RL14_HUMAN
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 03-AUG-2022, entry version 218.
DE RecName: Full=60S ribosomal protein L14;
DE AltName: Full=CAG-ISL 7;
DE AltName: Full=Large ribosomal subunit protein eL14 {ECO:0000303|PubMed:24524803};
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}.
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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 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 AlphaFoldDB; P50914; -.
DR SMR; P50914; -.
DR BioGRID; 114507; 438.
DR ComplexPortal; CPX-5183; 60S cytosolic large ribosomal subunit.
DR CORUM; P50914; -.
DR IntAct; P50914; 138.
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 SWISS-2DPAGE; P50914; -.
DR EPD; P50914; -.
DR jPOST; P50914; -.
DR MassIVE; P50914; -.
DR MaxQB; P50914; -.
DR PaxDb; P50914; -.
DR PeptideAtlas; P50914; -.
DR PRIDE; P50914; -.
DR ProteomicsDB; 56271; -.
DR TopDownProteomics; P50914; -.
DR Antibodypedia; 29027; 260 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 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; RWANCAW; -.
DR OrthoDB; 1433759at2759; -.
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; 775 hits in 1085 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 176 other tissues.
DR ExpressionAtlas; P50914; baseline and differential.
DR Genevisible; P50914; 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; IPI:ComplexPortal.
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:FlyBase.
DR GO; GO:0002181; P:cytoplasmic translation; IC:FlyBase.
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 InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR002784; Ribosomal_L14e_dom.
DR InterPro; IPR039660; Ribosomal_protein_L14.
DR InterPro; IPR041985; RPL14_KOW.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR11127; PTHR11127; 1.
DR Pfam; PF01929; Ribosomal_L14e; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
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="60S ribosomal protein L14"
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
