RL38_HUMAN
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 03-AUG-2022, entry version 164.
DE RecName: Full=60S ribosomal protein L38;
DE AltName: Full=Large ribosomal subunit protein eL38 {ECO:0000303|PubMed:24524803};
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 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 AlphaFoldDB; P63173; -.
DR SMR; P63173; -.
DR BioGRID; 112088; 233.
DR ComplexPortal; CPX-5183; 60S cytosolic large ribosomal subunit.
DR CORUM; P63173; -.
DR IntAct; P63173; 56.
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; P63173; -.
DR PeptideAtlas; P63173; -.
DR PRIDE; P63173; -.
DR ProteomicsDB; 57503; -.
DR TopDownProteomics; P63173; -.
DR Antibodypedia; 45939; 112 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 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; RCHRHLY; -.
DR OrthoDB; 1619070at2759; -.
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; 790 hits in 1078 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 210 other tissues.
DR ExpressionAtlas; P63173; baseline and differential.
DR Genevisible; P63173; 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; 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:0042788; C:polysomal ribosome; IDA: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:FlyBase.
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:0006417; P:regulation of translation; IEA:Ensembl.
DR GO; GO:0022618; P:ribonucleoprotein complex assembly; IBA:GO_Central.
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_L38e.
DR InterPro; IPR038464; Ribosomal_L38e_sf.
DR PANTHER; PTHR10965; PTHR10965; 1.
DR Pfam; PF01781; Ribosomal_L38e; 1.
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="60S ribosomal protein L38"
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
