RL4_HUMAN
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 03-AUG-2022, entry version 214.
DE RecName: Full=60S ribosomal protein L4;
DE AltName: Full=60S ribosomal protein L1;
DE AltName: Full=Large ribosomal subunit protein uL4 {ECO:0000303|PubMed:24524803};
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, and
RC 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 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 AlphaFoldDB; P36578; -.
DR SMR; P36578; -.
DR BioGRID; 112044; 609.
DR ComplexPortal; CPX-5183; 60S cytosolic large ribosomal subunit.
DR CORUM; P36578; -.
DR DIP; DIP-27559N; -.
DR IntAct; P36578; 125.
DR MINT; P36578; -.
DR STRING; 9606.ENSP00000311430; -.
DR DrugBank; DB11638; Artenimol.
DR GlyGen; P36578; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P36578; -.
DR MetOSite; P36578; -.
DR PhosphoSitePlus; P36578; -.
DR SwissPalm; P36578; -.
DR BioMuta; RPL4; -.
DR DMDM; 22002063; -.
DR SWISS-2DPAGE; P36578; -.
DR EPD; P36578; -.
DR jPOST; P36578; -.
DR MassIVE; P36578; -.
DR MaxQB; P36578; -.
DR PaxDb; P36578; -.
DR PeptideAtlas; P36578; -.
DR PRIDE; P36578; -.
DR ProteomicsDB; 55216; -.
DR TopDownProteomics; P36578; -.
DR Antibodypedia; 26140; 175 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 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; WHQKVNV; -.
DR OrthoDB; 878848at2759; -.
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; 786 hits in 1084 CRISPR screens.
DR ChiTaRS; RPL4; human.
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 218 other tissues.
DR ExpressionAtlas; P36578; baseline and differential.
DR Genevisible; P36578; HS.
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; IPI:ComplexPortal.
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:FlyBase.
DR GO; GO:0002181; P:cytoplasmic translation; IC:FlyBase.
DR GO; GO:0006412; P:translation; TAS:ProtInc.
DR DisProt; DP01654; -.
DR Gene3D; 3.40.1370.10; -; 1.
DR InterPro; IPR025755; Ribos_L4_C_dom.
DR InterPro; IPR002136; Ribosomal_L4/L1e.
DR InterPro; IPR013000; Ribosomal_L4/L1e_euk/arc_CS.
DR InterPro; IPR023574; Ribosomal_L4_dom_sf.
DR InterPro; IPR045240; Ribosomal_L4_euk/arch.
DR PANTHER; PTHR19431; PTHR19431; 1.
DR Pfam; PF14374; Ribos_L4_asso_C; 1.
DR Pfam; PF00573; Ribosomal_L4; 1.
DR SUPFAM; SSF52166; SSF52166; 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="60S ribosomal protein L4"
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
