO:0000269|PubMed:19061985,
CC       ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:24120868}.
CC   -!- SUBUNIT: Component of the large ribosomal subunit (LSU). Part of a LSU
CC       subcomplex, the 5S RNP which is composed of the 5S RNA, RPL5 and RPL11
CC       (PubMed:24120868). Interacts with isoform 1 of NVL in an ATP-dependent
CC       manner (PubMed:15469983). Interacts with RRP1B (PubMed:20926688).
CC       Interacts with IPO5, IPO7 and KPNB1; these interactions may be involved
CC       in RPL5 nuclear import for the assembly of ribosomal subunits
CC       (PubMed:9687515). {ECO:0000269|PubMed:15469983,
CC       ECO:0000269|PubMed:20926688, ECO:0000269|PubMed:24120868,
CC       ECO:0000269|PubMed:9687515}.
CC   -!- INTERACTION:
CC       P46777; P43146: DCC; NbExp=7; IntAct=EBI-358018, EBI-1222919;
CC       P46777; Q00987: MDM2; NbExp=5; IntAct=EBI-358018, EBI-389668;
CC       P46777; Q14684: RRP1B; NbExp=2; IntAct=EBI-358018, EBI-372051;
CC       P46777; Q63155: Dcc; Xeno; NbExp=4; IntAct=EBI-358018, EBI-1798965;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15469983,
CC       ECO:0000269|Ref.7}. Nucleus, nucleolus {ECO:0000269|PubMed:15469983,
CC       ECO:0000269|Ref.7}. Note=Although RP5 is functional within the
CC       cytoplasm, the assembly of ribosomal subunits occurs in the nucleus.
CC       RPL5 nuclear import is mediated by IPO5/RanBP5, IPO7/RanBP7,
CC       KPNB1/importin-beta or TPNO1/Trn. {ECO:0000269|PubMed:9687515}.
CC   -!- DISEASE: Diamond-Blackfan anemia 6 (DBA6) [MIM:612561]: 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.
CC       {ECO:0000269|PubMed:19061985, ECO:0000269|PubMed:19191325}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL18 family.
CC       {ECO:0000305}.
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DR   EMBL; U14966; AAA85654.1; -; mRNA.
DR   EMBL; AF113210; AAG39281.1; -; mRNA.
DR   EMBL; AK222604; BAD96324.1; -; mRNA.
DR   EMBL; AL162740; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC109370; AAI09371.1; -; mRNA.
DR   EMBL; U76609; AAB18361.1; -; mRNA.
DR   EMBL; Z35312; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS741.1; -.
DR   PIR; S55912; S55912.
DR   RefSeq; NP_000960.2; NM_000969.3.
DR   PDB; 4UG0; EM; -; LD=1-297.
DR   PDB; 4V6X; EM; 5.00 A; CD=1-297.
DR   PDB; 5AJ0; EM; 3.50 A; AD=1-297.
DR   PDB; 5LKS; EM; 3.60 A; LD=1-297.
DR   PDB; 5T2C; EM; 3.60 A; G=1-297.
DR   PDB; 6IP5; EM; 3.90 A; 1G=1-297.
DR   PDB; 6IP6; EM; 4.50 A; 1G=1-297.
DR   PDB; 6IP8; EM; 3.90 A; 1G=1-297.
DR   PDB; 6LQM; EM; 3.09 A; r=1-297.
DR   PDB; 6LSR; EM; 3.13 A; r=1-297.
DR   PDB; 6LSS; EM; 3.23 A; r=1-297.
DR   PDB; 6LU8; EM; 3.13 A; r=1-297.
DR   PDB; 6OLE; EM; 3.10 A; F=4-297.
DR   PDB; 6OLF; EM; 3.90 A; F=4-297.
DR   PDB; 6OLG; EM; 3.40 A; AD=4-297.
DR   PDB; 6OLI; EM; 3.50 A; F=4-297.
DR   PDB; 6OLZ; EM; 3.90 A; AD=4-297.
DR   PDB; 6OM0; EM; 3.10 A; F=4-297.
DR   PDB; 6OM7; EM; 3.70 A; F=4-297.
DR   PDB; 6QZP; EM; 2.90 A; LD=2-294.
