ID RL14_HUMAN Reviewed; 215 AA. AC P50914; Q45RF0; Q53G20; Q8TBD5; Q8WUT0; Q92579; Q96GR0; Q9BSB8; Q9BW65; AC Q9BYF6; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 04-NOV-2008, sequence version 4. DT 27-MAR-2024, entry version 227. DE RecName: Full=Large ribosomal subunit protein eL14 {ECO:0000303|PubMed:24524803}; DE AltName: Full=60S ribosomal protein L14; DE AltName: Full=CAG-ISL 7; GN Name=RPL14; 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], AND VARIANT 158-ALA-ALA-159 DEL. RC TISSUE=Pancreas; RX PubMed=8549859; DOI=10.2337/diab.45.2.157; RA Aoki M., Koranyi L., Riggs A.C., Wasson J., Chiu K.C., Vaxillaire M., RA Froguel P., Gough S., Liu L., Donis-Keller H., Permutt M.A.; RT "Identification of trinucleotide repeat-containing genes in human RT pancreatic islets."; RL Diabetes 45:157-164(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-ALA-ALA-ALA-ALA-159 INS. RC TISSUE=Umbilical vein; RX PubMed=9480843; DOI=10.1006/bbrc.1998.8125; RA Tanaka M., Tanaka T., Harata M., Suzuki T., Mitsui Y.; RT "Triplet repeat-containing ribosomal protein L14 gene in immortalized human RT endothelial cell line (t-HUE4)."; RL Biochem. Biophys. Res. Commun. 243:531-537(1998). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-ALA-ALA-ALA-ALA-159 INS. 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 [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Lin L., Nong W., Zhou G., Ke R., Shen C., Zhong G., Zheng Z., Liang M., RA Wen S., Li H., Yang S.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-ALA-ALA-ALA-ALA-159 RP INS. 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND POLYMORPHISM OF POLY-ALA RP REGION. RC TISSUE=Brain, Kidney, Muscle, Ovary, and Skin; 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 85-116. RX PubMed=11401437; DOI=10.1006/geno.2000.6470; RA Uechi T., Tanaka T., Kenmochi N.; RT "A complete map of the human ribosomal protein genes: assignment of 80 RT genes to the cytogenetic map and implications for human disorders."; RL Genomics 72:223-230(2001). RN [9] RP PROTEIN SEQUENCE OF 2-10, 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 SEQUENCE OF 12-46; 80-85; 104-109; 148-158 AND 188-193, VARIANT RP 158-ALA-ALA-159 DEL, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Cervix carcinoma; RA Bienvenut W.V.; RL Submitted (AUG-2005) to UniProtKB. 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17924679; DOI=10.1021/pr070152u; RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells RT and high confident phosphopeptide identification by cross-validation of RT MS/MS and MS/MS/MS spectra."; RL J. Proteome Res. 6:4150-4162(2007). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, 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 [15] 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 [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [18] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-79 AND LYS-85, 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 [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, 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 [20] 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 [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, 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 [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, 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 [23] 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 [24] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-124, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(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 SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-124, AND IDENTIFICATION BY MASS RP 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 [27] 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 [28] {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 (PubMed:12962325, CC PubMed:23636399, PubMed:32669547). The ribosome is a large CC ribonucleoprotein complex responsible for the synthesis of proteins in CC the cell (PubMed:12962325, PubMed:23636399, PubMed:32669547). CC {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:32669547, CC ECO:0000305|PubMed:12962325}. CC -!- SUBUNIT: Component of the large ribosomal subunit (PubMed:12962325, CC PubMed:23636399, PubMed:32669547). {ECO:0000269|PubMed:23636399, CC ECO:0000269|PubMed:32669547, ECO:0000305|PubMed:12962325}. CC -!- INTERACTION: CC P50914; Q5S007: LRRK2; NbExp=2; IntAct=EBI-356746, EBI-5323863; CC P50914; Q8WV24: PHLDA1; NbExp=2; IntAct=EBI-356746, EBI-738731; CC P50914; P36578: RPL4; NbExp=2; IntAct=EBI-356746, EBI-348313; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399}. CC -!- POLYMORPHISM: The poly-Ala stretch is highly polymorphic. CC {ECO:0000305|PubMed:11875025, ECO:0000305|PubMed:8549859, CC ECO:0000305|PubMed:9480843, ECO:0000305|Ref.5}. CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL14 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; U16738; AAC16021.1; -; mRNA. DR EMBL; D87735; BAA13443.1; -; mRNA. DR EMBL; AB061822; BAB79460.1; -; Genomic_DNA. DR EMBL; DQ118667; AAZ38460.1; -; mRNA. DR EMBL; AK223111; BAD96831.1; -; mRNA. DR EMBL; AC104186; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC000606; AAH00606.1; -; mRNA. DR EMBL; BC005134; AAH05134.1; -; mRNA. DR EMBL; BC009294; AAH09294.1; -; mRNA. DR EMBL; BC019651; AAH19651.1; -; mRNA. DR EMBL; BC022805; AAH22805.1; -; mRNA. DR EMBL; BC029036; AAH29036.1; -; mRNA. DR EMBL; AB046407; BAB21253.1; -; Genomic_DNA. DR CCDS; CCDS33739.1; -. DR CCDS; CCDS43070.1; -. DR RefSeq; NP_001030168.1; NM_001034996.2. DR RefSeq; NP_003964.3; NM_003973.4. DR PDB; 4UG0; EM; -; LM=1-215. DR PDB; 4V6X; EM; 5.00 A; CM=1-215. DR PDB; 5AJ0; EM; 3.50 A; AM=1-215. DR PDB; 5LKS; EM; 3.60 A; LM=1-215. DR PDB; 5T2C; EM; 3.60 A; s=1-215. DR PDB; 6IP5; EM; 3.90 A; 2G=1-215. DR PDB; 6IP6; EM; 4.50 A; 2G=1-215. DR PDB; 6IP8; EM; 3.90 A; 2G=1-215. DR PDB; 6LQM; EM; 3.09 A; S=1-215. DR PDB; 6LSR; EM; 3.13 A; S=1-215. DR PDB; 6LSS; EM; 3.23 A; S=1-215. DR PDB; 6LU8; EM; 3.13 A; S=1-215. DR PDB; 6OLE; EM; 3.10 A; N=2-140. DR PDB; 6OLF; EM; 3.90 A; N=2-140. DR PDB; 6OLG; EM; 3.40 A; AM=2-140. DR PDB; 6OLI; EM; 3.50 A; N=2-140. DR PDB; 6OLZ; EM; 3.90 A; AM=2-140. DR PDB; 6OM0; EM; 3.10 A; N=2-140. DR PDB; 6OM7; EM; 3.70 A; N=2-140. DR PDB; 6QZP; EM; 2.90 A; LM=2-140. DR PDB; 6W6L; EM; 3.84 A; N=1-215. DR PDB; 6XA1; EM; 2.80 A; LM=2-140. DR PDB; 6Y0G; EM; 3.20 A; LM=1-215. DR PDB; 6Y2L; EM; 3.00 A; LM=1-215. DR PDB; 6Y57; EM; 3.50 A; LM=1-215. DR PDB; 6Y6X; EM; 2.80 A; LM=2-140. DR PDB; 6Z6L; EM; 3.00 A; LM=1-215. DR PDB; 6Z6M; EM; 3.10 A; LM=1-215. DR PDB; 6Z6N; EM; 2.90 A; LM=1-215. DR PDB; 6ZM7; EM; 2.70 A; LM=1-215. DR PDB; 6ZME; EM; 3.00 A; LM=1-215. DR PDB; 6ZMI; EM; 2.60 A; LM=1-215. DR PDB; 6ZMO; EM; 3.10 A; LM=1-215. DR PDB; 7BHP; EM; 3.30 A; LM=1-215. DR PDB; 7F5S; EM; 2.72 A; LM=1-215. DR PDB; 7QVP; EM; 3.00 A; LM/MM=1-215. DR PDB; 7XNX; EM; 2.70 A; LM=1-215. DR PDB; 7XNY; EM; 2.50 A; LM=1-215. DR PDB; 8FKP; EM; 2.85 A; L8=1-215. DR PDB; 8FKQ; EM; 2.76 A; L8=1-215. DR PDB; 8FKR; EM; 2.89 A; L8=1-215. DR PDB; 8FKS; EM; 2.88 A; L8=1-215. DR PDB; 8FKT; EM; 2.81 A; L8=1-215. DR PDB; 8FKU; EM; 2.82 A; L8=1-215. DR PDB; 