ID RL4_HUMAN Reviewed; 427 AA. AC P36578; A8K502; P39029; Q4VBR0; Q969Z9; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 5. DT 24-JUL-2024, entry version 225. DE RecName: Full=Large ribosomal subunit protein uL4 {ECO:0000303|PubMed:24524803}; DE AltName: Full=60S ribosomal protein L1; DE AltName: Full=60S ribosomal protein L4; GN Name=RPL4; Synonyms=RPL1; 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=Brain; RX PubMed=8268230; DOI=10.1016/0167-4781(93)90017-8; RA Bagni C., Mariottini P., Annesi F., Amaldi F.; RT "Human ribosomal protein L4: cloning and sequencing of the cDNA and primary RT structure of the protein."; RL Biochim. Biophys. Acta 1216:475-478(1993). RN [2] RP SEQUENCE REVISION. RA Bagni C.; RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Lymphoma; RA Kato S.; RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=11875025; DOI=10.1101/gr.214202; RA Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S., RA Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.; RT "The human ribosomal protein genes: sequencing and comparative analysis of RT 73 genes."; RL Genome Res. 12:379-390(2002). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skeletal muscle; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Colon, Embryonic stem cell, Eye, Hippocampus, Muscle, Pancreas, RC 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 PROTEIN SEQUENCE OF 2-13, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT RP ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=T-cell; RA Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.; RL Submitted (MAY-2006) to UniProtKB. RN [9] RP INTERACTION WITH IPO9. RX PubMed=11823430; DOI=10.1093/emboj/21.3.377; RA Jaekel S., Mingot J.-M., Schwarzmaier P., Hartmann E., Goerlich D.; RT "Importins fulfill a dual function as nuclear import receptors and RT cytoplasmic chaperones for exposed basic domains."; RL EMBO J. 21:377-386(2002). RN [10] 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295 AND SER-365, AND RP IDENTIFICATION BY 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 [12] 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 [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-14; LYS-106 AND LYS-333, AND RP IDENTIFICATION 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295 AND SER-365, AND RP IDENTIFICATION BY 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 [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 THR-266 AND SER-295, 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 [18] 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 [19] 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 [20] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-364, 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 [21] 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 [22] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-239 AND LYS-327, 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 [23] 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 [24] {ECO:0007744|PDB:6LQM, ECO:0007744|PDB:6LSR, ECO:0007744|PDB:6LSS, ECO:0007744|PDB:6LU8} RP STRUCTURE BY ELECTRON MICROSCOPY (3.09 ANGSTROMS), FUNCTION, AND SUBUNIT. RX PubMed=32669547; DOI=10.1038/s41467-020-17237-x; RA Liang X., Zuo M.Q., Zhang Y., Li N., Ma C., Dong M.Q., Gao N.; RT "Structural snapshots of human pre-60S ribosomal particles before and after RT nuclear export."; RL Nat. Commun. 