DR   PDB; 6W6L; EM; 3.84 A; F=1-297.
DR   PDB; 6XA1; EM; 2.80 A; LD=2-291.
DR   PDB; 6Y0G; EM; 3.20 A; LD=1-297.
DR   PDB; 6Y2L; EM; 3.00 A; LD=1-297.
DR   PDB; 6Y57; EM; 3.50 A; LD=1-297.
DR   PDB; 6Y6X; EM; 2.80 A; LD=2-294.
DR   PDB; 6Z6L; EM; 3.00 A; LD=1-297.
DR   PDB; 6Z6M; EM; 3.10 A; LD=1-297.
DR   PDB; 6Z6N; EM; 2.90 A; LD=1-297.
DR   PDB; 6ZM7; EM; 2.70 A; LD=1-297.
DR   PDB; 6ZME; EM; 3.00 A; LD=1-297.
DR   PDB; 6ZMI; EM; 2.60 A; LD=1-297.
DR   PDB; 6ZMO; EM; 3.10 A; LD=1-297.
DR   PDB; 7BHP; EM; 3.30 A; LD=1-297.
DR   PDB; 7F5S; EM; 2.72 A; LD=1-297.
DR   PDB; 7OW7; EM; 2.20 A; G=1-297.
DR   PDB; 7QVP; EM; 3.00 A; LD/MD=1-297.
DR   PDB; 7XNX; EM; 2.70 A; LD=1-297.
DR   PDB; 7XNY; EM; 2.50 A; LD=1-297.
DR   PDB; 8A3D; EM; 1.67 A; G=1-297.
DR   PDB; 8BGU; EM; 4.10 A; A=1-297.
DR   PDB; 8FL0; EM; 2.91 A; SB=1-297.
DR   PDB; 8FL2; EM; 2.67 A; SB=1-297.
DR   PDB; 8FL3; EM; 2.53 A; SB=1-297.
DR   PDB; 8FL4; EM; 2.89 A; SB=1-297.
DR   PDB; 8FL6; EM; 2.62 A; SB=1-297.
DR   PDB; 8FL7; EM; 2.55 A; SB=1-297.
DR   PDB; 8FL9; EM; 2.75 A; SB=1-297.
DR   PDB; 8FLA; EM; 2.63 A; SB=1-297.
DR   PDB; 8FLB; EM; 2.55 A; SB=1-297.
DR   PDB; 8FLC; EM; 2.76 A; SB=1-297.
DR   PDB; 8FLD; EM; 2.58 A; SB=1-297.
DR   PDB; 8FLE; EM; 2.48 A; SB=1-297.
DR   PDB; 8FLF; EM; 2.65 A; SB=1-297.
DR   PDB; 8G5Y; EM; 2.29 A; LD=1-297.
DR   PDB; 8G5Z; EM; 2.64 A; LD=2-295.
DR   PDB; 8G60; EM; 2.54 A; LD=1-297.
DR   PDB; 8G61; EM; 2.94 A; LD=1-297.
DR   PDB; 8G6J; EM; 2.80 A; LD=1-297.
DR   PDB; 8GLP; EM; 1.67 A; LD=1-297.
DR   PDB; 8IDT; EM; 2.80 A; r=1-297.
DR   PDB; 8IDY; EM; 3.00 A; r=1-297.
DR   PDB; 8IE3; EM; 3.30 A; r=1-297.
DR   PDB; 8INE; EM; 3.20 A; r=1-297.
DR   PDB; 8INF; EM; 3.00 A; r=1-297.
DR   PDB; 8INK; EM; 3.20 A; R=1-297.
DR   PDB; 8IPD; EM; 3.20 A; R=1-297.
DR   PDB; 8IPX; EM; 4.30 A; R=1-297.
DR   PDB; 8IPY; EM; 3.20 A; R=1-297.
DR   PDB; 8IR1; EM; 3.30 A; C=1-297.
DR   PDB; 8IR3; EM; 3.50 A; C=1-297.
DR   PDB; 8JDJ; EM; 2.50 A; J=1-297.
DR   PDB; 8JDK; EM; 2.26 A; J=1-297.
DR   PDB; 8JDL; EM; 2.42 A; J=1-297.
DR   PDB; 8JDM; EM; 2.67 A; J=1-297.
