ID RL38_HUMAN Reviewed; 70 AA. AC P63173; B2R5A8; P23411; DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 173. DE RecName: Full=Large ribosomal subunit protein eL38 {ECO:0000303|PubMed:24524803}; DE AltName: Full=60S ribosomal protein L38; GN Name=RPL38; 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]. RX PubMed=9375793; DOI=10.1016/s0167-4781(97)00124-3; RA Espinosa L., Martin M., Nicolas A., Fabre M., Navarro E.; RT "Primary sequence of the human, lysine-rich, ribosomal protein RPL38 and RT detection of an unusual RPL38 processed pseudogene in the promoter region RT of the type-1 angiotensin II receptor gene."; RL Biochim. Biophys. Acta 1354:58-64(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Thymus; 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 [3] 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=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 [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-70. RX PubMed=9582194; DOI=10.1101/gr.8.5.509; RA Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J., RA Tanaka T., Page D.C.; RT "A map of 75 human ribosomal protein genes."; RL Genome Res. 8:509-523(1998). RN [6] 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 [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-9 AND LYS-67, 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 [8] 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 [9] 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 [10] 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 [11] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-4 AND LYS-9, AND IDENTIFICATION RP 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 [12] 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 [13] {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. CC {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:32669547}. CC -!- INTERACTION: CC P63173; Q9P287: BCCIP; NbExp=3; IntAct=EBI-359141, EBI-711154; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399}. CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL38 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; Z26876; CAA81488.1; -; mRNA. DR EMBL; AK312119; BAG35055.1; -; mRNA. DR EMBL; CH471099; EAW89137.1; -; Genomic_DNA. DR EMBL; BC000603; AAH00603.1; -; mRNA. DR EMBL; AB007185; BAA25844.1; -; Genomic_DNA. DR CCDS; CCDS11696.1; -. DR PIR; S38385; S38385. DR RefSeq; NP_000990.1; NM_000999.3. DR RefSeq; NP_001030335.1; NM_001035258.1. DR PDB; 4UG0; EM; -; Lk=1-70. DR PDB; 4V6X; EM; 5.00 A; Ck=1-70. DR PDB; 5AJ0; EM; 3.50 A; Ak=1-70. DR PDB; 5LKS; EM; 3.60 A; Lk=1-70. DR PDB; 5T2C; EM; 3.60 A; e=1-70. DR PDB; 6IP5; EM; 3.90 A; 2e=1-70. DR PDB; 6IP6; EM; 4.50 A; 2e=1-70. DR PDB; 6IP8; EM; 3.90 A; 2e=1-70. DR PDB; 6LQM; EM; 3.09 A; O=1-70. DR PDB; 6LSR; EM; 3.13 A; O=1-70. DR PDB; 6LSS; EM; 3.23 A; O=1-70. DR PDB; 6LU8; EM; 3.13 A; O=1-70. DR PDB; 6OLE; EM; 3.10 A; l=2-70. DR PDB; 6OLF; EM; 3.90 A; l=2-70. DR PDB; 6OLG; EM; 3.40 A; Ak=2-70. DR PDB; 6OLI; EM; 3.50 A; l=2-70. DR PDB; 6OLZ; EM; 3.90 A; Ak=2-70. DR PDB; 6OM0; EM; 3.10 A; l=2-70. DR PDB; 6OM7; EM; 3.70 A; l=2-70. DR PDB; 