11:3542-3542(2020). CC -!- FUNCTION: Component of the large ribosomal subunit. The ribosome is a CC large ribonucleoprotein complex responsible for the synthesis of CC proteins in the cell. {ECO:0000269|PubMed:23636399, CC ECO:0000269|PubMed:32669547}. CC -!- SUBUNIT: Component of the large ribosomal subunit (PubMed:23636399, CC PubMed:32669547). May bind IPO9 with low affinity (PubMed:11823430). CC Interacts with RBM3 (By similarity). {ECO:0000250|UniProtKB:P50878, CC ECO:0000269|PubMed:11823430, ECO:0000269|PubMed:23636399, CC ECO:0000269|PubMed:32669547}. CC -!- INTERACTION: CC P36578; P42858: HTT; NbExp=14; IntAct=EBI-348313, EBI-466029; CC P36578; Q99558: MAP3K14; NbExp=3; IntAct=EBI-348313, EBI-358011; CC P36578; P50914: RPL14; NbExp=2; IntAct=EBI-348313, EBI-356746; CC P36578; Q02543: RPL18A; NbExp=2; IntAct=EBI-348313, EBI-350523; CC P36578; P46779: RPL28; NbExp=2; IntAct=EBI-348313, EBI-366357; CC P36578; P60866: RPS20; NbExp=4; IntAct=EBI-348313, EBI-353105; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399}. CC -!- PTM: Citrullinated by PADI4. {ECO:0000250|UniProtKB:Q9D8E6}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL4 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; L20868; AAA60281.2; -; mRNA. DR EMBL; D23660; BAA04887.1; -; mRNA. DR EMBL; AB061820; BAB79458.1; -; Genomic_DNA. DR EMBL; AK291117; BAF83806.1; -; mRNA. DR EMBL; AK291859; BAF84548.1; -; mRNA. DR EMBL; CH471082; EAW77776.1; -; Genomic_DNA. DR EMBL; BC001365; AAH01365.1; -; mRNA. DR EMBL; BC005817; AAH05817.1; -; mRNA. DR EMBL; BC007748; AAH07748.1; -; mRNA. DR EMBL; BC007996; AAH07996.1; -; mRNA. DR EMBL; BC009888; AAH09888.1; -; mRNA. DR EMBL; BC010151; AAH10151.1; -; mRNA. DR EMBL; BC014653; AAH14653.1; -; mRNA. DR EMBL; BC066925; AAH66925.1; -; mRNA. DR EMBL; BC095427; AAH95427.1; -; mRNA. DR CCDS; CCDS10218.1; -. DR PIR; T09551; T09551. DR RefSeq; NP_000959.2; NM_000968.3. DR PDB; 4UG0; EM; -; LC=1-427. DR PDB; 4V6X; EM; 5.00 A; CC=1-427. DR PDB; 5A8L; EM; 3.80 A; H=1-427. DR PDB; 5AJ0; EM; 3.50 A; AC=1-427. DR PDB; 5LKS; EM; 3.60 A; LC=1-427. DR PDB; 5T2C; EM; 3.60 A; F=1-427. DR PDB; 6IP5; EM; 3.90 A; 1F=1-427. DR PDB; 6IP6; EM; 4.50 A; 1F=1-427. DR PDB; 6IP8; EM; 3.90 A; 1F=1-427. DR PDB; 6LQM; EM; 3.09 A; D=1-427. DR PDB; 6LSR; EM; 3.13 A; D=1-427. DR PDB; 6LSS; EM; 3.23 A; D=1-427. DR PDB; 6LU8; EM; 3.13 A; D=1-427. DR PDB; 6OLE; EM; 3.10 A; C=3-365. DR PDB; 6OLF; EM; 3.90 A; C=3-365. DR PDB; 6OLG; EM; 3.40 A; AC=3-365. DR PDB; 6OLI; EM; 3.50 A; C=3-365. DR PDB; 6OLZ; EM; 3.90 A; AC=3-365. DR PDB; 6OM0; EM; 3.10 