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; 7BHP; -.
DR   PDBsum; 7F5S; -.
DR   PDBsum; 7OW7; -.
DR   PDBsum; 7QVP; -.
DR   PDBsum; 7XNX; -.
DR   PDBsum; 7XNY; -.
DR   PDBsum; 8A3D; -.
DR   PDBsum; 8BGU; -.
DR   PDBsum; 8FL0; -.
DR   PDBsum; 8FL2; -.
DR   PDBsum; 8FL3; -.
DR   PDBsum; 8FL4; -.
DR   PDBsum; 8FL6; -.
DR   PDBsum; 8FL7; -.
DR   PDBsum; 8FL9; -.
DR   PDBsum; 8FLA; -.
DR   PDBsum; 8FLB; -.
DR   PDBsum; 8FLC; -.
DR   PDBsum; 8FLD; -.
DR   PDBsum; 8FLE; -.
DR   PDBsum; 8FLF; -.
DR   PDBsum; 8G5Y; -.
DR   PDBsum; 8G5Z; -.
DR   PDBsum; 8G60; -.
DR   PDBsum; 8G61; -.
DR   PDBsum; 8G6J; -.
DR   PDBsum; 8GLP; -.
DR   PDBsum; 8IDT; -.
DR   PDBsum; 8IDY; -.
DR   PDBsum; 8IE3; -.
DR   PDBsum; 8INE; -.
DR   PDBsum; 8INF; -.
DR   PDBsum; 8INK; -.
DR   PDBsum; 8IPD; -.
DR   PDBsum; 8IPX; -.
DR   PDBsum; 8IPY; -.
DR   PDBsum; 8IR1; -.
DR   PDBsum; 8IR3; -.
DR   PDBsum; 8JDJ; -.
DR   PDBsum; 8JDK; -.
DR   PDBsum; 8JDL; -.
DR   PDBsum; 8JDM; -.
DR   AlphaFoldDB; P46777; -.
DR   EMDB; EMD-0948; -.
DR   EMDB; EMD-0963; -.
DR   EMDB; EMD-0964; -.
DR   EMDB; EMD-0978; -.
DR   EMDB; EMD-10668; -.
DR   EMDB; EMD-10674; -.
DR   EMDB; EMD-10690; -.
DR   EMDB; EMD-10709; -.
DR   EMDB; EMD-11098; -.
DR   EMDB; EMD-11099; -.
DR   EMDB; EMD-11100; -.
DR   EMDB; EMD-11288; -.
DR   EMDB; EMD-11289; -.
DR   EMDB; EMD-11292; -.
DR   EMDB; EMD-11299; -.
DR   EMDB; EMD-12189; -.
DR   EMDB; EMD-13094; -.
DR   EMDB; EMD-14181; -.
DR   EMDB; EMD-15113; -.
DR   EMDB; EMD-16036; -.
DR   EMDB; EMD-29263; -.
DR   EMDB; EMD-29265; -.
DR   EMDB; EMD-29266; -.
DR   EMDB; EMD-29267; -.
DR   EMDB; EMD-29268; -.
DR   EMDB; EMD-29269; -.
DR   EMDB; EMD-29271; -.
DR   EMDB; EMD-29272; -.
DR   EMDB; EMD-29273; -.
DR   EMDB; EMD-29274; -.
DR   EMDB; EMD-29275; -.
DR   EMDB; EMD-29276; -.
DR   EMDB; EMD-29277; -.
DR   EMDB; EMD-29757; -.
DR   EMDB; EMD-29758; -.
DR   EMDB; EMD-29759; -.
DR   EMDB; EMD-29760; -.
DR   EMDB; EMD-29771; -.
DR   EMDB; EMD-31465; -.
DR   EMDB; EMD-33329; -.
DR   EMDB; EMD-33330; -.
DR   EMDB; EMD-35370; -.
DR   EMDB; EMD-35371; -.
DR   EMDB; EMD-35375; -.
DR   EMDB; EMD-35596; -.
DR   EMDB; EMD-35597; -.
DR   EMDB; EMD-35599; -.
DR   EMDB; EMD-35639; -.
DR   EMDB; EMD-35649; -.
DR   EMDB; EMD-35651; -.
DR   EMDB; EMD-35672; -.