6QZP; EM; 2.90 A; Lk=2-70. DR PDB; 6SXO; EM; 3.30 A; Lk=1-70. DR PDB; 6W6L; EM; 3.84 A; l=1-70. DR PDB; 6XA1; EM; 2.80 A; Lk=2-70. DR PDB; 6Y0G; EM; 3.20 A; Lk=1-70. DR PDB; 6Y2L; EM; 3.00 A; Lk=1-70. DR PDB; 6Y57; EM; 3.50 A; Lk=1-70. DR PDB; 6Y6X; EM; 2.80 A; Lk=2-70. DR PDB; 6Z6L; EM; 3.00 A; Lk=1-70. DR PDB; 6Z6M; EM; 3.10 A; Lk=1-70. DR PDB; 6Z6N; EM; 2.90 A; Lk=1-70. DR PDB; 6ZM7; EM; 2.70 A; Lk=1-70. DR PDB; 6ZME; EM; 3.00 A; Lk=1-70. DR PDB; 6ZMI; EM; 2.60 A; Lk=1-70. DR PDB; 6ZMO; EM; 3.10 A; Lk=1-70. DR PDB; 7BHP; EM; 3.30 A; Lk=1-70. DR PDB; 7F5S; EM; 2.72 A; Lk=1-70. DR PDB; 7OW7; EM; 2.20 A; e=1-70. DR PDB; 7XNX; EM; 2.70 A; Lk=1-70. DR PDB; 7XNY; EM; 2.50 A; Lk=1-70. DR PDB; 8A3D; EM; 1.67 A; e=1-70. DR PDB; 8FKZ; EM; 3.04 A; LY=1-70. DR PDB; 8FL2; EM; 2.67 A; LY=1-70. DR PDB; 8FL3; EM; 2.53 A; LY=1-70. DR PDB; 8FL4; EM; 2.89 A; LY=1-70. DR PDB; 8FL6; EM; 2.62 A; LY=1-70. DR PDB; 8FL7; EM; 2.55 A; LY=1-70. DR PDB; 8FL9; EM; 2.75 A; LY=1-70. DR PDB; 8FLA; EM; 2.63 A; LY=1-70. DR PDB; 8FLB; EM; 2.55 A; LY=1-70. DR PDB; 8FLC; EM; 2.76 A; LY=1-70. DR PDB; 8FLD; EM; 2.58 A; LY=1-70. DR PDB; 8FLE; EM; 2.48 A; LY=1-70. DR PDB; 8FLF; EM; 2.65 A; LY=1-70. DR PDB; 8G5Y; EM; 2.29 A; Lk=1-70. DR PDB; 8G5Z; EM; 2.64 A; Lk=2-70. DR PDB; 8G60; EM; 2.54 A; Lk=1-70. DR PDB; 8G61; EM; 2.94 A; Lk=1-70. DR PDB; 8G6J; EM; 2.80 A; Lk=1-70. DR PDB; 8GLP; EM; 1.67 A; Lk=1-70. DR PDB; 8IDT; EM; 2.80 A; O=1-70. DR PDB; 8IDY; EM; 3.00 A; O=1-70. DR PDB; 8IE3; EM; 3.30 A; O=1-70. DR PDB; 8INE; EM; 3.20 A; O=1-70. DR PDB; 8INF; EM; 3.00 A; O=1-70. DR PDB; 8INK; EM; 3.20 A; O=1-70. DR PDB; 8IPD; EM; 3.20 A; O=1-70. DR PDB; 8IPX; EM; 4.30 A; O=1-70. DR PDB; 8IPY; EM; 3.20 A; O=1-70. DR PDB; 8IR1; EM; 3.30 A; O=1-70. DR PDB; 8IR3; EM; 3.50 A; O=1-70. DR PDB; 8JDJ; EM; 2.50 A; p=1-70. DR PDB; 8JDK; EM; 2.26 A; p=1-70. DR PDB; 8JDL; EM; 2.42 A; p=1-70. DR PDB; 8JDM; EM; 2.67 A; p=1-70. 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; 6SXO; -. 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; 7XNX; -. DR PDBsum; 7XNY; -. DR PDBsum; 8A3D; -. DR PDBsum; 8FKZ; -. 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; P63173; -. DR EMDB; EMD-0948; -. DR EMDB; EMD-0963; -. DR EMDB; EMD-0964; -. DR EMDB; EMD-0978; -. DR EMDB; EMD-10344; -. 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-15113; -. DR EMDB; EMD-29262; -. 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; P63173; -. DR BioGRID; 112088; 307. 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; P63173; -. DR IntAct; P63173; 59. DR MINT; P63173; -. DR STRING; 9606.ENSP00000309830; -. DR GlyGen; P63173; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P63173; -. DR PhosphoSitePlus; P63173; -. DR SwissPalm; P63173; -. DR BioMuta; RPL38; -. DR DMDM; 52783779; -. DR EPD; P63173; -. DR jPOST; P63173; -. DR MassIVE; P63173; -. DR MaxQB; P63173; -. DR PaxDb; 9606-ENSP00000309830; -. DR PeptideAtlas; P63173; -. DR ProteomicsDB; 57503; -. DR Pumba; P63173; -. DR TopDownProteomics; P63173; -. DR Antibodypedia; 45939; 125 antibodies from 19 providers. DR DNASU; 6169; -. DR