A; C=3-365. DR PDB; 6OM7; EM; 3.70 A; C=3-365. DR PDB; 6QZP; EM; 2.90 A; LC=1-368. DR PDB; 6W6L; EM; 3.84 A; C=1-427. DR PDB; 6XA1; EM; 2.80 A; LC=1-358. DR PDB; 6Y0G; EM; 3.20 A; LC=1-427. DR PDB; 6Y2L; EM; 3.00 A; LC=1-427. DR PDB; 6Y57; EM; 3.50 A; LC=1-427. DR PDB; 6Y6X; EM; 2.80 A; LC=1-368. DR PDB; 6Z6L; EM; 3.00 A; LC=1-427. DR PDB; 6Z6M; EM; 3.10 A; LC=1-427. DR PDB; 6Z6N; EM; 2.90 A; LC=1-427. DR PDB; 6ZM7; EM; 2.70 A; LC=1-427. DR PDB; 6ZME; EM; 3.00 A; LC=1-427. DR PDB; 6ZMI; EM; 2.60 A; LC=1-427. DR PDB; 6ZMO; EM; 3.10 A; LC=1-427. DR PDB; 7BHP; EM; 3.30 A; LC=1-427. DR PDB; 7F5S; EM; 2.72 A; LC=1-427. DR PDB; 7OW7; EM; 2.20 A; F=1-427. DR PDB; 7QVP; EM; 3.00 A; LC/MC=1-427. DR PDB; 7XNX; EM; 2.70 A; LC=1-427. DR PDB; 7XNY; EM; 2.50 A; LC=1-427. DR PDB; 8A3D; EM; 1.67 A; F=1-427. DR PDB; 8FKP; EM; 2.85 A; SA=1-427. DR PDB; 8FKQ; EM; 2.76 A; SA=1-427. DR PDB; 8FKR; EM; 2.89 A; SA=1-427. DR PDB; 8FKS; EM; 2.88 A; SA=1-427. DR PDB; 8FKT; EM; 2.81 A; SA=1-427. DR PDB; 8FKU; EM; 2.82 A; SA=1-427. DR PDB; 8FKV; EM; 2.47 A; SA=1-427. DR PDB; 8FKW; EM; 2.50 A; SA=1-427. DR PDB; 8FKX; EM; 2.59 A; SA=1-427. DR PDB; 8FKY; EM; 2.67 A; SA=1-427. DR PDB; 8FKZ; EM; 3.04 A; SA=1-427. DR PDB; 8FL0; EM; 2.91 A; SA=1-427. DR PDB; 8FL2; EM; 2.67 A; SA=1-427. DR PDB; 8FL3; EM; 2.53 A; SA=1-427. DR PDB; 8FL4; EM; 2.89 A; SA=1-427. DR PDB; 8FL6; EM; 2.62 A; SA=1-427. DR PDB; 8FL7; EM; 2.55 A; SA=1-427. DR PDB; 8FL9; EM; 2.75 A; SA=1-427. DR PDB; 8FLA; EM; 2.63 A; SA=1-427. DR PDB; 8FLB; EM; 2.55 A; SA=1-427. DR PDB; 8FLC; EM; 2.76 A; SA=1-427. DR PDB; 8FLD; EM; 2.58 A; SA=1-427. DR PDB; 8FLE; EM; 2.48 A; SA=1-427. DR PDB; 8FLF; EM; 2.65 A; SA=1-427. DR PDB; 8G5Y; EM; 2.29 A; LC=1-427. DR PDB; 8G5Z; EM; 2.64 A; LC=1-368. DR PDB; 8G60; EM; 2.54 A; LC=1-427. DR PDB; 8G61; EM; 2.94 A; LC=1-427. DR PDB; 8G6J; EM; 2.80 A; LC=1-427. DR PDB; 8GLP; EM; 1.67 A; LC=1-427. DR PDB; 8IDT; EM; 2.80 A; D=1-427. DR PDB; 8IDY; EM; 3.00 A; D=1-427. DR PDB; 8IE3; EM; 3.30 A; D=1-427. DR PDB; 8IFD; EM; 2.59 A; 1F=1-427. DR PDB; 8IFE; EM; 2.57 A; 1F=1-427. DR PDB; 8INE; EM; 3.20 A; D=1-427. DR PDB; 8INF; EM; 3.00 A; D=1-427. DR PDB; 8INK; EM; 3.20 A; D=1-427. DR PDB; 8IPD; EM; 3.20 A; D=1-427. DR PDB; 8IPX; EM; 4.30 A; D=1-427. DR PDB; 8IPY; EM; 3.20 A; D=1-427. DR PDB; 8IR1; EM; 3.30 A; D=1-427. DR PDB; 8IR3; EM; 3.50 A; D=1-427. DR PDB; 8JDJ; EM; 2.50 A; I=1-427. DR PDB; 8JDK; EM; 2.26 A; I=1-427. DR PDB; 8JDL; EM; 2.42 A; I=1-427. DR PDB; 8JDM; EM; 2.67 A; I=1-427. DR PDB; 8OHD; EM; 3.10 A; LC=1-427. DR PDB; 8OJ0; EM; 3.30 A; LC=1-427. DR PDB; 8OJ5; EM; 2.90 A; LC=1-427. DR PDB; 8OJ8; EM; 3.30 A; LC=1-427. DR PDB; 8QFD; EM; 2.20 A; C=1-427. DR PDB; 8Y0W; EM; 3.40 A; LC=1-427. DR PDB; 8Y0X; EM; 3.30 A; LC=1-427. DR PDBsum; 4UG0; -. DR PDBsum; 4V6X; -. DR PDBsum; 5A8L; -. 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; 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; 8IFD; -. DR PDBsum; 8IFE; -. 