DR   EMDB; EMD-35673; -.
DR   EMDB; EMD-3883; -.
DR   EMDB; EMD-40205; -.
DR   EMDB; EMD-4070; -.
DR   EMDB; EMD-9701; -.
DR   EMDB; EMD-9702; -.
DR   EMDB; EMD-9703; -.
DR   SMR; P46777; -.
DR   BioGRID; 112045; 597.
DR   ComplexPortal; CPX-5183; 60S cytosolic large ribosomal subunit.
DR   ComplexPortal; CPX-7664; 60S cytosolic large ribosomal subunit, testis-specific variant.
DR   ComplexPortal; CPX-7665; 60S cytosolic large ribosomal subunit, striated muscle variant.
DR   CORUM; P46777; -.
DR   DIP; DIP-31152N; -.
DR   IntAct; P46777; 104.
DR   MINT; P46777; -.
DR   STRING; 9606.ENSP00000359345; -.
DR   MoonProt; P46777; -.
DR   GlyGen; P46777; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P46777; -.
DR   MetOSite; P46777; -.
DR   PhosphoSitePlus; P46777; -.
DR   SwissPalm; P46777; -.
DR   BioMuta; RPL5; -.
DR   DMDM; 81175191; -.
DR   EPD; P46777; -.
DR   jPOST; P46777; -.
DR   MassIVE; P46777; -.
DR   MaxQB; P46777; -.
DR   PaxDb; 9606-ENSP00000359345; -.
DR   PeptideAtlas; P46777; -.
DR   ProteomicsDB; 55759; -.
DR   Pumba; P46777; -.
DR   TopDownProteomics; P46777; -.
DR   Antibodypedia; 33652; 347 antibodies from 33 providers.
DR   DNASU; 6125; -.
DR   Ensembl; ENST00000370321.8; ENSP00000359345.2; ENSG00000122406.14.
DR   GeneID; 6125; -.
DR   KEGG; hsa:6125; -.
DR   MANE-Select; ENST00000370321.8; ENSP00000359345.2; NM_000969.5; NP_000960.2.
DR   UCSC; uc001doz.4; human.
DR   AGR; HGNC:10360; -.
DR   CTD; 6125; -.
DR   DisGeNET; 6125; -.
DR   GeneCards; RPL5; -.
DR   GeneReviews; RPL5; -.
DR   HGNC; HGNC:10360; RPL5.
DR   HPA; ENSG00000122406; Low tissue specificity.
DR   MalaCards; RPL5; -.
DR   MIM; 603634; gene.
DR   MIM; 612561; phenotype.
DR   neXtProt; NX_P46777; -.
DR   OpenTargets; ENSG00000122406; -.
DR   Orphanet; 124; Diamond-Blackfan anemia.
DR   PharmGKB; PA34755; -.
DR   VEuPathDB; HostDB:ENSG00000122406; -.
DR   eggNOG; KOG0875; Eukaryota.
DR   GeneTree; ENSGT00950000183210; -.
DR   HOGENOM; CLU_056222_1_0_1; -.
DR   InParanoid; P46777; -.
DR   OMA; CQIASAH; -.
DR   OrthoDB; 1105861at2759; -.
DR   PhylomeDB; P46777; -.
DR   TreeFam; TF300044; -.
DR   PathwayCommons; P46777; -.
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; P46777; -.
DR   SIGNOR; P46777; -.
DR   BioGRID-ORCS; 6125; 819 hits in 1116 CRISPR screens.
DR   ChiTaRS; RPL5; human.
DR   GeneWiki; Ribosomal_protein_L5; -.
DR   GenomeRNAi; 6125; -.
DR   Pharos; P46777; Tbio.
DR   PRO; PR:P46777; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P46777; Protein.
DR   Bgee; ENSG00000122406; Expressed in germinal epithelium of ovary and 204 other cell types or tissues.
DR   ExpressionAtlas; P46777; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
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:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI.
DR   GO; GO:0008097; F:5S rRNA binding; IDA:CAFA.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:CAFA.
DR   GO; GO:0048027; F:mRNA 5'-UTR binding; IDA:CAFA.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB.
DR   GO; GO:1990948; F:ubiquitin ligase inhibitor activity; IDA:CAFA.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:CAFA.