8FKV; EM; 2.47 A; L8=1-215. DR PDB; 8FKW; EM; 2.50 A; L8=1-215. DR PDB; 8FKX; EM; 2.59 A; L8=1-215. DR PDB; 8FKY; EM; 2.67 A; L8=1-215. DR PDB; 8FKZ; EM; 3.04 A; L8=1-215. DR PDB; 8FL0; EM; 2.91 A; L8=1-215. DR PDB; 8FL2; EM; 2.67 A; L8=1-215. DR PDB; 8FL3; EM; 2.53 A; L8=1-215. DR PDB; 8FL4; EM; 2.89 A; L8=1-215. DR PDB; 8FL6; EM; 2.62 A; L8=1-215. DR PDB; 8FL7; EM; 2.55 A; L8=1-215. DR PDB; 8FL9; EM; 2.75 A; L8=1-215. DR PDB; 8FLA; EM; 2.63 A; L8=1-215. DR PDB; 8FLB; EM; 2.55 A; L8=1-215. DR PDB; 8FLC; EM; 2.76 A; L8=1-215. DR PDB; 8FLD; EM; 2.58 A; L8=1-215. DR PDB; 8FLE; EM; 2.48 A; L8=1-215. DR PDB; 8FLF; EM; 2.65 A; L8=1-215. DR PDB; 8G5Y; EM; 2.29 A; LM=1-215. DR PDB; 8G5Z; EM; 2.64 A; LM=2-137. DR PDB; 8G60; EM; 2.54 A; LM=1-215. DR PDB; 8G61; EM; 2.94 A; LM=1-215. DR PDB; 8G6J; EM; 2.80 A; LM=1-215. DR PDB; 8GLP; EM; 1.67 A; LM=1-215. DR PDB; 8IDT; EM; 2.80 A; S=1-215. DR PDB; 8IDY; EM; 3.00 A; S=1-215. DR PDB; 8IE3; EM; 3.30 A; S=1-215. DR PDB; 8INE; EM; 3.20 A; S=1-215. DR PDB; 8INF; EM; 3.00 A; S=1-215. DR PDB; 8INK; EM; 3.20 A; S=1-215. DR PDB; 8IPD; EM; 3.20 A; S=1-215. DR PDB; 8IPX; EM; 4.30 A; S=1-215. DR PDB; 8IPY; EM; 3.20 A; S=1-215. DR PDB; 8IR1; EM; 3.30 A; S=1-215. DR PDB; 8IR3; EM; 3.50 A; S=1-215. DR PDB; 8JDJ; EM; 2.50 A; R=1-215. DR PDB; 8JDK; EM; 2.26 A; R=1-215. DR PDB; 8JDL; EM; 2.42 A; R=1-215. DR PDB; 8JDM; EM; 2.67 A; R=1-215. 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; 7QVP; -. DR PDBsum; 7XNX; -. DR PDBsum; 7XNY; -. DR PDBsum; 8FKP; -. DR PDBsum; 8FKQ; -. DR PDBsum; 8FKR; -. DR PDBsum; 8FKS; -. DR PDBsum; 8FKT; -. DR PDBsum; 8FKU; -. DR PDBsum; 8FKV; -. DR PDBsum; 8FKW; -. DR PDBsum; 8FKX; -. DR PDBsum; 8FKY; -. DR PDBsum; 8FKZ; -. 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; P50914; -. 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-14181; -. DR EMDB; EMD-29252; -. DR EMDB; EMD-29253; -. DR EMDB; EMD-29254; -. DR EMDB; EMD-29255; -. DR EMDB; EMD-29256; -. DR EMDB; EMD-29257; -. DR EMDB; EMD-29258; -. DR EMDB; EMD-29259; -. DR EMDB; EMD-29260; -. DR EMDB; EMD-29261; -. DR EMDB; EMD-29262; -. 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; P50914; -. DR BioGRID; 114507; 506. 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; P50914; -. DR IntAct; P50914; 145. DR MINT; P50914; -. DR STRING; 9606.ENSP00000379506; -. DR DrugBank; DB11638; Artenimol. DR GlyGen; P50914; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P50914; -. DR MetOSite; P50914; -. DR PhosphoSitePlus; P50914; -. DR SwissPalm; P50914; -. DR BioMuta; RPL14; -. DR DMDM; 212276521; -. DR EPD; P50914; -. DR jPOST; P50914; -. DR MassIVE; P50914; -. DR MaxQB; P50914; -. DR PaxDb; 9606-ENSP00000379506; -. DR PeptideAtlas; P50914; -. DR ProteomicsDB; 56271; -. DR Pumba; P50914; -. DR TopDownProteomics; P50914; -. DR Antibodypedia; 29027; 288 antibodies from 31 providers. DR DNASU; 9045; -. DR Ensembl; ENST00000338970.10; ENSP00000345156.6; ENSG00000188846.14. DR Ensembl; ENST00000396203.7; ENSP00000379506.2; ENSG00000188846.14. DR GeneID; 9045; -. DR KEGG; hsa:9045; -. DR MANE-Select; ENST00000396203.7; ENSP00000379506.2; NM_001034996.3; NP_001030168.1. DR UCSC; uc003ckg.5; human. DR AGR; HGNC:10305; -. DR CTD; 9045; -. DR DisGeNET; 9045; -. DR GeneCards; RPL14; -. DR HGNC; HGNC:10305; RPL14. DR HPA; ENSG00000188846; Low tissue specificity. DR MIM; 617414; gene. DR neXtProt; NX_P50914; -. DR OpenTargets; ENSG00000188846; -. DR PharmGKB; PA34673; -. DR VEuPathDB; HostDB:ENSG00000188846; -. DR eggNOG; KOG3421; Eukaryota. DR GeneTree; ENSGT00390000007888; -. DR HOGENOM; CLU_082438_0_0_1; -. DR InParanoid; P50914; -. DR OMA; PCLFSPN; -. DR OrthoDB; 2658719at2759; -. DR PhylomeDB; P50914; -. DR TreeFam; TF314356; -. DR PathwayCommons; P50914; -. 