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   11-NOV-2015, entry version 110.
DE   RecName: Full=60S ribosomal protein L38;
GN   Name=RPL38;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
RT   and detection of an unusual RPL38 processed pseudogene in the promoter
RT   region 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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RT   project: 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;
RA   Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N.,
RA   Hudson T.J., Tanaka T., Page D.C.;
RT   "A map of 75 human ribosomal protein genes.";
RL   Genome Res. 8:509-523(1998).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-9 AND LYS-67, 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.,
RA   Walther T.C., 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   [7]
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.,
RA   Buerckstuemmer T., 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   [8]
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.,
RA   Ayoub D., 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   [9]
RP   STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).
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).
CC   -!- INTERACTION:
CC       P22392:NME2; NbExp=1; IntAct=EBI-359141, EBI-713693;
CC       O43353:RIPK2; NbExp=1; IntAct=EBI-359141, EBI-358522;
CC       P19532:TFE3; NbExp=1; IntAct=EBI-359141, EBI-1048957;
CC   -!- SIMILARITY: Belongs to the ribosomal protein L38e family.
CC       {ECO:0000305}.
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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   UniGene; Hs.380953; -.
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   PDBsum; 4UG0; -.
DR   PDBsum; 4V6X; -.
DR   PDBsum; 5AJ0; -.
DR   ProteinModelPortal; P63173; -.
DR   SMR; P63173; 2-70.
DR   BioGrid; 112088; 77.
DR   IntAct; P63173; 12.
DR   MINT; MINT-5002686; -.
DR   STRING; 9606.ENSP00000309830; -.
DR   PhosphoSite; P63173; -.
DR   DMDM; 52783779; -.
DR   MaxQB; P63173; -.
DR   PaxDb; P63173; -.
DR   PRIDE; P63173; -.
DR   DNASU; 6169; -.
DR   Ensembl; ENST00000311111; ENSP00000309830; ENSG00000172809.
DR   Ensembl; ENST00000439590; ENSP00000390279; ENSG00000172809.
DR   Ensembl; ENST00000533498; ENSP00000434243; ENSG00000172809.
DR   GeneID; 6169; -.
DR   KEGG; hsa:6169; -.
DR   UCSC; uc002jjz.3; human.
DR   CTD; 6169; -.
DR   GeneCards; RPL38; -.
DR   HGNC; HGNC:10349; RPL38.
DR   HPA; HPA052543; -.
DR   MIM; 604182; gene.
DR   neXtProt; NX_P63173; -.
DR   PharmGKB; PA34741; -.
DR   eggNOG; KOG3499; Eukaryota.
DR   eggNOG; ENOG4112229; LUCA.
DR   GeneTree; ENSGT00390000003718; -.
DR   HOGENOM; HOG000188979; -.
DR   HOVERGEN; HBG001013; -.
DR   InParanoid; P63173; -.
DR   KO; K02923; -.
DR   OMA; LYTLVIQ; -.
DR   OrthoDB; EOG79W98H; -.
DR   PhylomeDB; P63173; -.
DR   TreeFam; TF300215; -.
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-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-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   ChiTaRS; RPL38; human.
DR   GeneWiki; 60S_ribosomal_protein_L38; -.
DR   GenomeRNAi; 6169; -.
DR   NextBio; 23965; -.
DR   PRO; PR:P63173; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   Bgee; P63173; -.
DR   CleanEx; HS_RPL38; -.
DR   ExpressionAtlas; P63173; baseline and differential.
DR   Genevisible; P63173; HS.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR   GO; GO:0033291; C:eukaryotic 80S initiation complex; IEA:Ensembl.
DR   GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR   GO; GO:0003735; F:structural constituent of ribosome; NAS:UniProtKB.
DR   GO; GO:0034463; P:90S preribosome assembly; IEA:Ensembl.
DR   GO; GO:0048318; P:axial mesoderm development; IEA:Ensembl.
DR   GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
DR   GO; GO:0010467; P:gene expression; TAS:Reactome.
DR   GO; GO:0042474; P:middle ear morphogenesis; IEA:Ensembl.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
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:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
DR   GO; GO:0006412; P:translation; NAS:UniProtKB.
DR   GO; GO:0006414; P:translational elongation; TAS:Reactome.
DR   GO; GO:0006413; P:translational initiation; TAS:Reactome.
DR   GO; GO:0006415; P:translational termination; TAS:Reactome.
DR   GO; GO:0019058; P:viral life cycle; TAS:Reactome.
DR   GO; GO:0016032; P:viral process; TAS:Reactome.
DR   GO; GO:0019083; P:viral transcription; TAS:Reactome.
DR   InterPro; IPR002675; Ribosomal_L38e.
DR   PANTHER; PTHR10965; PTHR10965; 1.
DR   Pfam; PF01781; Ribosomal_L38e; 1.
DR   ProDom; PD010361; Ribosomal_L38e; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Complete proteome; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:P63174}.
FT   CHAIN         2     70       60S ribosomal protein L38.
FT                                /FTId=PRO_0000215434.
FT   MOD_RES       9      9       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES      67     67       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
SQ   SEQUENCE   70 AA;  8218 MW;  FDD9A107BC98DBBA CRC64;
     MPRKIEEIKD FLLTARRKDA KSVKIKKNKD NVKFKVRCSR YLYTLVITDK EKAEKLKQSL
     PPGLAVKELK
//