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 PDBsum; 8OHD; -. DR PDBsum; 8OJ0; -. DR PDBsum; 8OJ5; -. DR PDBsum; 8OJ8; -. DR PDBsum; 8QFD; -. DR PDBsum; 8Y0W; -. DR PDBsum; 8Y0X; -. DR AlphaFoldDB; P36578; -. 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-16880; -. DR EMDB; EMD-16902; -. DR EMDB; EMD-16905; -. DR EMDB; EMD-16908; -. DR EMDB; EMD-18382; -. 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-35413; -. DR EMDB; EMD-35414; -. 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-36178; -. DR EMDB; EMD-36179; -. DR EMDB; EMD-36180; -. DR EMDB; EMD-36181; -. 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; P36578; -. DR BioGRID; 112044; 734. 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; P36578; -. DR DIP; DIP-27559N; -. DR IntAct; P36578; 145. DR MINT; P36578; -. DR STRING; 9606.ENSP00000311430; -. DR DrugBank; DB11638; Artenimol. DR GlyGen; P36578; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P36578; -. DR MetOSite; P36578; -. DR PhosphoSitePlus; P36578; -. DR SwissPalm; P36578; -. DR BioMuta; RPL4; -. DR DMDM; 22002063; -. DR jPOST; P36578; -. DR MassIVE; P36578; -. DR PaxDb; 9606-ENSP00000311430; -. DR PeptideAtlas; P36578; -. DR ProteomicsDB; 55216; -. DR Pumba; P36578; -. DR TopDownProteomics; P36578; -. DR Antibodypedia; 26140; 176 antibodies from 29 providers. DR DNASU; 6124; -. DR Ensembl; ENST00000307961.11; ENSP00000311430.6; ENSG00000174444.15. DR GeneID; 6124; -. DR KEGG; hsa:6124; -. DR MANE-Select; ENST00000307961.11; ENSP00000311430.6; NM_000968.4; NP_000959.2. DR UCSC; uc002apv.4; human. DR AGR; HGNC:10353; -. DR CTD; 6124; -. DR DisGeNET; 6124; -. DR GeneCards; RPL4; -. DR HGNC; HGNC:10353; RPL4. DR HPA; ENSG00000174444; Low tissue specificity. DR MIM; 180479; gene. DR neXtProt; NX_P36578; -. DR OpenTargets; ENSG00000174444; -. DR PharmGKB; PA34749; -. DR VEuPathDB; HostDB:ENSG00000174444; -. DR eggNOG; KOG1475; Eukaryota. DR GeneTree; ENSGT00390000018145; -. DR HOGENOM; CLU_026535_4_0_1; -. DR InParanoid; P36578; -. DR OMA; ASWTHRI; -. DR OrthoDB; 275636at2759; -. DR PhylomeDB; P36578; -. DR TreeFam; TF300593; -. DR PathwayCommons; P36578; -. 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; P36578; -. DR SIGNOR; P36578; -. DR BioGRID-ORCS; 6124; 824 hits in 1165 CRISPR screens. DR ChiTaRS; RPL4; human. DR EvolutionaryTrace; P36578; -. DR GeneWiki; Ribosomal_protein_L4; -. DR GenomeRNAi; 6124; -. DR Pharos; P36578; Tbio. DR PRO; PR:P36578; -. DR Proteomes; UP000005640; Chromosome 15. DR RNAct; P36578; Protein. DR Bgee; ENSG00000174444; Expressed in cortical plate and 220 other cell types or tissues. DR ExpressionAtlas; P36578; baseline and differential. DR GO; GO:0005737; C:cytoplasm; HDA:UniProtKB. 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:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; HDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI. DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:UniProtKB. 