DR   GO; GO:0002181; P:cytoplasmic translation; NAS:ComplexPortal.
DR   GO; GO:2000435; P:negative regulation of protein neddylation; IDA:CAFA.
DR   GO; GO:1904667; P:negative regulation of ubiquitin protein ligase activity; IDA:CAFA.
DR   GO; GO:2000059; P:negative regulation of ubiquitin-dependent protein catabolic process; IDA:CAFA.
DR   GO; GO:0010628; P:positive regulation of gene expression; IDA:CAFA.
DR   GO; GO:0045727; P:positive regulation of translation; IDA:CAFA.
DR   GO; GO:0050821; P:protein stabilization; IMP:CAFA.
DR   GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; IMP:UniProtKB.
DR   GO; GO:0000027; P:ribosomal large subunit assembly; IMP:UniProtKB.
DR   GO; GO:0042273; P:ribosomal large subunit biogenesis; IMP:UniProtKB.
DR   GO; GO:0006364; P:rRNA processing; IMP:UniProtKB.
DR   GO; GO:0006412; P:translation; TAS:ProtInc.
DR   CDD; cd00432; Ribosomal_L18_L5e; 1.
DR   Gene3D; 3.30.420.100; -; 1.
DR   HAMAP; MF_01337_A; Ribosomal_uL18_A; 1.
DR   InterPro; IPR005485; Rbsml_uL18_euk/arc.
DR   InterPro; IPR025607; Ribosomal_uL18_C_euk.
DR   PANTHER; PTHR23410:SF37; 60S RIBOSOMAL PROTEIN L5; 1.
DR   PANTHER; PTHR23410; RIBOSOMAL PROTEIN L5-RELATED; 1.
DR   Pfam; PF14204; Ribosomal_L18_c; 1.
DR   Pfam; PF17144; Ribosomal_L5e; 1.
DR   PRINTS; PR00058; RIBOSOMALL5.
DR   SUPFAM; SSF53137; Translational machinery components; 1.
DR   Genevisible; P46777; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Diamond-Blackfan anemia;
KW   Direct protein sequencing; Disease variant; Isopeptide bond; Nucleus;
KW   Phosphoprotein; 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                   ECO:0007744|PubMed:22814378"
FT   CHAIN           2..297
FT                   /note="Large ribosomal subunit protein uL18"
FT                   /id="PRO_0000131431"
FT   REGION          253..297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..297
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         5
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         48
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         185
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         220
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P47962"
FT   MOD_RES         232
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         272
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   CROSSLNK        220
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0007744|PubMed:25114211"
FT   CROSSLNK        220
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0007744|PubMed:25114211"
FT   VARIANT         140
FT                   /note="G -> S (in DBA6; dbSNP:rs121434406)"
FT                   /evidence="ECO:0000269|PubMed:19061985"
FT                   /id="VAR_055450"
FT   VARIANT         210
FT                   /note="Y -> C (in dbSNP:rs11540832)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_052009"
FT   VARIANT         285
FT                   /note="A -> V (in DBA6)"
FT                   /evidence="ECO:0000269|PubMed:19191325"
FT                   /id="VAR_055451"
FT   CONFLICT        78
FT                   /note="A -> R (in Ref. 1; AAA85654)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        176
FT                   /note="S -> R (in Ref. 9)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        264
FT                   /note="K -> E (in Ref. 3; BAD96324)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   297 AA;  34363 MW;  07CA9FBA842BD2A3 CRC64;
     MGFVKVVKNK AYFKRYQVKF RRRREGKTDY YARKRLVIQD KNKYNTPKYR MIVRVTNRDI
     ICQIAYARIE GDMIVCAAYA HELPKYGVKV GLTNYAAAYC TGLLLARRLL NRFGMDKIYE
     GQVEVTGDEY NVESIDGQPG AFTCYLDAGL ARTTTGNKVF GALKGAVDGG LSIPHSTKRF
     PGYDSESKEF NAEVHRKHIM GQNVADYMRY LMEEDEDAYK KQFSQYIKNS VTPDMMEEMY
     KKAHAAIREN PVYEKKPKKE VKKKRWNRPK MSLAQKKDRV AQKKASFLRA QERAAES
//