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; P50914; -. DR SIGNOR; P50914; -. DR BioGRID-ORCS; 9045; 809 hits in 1167 CRISPR screens. DR ChiTaRS; RPL14; human. DR GeneWiki; 60S_ribosomal_protein_L14; -. DR GenomeRNAi; 9045; -. DR Pharos; P50914; Tbio. DR PRO; PR:P50914; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; P50914; Protein. DR Bgee; ENSG00000188846; Expressed in left ovary and 178 other cell types or tissues. DR ExpressionAtlas; P50914; baseline and differential. DR GO; GO:0005737; C:cytoplasm; NAS: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:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB. DR GO; GO:0002181; P:cytoplasmic translation; NAS:ComplexPortal. 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; cd06088; KOW_RPL14; 1. DR Gene3D; 2.30.30.30; -; 1. DR Gene3D; 6.10.250.2270; -; 1. DR InterPro; IPR014722; Rib_uL2_dom2. DR InterPro; IPR039660; Ribosomal_eL14. DR InterPro; IPR002784; Ribosomal_eL14_dom. DR InterPro; IPR041985; Ribosomal_eL14_KOW. DR InterPro; IPR008991; Translation_prot_SH3-like_sf. DR PANTHER; PTHR11127; 60S RIBOSOMAL PROTEIN L14; 1. DR PANTHER; PTHR11127:SF4; 60S RIBOSOMAL PROTEIN L14; 1. DR Pfam; PF01929; Ribosomal_L14e; 1. DR SUPFAM; SSF50104; Translation proteins SH3-like domain; 1. DR SWISS-2DPAGE; P50914; -. DR Genevisible; P50914; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; KW Isopeptide bond; Phosphoprotein; Reference proteome; Repeat; KW Ribonucleoprotein; Ribosomal protein; Triplet repeat expansion; KW Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:12962325" FT CHAIN 2..215 FT /note="Large ribosomal subunit protein eL14" FT /id="PRO_0000132031" FT REPEAT 171..175 FT /note="1-1" FT REPEAT 176..180 FT /note="1-2" FT REPEAT 181..185 FT /note="1-3" FT REPEAT 186..190 FT /note="1-4" FT REPEAT 193..195 FT /note="2-1" FT REPEAT 196..198 FT /note="2-2" FT REGION 161..215 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 171..190 FT /note="4 X 5 AA tandem repeats of Q-K-A-[PAS]-X" FT REGION 193..198 FT /note="2 X 3 AA tandem repeats of K-[GA]-Q" FT MOD_RES 79 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 85 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 85 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9CR57" FT MOD_RES 139 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 204 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9CR57" FT CROSSLNK 124 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT VARIANT 138 FT /note="A -> S (in dbSNP:rs929099541)" FT /id="VAR_013633" FT VARIANT 158..159 FT /note="Missing" FT /evidence="ECO:0000269|PubMed:8549859, ECO:0000269|Ref.10" FT /id="VAR_047109" FT VARIANT 159 FT /note="A -> AA" FT /id="VAR_013634" FT VARIANT 159 FT /note="A -> AAA" FT /id="VAR_014070" FT VARIANT 159 FT /note="A -> AAAA" FT /id="VAR_013635" FT VARIANT 159 FT /note="A -> AAAAA" FT /id="VAR_013636" FT VARIANT 159 FT /note="A -> AAAAAA" FT /evidence="ECO:0000269|PubMed:11875025, FT ECO:0000269|PubMed:9480843, ECO:0000269|Ref.5" FT /id="VAR_006923" FT VARIANT 159 FT /note="A -> AAAAAAAA" FT /id="VAR_013637" FT CONFLICT 65 FT /note="P -> L (in Ref. 2; BAA13443)" FT /evidence="ECO:0000305" SQ SEQUENCE 215 AA; 23432 MW; 4C63DE4FC8E687FE CRC64; MVFRRFVEVG RVAYVSFGPH AGKLVAIVDV IDQNRALVDG PCTQVRRQAM PFKCMQLTDF ILKFPHSAHQ KYVRQAWQKA DINTKWAATR WAKKIEARER KAKMTDFDRF KVMKAKKMRN RIIKNEVKKL QKAALLKASP KKAPGTKGTA AAAAAAAAAK VPAKKITAAS KKAPAQKVPA QKATGQKAAP APKAQKGQKA PAQKAPAPKA SGKKA //