Ensembl; ENST00000311111.11; ENSP00000309830.6; ENSG00000172809.13. DR Ensembl; ENST00000439590.6; ENSP00000390279.2; ENSG00000172809.13. DR Ensembl; ENST00000533498.1; ENSP00000434243.1; ENSG00000172809.13. DR GeneID; 6169; -. DR KEGG; hsa:6169; -. DR MANE-Select; ENST00000311111.11; ENSP00000309830.6; NM_000999.4; NP_000990.1. DR UCSC; uc002jjz.4; human. DR AGR; HGNC:10349; -. DR CTD; 6169; -. DR DisGeNET; 6169; -. DR GeneCards; RPL38; -. DR HGNC; HGNC:10349; RPL38. DR HPA; ENSG00000172809; Low tissue specificity. DR MIM; 604182; gene. DR neXtProt; NX_P63173; -. DR OpenTargets; ENSG00000172809; -. DR PharmGKB; PA34741; -. DR VEuPathDB; HostDB:ENSG00000172809; -. DR eggNOG; KOG3499; Eukaryota. DR GeneTree; ENSGT00390000003718; -. DR InParanoid; P63173; -. DR OMA; RCHRFIY; -. DR OrthoDB; 242478at2759; -. DR PhylomeDB; P63173; -. DR TreeFam; TF300215; -. DR PathwayCommons; P63173; -. 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; P63173; -. DR SIGNOR; P63173; -. DR BioGRID-ORCS; 6169; 824 hits in 1160 CRISPR screens. DR ChiTaRS; RPL38; human. DR GeneWiki; 60S_ribosomal_protein_L38; -. DR GenomeRNAi; 6169; -. DR Pharos; P63173; Tbio. DR PRO; PR:P63173; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; P63173; Protein. DR Bgee; ENSG00000172809; Expressed in calcaneal tendon and 212 other cell types or tissues. DR ExpressionAtlas; P63173; 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:0033291; C:eukaryotic 80S initiation complex; IEA:Ensembl. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO. DR GO; GO:0003723; F:RNA binding; TAS:ProtInc. DR GO; GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB. DR GO; GO:0034463; P:90S preribosome assembly; IEA:Ensembl. DR GO; GO:0048318; P:axial mesoderm development; IEA:Ensembl. DR GO; GO:0002181; P:cytoplasmic translation; IDA:UniProtKB. DR GO; GO:0042474; P:middle ear morphogenesis; IEA:Ensembl. DR GO; GO:0001503; P:ossification; IEA:Ensembl. DR GO; GO:0022618; P:protein-RNA complex assembly; IBA:GO_Central. DR GO; GO:0006417; P:regulation of translation; IEA:Ensembl. DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl. DR GO; GO:0001501; P:skeletal system development; IEA:Ensembl. DR GO; GO:0006412; P:translation; TAS:ProtInc. DR Gene3D; 3.30.720.90; -; 1. DR InterPro; IPR002675; Ribosomal_eL38. DR InterPro; IPR038464; Ribosomal_eL38_sf. DR PANTHER; PTHR10965; 60S RIBOSOMAL PROTEIN L38; 1. DR PANTHER; PTHR10965:SF0; 60S RIBOSOMAL PROTEIN L38; 1. DR Pfam; PF01781; Ribosomal_L38e; 1. DR Genevisible; P63173; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Isopeptide bond; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; Ubl conjugation. FT CHAIN 1..70 FT /note="Large ribosomal subunit protein eL38" FT /id="PRO_0000215434" FT MOD_RES 9 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 67 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT CROSSLNK 4 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 9 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:28112733" SQ SEQUENCE 70 AA; 8218 MW; FDD9A107BC98DBBA CRC64; MPRKIEEIKD FLLTARRKDA KSVKIKKNKD NVKFKVRCSR YLYTLVITDK EKAEKLKQSL PPGLAVKELK //