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:0006412; P:translation; TAS:ProtInc. DR DisProt; DP01654; -. DR Gene3D; 3.40.1370.10; -; 1. DR InterPro; IPR025755; Ribos_uL4_C_dom. DR InterPro; IPR002136; Ribosomal_uL4. DR InterPro; IPR023574; Ribosomal_uL4_dom_sf. DR InterPro; IPR013000; Ribosomal_uL4_euk/arc_CS. DR InterPro; IPR045240; Ribosomal_uL4_euk/arch. DR PANTHER; PTHR19431; 60S RIBOSOMAL PROTEIN L4; 1. DR PANTHER; PTHR19431:SF0; 60S RIBOSOMAL PROTEIN L4; 1. DR Pfam; PF14374; Ribos_L4_asso_C; 1. DR Pfam; PF00573; Ribosomal_L4; 1. DR SUPFAM; SSF52166; Ribosomal protein L4; 1. DR PROSITE; PS00939; RIBOSOMAL_L1E; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Citrullination; Cytoplasm; KW Direct protein sequencing; Isopeptide bond; Methylation; Phosphoprotein; KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330" FT CHAIN 2..427 FT /note="Large ribosomal subunit protein uL4" FT /id="PRO_0000129350" FT REGION 369..427 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 377..400 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 404..427 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330" FT MOD_RES 14 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 97 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q9D8E6" FT MOD_RES 106 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 259 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9D8E6" FT MOD_RES 266 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 290 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P50878" FT MOD_RES 295 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 300 FT /note="Citrulline" FT /evidence="ECO:0000250|UniProtKB:Q9D8E6" FT MOD_RES 333 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 353 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9D8E6" FT MOD_RES 364 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9D8E6" FT MOD_RES 365 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:20068231" FT CROSSLNK 239 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 327 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 364 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CONFLICT 3 FT /note="C -> V (in Ref. 1; AAA60281)" FT /evidence="ECO:0000305" FT CONFLICT 36 FT /note="I -> M (in Ref. 1; AAA60281)" FT /evidence="ECO:0000305" FT CONFLICT 63 FT /note="S -> R (in Ref. 1; AAA60281)" FT /evidence="ECO:0000305" FT CONFLICT 147 FT /note="V -> F (in Ref. 1; AAA60281)" FT /evidence="ECO:0000305" FT CONFLICT 201 FT /note="Missing (in Ref. 1; AAA60281)" FT /evidence="ECO:0000305" SQ SEQUENCE 427 AA; 47697 MW; 4785ED31699CD792 CRC64; MACARPLISV YSEKGESSGK NVTLPAVFKA PIRPDIVNFV HTNLRKNNRQ PYAVSELAGH QTSAESWGTG RAVARIPRVR GGGTHRSGQG AFGNMCRGGR MFAPTKTWRR WHRRVNTTQK RYAICSALAA SALPALVMSK GHRIEEVPEL PLVVEDKVEG YKKTKEAVLL LKKLKAWNDI KKVYASQRMR AGKGKMRNRR RIQRRGPCII YNEDNGIIKA FRNIPGITLL NVSKLNILKL APGGHVGRFC IWTESAFRKL DELYGTWRKA ASLKSNYNLP MHKMINTDLS RILKSPEIQR ALRAPRKKIH RRVLKKNPLK NLRIMLKLNP YAKTMRRNTI LRQARNHKLR VDKAAAAAAA LQAKSDEKAA VAGKKPVVGK KGKKAAVGVK KQKKPLVGKK AAATKKPAPE KKPAEKKPTT EEKKPAA //